Log page index: User:ProteinBoxBot/PBB_Log_Index
Protein Status Quick Log - Date: 05:52, 4 October 2007 (UTC)
[edit]Proteins without matches (19)
[edit]Proteins with a High Potential Match (31)
[edit]Manual Inspection (Page not found) (46)
[edit]
Protein Status Grid - Date: 05:52, 4 October 2007 (UTC)
[edit]Vebose Log - Date: 05:52, 4 October 2007 (UTC)
[edit]- INFO: Beginning work on ABCB1... {October 3, 2007 10:34:32 PM PDT}
- AMBIGUITY: Did not locate an acceptable page to update. {October 3, 2007 10:35:54 PM PDT}
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = ATP-binding cassette, sub-family B (MDR/TAP), member 1
| HGNCid = 40
| Symbol = ABCB1
| AltSymbols =; ABC20; CD243; CLCS; GP170; MDR1; MGC163296; P-gp; PGY1
| OMIM = 171050
| ECnumber =
| Homologene = 55496
| MGIid = 97570
| GeneAtlas_image1 = PBB_GE_ABCB1_209994_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_ABCB1_209993_at_tn.png
<!-- The Following entry is a time stamp of the last bot update. It is typically hidden data -->
| DateOfBotUpdate = ~~~~~
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0005215 |text = transporter activity}} {{GNF_GO|id=GO:0005524 |text = ATP binding}} {{GNF_GO|id=GO:0008559 |text = xenobiotic-transporting ATPase activity}} {{GNF_GO|id=GO:0016787 |text = hydrolase activity}} {{GNF_GO|id=GO:0016887 |text = ATPase activity}}
| Component = {{GNF_GO|id=GO:0005624 |text = membrane fraction}} {{GNF_GO|id=GO:0009986 |text = cell surface}} {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}}
| Process = {{GNF_GO|id=GO:0006810 |text = transport}} {{GNF_GO|id=GO:0042493 |text = response to drug}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 5243
| Hs_Ensembl = ENSG00000085563
| Hs_RefseqProtein = NP_000918
| Hs_RefseqmRNA = NM_000927
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 7
| Hs_GenLoc_start = 86970884
| Hs_GenLoc_end = 87180500
| Hs_Uniprot = P08183
| Mm_EntrezGene = 18671
| Mm_Ensembl = ENSMUSG00000040584
| Mm_RefseqmRNA = NM_011076
| Mm_RefseqProtein = NP_035206
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 5
| Mm_GenLoc_start = 8666098
| Mm_GenLoc_end = 8754140
| Mm_Uniprot = Q9QX25
}}
}}
'''ATP-binding cassette, sub-family B (MDR/TAP), member 1''', also known as '''ABCB1''', is a human [[gene]].
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = The membrane-associated protein encoded by this gene is a member of the superfamily of ATP-binding cassette (ABC) transporters. ABC proteins transport various molecules across extra- and intra-cellular membranes. ABC genes are divided into seven distinct subfamilies (ABC1, MDR/TAP, MRP, ALD, OABP, GCN20, White). This protein is a member of the MDR/TAP subfamily. Members of the MDR/TAP subfamily are involved in multidrug resistance. The protein encoded by this gene is an ATP-dependent drug efflux pump for xenobiotic compounds with broad substrate specificity. It is responsible for decreased drug accumulation in multidrug-resistant cells and often mediates the development of resistance to anticancer drugs. This protein also functions as a transporter in the blood-brain barrier.<ref>{{cite web | title = Entrez Gene: ABCB1 ATP-binding cassette, sub-family B (MDR/TAP), member 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5243| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Ling V |title=Multidrug resistance: molecular mechanisms and clinical relevance. |journal=Cancer Chemother. Pharmacol. |volume=40 Suppl |issue= |pages= S3-8 |year= 1997 |pmid= 9272126 |doi= }}
*{{cite journal | author=Kerb R, Hoffmeyer S, Brinkmann U |title=ABC drug transporters: hereditary polymorphisms and pharmacological impact in MDR1, MRP1 and MRP2. |journal=Pharmacogenomics |volume=2 |issue= 1 |pages= 51-64 |year= 2001 |pmid= 11258197 |doi= 10.1517/14622416.2.1.51 }}
*{{cite journal | author=Akiyama S |title=[Mechanisms of drug resistance and reversal of the resistance] |journal=Hum. Cell |volume=14 |issue= 4 |pages= 257-60 |year= 2002 |pmid= 11925925 |doi= }}
*{{cite journal | author=Brinkmann U |title=Functional polymorphisms of the human multidrug resistance (MDR1) gene: correlation with P glycoprotein expression and activity in vivo. |journal=Novartis Found. Symp. |volume=243 |issue= |pages= 207-10; discussion 210-2, 231-5 |year= 2002 |pmid= 11990778 |doi= }}
*{{cite journal | author=Váradi A, Szakács G, Bakos E, Sarkadi B |title=P glycoprotein and the mechanism of multidrug resistance. |journal=Novartis Found. Symp. |volume=243 |issue= |pages= 54-65; discussion 65-8, 180-5 |year= 2002 |pmid= 11990782 |doi= }}
*{{cite journal | author=Hegedus T, Orfi L, Seprodi A, ''et al.'' |title=Interaction of tyrosine kinase inhibitors with the human multidrug transporter proteins, MDR1 and MRP1. |journal=Biochim. Biophys. Acta |volume=1587 |issue= 2-3 |pages= 318-25 |year= 2002 |pmid= 12084474 |doi= }}
*{{cite journal | author=Pallis M, Turzanski J, Higashi Y, Russell N |title=P-glycoprotein in acute myeloid leukaemia: therapeutic implications of its association with both a multidrug-resistant and an apoptosis-resistant phenotype. |journal=Leuk. Lymphoma |volume=43 |issue= 6 |pages= 1221-8 |year= 2003 |pmid= 12152989 |doi= }}
*{{cite journal | author=Schaich M, Illmer T |title=Mdr1 gene expression and mutations in Ras proto-oncogenes in acute myeloid leukemia. |journal=Leuk. Lymphoma |volume=43 |issue= 7 |pages= 1345-54 |year= 2003 |pmid= 12389613 |doi= }}
*{{cite journal | author=Fromm MF |title=The influence of MDR1 polymorphisms on P-glycoprotein expression and function in humans. |journal=Adv. Drug Deliv. Rev. |volume=54 |issue= 10 |pages= 1295-310 |year= 2003 |pmid= 12406646 |doi= }}
*{{cite journal | author=Ambudkar SV, Kimchi-Sarfaty C, Sauna ZE, Gottesman MM |title=P-glycoprotein: from genomics to mechanism. |journal=Oncogene |volume=22 |issue= 47 |pages= 7468-85 |year= 2003 |pmid= 14576852 |doi= 10.1038/sj.onc.1206948 }}
*{{cite journal | author=Jamroziak K, Robak T |title=Pharmacogenomics of MDR1/ABCB1 gene: the influence on risk and clinical outcome of haematological malignancies. |journal=Hematology |volume=9 |issue= 2 |pages= 91-105 |year= 2004 |pmid= 15203864 |doi= 10.1080/10245330310001638974 }}
*{{cite journal | author=Ishikawa T, Onishi Y, Hirano H, ''et al.'' |title=Pharmacogenomics of drug transporters: a new approach to functional analysis of the genetic polymorphisms of ABCB1 (P-glycoprotein/MDR1). |journal=Biol. Pharm. Bull. |volume=27 |issue= 7 |pages= 939-48 |year= 2005 |pmid= 15256718 |doi= }}
*{{cite journal | author=Lee W, Lockhart AC, Kim RB, Rothenberg ML |title=Cancer pharmacogenomics: powerful tools in cancer chemotherapy and drug development. |journal=Oncologist |volume=10 |issue= 2 |pages= 104-11 |year= 2005 |pmid= 15709212 |doi= 10.1634/theoncologist.10-2-104 }}
*{{cite journal | author=Gambrelle J, Labialle S, Dayan G, ''et al.'' |title=[Multidrug resistance in uveal melanoma.] |journal=Journal français d'ophtalmologie |volume=28 |issue= 6 |pages= 652-9 |year= 2005 |pmid= 16141933 |doi= }}
*{{cite journal | author=Al-Shawi MK, Omote H |title=The remarkable transport mechanism of P-glycoprotein: a multidrug transporter. |journal=J. Bioenerg. Biomembr. |volume=37 |issue= 6 |pages= 489-96 |year= 2006 |pmid= 16691488 |doi= 10.1007/s10863-005-9497-5 }}
*{{cite journal | author=Orlowski S, Martin S, Escargueil A |title=P-glycoprotein and 'lipid rafts': some ambiguous mutual relationships (floating on them, building them or meeting them by chance?). |journal=Cell. Mol. Life Sci. |volume=63 |issue= 9 |pages= 1038-59 |year= 2006 |pmid= 16721513 |doi= 10.1007/s00018-005-5554-9 }}
*{{cite journal | author=Annese V, Valvano MR, Palmieri O, ''et al.'' |title=Multidrug resistance 1 gene in inflammatory bowel disease: a meta-analysis. |journal=World J. Gastroenterol. |volume=12 |issue= 23 |pages= 3636-44 |year= 2006 |pmid= 16773678 |doi= }}
*{{cite journal | author=Sekine I, Minna JD, Nishio K, ''et al.'' |title=A literature review of molecular markers predictive of clinical response to cytotoxic chemotherapy in patients with lung cancer. |journal=Journal of thoracic oncology : official publication of the International Association for the Study of Lung Cancer |volume=1 |issue= 1 |pages= 31-7 |year= 2007 |pmid= 17409824 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on ADIPOQ... {October 3, 2007 10:50:22 PM PDT}
- AMBIGUITY: Did not locate an acceptable page to update. {October 3, 2007 10:51:08 PM PDT}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB = {{PDB2|1c28}}, {{PDB2|1c3h}}
| Name = Adiponectin, C1Q and collagen domain containing
| HGNCid = 13633
| Symbol = ADIPOQ
| AltSymbols =; ACDC; ACRP30; APM-1; APM1; GBP28; adiponectin
| OMIM = 605441
| ECnumber =
| Homologene = 3525
| MGIid = 106675
| GeneAtlas_image1 = PBB_GE_ADIPOQ_207175_at_tn.png
<!-- The Following entry is a time stamp of the last bot update. It is typically hidden data -->
| DateOfBotUpdate = ~~~~~
| Function = {{GNF_GO|id=GO:0005179 |text = hormone activity}}
| Component = {{GNF_GO|id=GO:0005576 |text = extracellular region}} {{GNF_GO|id=GO:0005615 |text = extracellular space}} {{GNF_GO|id=GO:0005737 |text = cytoplasm}} {{GNF_GO|id=GO:0005783 |text = endoplasmic reticulum}}
| Process = {{GNF_GO|id=GO:0006006 |text = glucose metabolic process}} {{GNF_GO|id=GO:0006091 |text = generation of precursor metabolites and energy}} {{GNF_GO|id=GO:0006635 |text = fatty acid beta-oxidation}} {{GNF_GO|id=GO:0006817 |text = phosphate transport}} {{GNF_GO|id=GO:0009749 |text = response to glucose stimulus}} {{GNF_GO|id=GO:0042593 |text = glucose homeostasis}} {{GNF_GO|id=GO:0043123 |text = positive regulation of I-kappaB kinase/NF-kappaB cascade}} {{GNF_GO|id=GO:0045721 |text = negative regulation of gluconeogenesis}} {{GNF_GO|id=GO:0045923 |text = positive regulation of fatty acid metabolic process}} {{GNF_GO|id=GO:0046326 |text = positive regulation of glucose import}} {{GNF_GO|id=GO:0051260 |text = protein homooligomerization}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 9370
| Hs_Ensembl = ENSG00000181092
| Hs_RefseqProtein = NP_004788
| Hs_RefseqmRNA = NM_004797
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 3
| Hs_GenLoc_start = 188043157
| Hs_GenLoc_end = 188058944
| Hs_Uniprot = Q15848
| Mm_EntrezGene = 11450
| Mm_Ensembl = ENSMUSG00000022878
| Mm_RefseqmRNA = NM_009605
| Mm_RefseqProtein = NP_033735
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 16
| Mm_GenLoc_start = 23061870
| Mm_GenLoc_end = 23073302
| Mm_Uniprot = Q6GTX4
}}
}}
'''Adiponectin, C1Q and collagen domain containing''', also known as '''ADIPOQ''', is a human [[gene]].
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = This gene is expressed in adipose tissue exclusively. It encodes a protein with similarity to collagens X and VIII and complement factor C1q. The encoded protein circulates in the plasma and is involved with metabolic and hormonal processes.<ref>{{cite web | title = Entrez Gene: ADIPOQ adiponectin, C1Q and collagen domain containing| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=9370| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Ukkola O, Santaniemi M |title=Adiponectin: a link between excess adiposity and associated comorbidities? |journal=J. Mol. Med. |volume=80 |issue= 11 |pages= 696-702 |year= 2003 |pmid= 12436346 |doi= 10.1007/s00109-002-0378-7 }}
*{{cite journal | author=Díez JJ, Iglesias P |title=The role of the novel adipocyte-derived hormone adiponectin in human disease. |journal=Eur. J. Endocrinol. |volume=148 |issue= 3 |pages= 293-300 |year= 2003 |pmid= 12611609 |doi= }}
*{{cite journal | author=Vasseur F, Leprêtre F, Lacquemant C, Froguel P |title=The genetics of adiponectin. |journal=Curr. Diab. Rep. |volume=3 |issue= 2 |pages= 151-8 |year= 2003 |pmid= 12728641 |doi= }}
*{{cite journal | author=Matsuzawa Y, Funahashi T, Kihara S, Shimomura I |title=Adiponectin and metabolic syndrome. |journal=Arterioscler. Thromb. Vasc. Biol. |volume=24 |issue= 1 |pages= 29-33 |year= 2004 |pmid= 14551151 |doi= 10.1161/01.ATV.0000099786.99623.EF }}
*{{cite journal | author=Nedvídková J, Smitka K, Kopský V, Hainer V |title=Adiponectin, an adipocyte-derived protein. |journal=Physiological research / Academia Scientiarum Bohemoslovaca |volume=54 |issue= 2 |pages= 133-40 |year= 2006 |pmid= 15544426 |doi= }}
*{{cite journal | author=Hug C, Lodish HF |title=The role of the adipocyte hormone adiponectin in cardiovascular disease. |journal=Current opinion in pharmacology |volume=5 |issue= 2 |pages= 129-34 |year= 2005 |pmid= 15780820 |doi= 10.1016/j.coph.2005.01.001 }}
*{{cite journal | author=Hara K, Yamauchi T, Kadowaki T |title=Adiponectin: an adipokine linking adipocytes and type 2 diabetes in humans. |journal=Curr. Diab. Rep. |volume=5 |issue= 2 |pages= 136-40 |year= 2005 |pmid= 15794918 |doi= }}
*{{cite journal | author=Menzaghi C, Trischitta V, Doria A |title=Genetic influences of adiponectin on insulin resistance, type 2 diabetes, and cardiovascular disease. |journal=Diabetes |volume=56 |issue= 5 |pages= 1198-209 |year= 2007 |pmid= 17303804 |doi= 10.2337/db06-0506 }}
*{{cite journal | author=Lara-Castro C, Fu Y, Chung BH, Garvey WT |title=Adiponectin and the metabolic syndrome: mechanisms mediating risk for metabolic and cardiovascular disease. |journal=Curr. Opin. Lipidol. |volume=18 |issue= 3 |pages= 263-70 |year= 2007 |pmid= 17495599 |doi= 10.1097/MOL.0b013e32814a645f }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on ATM... {October 3, 2007 10:02:25 PM PDT}
- AMBIGUITY: Did not locate an acceptable page to update. {October 3, 2007 10:03:05 PM PDT}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
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| update_protein_box = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Ataxia telangiectasia mutated (includes complementation groups A, C and D)
| HGNCid = 795
| Symbol = ATM
| AltSymbols =; AT1; ATD; ATA; ATC; ATDC; ATE; DKFZp781A0353; MGC74674; TEL1; TELO1
| OMIM = 607585
| ECnumber =
| Homologene = 30952
| MGIid = 107202
<!-- The Following entry is a time stamp of the last bot update. It is typically hidden data -->
| DateOfBotUpdate = ~~~~~
| Function = {{GNF_GO|id=GO:0003677 |text = DNA binding}} {{GNF_GO|id=GO:0004674 |text = protein serine/threonine kinase activity}} {{GNF_GO|id=GO:0016303 |text = 1-phosphatidylinositol-3-kinase activity}} {{GNF_GO|id=GO:0016740 |text = transferase activity}} {{GNF_GO|id=GO:0016773 |text = phosphotransferase activity, alcohol group as acceptor}} {{GNF_GO|id=GO:0047485 |text = protein N-terminus binding}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}}
| Process = {{GNF_GO|id=GO:0006281 |text = DNA repair}} {{GNF_GO|id=GO:0007049 |text = cell cycle}} {{GNF_GO|id=GO:0007094 |text = mitotic cell cycle spindle assembly checkpoint}} {{GNF_GO|id=GO:0007131 |text = meiotic recombination}} {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0010212 |text = response to ionizing radiation}} {{GNF_GO|id=GO:0045786 |text = negative regulation of progression through cell cycle}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 472
| Hs_Ensembl =
| Hs_RefseqProtein = NP_000042
| Hs_RefseqmRNA = NM_000051
| Hs_GenLoc_db =
| Hs_GenLoc_chr =
| Hs_GenLoc_start =
| Hs_GenLoc_end =
| Hs_Uniprot =
| Mm_EntrezGene = 11920
| Mm_Ensembl = ENSMUSG00000034218
| Mm_RefseqmRNA = NM_007499
| Mm_RefseqProtein = NP_031525
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 9
| Mm_GenLoc_start = 53201763
| Mm_GenLoc_end = 53296362
| Mm_Uniprot = Q3UT15
}}
}}
'''Ataxia telangiectasia mutated (includes complementation groups A, C and D)''', also known as '''ATM''', is a human [[gene]].
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = The protein encoded by this gene belongs to the PI3/PI4-kinase family. This protein is an important cell cycle checkpoint kinase that phosphorylates; thus, it functions as a regulator of a wide variety of downstream proteins, including tumor suppressor proteins p53 and BRCA1, checkpoint kinase CHK2, checkpoint proteins RAD17 and RAD9, and DNA repair protein NBS1. This protein and the closely related kinase ATR are thought to be master controllers of cell cycle checkpoint signaling pathways that are required for cell response to DNA damage and for genome stability. Mutations in this gene are associated with ataxia telangiectasia, an autosomal recessive disorder. Two transcript variants encoding different isoforms have been found for this gene.<ref>{{cite web | title = Entrez Gene: ATM ataxia telangiectasia mutated (includes complementation groups A, C and D)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=472| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Giaccia AJ, Kastan MB |title=The complexity of p53 modulation: emerging patterns from divergent signals. |journal=Genes Dev. |volume=12 |issue= 19 |pages= 2973-83 |year= 1998 |pmid= 9765199 |doi= }}
*{{cite journal | author=Kastan MB, Lim DS |title=The many substrates and functions of ATM. |journal=Nat. Rev. Mol. Cell Biol. |volume=1 |issue= 3 |pages= 179-86 |year= 2001 |pmid= 11252893 |doi= 10.1038/35043058 }}
*{{cite journal | author=Shiloh Y |title=ATM: from phenotype to functional genomics--and back. |journal=Ernst Schering Res. Found. Workshop |volume= |issue= 36 |pages= 51-70 |year= 2002 |pmid= 11859564 |doi= }}
*{{cite journal | author=Redon C, Pilch D, Rogakou E, ''et al.'' |title=Histone H2A variants H2AX and H2AZ. |journal=Curr. Opin. Genet. Dev. |volume=12 |issue= 2 |pages= 162-9 |year= 2002 |pmid= 11893489 |doi= }}
*{{cite journal | author=Tang Y |title=[ATM and Cancer] |journal=Zhongguo Shi Yan Xue Ye Xue Za Zhi |volume=10 |issue= 1 |pages= 77-80 |year= 2003 |pmid= 12513844 |doi= }}
*{{cite journal | author=Shiloh Y |title=ATM and related protein kinases: safeguarding genome integrity. |journal=Nat. Rev. Cancer |volume=3 |issue= 3 |pages= 155-68 |year= 2003 |pmid= 12612651 |doi= 10.1038/nrc1011 }}
*{{cite journal | author=Gumy-Pause F, Wacker P, Sappino AP |title=ATM gene and lymphoid malignancies. |journal=Leukemia |volume=18 |issue= 2 |pages= 238-42 |year= 2004 |pmid= 14628072 |doi= 10.1038/sj.leu.2403221 }}
*{{cite journal | author=Kurz EU, Lees-Miller SP |title=DNA damage-induced activation of ATM and ATM-dependent signaling pathways. |journal=DNA Repair (Amst.) |volume=3 |issue= 8-9 |pages= 889-900 |year= 2005 |pmid= 15279774 |doi= 10.1016/j.dnarep.2004.03.029 }}
*{{cite journal | author=Abraham RT |title=The ATM-related kinase, hSMG-1, bridges genome and RNA surveillance pathways. |journal=DNA Repair (Amst.) |volume=3 |issue= 8-9 |pages= 919-25 |year= 2005 |pmid= 15279777 |doi= 10.1016/j.dnarep.2004.04.003 }}
*{{cite journal | author=Lavin MF, Scott S, Gueven N, ''et al.'' |title=Functional consequences of sequence alterations in the ATM gene. |journal=DNA Repair (Amst.) |volume=3 |issue= 8-9 |pages= 1197-205 |year= 2005 |pmid= 15279808 |doi= 10.1016/j.dnarep.2004.03.011 }}
*{{cite journal | author=Meulmeester E, Pereg Y, Shiloh Y, Jochemsen AG |title=ATM-mediated phosphorylations inhibit Mdmx/Mdm2 stabilization by HAUSP in favor of p53 activation. |journal=Cell Cycle |volume=4 |issue= 9 |pages= 1166-70 |year= 2006 |pmid= 16082221 |doi= }}
*{{cite journal | author=Ahmed M, Rahman N |title=ATM and breast cancer susceptibility. |journal=Oncogene |volume=25 |issue= 43 |pages= 5906-11 |year= 2006 |pmid= 16998505 |doi= 10.1038/sj.onc.1209873 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on BAX... {October 3, 2007 10:03:05 PM PDT}
- AMBIGUITY: Did not locate an acceptable page to update. {October 3, 2007 10:03:57 PM PDT}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB = {{PDB2|1f16}}
| Name = BCL2-associated X protein
| HGNCid = 959
| Symbol = BAX
| AltSymbols =; Bax zeta
| OMIM = 600040
| ECnumber =
| Homologene = 7242
| MGIid = 99702
| GeneAtlas_image1 = PBB_GE_BAX_208478_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_BAX_211833_s_at_tn.png
<!-- The Following entry is a time stamp of the last bot update. It is typically hidden data -->
| DateOfBotUpdate = ~~~~~
| Function = {{GNF_GO|id=GO:0003674 |text = molecular_function}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0051434 |text = BH3 domain binding}}
| Component = {{GNF_GO|id=GO:0005575 |text = cellular_component}} {{GNF_GO|id=GO:0005625 |text = soluble fraction}} {{GNF_GO|id=GO:0005737 |text = cytoplasm}} {{GNF_GO|id=GO:0005739 |text = mitochondrion}} {{GNF_GO|id=GO:0005741 |text = mitochondrial outer membrane}} {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}} {{GNF_GO|id=GO:0044445 |text = cytosolic part}}
| Process = {{GNF_GO|id=GO:0001836 |text = release of cytochrome c from mitochondria}} {{GNF_GO|id=GO:0001844 |text = protein insertion into mitochondrial membrane during induction of apoptosis}} {{GNF_GO|id=GO:0006915 |text = apoptosis}} {{GNF_GO|id=GO:0006917 |text = induction of apoptosis}} {{GNF_GO|id=GO:0006974 |text = response to DNA damage stimulus}} {{GNF_GO|id=GO:0007049 |text = cell cycle}} {{GNF_GO|id=GO:0007281 |text = germ cell development}} {{GNF_GO|id=GO:0007283 |text = spermatogenesis}} {{GNF_GO|id=GO:0007399 |text = nervous system development}} {{GNF_GO|id=GO:0008624 |text = induction of apoptosis by extracellular signals}} {{GNF_GO|id=GO:0008629 |text = induction of apoptosis by intracellular signals}} {{GNF_GO|id=GO:0008634 |text = negative regulation of survival gene product activity}} {{GNF_GO|id=GO:0008635 |text = caspase activation via cytochrome c}} {{GNF_GO|id=GO:0008637 |text = apoptotic mitochondrial changes}} {{GNF_GO|id=GO:0009611 |text = response to wounding}} {{GNF_GO|id=GO:0030264 |text = nuclear fragmentation during apoptosis}} {{GNF_GO|id=GO:0042981 |text = regulation of apoptosis}} {{GNF_GO|id=GO:0043281 |text = regulation of caspase activity}} {{GNF_GO|id=GO:0045786 |text = negative regulation of progression through cell cycle}} {{GNF_GO|id=GO:0046666 |text = retinal cell programmed cell death}} {{GNF_GO|id=GO:0048147 |text = negative regulation of fibroblast proliferation}} {{GNF_GO|id=GO:0051260 |text = protein homooligomerization}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 581
| Hs_Ensembl = ENSG00000087088
| Hs_RefseqProtein = NP_004315
| Hs_RefseqmRNA = NM_004324
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 19
| Hs_GenLoc_start = 54149929
| Hs_GenLoc_end = 54156864
| Hs_Uniprot = Q07814
| Mm_EntrezGene = 12028
| Mm_Ensembl = ENSMUSG00000003873
| Mm_RefseqmRNA = NM_007527
| Mm_RefseqProtein = NP_031553
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 7
| Mm_GenLoc_start = 45329742
| Mm_GenLoc_end = 45334871
| Mm_Uniprot = Q3TXJ7
}}
}}
'''BCL2-associated X protein''', also known as '''BAX''', is a human [[gene]].
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = The protein encoded by this gene belongs to the BCL2 protein family. BCL2 family members form hetero- or homodimers and act as anti- or pro-apoptotic regulators that are involved in a wide variety of cellular activities. This protein forms a heterodimer with BCL2, and functions as an apoptotic activator. This protein is reported to interact with, and increase the opening of, the mitochondrial voltage-dependent anion channel (VDAC), which leads to the loss in membrane potential and the release of cytochrome c. The expression of this gene is regulated by the tumor suppressor P53 and has been shown to be involved in P53-mediated apoptosis. Multiple alternatively spliced transcript variants, which encode different isoforms, have been reported for this gene.<ref>{{cite web | title = Entrez Gene: BAX BCL2-associated X protein| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=581| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Vieira HL, Haouzi D, El Hamel C, ''et al.'' |title=Permeabilization of the mitochondrial inner membrane during apoptosis: impact of the adenine nucleotide translocator. |journal=Cell Death Differ. |volume=7 |issue= 12 |pages= 1146-54 |year= 2001 |pmid= 11175251 |doi= 10.1038/sj.cdd.4400778 }}
*{{cite journal | author=Buytaert E, Callewaert G, Vandenheede JR, Agostinis P |title=Deficiency in apoptotic effectors Bax and Bak reveals an autophagic cell death pathway initiated by photodamage to the endoplasmic reticulum. |journal=Autophagy |volume=2 |issue= 3 |pages= 238-40 |year= 2007 |pmid= 16874066 |doi= }}
*{{cite journal | author=Steele AD, Yi CH |title=Neuromuscular denervation: Bax up against the wall in amyotrophic lateral sclerosis. |journal=J. Neurosci. |volume=26 |issue= 50 |pages= 12849-51 |year= 2007 |pmid= 17171827 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on CASP8... {October 3, 2007 10:04:58 PM PDT}
- AMBIGUITY: Did not locate an acceptable page to update. {October 3, 2007 10:05:56 PM PDT}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB = {{PDB2|1f9e}}, {{PDB2|1i4e}}, {{PDB2|1qdu}}, {{PDB2|1qtn}}, {{PDB2|2c2z}}, {{PDB2|2fun}}
| Name = Caspase 8, apoptosis-related cysteine peptidase
| HGNCid = 1509
| Symbol = CASP8
| AltSymbols =; CAP4; FLICE; MACH; MCH5; MGC78473
| OMIM = 601763
| ECnumber =
| Homologene = 7657
| MGIid = 1261423
| GeneAtlas_image1 = PBB_GE_CASP8_213373_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_CASP8_207686_s_at_tn.png
<!-- The Following entry is a time stamp of the last bot update. It is typically hidden data -->
| DateOfBotUpdate = ~~~~~
| Function = {{GNF_GO|id=GO:0004871 |text = signal transducer activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0008234 |text = cysteine-type peptidase activity}} {{GNF_GO|id=GO:0030693 |text = caspase activity}} {{GNF_GO|id=GO:0042802 |text = identical protein binding}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005737 |text = cytoplasm}} {{GNF_GO|id=GO:0005739 |text = mitochondrion}} {{GNF_GO|id=GO:0005856 |text = cytoskeleton}} {{GNF_GO|id=GO:0030690 |text = Noc1p-Noc2p complex}}
| Process = {{GNF_GO|id=GO:0001525 |text = angiogenesis}} {{GNF_GO|id=GO:0001841 |text = neural tube formation}} {{GNF_GO|id=GO:0006508 |text = proteolysis}} {{GNF_GO|id=GO:0007507 |text = heart development}} {{GNF_GO|id=GO:0008632 |text = apoptotic program}} {{GNF_GO|id=GO:0030225 |text = macrophage differentiation}} {{GNF_GO|id=GO:0042981 |text = regulation of apoptosis}} {{GNF_GO|id=GO:0043123 |text = positive regulation of I-kappaB kinase/NF-kappaB cascade}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 841
| Hs_Ensembl = ENSG00000064012
| Hs_RefseqProtein = NP_001073593
| Hs_RefseqmRNA = NM_001080124
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 2
| Hs_GenLoc_start = 201806426
| Hs_GenLoc_end = 201860677
| Hs_Uniprot = Q14790
| Mm_EntrezGene = 12370
| Mm_Ensembl = ENSMUSG00000026029
| Mm_RefseqmRNA = NM_001080126
| Mm_RefseqProtein = NP_001073595
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 1
| Mm_GenLoc_start = 58739978
| Mm_GenLoc_end = 58791553
| Mm_Uniprot = Q3U607
}}
}}
'''Caspase 8, apoptosis-related cysteine peptidase''', also known as '''CASP8''', is a human [[gene]].
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = This gene encodes a member of the cysteine-aspartic acid protease (caspase) family. Sequential activation of caspases plays a central role in the execution-phase of cell apoptosis. Caspases exist as inactive proenzymes composed of a prodomain, a large protease subunit, and a small protease subunit. Activation of caspases requires proteolytic processing at conserved internal aspartic residues to generate a heterodimeric enzyme consisting of the large and small subunits. This protein is involved in the programmed cell death induced by Fas and various apoptotic stimuli. The N-terminal FADD-like death effector domain of this protein suggests that it may interact with Fas-interacting protein FADD. This protein was detected in the insoluble fraction of the affected brain region from Huntington disease patients but not in those from normal controls, which implicated the role in neurodegenerative diseases. Many alternatively spliced transcript variants encoding different isoforms have been described, although not all variants have had their full-length sequences determined.<ref>{{cite web | title = Entrez Gene: CASP8 caspase 8, apoptosis-related cysteine peptidase| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=841| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Cohen GM |title=Caspases: the executioners of apoptosis. |journal=Biochem. J. |volume=326 ( Pt 1) |issue= |pages= 1-16 |year= 1997 |pmid= 9337844 |doi= }}
*{{cite journal | author=Siegel RM, Chan FK, Chun HJ, Lenardo MJ |title=The multifaceted role of Fas signaling in immune cell homeostasis and autoimmunity. |journal=Nat. Immunol. |volume=1 |issue= 6 |pages= 469-74 |year= 2001 |pmid= 11101867 |doi= 10.1038/82712 }}
*{{cite journal | author=Ye S, Goldsmith EJ |title=Serpins and other covalent protease inhibitors. |journal=Curr. Opin. Struct. Biol. |volume=11 |issue= 6 |pages= 740-5 |year= 2002 |pmid= 11751056 |doi= }}
*{{cite journal | author=Gupta S |title=Tumor necrosis factor-alpha-induced apoptosis in T cells from aged humans: a role of TNFR-I and downstream signaling molecules. |journal=Exp. Gerontol. |volume=37 |issue= 2-3 |pages= 293-9 |year= 2002 |pmid= 11772515 |doi= }}
*{{cite journal | author=Pomerantz RJ |title=Effects of HIV-1 Vpr on neuroinvasion and neuropathogenesis. |journal=DNA Cell Biol. |volume=23 |issue= 4 |pages= 227-38 |year= 2004 |pmid= 15142380 |doi= 10.1089/104454904773819815 }}
*{{cite journal | author=Zhao LJ, Zhu H |title=Structure and function of HIV-1 auxiliary regulatory protein Vpr: novel clues to drug design. |journal=Curr. Drug Targets Immune Endocr. Metabol. Disord. |volume=4 |issue= 4 |pages= 265-75 |year= 2005 |pmid= 15578977 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on CCL2... {October 3, 2007 10:43:11 PM PDT}
- AMBIGUITY: Did not locate an acceptable page to update. {October 3, 2007 10:44:00 PM PDT}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB = {{PDB2|1dok}}, {{PDB2|1dol}}, {{PDB2|1dom}}, {{PDB2|1don}}, {{PDB2|1ml0}}, {{PDB2|2bdn}}
| Name = Chemokine (C-C motif) ligand 2
| HGNCid = 10618
| Symbol = CCL2
| AltSymbols =; GDCF-2; GDCF-2 HC11; HC11; HSMCR30; MCAF; MCP-1; MCP1; MGC9434; SCYA2; SMC-CF
| OMIM = 158105
| ECnumber =
| Homologene = 2245
| MGIid = 108224
| GeneAtlas_image1 = PBB_GE_CCL2_216598_s_at_tn.png
<!-- The Following entry is a time stamp of the last bot update. It is typically hidden data -->
| DateOfBotUpdate = ~~~~~
| Function = {{GNF_GO|id=GO:0004672 |text = protein kinase activity}} {{GNF_GO|id=GO:0004871 |text = signal transducer activity}} {{GNF_GO|id=GO:0008009 |text = chemokine activity}}
| Component = {{GNF_GO|id=GO:0005576 |text = extracellular region}} {{GNF_GO|id=GO:0005615 |text = extracellular space}} {{GNF_GO|id=GO:0016020 |text = membrane}}
| Process = {{GNF_GO|id=GO:0006468 |text = protein amino acid phosphorylation}} {{GNF_GO|id=GO:0006874 |text = cellular calcium ion homeostasis}} {{GNF_GO|id=GO:0006916 |text = anti-apoptosis}} {{GNF_GO|id=GO:0006935 |text = chemotaxis}} {{GNF_GO|id=GO:0006954 |text = inflammatory response}} {{GNF_GO|id=GO:0006959 |text = humoral immune response}} {{GNF_GO|id=GO:0007155 |text = cell adhesion}} {{GNF_GO|id=GO:0007187 |text = G-protein signaling, coupled to cyclic nucleotide second messenger}} {{GNF_GO|id=GO:0007259 |text = JAK-STAT cascade}} {{GNF_GO|id=GO:0007267 |text = cell-cell signaling}} {{GNF_GO|id=GO:0009887 |text = organ morphogenesis}} {{GNF_GO|id=GO:0019079 |text = viral genome replication}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 6347
| Hs_Ensembl = ENSG00000108691
| Hs_RefseqProtein = NP_002973
| Hs_RefseqmRNA = NM_002982
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 17
| Hs_GenLoc_start = 29606409
| Hs_GenLoc_end = 29608329
| Hs_Uniprot = P13500
| Mm_EntrezGene = 20293
| Mm_Ensembl = ENSMUSG00000035352
| Mm_RefseqmRNA = NM_011331
| Mm_RefseqProtein = NP_035461
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 11
| Mm_GenLoc_start = 81918040
| Mm_GenLoc_end = 81919598
| Mm_Uniprot = Q5SVB4
}}
}}
'''Chemokine (C-C motif) ligand 2''', also known as '''CCL2''', is a human [[gene]].
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = This gene is one of several cytokine genes clustered on the q-arm of chromosome 17. Cytokines are a family of secreted proteins involved in immunoregulatory and inflammatory processes. The protein encoded by this gene is structurally related to the CXC subfamily of cytokines. Members of this subfamily are characterized by two cysteines separated by a single amino acid. This cytokine displays chemotactic activity for monocytes and basophils but not for neutrophils or eosinophils. It has been implicated in the pathogenesis of diseases characterized by monocytic infiltrates, like psoriasis, rheumatoid arthritis and atherosclerosis. It binds to chemokine receptors CCR2 and CCR4.<ref>{{cite web | title = Entrez Gene: CCL2 chemokine (C-C motif) ligand 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6347| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Yoshimura T, Leonard EJ |title=Human monocyte chemoattractant protein-1 (MCP-1). |journal=Adv. Exp. Med. Biol. |volume=305 |issue= |pages= 47-56 |year= 1992 |pmid= 1661560 |doi= }}
*{{cite journal | author=Wahl SM, Greenwell-Wild T, Hale-Donze H, ''et al.'' |title=Permissive factors for HIV-1 infection of macrophages. |journal=J. Leukoc. Biol. |volume=68 |issue= 3 |pages= 303-10 |year= 2000 |pmid= 10985244 |doi= }}
*{{cite journal | author=Sell H, Eckel J |title=Monocyte chemotactic protein-1 and its role in insulin resistance. |journal=Curr. Opin. Lipidol. |volume=18 |issue= 3 |pages= 258-62 |year= 2007 |pmid= 17495598 |doi= 10.1097/MOL.0b013e3281338546 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on CCND1... {October 3, 2007 10:03:57 PM PDT}
- AMBIGUITY: Did not locate an acceptable page to update. {October 3, 2007 10:04:58 PM PDT}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Cyclin D1
| HGNCid = 1582
| Symbol = CCND1
| AltSymbols =; BCL1; D11S287E; PRAD1; U21B31
| OMIM = 168461
| ECnumber =
| Homologene = 1334
| MGIid = 88313
| GeneAtlas_image1 = PBB_GE_CCND1_208712_at_tn.png
| GeneAtlas_image2 = PBB_GE_CCND1_208711_s_at_tn.png
<!-- The Following entry is a time stamp of the last bot update. It is typically hidden data -->
| DateOfBotUpdate = ~~~~~
| Function = {{GNF_GO|id=GO:0004672 |text = protein kinase activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0016538 |text = cyclin-dependent protein kinase regulator activity}}
| Component = {{GNF_GO|id=GO:0000307 |text = cyclin-dependent protein kinase holoenzyme complex}} {{GNF_GO|id=GO:0005575 |text = cellular_component}} {{GNF_GO|id=GO:0005622 |text = intracellular}} {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005829 |text = cytosol}}
| Process = {{GNF_GO|id=GO:0000082 |text = G1/S transition of mitotic cell cycle}} {{GNF_GO|id=GO:0000320 |text = re-entry into mitotic cell cycle}} {{GNF_GO|id=GO:0006468 |text = protein amino acid phosphorylation}} {{GNF_GO|id=GO:0007049 |text = cell cycle}} {{GNF_GO|id=GO:0030968 |text = unfolded protein response}} {{GNF_GO|id=GO:0045444 |text = fat cell differentiation}} {{GNF_GO|id=GO:0051301 |text = cell division}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 595
| Hs_Ensembl = ENSG00000110092
| Hs_RefseqProtein = NP_444284
| Hs_RefseqmRNA = NM_053056
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 11
| Hs_GenLoc_start = 69165054
| Hs_GenLoc_end = 69178422
| Hs_Uniprot = P24385
| Mm_EntrezGene = 12443
| Mm_Ensembl = ENSMUSG00000070348
| Mm_RefseqmRNA = XM_001002530
| Mm_RefseqProtein = XP_001002530
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 7
| Mm_GenLoc_start = 144739321
| Mm_GenLoc_end = 144749220
| Mm_Uniprot = Q3TC96
}}
}}
'''Cyclin D1''', also known as '''CCND1''', is a human [[gene]].
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = The protein encoded by this gene belongs to the highly conserved cyclin family, whose members are characterized by a dramatic periodicity in protein abundance throughout the cell cycle. Cyclins function as regulators of CDK kinases. Different cyclins exhibit distinct expression and degradation patterns which contribute to the temporal coordination of each mitotic event. This cyclin forms a complex with and functions as a regulatory subunit of CDK4 or CDK6, whose activity is required for cell cycle G1/S transition. This protein has been shown to interact with tumor suppressor protein Rb and the expression of this gene is regulated positively by Rb. Mutations, amplification and overexpression of this gene, which alters cell cycle progression, are observed frequently in a variety of tumors and may contribute to tumorigenesis.<ref>{{cite web | title = Entrez Gene: CCND1 cyclin D1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=595| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Akita H |title=[Prognostic importance of altered expression of cell cycle regulators in lung cancer] |journal=Nippon Rinsho |volume=60 Suppl 5 |issue= |pages= 267-71 |year= 2003 |pmid= 12101670 |doi= }}
*{{cite journal | author=Chung DC |title=Cyclin D1 in human neuroendocrine: tumorigenesis. |journal=Ann. N. Y. Acad. Sci. |volume=1014 |issue= |pages= 209-17 |year= 2004 |pmid= 15153436 |doi= }}
*{{cite journal | author=Jain S, Khuri FR, Shin DM |title=Prevention of head and neck cancer: current status and future prospects. |journal=Current problems in cancer |volume=28 |issue= 5 |pages= 265-86 |year= 2004 |pmid= 15375804 |doi= }}
*{{cite journal | author=Gladden AB, Diehl JA |title=Location, location, location: the role of cyclin D1 nuclear localization in cancer. |journal=J. Cell. Biochem. |volume=96 |issue= 5 |pages= 906-13 |year= 2006 |pmid= 16163738 |doi= 10.1002/jcb.20613 }}
*{{cite journal | author=Walker JL, Assoian RK |title=Integrin-dependent signal transduction regulating cyclin D1 expression and G1 phase cell cycle progression. |journal=Cancer Metastasis Rev. |volume=24 |issue= 3 |pages= 383-93 |year= 2006 |pmid= 16258726 |doi= 10.1007/s10555-005-5130-7 }}
*{{cite journal | author=Gautschi O, Ratschiller D, Gugger M, ''et al.'' |title=Cyclin D1 in non-small cell lung cancer: a key driver of malignant transformation. |journal=Lung Cancer |volume=55 |issue= 1 |pages= 1-14 |year= 2007 |pmid= 17070615 |doi= 10.1016/j.lungcan.2006.09.024 }}
*{{cite journal | author=Li Z, Wang C, Prendergast GC, Pestell RG |title=Cyclin D1 functions in cell migration. |journal=Cell Cycle |volume=5 |issue= 21 |pages= 2440-2 |year= 2007 |pmid= 17106256 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on CCR5... {October 3, 2007 10:08:18 PM PDT}
- AMBIGUITY: Did not locate an acceptable page to update. {October 3, 2007 10:08:44 PM PDT}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Chemokine (C-C motif) receptor 5
| HGNCid = 1606
| Symbol = CCR5
| AltSymbols =; CC-CKR-5; CCCKR5; CD195; CKR-5; CKR5; CMKBR5
| OMIM = 601373
| ECnumber =
| Homologene = 37325
| MGIid = 107182
<!-- The Following entry is a time stamp of the last bot update. It is typically hidden data -->
| DateOfBotUpdate = ~~~~~
| Function = {{GNF_GO|id=GO:0001584 |text = rhodopsin-like receptor activity}} {{GNF_GO|id=GO:0003779 |text = actin binding}} {{GNF_GO|id=GO:0004435 |text = phosphoinositide phospholipase C activity}} {{GNF_GO|id=GO:0004872 |text = receptor activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0015026 |text = coreceptor activity}} {{GNF_GO|id=GO:0016493 |text = C-C chemokine receptor activity}}
| Component = {{GNF_GO|id=GO:0005737 |text = cytoplasm}} {{GNF_GO|id=GO:0005768 |text = endosome}} {{GNF_GO|id=GO:0005886 |text = plasma membrane}} {{GNF_GO|id=GO:0005887 |text = integral to plasma membrane}} {{GNF_GO|id=GO:0009986 |text = cell surface}} {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}}
| Process = {{GNF_GO|id=GO:0006935 |text = chemotaxis}} {{GNF_GO|id=GO:0006954 |text = inflammatory response}} {{GNF_GO|id=GO:0006955 |text = immune response}} {{GNF_GO|id=GO:0006968 |text = cellular defense response}} {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0007186 |text = G-protein coupled receptor protein signaling pathway}} {{GNF_GO|id=GO:0007204 |text = elevation of cytosolic calcium ion concentration}} {{GNF_GO|id=GO:0007267 |text = cell-cell signaling}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 1234
| Hs_Ensembl =
| Hs_RefseqProtein = NP_000570
| Hs_RefseqmRNA = NM_000579
| Hs_GenLoc_db =
| Hs_GenLoc_chr =
| Hs_GenLoc_start =
| Hs_GenLoc_end =
| Hs_Uniprot =
| Mm_EntrezGene = 12774
| Mm_Ensembl = ENSMUSG00000073993
| Mm_RefseqmRNA = NM_009917
| Mm_RefseqProtein = NP_034047
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 9
| Mm_GenLoc_start = 123970372
| Mm_GenLoc_end = 123975980
| Mm_Uniprot = Q3TDA4
}}
}}
'''Chemokine (C-C motif) receptor 5''', also known as '''CCR5''', is a human [[gene]].
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = This gene encodes a member of the beta chemokine receptor family, which is predicted to be a seven transmembrane protein similar to G protein-coupled receptors. This protein is expressed by T cells and macrophages, and is known to be an important co-receptor for macrophage-tropic virus, including HIV, to enter host cells. Defective alleles of this gene have been associated with the HIV infection resistance. The ligands of this receptor include monocyte chemoattractant protein 2 (MCP-2), macrophage inflammatory protein 1 alpha (MIP-1 alpha), macrophage inflammatory protein 1 beta (MIP-1 beta) and regulated on activation normal T expressed and secreted protein (RANTES). Expression of this gene was also detected in a promyeloblastic cell line, suggesting that this protein may play a role in granulocyte lineage proliferation and differentiation. This gene is located at the chemokine receptor gene cluster region.<ref>{{cite web | title = Entrez Gene: CCR5 chemokine (C-C motif) receptor 5| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1234| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Sheppard HW, Celum C, Michael NL, ''et al.'' |title=HIV-1 infection in individuals with the CCR5-Delta32/Delta32 genotype: acquisition of syncytium-inducing virus at seroconversion. |journal=J. Acquir. Immune Defic. Syndr. |volume=29 |issue= 3 |pages= 307-13 |year= 2002 |pmid= 11873082 |doi= }}
*{{cite journal | author=Lee C, Liu QH, Tomkowicz B, ''et al.'' |title=Macrophage activation through CCR5- and CXCR4-mediated gp120-elicited signaling pathways. |journal=J. Leukoc. Biol. |volume=74 |issue= 5 |pages= 676-82 |year= 2004 |pmid= 12960231 |doi= 10.1189/jlb.0503206 }}
*{{cite journal | author=Yi Y, Lee C, Liu QH, ''et al.'' |title=Chemokine receptor utilization and macrophage signaling by human immunodeficiency virus type 1 gp120: Implications for neuropathogenesis. |journal=J. Neurovirol. |volume=10 Suppl 1 |issue= |pages= 91-6 |year= 2004 |pmid= 14982745 |doi= }}
*{{cite journal | author=Ajuebor MN, Carey JA, Swain MG |title=CCR5 in T cell-mediated liver diseases: what's going on? |journal=J. Immunol. |volume=177 |issue= 4 |pages= 2039-45 |year= 2006 |pmid= 16887960 |doi= }}
*{{cite journal | author=Lipp M, Müller G |title=Shaping up adaptive immunity: the impact of CCR7 and CXCR5 on lymphocyte trafficking. |journal=Verhandlungen der Deutschen Gesellschaft für Pathologie |volume=87 |issue= |pages= 90-101 |year= 2006 |pmid= 16888899 |doi= }}
*{{cite journal | author=Balistreri CR, Caruso C, Grimaldi MP, ''et al.'' |title=CCR5 receptor: biologic and genetic implications in age-related diseases. |journal=Ann. N. Y. Acad. Sci. |volume=1100 |issue= |pages= 162-72 |year= 2007 |pmid= 17460174 |doi= 10.1196/annals.1395.014 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on CDC2... {October 3, 2007 10:05:56 PM PDT}
- CREATE: Found no pages, creating new page. {October 3, 2007 10:07:11 PM PDT}
- CREATED: Created new protein page: CDC2 {October 3, 2007 10:07:20 PM PDT}
- INFO: Beginning work on CDKN1B... {October 3, 2007 10:07:20 PM PDT}
- CREATE: Found no pages, creating new page. {October 3, 2007 10:07:58 PM PDT}
- UPLOAD: Added new Image to wikiCreated new protein page: <a href=http://en.wikipedia.org/w/index.php?title=CDKN1B>CDKN1B</a> {October 3, 2007 10:08:05 PM PDT}
- CREATED: Created new protein page: CDKN1B {October 3, 2007 10:08:18 PM PDT}
- INFO: Beginning work on CREBBP... {October 3, 2007 10:08:44 PM PDT}
- AMBIGUITY: Did not locate an acceptable page to update. {October 3, 2007 10:09:41 PM PDT}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
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| update_citations = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB = {{PDB2|1f81}}, {{PDB2|1jjs}}, {{PDB2|1jsp}}, {{PDB2|1kbh}}, {{PDB2|1kdx}}, {{PDB2|1l3e}}, {{PDB2|1l8c}}, {{PDB2|1liq}}, {{PDB2|1p4q}}, {{PDB2|1r8u}}, {{PDB2|1sb0}}, {{PDB2|1tot}}, {{PDB2|1u2n}}, {{PDB2|1zoq}}, {{PDB2|2agh}}, {{PDB2|2c52}}, {{PDB2|2d82}}
| Name = CREB binding protein (Rubinstein-Taybi syndrome)
| HGNCid = 2348
| Symbol = CREBBP
| AltSymbols =; CBP; RSTS; RTS
| OMIM = 600140
| ECnumber =
| Homologene = 68393
| MGIid = 1098280
| GeneAtlas_image1 = PBB_GE_CREBBP_202160_at_tn.png
| GeneAtlas_image2 = PBB_GE_CREBBP_211808_s_at_tn.png
<!-- The Following entry is a time stamp of the last bot update. It is typically hidden data -->
| DateOfBotUpdate = ~~~~~
| Function = {{GNF_GO|id=GO:0003700 |text = transcription factor activity}} {{GNF_GO|id=GO:0003713 |text = transcription coactivator activity}} {{GNF_GO|id=GO:0004402 |text = histone acetyltransferase activity}} {{GNF_GO|id=GO:0004871 |text = signal transducer activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0008270 |text = zinc ion binding}} {{GNF_GO|id=GO:0016407 |text = acetyltransferase activity}} {{GNF_GO|id=GO:0016740 |text = transferase activity}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}} {{GNF_GO|id=GO:0051577 |text = MyoD binding}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005737 |text = cytoplasm}}
| Process = {{GNF_GO|id=GO:0001666 |text = response to hypoxia}} {{GNF_GO|id=GO:0006355 |text = regulation of transcription, DNA-dependent}} {{GNF_GO|id=GO:0006461 |text = protein complex assembly}} {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0016573 |text = histone acetylation}} {{GNF_GO|id=GO:0042592 |text = homeostatic process}} {{GNF_GO|id=GO:0045941 |text = positive regulation of transcription}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 1387
| Hs_Ensembl = ENSG00000005339
| Hs_RefseqProtein = NP_001073315
| Hs_RefseqmRNA = NM_001079846
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 16
| Hs_GenLoc_start = 3716572
| Hs_GenLoc_end = 3870723
| Hs_Uniprot = Q92793
| Mm_EntrezGene = 12914
| Mm_Ensembl = ENSMUSG00000022521
| Mm_RefseqmRNA = NM_001025432
| Mm_RefseqProtein = NP_001020603
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 16
| Mm_GenLoc_start = 3999276
| Mm_GenLoc_end = 4128632
| Mm_Uniprot = P45481
}}
}}
'''CREB binding protein (Rubinstein-Taybi syndrome)''', also known as '''CREBBP''', is a human [[gene]].
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text =
}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Goldman PS, Tran VK, Goodman RH |title=The multifunctional role of the co-activator CBP in transcriptional regulation. |journal=Recent Prog. Horm. Res. |volume=52 |issue= |pages= 103-19; discussion 119-20 |year= 1997 |pmid= 9238849 |doi= }}
*{{cite journal | author=Marcello A, Zoppé M, Giacca M |title=Multiple modes of transcriptional regulation by the HIV-1 Tat transactivator. |journal=IUBMB Life |volume=51 |issue= 3 |pages= 175-81 |year= 2002 |pmid= 11547919 |doi= }}
*{{cite journal | author=Matt T |title=Transcriptional control of the inflammatory response: a role for the CREB-binding protein (CBP). |journal=Acta Med. Austriaca |volume=29 |issue= 3 |pages= 77-9 |year= 2002 |pmid= 12168567 |doi= }}
*{{cite journal | author=Combes R, Balls M, Bansil L, ''et al.'' |title=An assessment of progress in the use of alternatives in toxicity testing since the publication of the report of the second FRAME Toxicity Committee (1991). |journal=Alternatives to laboratory animals : ATLA |volume=30 |issue= 4 |pages= 365-406 |year= 2002 |pmid= 12234245 |doi= }}
*{{cite journal | author=Minghetti L, Visentin S, Patrizio M, ''et al.'' |title=Multiple actions of the human immunodeficiency virus type-1 Tat protein on microglial cell functions. |journal=Neurochem. Res. |volume=29 |issue= 5 |pages= 965-78 |year= 2004 |pmid= 15139295 |doi= }}
*{{cite journal | author=Kino T, Pavlakis GN |title=Partner molecules of accessory protein Vpr of the human immunodeficiency virus type 1. |journal=DNA Cell Biol. |volume=23 |issue= 4 |pages= 193-205 |year= 2004 |pmid= 15142377 |doi= 10.1089/104454904773819789 }}
*{{cite journal | author=Greene WC, Chen LF |title=Regulation of NF-kappaB action by reversible acetylation. |journal=Novartis Found. Symp. |volume=259 |issue= |pages= 208-17; discussion 218-25 |year= 2004 |pmid= 15171256 |doi= }}
*{{cite journal | author=Liou LY, Herrmann CH, Rice AP |title=HIV-1 infection and regulation of Tat function in macrophages. |journal=Int. J. Biochem. Cell Biol. |volume=36 |issue= 9 |pages= 1767-75 |year= 2005 |pmid= 15183343 |doi= 10.1016/j.biocel.2004.02.018 }}
*{{cite journal | author=Pugliese A, Vidotto V, Beltramo T, ''et al.'' |title=A review of HIV-1 Tat protein biological effects. |journal=Cell Biochem. Funct. |volume=23 |issue= 4 |pages= 223-7 |year= 2005 |pmid= 15473004 |doi= 10.1002/cbf.1147 }}
*{{cite journal | author=Bannwarth S, Gatignol A |title=HIV-1 TAR RNA: the target of molecular interactions between the virus and its host. |journal=Curr. HIV Res. |volume=3 |issue= 1 |pages= 61-71 |year= 2005 |pmid= 15638724 |doi= }}
*{{cite journal | author=Le Rouzic E, Benichou S |title=The Vpr protein from HIV-1: distinct roles along the viral life cycle. |journal=Retrovirology |volume=2 |issue= |pages= 11 |year= 2006 |pmid= 15725353 |doi= 10.1186/1742-4690-2-11 }}
*{{cite journal | author=Gibellini D, Vitone F, Schiavone P, Re MC |title=HIV-1 tat protein and cell proliferation and survival: a brief review. |journal=New Microbiol. |volume=28 |issue= 2 |pages= 95-109 |year= 2005 |pmid= 16035254 |doi= }}
*{{cite journal | author=Hetzer C, Dormeyer W, Schnölzer M, Ott M |title=Decoding Tat: the biology of HIV Tat posttranslational modifications. |journal=Microbes Infect. |volume=7 |issue= 13 |pages= 1364-9 |year= 2006 |pmid= 16046164 |doi= 10.1016/j.micinf.2005.06.003 }}
*{{cite journal | author=Peruzzi F |title=The multiple functions of HIV-1 Tat: proliferation versus apoptosis. |journal=Front. Biosci. |volume=11 |issue= |pages= 708-17 |year= 2006 |pmid= 16146763 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on CSNK2A1... {October 3, 2007 10:09:41 PM PDT}
- AMBIGUITY: Did not locate an acceptable page to update. {October 3, 2007 10:11:12 PM PDT}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
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| update_protein_box = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB = {{PDB2|1jwh}}, {{PDB2|1na7}}, {{PDB2|1pjk}}, {{PDB2|1ymi}}
| Name = Casein kinase 2, alpha 1 polypeptide
| HGNCid = 2457
| Symbol = CSNK2A1
| AltSymbols =; CK2A1; CKII; CKII alpha
| OMIM = 115440
| ECnumber =
| Homologene = 1429
| MGIid = 88543
| GeneAtlas_image1 = PBB_GE_CSNK2A1_212072_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_CSNK2A1_206075_s_at_tn.png
| GeneAtlas_image3 = PBB_GE_CSNK2A1_212073_at_tn.png
<!-- The Following entry is a time stamp of the last bot update. It is typically hidden data -->
| DateOfBotUpdate = ~~~~~
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0004674 |text = protein serine/threonine kinase activity}} {{GNF_GO|id=GO:0004682 |text = protein kinase CK2 activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0005524 |text = ATP binding}} {{GNF_GO|id=GO:0016740 |text = transferase activity}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005886 |text = plasma membrane}}
| Process = {{GNF_GO|id=GO:0006468 |text = protein amino acid phosphorylation}} {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0016055 |text = Wnt receptor signaling pathway}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 1457
| Hs_Ensembl = ENSG00000101266
| Hs_RefseqProtein = NP_001886
| Hs_RefseqmRNA = NM_001895
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 20
| Hs_GenLoc_start = 411340
| Hs_GenLoc_end = 472482
| Hs_Uniprot = P68400
| Mm_EntrezGene = 12995
| Mm_Ensembl = ENSMUSG00000057808
| Mm_RefseqmRNA = NM_007788
| Mm_RefseqProtein = NP_031814
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 1
| Mm_GenLoc_start = 158360908
| Mm_GenLoc_end = 158362083
| Mm_Uniprot = Q61177
}}
}}
'''Casein kinase 2, alpha 1 polypeptide''', also known as '''CSNK2A1''', is a human [[gene]].
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = Casein kinase II is a serine/threonine protein kinase that phosphorylates acidic proteins such as casein. The kinase exists as a tetramer and is composed of an alpha, an alpha-prime, and two beta subunits. The alpha subunits contain the catalytic activity while the beta subunits undergo autophosphorylation. The protein encoded by this gene represents the alpha subunit. While this gene is found on chromosome 20, a related transcribed pseudogene is found on chromosome 11. Three transcript variants encoding two different proteins have been found for this gene.<ref>{{cite web | title = Entrez Gene: CSNK2A1 casein kinase 2, alpha 1 polypeptide| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1457| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=ole-MoiYoi OK |title=Casein kinase II in theileriosis. |journal=Science |volume=267 |issue= 5199 |pages= 834-6 |year= 1995 |pmid= 7846527 |doi= }}
*{{cite journal | author=Allende JE, Allende CC |title=Protein kinases. 4. Protein kinase CK2: an enzyme with multiple substrates and a puzzling regulation. |journal=FASEB J. |volume=9 |issue= 5 |pages= 313-23 |year= 1995 |pmid= 7896000 |doi= }}
*{{cite journal | author=Faust M, Montenarh M |title=Subcellular localization of protein kinase CK2. A key to its function? |journal=Cell Tissue Res. |volume=301 |issue= 3 |pages= 329-40 |year= 2001 |pmid= 10994779 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on CXCR4... {October 3, 2007 10:48:36 PM PDT}
- AMBIGUITY: Did not locate an acceptable page to update. {October 3, 2007 10:50:22 PM PDT}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Chemokine (C-X-C motif) receptor 4
| HGNCid = 2561
| Symbol = CXCR4
| AltSymbols =; NPYR; CD184; D2S201E; FB22; HM89; HSY3RR; LAP3; LCR1; LESTR; NPY3R; NPYRL; NPYY3R; WHIM
| OMIM = 162643
| ECnumber =
| Homologene = 20739
| MGIid = 109563
| GeneAtlas_image1 = PBB_GE_CXCR4_217028_at_tn.png
| GeneAtlas_image2 = PBB_GE_CXCR4_209201_x_at_tn.png
| GeneAtlas_image3 = PBB_GE_CXCR4_211919_s_at_tn.png
<!-- The Following entry is a time stamp of the last bot update. It is typically hidden data -->
| DateOfBotUpdate = ~~~~~
| Function = {{GNF_GO|id=GO:0001584 |text = rhodopsin-like receptor activity}} {{GNF_GO|id=GO:0003779 |text = actin binding}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0015026 |text = coreceptor activity}} {{GNF_GO|id=GO:0016493 |text = C-C chemokine receptor activity}} {{GNF_GO|id=GO:0016494 |text = C-X-C chemokine receptor activity}} {{GNF_GO|id=GO:0032027 |text = myosin light chain binding}}
| Component = {{GNF_GO|id=GO:0005737 |text = cytoplasm}} {{GNF_GO|id=GO:0005886 |text = plasma membrane}} {{GNF_GO|id=GO:0005887 |text = integral to plasma membrane}} {{GNF_GO|id=GO:0030426 |text = growth cone}} {{GNF_GO|id=GO:0031252 |text = leading edge}}
| Process = {{GNF_GO|id=GO:0000187 |text = activation of MAPK activity}} {{GNF_GO|id=GO:0001569 |text = patterning of blood vessels}} {{GNF_GO|id=GO:0001667 |text = ameboidal cell migration}} {{GNF_GO|id=GO:0001764 |text = neuron migration}} {{GNF_GO|id=GO:0006915 |text = apoptosis}} {{GNF_GO|id=GO:0006935 |text = chemotaxis}} {{GNF_GO|id=GO:0006954 |text = inflammatory response}} {{GNF_GO|id=GO:0006955 |text = immune response}} {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0007186 |text = G-protein coupled receptor protein signaling pathway}} {{GNF_GO|id=GO:0007204 |text = elevation of cytosolic calcium ion concentration}} {{GNF_GO|id=GO:0007281 |text = germ cell development}} {{GNF_GO|id=GO:0007420 |text = brain development}} {{GNF_GO|id=GO:0008045 |text = motor axon guidance}} {{GNF_GO|id=GO:0008354 |text = germ cell migration}} {{GNF_GO|id=GO:0009615 |text = response to virus}} {{GNF_GO|id=GO:0030334 |text = regulation of cell migration}} {{GNF_GO|id=GO:0042098 |text = T cell proliferation}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 7852
| Hs_Ensembl = ENSG00000121966
| Hs_RefseqProtein = NP_001008540
| Hs_RefseqmRNA = NM_001008540
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 2
| Hs_GenLoc_start = 136588909
| Hs_GenLoc_end = 136589979
| Hs_Uniprot = P61073
| Mm_EntrezGene = 12767
| Mm_Ensembl = ENSMUSG00000045382
| Mm_RefseqmRNA = NM_009911
| Mm_RefseqProtein = NP_034041
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 1
| Mm_GenLoc_start = 130415745
| Mm_GenLoc_end = 130419836
| Mm_Uniprot = A1E2I3
}}
}}
'''Chemokine (C-X-C motif) receptor 4''', also known as '''CXCR4''', is a human [[gene]].
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = This gene encodes a CXC chemokine receptor specific for stromal cell-derived factor-1. The protein has 7 transmembrane regions and is located on the cell surface. It acts with the CD4 protein to support HIV entry into cells and is also highly expressed in breast cancer cells. Mutations in this gene have been associated with WHIM (warts, hypogammaglobulinemia, infections, and myelokathexis) syndrome. Alternate transcriptional splice variants, encoding different isoforms, have been characterized.<ref>{{cite web | title = Entrez Gene: CXCR4 chemokine (C-X-C motif) receptor 4| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7852| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Lee C, Liu QH, Tomkowicz B, ''et al.'' |title=Macrophage activation through CCR5- and CXCR4-mediated gp120-elicited signaling pathways. |journal=J. Leukoc. Biol. |volume=74 |issue= 5 |pages= 676-82 |year= 2004 |pmid= 12960231 |doi= 10.1189/jlb.0503206 }}
*{{cite journal | author=Yi Y, Lee C, Liu QH, ''et al.'' |title=Chemokine receptor utilization and macrophage signaling by human immunodeficiency virus type 1 gp120: Implications for neuropathogenesis. |journal=J. Neurovirol. |volume=10 Suppl 1 |issue= |pages= 91-6 |year= 2004 |pmid= 14982745 |doi= }}
*{{cite journal | author=Kryczek I, Wei S, Keller E, ''et al.'' |title=Stroma-derived factor (SDF-1/CXCL12) and human tumor pathogenesis. |journal=Am. J. Physiol., Cell Physiol. |volume=292 |issue= 3 |pages= C987-95 |year= 2007 |pmid= 16943240 |doi= 10.1152/ajpcell.00406.2006 }}
*{{cite journal | author=Arya M, Ahmed H, Silhi N, ''et al.'' |title=Clinical importance and therapeutic implications of the pivotal CXCL12-CXCR4 (chemokine ligand-receptor) interaction in cancer cell migration. |journal=Tumour Biol. |volume=28 |issue= 3 |pages= 123-31 |year= 2007 |pmid= 17510563 |doi= 10.1159/000102979 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on EP300... {October 3, 2007 10:11:12 PM PDT}
- AMBIGUITY: Did not locate an acceptable page to update. {October 3, 2007 10:12:02 PM PDT}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB = {{PDB2|1f81}}, {{PDB2|1jsp}}, {{PDB2|1kdx}}, {{PDB2|1l3e}}, {{PDB2|1l8c}}, {{PDB2|1p4q}}, {{PDB2|1r8u}}, {{PDB2|1tot}}, {{PDB2|1u2n}}, {{PDB2|2d82}}
| Name = E1A binding protein p300
| HGNCid = 3373
| Symbol = EP300
| AltSymbols =; p300
| OMIM = 602700
| ECnumber =
| Homologene = 1094
| MGIid = 1276116
| GeneAtlas_image1 = PBB_GE_EP300_202221_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_EP300_213579_s_at_tn.png
<!-- The Following entry is a time stamp of the last bot update. It is typically hidden data -->
| DateOfBotUpdate = ~~~~~
| Function = {{GNF_GO|id=GO:0003700 |text = transcription factor activity}} {{GNF_GO|id=GO:0003713 |text = transcription coactivator activity}} {{GNF_GO|id=GO:0004402 |text = histone acetyltransferase activity}} {{GNF_GO|id=GO:0008022 |text = protein C-terminus binding}} {{GNF_GO|id=GO:0008270 |text = zinc ion binding}} {{GNF_GO|id=GO:0016740 |text = transferase activity}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}}
| Component = {{GNF_GO|id=GO:0000123 |text = histone acetyltransferase complex}} {{GNF_GO|id=GO:0005634 |text = nucleus}}
| Process = {{GNF_GO|id=GO:0001666 |text = response to hypoxia}} {{GNF_GO|id=GO:0001756 |text = somitogenesis}} {{GNF_GO|id=GO:0006915 |text = apoptosis}} {{GNF_GO|id=GO:0007049 |text = cell cycle}} {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0007399 |text = nervous system development}} {{GNF_GO|id=GO:0007507 |text = heart development}} {{GNF_GO|id=GO:0007519 |text = striated muscle development}} {{GNF_GO|id=GO:0030324 |text = lung development}} {{GNF_GO|id=GO:0042592 |text = homeostatic process}} {{GNF_GO|id=GO:0045893 |text = positive regulation of transcription, DNA-dependent}} {{GNF_GO|id=GO:0051091 |text = positive regulation of transcription factor activity}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 2033
| Hs_Ensembl = ENSG00000100393
| Hs_RefseqProtein = NP_001420
| Hs_RefseqmRNA = NM_001429
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 22
| Hs_GenLoc_start = 39817736
| Hs_GenLoc_end = 39905472
| Hs_Uniprot = Q09472
| Mm_EntrezGene = 328572
| Mm_Ensembl = ENSMUSG00000055024
| Mm_RefseqmRNA = NM_177821
| Mm_RefseqProtein = NP_808489
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 15
| Mm_GenLoc_start = 81413469
| Mm_GenLoc_end = 81479332
| Mm_Uniprot =
}}
}}
'''E1A binding protein p300''', also known as '''EP300''', is a human [[gene]].
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = EP300 encodes the adenovirus E1A-associated cellular p300 transcriptional co-activator protein. p300 is related by sequence to CBP (CREB-binding protein [CREB: cyclic-AMP responsive element binding protein]), and like CBP can stimulate transcription through activation of CREB. This EP300 activity is specifically inhibited by the adenovirus oncoprotein E1A. EP300 has also been identified as a co-activator of HIF1A (hypoxia-inducible factor 1 alpha), and thus plays a role in the stimulation of hypoxia-induced genes such as VEGF.<ref>{{cite web | title = Entrez Gene: EP300 E1A binding protein p300| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2033| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Condorelli G, Giordano A |title=Synergistic role of E1A-binding proteins and tissue-specific transcription factors in differentiation. |journal=J. Cell. Biochem. |volume=67 |issue= 4 |pages= 423-31 |year= 1998 |pmid= 9383702 |doi= }}
*{{cite journal | author=Marcello A, Zoppé M, Giacca M |title=Multiple modes of transcriptional regulation by the HIV-1 Tat transactivator. |journal=IUBMB Life |volume=51 |issue= 3 |pages= 175-81 |year= 2002 |pmid= 11547919 |doi= }}
*{{cite journal | author=Kino T, Pavlakis GN |title=Partner molecules of accessory protein Vpr of the human immunodeficiency virus type 1. |journal=DNA Cell Biol. |volume=23 |issue= 4 |pages= 193-205 |year= 2004 |pmid= 15142377 |doi= 10.1089/104454904773819789 }}
*{{cite journal | author=Ott M, Dorr A, Hetzer-Egger C, ''et al.'' |title=Tat acetylation: a regulatory switch between early and late phases in HIV transcription elongation. |journal=Novartis Found. Symp. |volume=259 |issue= |pages= 182-93; discussion 193-6, 223-5 |year= 2004 |pmid= 15171254 |doi= }}
*{{cite journal | author=Le Rouzic E, Benichou S |title=The Vpr protein from HIV-1: distinct roles along the viral life cycle. |journal=Retrovirology |volume=2 |issue= |pages= 11 |year= 2006 |pmid= 15725353 |doi= 10.1186/1742-4690-2-11 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on ESR2... {October 3, 2007 10:12:02 PM PDT}
- AMBIGUITY: Did not locate an acceptable page to update. {October 3, 2007 10:13:57 PM PDT}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
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| update_summary = yes
| update_citations = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB = {{PDB2|1hj1}}, {{PDB2|1l2j}}, {{PDB2|1nde}}, {{PDB2|1qkm}}, {{PDB2|1qkn}}, {{PDB2|1u3q}}, {{PDB2|1u3r}}, {{PDB2|1u3s}}, {{PDB2|1u9e}}, {{PDB2|1x76}}, {{PDB2|1x78}}, {{PDB2|1x7b}}, {{PDB2|1x7j}}, {{PDB2|1yy4}}, {{PDB2|1yye}}, {{PDB2|1zaf}}, {{PDB2|2fsz}}, {{PDB2|2giu}}, {{PDB2|2i0g}}, {{PDB2|2j7x}}, {{PDB2|2j7y}}
| Name = Estrogen receptor 2 (ER beta)
| HGNCid = 3468
| Symbol = ESR2
| AltSymbols =; ER-BETA; ESR-BETA; ESRB; ESTRB; Erb; NR3A2
| OMIM = 601663
| ECnumber =
| Homologene = 1100
| MGIid = 109392
| GeneAtlas_image1 = PBB_GE_ESR2_211117_x_at_tn.png
| GeneAtlas_image2 = PBB_GE_ESR2_211118_x_at_tn.png
| GeneAtlas_image3 = PBB_GE_ESR2_211120_x_at_tn.png
<!-- The Following entry is a time stamp of the last bot update. It is typically hidden data -->
| DateOfBotUpdate = ~~~~~
| Function = {{GNF_GO|id=GO:0003700 |text = transcription factor activity}} {{GNF_GO|id=GO:0003713 |text = transcription coactivator activity}} {{GNF_GO|id=GO:0005496 |text = steroid binding}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0008270 |text = zinc ion binding}} {{GNF_GO|id=GO:0008289 |text = lipid binding}} {{GNF_GO|id=GO:0030284 |text = estrogen receptor activity}} {{GNF_GO|id=GO:0043565 |text = sequence-specific DNA binding}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}} {{GNF_GO|id=GO:0048019 |text = receptor antagonist activity}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005739 |text = mitochondrion}}
| Process = {{GNF_GO|id=GO:0001764 |text = neuron migration}} {{GNF_GO|id=GO:0006350 |text = transcription}} {{GNF_GO|id=GO:0006355 |text = regulation of transcription, DNA-dependent}} {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0007267 |text = cell-cell signaling}} {{GNF_GO|id=GO:0007420 |text = brain development}} {{GNF_GO|id=GO:0030308 |text = negative regulation of cell growth}} {{GNF_GO|id=GO:0030520 |text = estrogen receptor signaling pathway}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 2100
| Hs_Ensembl = ENSG00000140009
| Hs_RefseqProtein = NP_001035365
| Hs_RefseqmRNA = NM_001040275
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 14
| Hs_GenLoc_start = 63621388
| Hs_GenLoc_end = 63875070
| Hs_Uniprot = Q92731
| Mm_EntrezGene = 13983
| Mm_Ensembl = ENSMUSG00000021055
| Mm_RefseqmRNA = NM_010157
| Mm_RefseqProtein = NP_034287
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 12
| Mm_GenLoc_start = 77039259
| Mm_GenLoc_end = 77096099
| Mm_Uniprot = Q9JM97
}}
}}
'''Estrogen receptor 2 (ER beta)''', also known as '''ESR2''', is a human [[gene]].
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = This gene encodes a member of the family of estrogen receptors and superfamily of nuclear receptor transcription factors. The gene product contains an N-terminal DNA binding domain and C-terminal ligand binding domain and is localized to the nucleus, cytoplasm, and mitochondria. Upon binding to 17beta-estradiol or related ligands, the encoded protein forms homo- or hetero-dimers that interact with specific DNA sequences to activate transcription. Some isoforms dominantly inhibit the activity of other estrogen receptor family members. Several alternatively spliced transcript variants of this gene have been described, but the full-length nature of some of these variants has not been fully characterized.<ref>{{cite web | title = Entrez Gene: ESR2 estrogen receptor 2 (ER beta)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2100| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Pettersson K, Gustafsson JA |title=Role of estrogen receptor beta in estrogen action. |journal=Annu. Rev. Physiol. |volume=63 |issue= |pages= 165-92 |year= 2001 |pmid= 11181953 |doi= 10.1146/annurev.physiol.63.1.165 }}
*{{cite journal | author=Warner M, Saji S, Gustafsson JA |title=The normal and malignant mammary gland: a fresh look with ER beta onboard. |journal=Journal of mammary gland biology and neoplasia |volume=5 |issue= 3 |pages= 289-94 |year= 2004 |pmid= 14973391 |doi= }}
*{{cite journal | author=Saxon LK, Turner CH |title=Estrogen receptor beta: the antimechanostat? |journal=Bone |volume=36 |issue= 2 |pages= 185-92 |year= 2005 |pmid= 15780944 |doi= 10.1016/j.bone.2004.08.003 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on F2... {October 3, 2007 10:13:57 PM PDT}
- AMBIGUITY: Did not locate an acceptable page to update. {October 3, 2007 10:14:27 PM PDT}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB = {{PDB2|1a2c}}, {{PDB2|1a3b}}, {{PDB2|1a3e}}, {{PDB2|1a46}}, {{PDB2|1a4w}}, {{PDB2|1a5g}}, {{PDB2|1a61}}, {{PDB2|1abi}}, {{PDB2|1abj}}, {{PDB2|1ad8}}, {{PDB2|1ae8}}, {{PDB2|1afe}}, {{PDB2|1aht}}, {{PDB2|1ai8}}, {{PDB2|1aix}}, {{PDB2|1awf}}, {{PDB2|1awh}}, {{PDB2|1ay6}}, {{PDB2|1b5g}}, {{PDB2|1b7x}}, {{PDB2|1ba8}}, {{PDB2|1bb0}}, {{PDB2|1bbr}}, {{PDB2|1bcu}}, {{PDB2|1bhx}}, {{PDB2|1bmm}}, {{PDB2|1bmn}}, {{PDB2|1bth}}, {{PDB2|1c1u}}, {{PDB2|1c1v}}, {{PDB2|1c1w}}, {{PDB2|1c4u}}, {{PDB2|1c4v}}, {{PDB2|1c4y}}, {{PDB2|1c5l}}, {{PDB2|1c5n}}, {{PDB2|1c5o}}, {{PDB2|1ca8}}, {{PDB2|1d3d}}, {{PDB2|1d3p}}, {{PDB2|1d3q}}, {{PDB2|1d3t}}, {{PDB2|1d4p}}, {{PDB2|1d6w}}, {{PDB2|1d9i}}, {{PDB2|1de7}}, {{PDB2|1dit}}, {{PDB2|1dm4}}, {{PDB2|1doj}}, {{PDB2|1dwb}}, {{PDB2|1dwc}}, {{PDB2|1dwd}}, {{PDB2|1dwe}}, {{PDB2|1dx5}}, {{PDB2|1e0f}}, {{PDB2|1eb1}}, {{PDB2|1eoj}}, {{PDB2|1eol}}, {{PDB2|1fpc}}, {{PDB2|1fph}}, {{PDB2|1g30}}, {{PDB2|1g32}}, {{PDB2|1g37}}, {{PDB2|1ghv}}, {{PDB2|1ghw}}, {{PDB2|1ghx}}, {{PDB2|1ghy}}, {{PDB2|1gj4}}, {{PDB2|1gj5}}, {{PDB2|1h8d}}, {{PDB2|1h8i}}, {{PDB2|1hag}}, {{PDB2|1hah}}, {{PDB2|1hai}}, {{PDB2|1hao}}, {{PDB2|1hap}}, {{PDB2|1hbt}}, {{PDB2|1hdt}}, {{PDB2|1hgt}}, {{PDB2|1hlt}}, {{PDB2|1hut}}, {{PDB2|1hxe}}, {{PDB2|1hxf}}, {{PDB2|1ihs}}, {{PDB2|1iht}}, {{PDB2|1jmo}}, {{PDB2|1jou}}, {{PDB2|1jwt}}, {{PDB2|1k21}}, {{PDB2|1k22}}, {{PDB2|1kts}}, {{PDB2|1ktt}}, {{PDB2|1lhc}}, {{PDB2|1lhd}}, {{PDB2|1lhe}}, {{PDB2|1lhf}}, {{PDB2|1lhg}}, {{PDB2|1mh0}}, {{PDB2|1mu6}}, {{PDB2|1mu8}}, {{PDB2|1mue}}, {{PDB2|1nm6}}, {{PDB2|1no9}}, {{PDB2|1nrn}}, {{PDB2|1nro}}, {{PDB2|1nrp}}, {{PDB2|1nrq}}, {{PDB2|1nrr}}, {{PDB2|1nrs}}, {{PDB2|1nt1}}, {{PDB2|1nu7}}, {{PDB2|1nu9}}, {{PDB2|1ny2}}, {{PDB2|1nzq}}, {{PDB2|1o0d}}, {{PDB2|1o2g}}, {{PDB2|1o5g}}, {{PDB2|1ook}}, {{PDB2|1oyt}}, {{PDB2|1p8v}}, {{PDB2|1ppb}}, {{PDB2|1qbv}}, {{PDB2|1qhr}}, {{PDB2|1qj1}}, {{PDB2|1qj6}}, {{PDB2|1qj7}}, {{PDB2|1qur}}, {{PDB2|1rd3}}, {{PDB2|1riw}}, {{PDB2|1sb1}}, {{PDB2|1sfq}}, {{PDB2|1sg8}}, {{PDB2|1sgi}}, {{PDB2|1shh}}, {{PDB2|1sl3}}, {{PDB2|1sr5}}, {{PDB2|1t4u}}, {{PDB2|1t4v}}, {{PDB2|1ta2}}, {{PDB2|1ta6}}, {{PDB2|1tb6}}, {{PDB2|1tbz}}, {{PDB2|1thp}}, {{PDB2|1thr}}, {{PDB2|1ths}}, {{PDB2|1tmb}}, {{PDB2|1tmt}}, {{PDB2|1tmu}}, {{PDB2|1tom}}, {{PDB2|1tq0}}, {{PDB2|1tq7}}, {{PDB2|1twx}}, {{PDB2|1ucy}}, {{PDB2|1uma}}, {{PDB2|1uvs}}, {{PDB2|1vit}}, {{PDB2|1vr1}}, {{PDB2|1vzq}}, {{PDB2|1w7g}}, {{PDB2|1way}}, {{PDB2|1wbg}}, {{PDB2|1xm1}}, {{PDB2|1xmn}}, {{PDB2|1ycp}}, {{PDB2|1ype}}, {{PDB2|1ypg}}, {{PDB2|1ypj}}, {{PDB2|1ypk}}, {{PDB2|1ypl}}, {{PDB2|1ypm}}, {{PDB2|1z71}}, {{PDB2|1z8i}}, {{PDB2|1z8j}}, {{PDB2|1zgi}}, {{PDB2|1zgv}}, {{PDB2|1zrb}}, {{PDB2|2a0q}}, {{PDB2|2a2x}}, {{PDB2|2a45}}, {{PDB2|2afq}}, {{PDB2|2ank}}, {{PDB2|2anm}}, {{PDB2|2b5t}}, {{PDB2|2bdy}}, {{PDB2|2bvr}}, {{PDB2|2bvs}}, {{PDB2|2bvx}}, {{PDB2|2bxt}}, {{PDB2|2bxu}}, {{PDB2|2c8w}}, {{PDB2|2c8x}}, {{PDB2|2c8y}}, {{PDB2|2c8z}}, {{PDB2|2c90}}, {{PDB2|2c93}}, {{PDB2|2cf8}}, {{PDB2|2cf9}}, {{PDB2|2cn0}}, {{PDB2|2feq}}, {{PDB2|2fes}}, {{PDB2|2gde}}, {{PDB2|2gp9}}, {{PDB2|2h9t}}, {{PDB2|2hgt}}, {{PDB2|2hnt}}, {{PDB2|2hpp}}, {{PDB2|2hpq}}, {{PDB2|2hwl}}, {{PDB2|2jh0}}, {{PDB2|2jh5}}, {{PDB2|2jh6}}, {{PDB2|2od3}}, {{PDB2|2thf}}, {{PDB2|3hat}}, {{PDB2|3htc}}, {{PDB2|4htc}}, {{PDB2|4thn}}, {{PDB2|5gds}}, {{PDB2|7kme}}, {{PDB2|8kme}}
| Name = Coagulation factor II (thrombin)
| HGNCid = 3535
| Symbol = F2
| AltSymbols =; PT
| OMIM = 176930
| ECnumber =
| Homologene = 426
| MGIid = 88380
| GeneAtlas_image1 = PBB_GE_F2_205754_at_tn.png
<!-- The Following entry is a time stamp of the last bot update. It is typically hidden data -->
| DateOfBotUpdate = ~~~~~
| Function = {{GNF_GO|id=GO:0003809 |text = thrombin activity}} {{GNF_GO|id=GO:0005102 |text = receptor binding}} {{GNF_GO|id=GO:0005509 |text = calcium ion binding}}
| Component = {{GNF_GO|id=GO:0005576 |text = extracellular region}} {{GNF_GO|id=GO:0005615 |text = extracellular space}} {{GNF_GO|id=GO:0005625 |text = soluble fraction}}
| Process = {{GNF_GO|id=GO:0000074 |text = regulation of progression through cell cycle}} {{GNF_GO|id=GO:0006508 |text = proteolysis}} {{GNF_GO|id=GO:0006915 |text = apoptosis}} {{GNF_GO|id=GO:0006919 |text = caspase activation}} {{GNF_GO|id=GO:0006953 |text = acute-phase response}} {{GNF_GO|id=GO:0007260 |text = tyrosine phosphorylation of STAT protein}} {{GNF_GO|id=GO:0007262 |text = STAT protein nuclear translocation}} {{GNF_GO|id=GO:0007275 |text = multicellular organismal development}} {{GNF_GO|id=GO:0007596 |text = blood coagulation}} {{GNF_GO|id=GO:0009611 |text = response to wounding}} {{GNF_GO|id=GO:0030168 |text = platelet activation}} {{GNF_GO|id=GO:0030193 |text = regulation of blood coagulation}} {{GNF_GO|id=GO:0042730 |text = fibrinolysis}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 2147
| Hs_Ensembl = ENSG00000180210
| Hs_RefseqProtein = NP_000497
| Hs_RefseqmRNA = NM_000506
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 11
| Hs_GenLoc_start = 46697331
| Hs_GenLoc_end = 46717631
| Hs_Uniprot = P00734
| Mm_EntrezGene = 14061
| Mm_Ensembl = ENSMUSG00000027249
| Mm_RefseqmRNA = NM_010168
| Mm_RefseqProtein = NP_034298
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 2
| Mm_GenLoc_start = 91426157
| Mm_GenLoc_end = 91437253
| Mm_Uniprot = Q3TJ94
}}
}}
'''Coagulation factor II (thrombin)''', also known as '''F2''', is a human [[gene]].
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = Coagulation factor II is proteolytically cleaved to form thrombin in the first step of the coagulation cascade which ultimately results in the stemming of blood loss. F2 also plays a role in maintaining vascular integrity during development and postnatal life. Mutations in F2 leads to various forms of thrombosis and dysprothrombinemia.<ref>{{cite web | title = Entrez Gene: F2 coagulation factor II (thrombin)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2147| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Esmon CT |title=Thrombomodulin as a model of molecular mechanisms that modulate protease specificity and function at the vessel surface. |journal=FASEB J. |volume=9 |issue= 10 |pages= 946-55 |year= 1995 |pmid= 7615164 |doi= }}
*{{cite journal | author=Lenting PJ, van Mourik JA, Mertens K |title=The life cycle of coagulation factor VIII in view of its structure and function. |journal=Blood |volume=92 |issue= 11 |pages= 3983-96 |year= 1999 |pmid= 9834200 |doi= }}
*{{cite journal | author=Plow EF, Cierniewski CS, Xiao Z, ''et al.'' |title=AlphaIIbbeta3 and its antagonism at the new millennium. |journal=Thromb. Haemost. |volume=86 |issue= 1 |pages= 34-40 |year= 2002 |pmid= 11487023 |doi= }}
*{{cite journal | author=Maragoudakis ME, Tsopanoglou NE, Andriopoulou P |title=Mechanism of thrombin-induced angiogenesis. |journal=Biochem. Soc. Trans. |volume=30 |issue= 2 |pages= 173-7 |year= 2002 |pmid= 12023846 |doi= 10.1042/ }}
*{{cite journal | author=Howell DC, Laurent GJ, Chambers RC |title=Role of thrombin and its major cellular receptor, protease-activated receptor-1, in pulmonary fibrosis. |journal=Biochem. Soc. Trans. |volume=30 |issue= 2 |pages= 211-6 |year= 2002 |pmid= 12023853 |doi= 10.1042/ }}
*{{cite journal | author=Firth SM, Baxter RC |title=Cellular actions of the insulin-like growth factor binding proteins. |journal=Endocr. Rev. |volume=23 |issue= 6 |pages= 824-54 |year= 2003 |pmid= 12466191 |doi= }}
*{{cite journal | author=Minami T, Sugiyama A, Wu SQ, ''et al.'' |title=Thrombin and phenotypic modulation of the endothelium. |journal=Arterioscler. Thromb. Vasc. Biol. |volume=24 |issue= 1 |pages= 41-53 |year= 2004 |pmid= 14551154 |doi= 10.1161/01.ATV.0000099880.09014.7D }}
*{{cite journal | author=De Cristofaro R, De Candia E |title=Thrombin domains: structure, function and interaction with platelet receptors. |journal=J. Thromb. Thrombolysis |volume=15 |issue= 3 |pages= 151-63 |year= 2004 |pmid= 14739624 |doi= 10.1023/B:THRO.0000011370.80989.7b }}
*{{cite journal | author=Tsopanoglou NE, Maragoudakis ME |title=Role of thrombin in angiogenesis and tumor progression. |journal=Semin. Thromb. Hemost. |volume=30 |issue= 1 |pages= 63-9 |year= 2004 |pmid= 15034798 |doi= 10.1055/s-2004-822971 }}
*{{cite journal | author=Bode W |title=Structure and interaction modes of thrombin. |journal=Blood Cells Mol. Dis. |volume=36 |issue= 2 |pages= 122-30 |year= 2007 |pmid= 16480903 |doi= 10.1016/j.bcmd.2005.12.027 }}
*{{cite journal | author=Wolberg AS |title=Thrombin generation and fibrin clot structure. |journal=Blood Rev. |volume=21 |issue= 3 |pages= 131-42 |year= 2007 |pmid= 17208341 |doi= 10.1016/j.blre.2006.11.001 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on FYN... {October 3, 2007 10:14:27 PM PDT}
- AMBIGUITY: Did not locate an acceptable page to update. {October 3, 2007 10:15:40 PM PDT}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
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| update_summary = yes
| update_citations = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB = {{PDB2|1a0n}}, {{PDB2|1aot}}, {{PDB2|1aou}}, {{PDB2|1avz}}, {{PDB2|1azg}}, {{PDB2|1efn}}, {{PDB2|1fyn}}, {{PDB2|1g83}}, {{PDB2|1m27}}, {{PDB2|1nyf}}, {{PDB2|1nyg}}, {{PDB2|1shf}}, {{PDB2|1zbj}}, {{PDB2|2dq7}}
| Name = FYN oncogene related to SRC, FGR, YES
| HGNCid = 4037
| Symbol = FYN
| AltSymbols =; MGC45350; SLK; SYN
| OMIM = 137025
| ECnumber =
| Homologene = 48068
| MGIid = 95602
| GeneAtlas_image1 = PBB_GE_FYN_210105_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_FYN_212486_s_at_tn.png
| GeneAtlas_image3 = PBB_GE_FYN_216033_s_at_tn.png
<!-- The Following entry is a time stamp of the last bot update. It is typically hidden data -->
| DateOfBotUpdate = ~~~~~
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0004713 |text = protein-tyrosine kinase activity}} {{GNF_GO|id=GO:0004715 |text = non-membrane spanning protein tyrosine kinase activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0005524 |text = ATP binding}} {{GNF_GO|id=GO:0015631 |text = tubulin binding}} {{GNF_GO|id=GO:0016740 |text = transferase activity}} {{GNF_GO|id=GO:0042802 |text = identical protein binding}}
| Component = {{GNF_GO|id=GO:0005575 |text = cellular_component}}
| Process = {{GNF_GO|id=GO:0001764 |text = neuron migration}} {{GNF_GO|id=GO:0006468 |text = protein amino acid phosphorylation}} {{GNF_GO|id=GO:0006816 |text = calcium ion transport}} {{GNF_GO|id=GO:0007242 |text = intracellular signaling cascade}} {{GNF_GO|id=GO:0007243 |text = protein kinase cascade}} {{GNF_GO|id=GO:0007612 |text = learning}} {{GNF_GO|id=GO:0007631 |text = feeding behavior}} {{GNF_GO|id=GO:0008360 |text = regulation of cell shape}} {{GNF_GO|id=GO:0018108 |text = peptidyl-tyrosine phosphorylation}} {{GNF_GO|id=GO:0030900 |text = forebrain development}} {{GNF_GO|id=GO:0050852 |text = T cell receptor signaling pathway}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 2534
| Hs_Ensembl = ENSG00000010810
| Hs_RefseqProtein = NP_002028
| Hs_RefseqmRNA = NM_002037
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 6
| Hs_GenLoc_start = 112088228
| Hs_GenLoc_end = 112301348
| Hs_Uniprot = P06241
| Mm_EntrezGene = 14360
| Mm_Ensembl = ENSMUSG00000019843
| Mm_RefseqmRNA = NM_008054
| Mm_RefseqProtein = NP_032080
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 10
| Mm_GenLoc_start = 39059219
| Mm_GenLoc_end = 39254797
| Mm_Uniprot = Q3TAT3
}}
}}
'''FYN oncogene related to SRC, FGR, YES''', also known as '''FYN''', is a human [[gene]].
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = This gene is a member of the protein-tyrosine kinase oncogene family. It encodes a membrane-associated tyrosine kinase that has been implicated in the control of cell growth. The protein associates with the p85 subunit of phosphatidylinositol 3-kinase and interacts with the fyn-binding protein. Alternatively spliced transcript variants encoding distinct isoforms exist.<ref>{{cite web | title = Entrez Gene: FYN FYN oncogene related to SRC, FGR, YES| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2534| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=O'Sullivan E, Kinnon C, Brickell P |title=Wiskott-Aldrich syndrome protein, WASP. |journal=Int. J. Biochem. Cell Biol. |volume=31 |issue= 3-4 |pages= 383-7 |year= 1999 |pmid= 10224664 |doi= }}
*{{cite journal | author=Sasaoka T, Kobayashi M |title=The functional significance of Shc in insulin signaling as a substrate of the insulin receptor. |journal=Endocr. J. |volume=47 |issue= 4 |pages= 373-81 |year= 2000 |pmid= 11075717 |doi= }}
*{{cite journal | author=Leavitt SA, SchOn A, Klein JC, ''et al.'' |title=Interactions of HIV-1 proteins gp120 and Nef with cellular partners define a novel allosteric paradigm. |journal=Curr. Protein Pept. Sci. |volume=5 |issue= 1 |pages= 1-8 |year= 2004 |pmid= 14965316 |doi= }}
*{{cite journal | author=Tolstrup M, Ostergaard L, Laursen AL, ''et al.'' |title=HIV/SIV escape from immune surveillance: focus on Nef. |journal=Curr. HIV Res. |volume=2 |issue= 2 |pages= 141-51 |year= 2004 |pmid= 15078178 |doi= }}
*{{cite journal | author=Joseph AM, Kumar M, Mitra D |title=Nef: "necessary and enforcing factor" in HIV infection. |journal=Curr. HIV Res. |volume=3 |issue= 1 |pages= 87-94 |year= 2005 |pmid= 15638726 |doi= }}
*{{cite journal | author=Stove V, Verhasselt B |title=Modelling thymic HIV-1 Nef effects. |journal=Curr. HIV Res. |volume=4 |issue= 1 |pages= 57-64 |year= 2006 |pmid= 16454711 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on GRB2... {October 3, 2007 10:15:40 PM PDT}
- AMBIGUITY: Did not locate an acceptable page to update. {October 3, 2007 10:16:27 PM PDT}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB = {{PDB2|1aze}}, {{PDB2|1bm2}}, {{PDB2|1bmb}}, {{PDB2|1cj1}}, {{PDB2|1fhs}}, {{PDB2|1fyr}}, {{PDB2|1gbq}}, {{PDB2|1gbr}}, {{PDB2|1gcq}}, {{PDB2|1gfc}}, {{PDB2|1gfd}}, {{PDB2|1ghu}}, {{PDB2|1gri}}, {{PDB2|1io6}}, {{PDB2|1jyq}}, {{PDB2|1jyr}}, {{PDB2|1jyu}}, {{PDB2|1qg1}}, {{PDB2|1tze}}, {{PDB2|1x0n}}, {{PDB2|1zfp}}, {{PDB2|2aoa}}, {{PDB2|2aob}}, {{PDB2|2gbq}}, {{PDB2|2h46}}, {{PDB2|2h5k}}, {{PDB2|2huw}}, {{PDB2|2huy}}, {{PDB2|3gbq}}, {{PDB2|4gbq}}
| Name = Growth factor receptor-bound protein 2
| HGNCid = 4566
| Symbol = GRB2
| AltSymbols =; ASH; EGFRBP-GRB2; Grb3-3; MST084; MSTP084
| OMIM = 108355
| ECnumber =
| Homologene = 1576
| MGIid = 95805
| GeneAtlas_image1 = PBB_GE_GRB2_215075_s_at_tn.png
<!-- The Following entry is a time stamp of the last bot update. It is typically hidden data -->
| DateOfBotUpdate = ~~~~~
| Function = {{GNF_GO|id=GO:0005070 |text = SH3/SH2 adaptor activity}} {{GNF_GO|id=GO:0005154 |text = epidermal growth factor receptor binding}} {{GNF_GO|id=GO:0043560 |text = insulin receptor substrate binding}}
| Component = {{GNF_GO|id=GO:0005737 |text = cytoplasm}} {{GNF_GO|id=GO:0005829 |text = cytosol}} {{GNF_GO|id=GO:0012506 |text = vesicle membrane}} {{GNF_GO|id=GO:0016020 |text = membrane}}
| Process = {{GNF_GO|id=GO:0000165 |text = MAPKKK cascade}} {{GNF_GO|id=GO:0007173 |text = epidermal growth factor receptor signaling pathway}} {{GNF_GO|id=GO:0007242 |text = intracellular signaling cascade}} {{GNF_GO|id=GO:0007265 |text = Ras protein signal transduction}} {{GNF_GO|id=GO:0007267 |text = cell-cell signaling}} {{GNF_GO|id=GO:0008286 |text = insulin receptor signaling pathway}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 2885
| Hs_Ensembl = ENSG00000177885
| Hs_RefseqProtein = NP_002077
| Hs_RefseqmRNA = NM_002086
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 17
| Hs_GenLoc_start = 70825753
| Hs_GenLoc_end = 70913384
| Hs_Uniprot = P62993
| Mm_EntrezGene = 14784
| Mm_Ensembl = ENSMUSG00000059923
| Mm_RefseqmRNA = NM_008163
| Mm_RefseqProtein = NP_032189
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 11
| Mm_GenLoc_start = 115460216
| Mm_GenLoc_end = 115524687
| Mm_Uniprot = Q3U1Q4
}}
}}
'''Growth factor receptor-bound protein 2''', also known as '''GRB2''', is a human [[gene]].
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = The protein encoded by this gene binds the epidermal growth factor receptor and contains one SH2 domain and two SH3 domains. Its two SH3 domains direct complex formation with proline-rich regions of other proteins, and its SH2 domain binds tyrosine phosphorylated sequences. This gene is similar to the Sem5 gene of C.elegans, which is involved in the signal transduction pathway. Two alternatively spliced transcript variants encoding different isoforms have been found for this gene.<ref>{{cite web | title = Entrez Gene: GRB2 growth factor receptor-bound protein 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2885| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Colledge M, Froehner SC |title=Interaction between the nicotinic acetylcholine receptor and Grb2. Implications for signaling at the neuromuscular junction. |journal=Ann. N. Y. Acad. Sci. |volume=841 |issue= |pages= 17-27 |year= 1998 |pmid= 9668219 |doi= }}
*{{cite journal | author=Ramesh N, Antón IM, Martínez-Quiles N, Geha RS |title=Waltzing with WASP. |journal=Trends Cell Biol. |volume=9 |issue= 1 |pages= 15-9 |year= 1999 |pmid= 10087612 |doi= }}
*{{cite journal | author=O'Sullivan E, Kinnon C, Brickell P |title=Wiskott-Aldrich syndrome protein, WASP. |journal=Int. J. Biochem. Cell Biol. |volume=31 |issue= 3-4 |pages= 383-7 |year= 1999 |pmid= 10224664 |doi= }}
*{{cite journal | author=Schlaepfer DD, Hauck CR, Sieg DJ |title=Signaling through focal adhesion kinase. |journal=Prog. Biophys. Mol. Biol. |volume=71 |issue= 3-4 |pages= 435-78 |year= 1999 |pmid= 10354709 |doi= }}
*{{cite journal | author=Vidal M, Liu WQ, Gril B, ''et al.'' |title=[Design of new anti-tumor agents interrupting deregulated signaling pathways induced by tyrosine kinase proteins. Inhibition of protein-protein interaction involving Grb2] |journal=J. Soc. Biol. |volume=198 |issue= 2 |pages= 133-7 |year= 2004 |pmid= 15368963 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on HBA1... {October 3, 2007 10:18:02 PM PDT}
- AMBIGUITY: Did not locate an acceptable page to update. {October 3, 2007 10:18:19 PM PDT}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB = {{PDB2|1a00}}, {{PDB2|1a01}}, {{PDB2|1a0u}}, {{PDB2|1a0z}}, {{PDB2|1a3n}}, {{PDB2|1a3o}}, {{PDB2|1a9w}}, {{PDB2|1abw}}, {{PDB2|1aby}}, {{PDB2|1aj9}}, {{PDB2|1b86}}, {{PDB2|1bab}}, {{PDB2|1bbb}}, {{PDB2|1bij}}, {{PDB2|1buw}}, {{PDB2|1bz0}}, {{PDB2|1bz1}}, {{PDB2|1bzz}}, {{PDB2|1c7b}}, {{PDB2|1c7c}}, {{PDB2|1c7d}}, {{PDB2|1cls}}, {{PDB2|1cmy}}, {{PDB2|1coh}}, {{PDB2|1dke}}, {{PDB2|1dxt}}, {{PDB2|1dxu}}, {{PDB2|1dxv}}, {{PDB2|1fdh}}, {{PDB2|1fn3}}, {{PDB2|1g9v}}, {{PDB2|1gbu}}, {{PDB2|1gbv}}, {{PDB2|1gli}}, {{PDB2|1gzx}}, {{PDB2|1hab}}, {{PDB2|1hac}}, {{PDB2|1hba}}, {{PDB2|1hbb}}, {{PDB2|1hbs}}, {{PDB2|1hco}}, {{PDB2|1hdb}}, {{PDB2|1hga}}, {{PDB2|1hgb}}, {{PDB2|1hgc}}, {{PDB2|1hho}}, {{PDB2|1ird}}, {{PDB2|1j3y}}, {{PDB2|1j3z}}, {{PDB2|1j40}}, {{PDB2|1j41}}, {{PDB2|1j7s}}, {{PDB2|1j7w}}, {{PDB2|1j7y}}, {{PDB2|1jy7}}, {{PDB2|1k0y}}, {{PDB2|1k1k}}, {{PDB2|1kd2}}, {{PDB2|1lfl}}, {{PDB2|1lfq}}, {{PDB2|1lft}}, {{PDB2|1lfv}}, {{PDB2|1lfy}}, {{PDB2|1lfz}}, {{PDB2|1ljw}}, {{PDB2|1m9p}}, {{PDB2|1mko}}, {{PDB2|1nej}}, {{PDB2|1nih}}, {{PDB2|1nqp}}, {{PDB2|1o1i}}, {{PDB2|1o1j}}, {{PDB2|1o1k}}, {{PDB2|1o1l}}, {{PDB2|1o1m}}, {{PDB2|1o1n}}, {{PDB2|1o1o}}, {{PDB2|1o1p}}, {{PDB2|1qi8}}, {{PDB2|1qsh}}, {{PDB2|1qsi}}, {{PDB2|1qxd}}, {{PDB2|1qxe}}, {{PDB2|1r1x}}, {{PDB2|1r1y}}, {{PDB2|1rps}}, {{PDB2|1rq3}}, {{PDB2|1rq4}}, {{PDB2|1rqa}}, {{PDB2|1rvw}}, {{PDB2|1sdk}}, {{PDB2|1sdl}}, {{PDB2|1shr}}, {{PDB2|1si4}}, {{PDB2|1thb}}, {{PDB2|1uiw}}, {{PDB2|1vwt}}, {{PDB2|1xxt}}, {{PDB2|1xy0}}, {{PDB2|1xye}}, {{PDB2|1xz2}}, {{PDB2|1xz4}}, {{PDB2|1xz5}}, {{PDB2|1xz7}}, {{PDB2|1xzu}}, {{PDB2|1xzv}}, {{PDB2|1y01}}, {{PDB2|1y09}}, {{PDB2|1y0a}}, {{PDB2|1y0c}}, {{PDB2|1y0d}}, {{PDB2|1y0t}}, {{PDB2|1y0w}}, {{PDB2|1y22}}, {{PDB2|1y2z}}, {{PDB2|1y31}}, {{PDB2|1y35}}, {{PDB2|1y45}}, {{PDB2|1y46}}, {{PDB2|1y4b}}, {{PDB2|1y4f}}, {{PDB2|1y4g}}, {{PDB2|1y4p}}, {{PDB2|1y4q}}, {{PDB2|1y4r}}, {{PDB2|1y4v}}, {{PDB2|1y5f}}, {{PDB2|1y5j}}, {{PDB2|1y5k}}, {{PDB2|1y7c}}, {{PDB2|1y7d}}, {{PDB2|1y7g}}, {{PDB2|1y7z}}, {{PDB2|1y83}}, {{PDB2|1y85}}, {{PDB2|1y8w}}, {{PDB2|1ydz}}, {{PDB2|1ye0}}, {{PDB2|1ye1}}, {{PDB2|1ye2}}, {{PDB2|1yen}}, {{PDB2|1yeo}}, {{PDB2|1yeq}}, {{PDB2|1yeu}}, {{PDB2|1yev}}, {{PDB2|1yff}}, {{PDB2|1yg5}}, {{PDB2|1ygd}}, {{PDB2|1ygf}}, {{PDB2|1yh9}}, {{PDB2|1yhe}}, {{PDB2|1yhr}}, {{PDB2|1yie}}, {{PDB2|1yih}}, {{PDB2|1yvq}}, {{PDB2|1yvt}}, {{PDB2|1yzi}}, {{PDB2|1z8u}}, {{PDB2|2d5z}}, {{PDB2|2d60}}, {{PDB2|2dn1}}, {{PDB2|2dn2}}, {{PDB2|2dn3}}, {{PDB2|2h35}}, {{PDB2|2hbc}}, {{PDB2|2hbd}}, {{PDB2|2hbe}}, {{PDB2|2hbf}}, {{PDB2|2hbs}}, {{PDB2|2hco}}, {{PDB2|2hhb}}, {{PDB2|2hhd}}, {{PDB2|2hhe}}, {{PDB2|3hhb}}, {{PDB2|4hhb}}, {{PDB2|6hbw}}
| Name = Hemoglobin, alpha 1
| HGNCid = 4823
| Symbol = HBA1
| AltSymbols =; CD31; MGC126895; MGC126897; HBA1
| OMIM = 141800
| ECnumber =
| Homologene = 469
| MGIid = 96015
<!-- The Following entry is a time stamp of the last bot update. It is typically hidden data -->
| DateOfBotUpdate = ~~~~~
| Function = {{GNF_GO|id=GO:0005344 |text = oxygen transporter activity}} {{GNF_GO|id=GO:0005506 |text = iron ion binding}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0019825 |text = oxygen binding}} {{GNF_GO|id=GO:0020037 |text = heme binding}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}}
| Component = {{GNF_GO|id=GO:0005833 |text = hemoglobin complex}}
| Process = {{GNF_GO|id=GO:0006810 |text = transport}} {{GNF_GO|id=GO:0015671 |text = oxygen transport}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 3039
| Hs_Ensembl =
| Hs_RefseqProtein = NP_000549
| Hs_RefseqmRNA = NM_000558
| Hs_GenLoc_db =
| Hs_GenLoc_chr =
| Hs_GenLoc_start =
| Hs_GenLoc_end =
| Hs_Uniprot =
| Mm_EntrezGene = 15122
| Mm_Ensembl = ENSMUSG00000069917
| Mm_RefseqmRNA = NM_008218
| Mm_RefseqProtein = NP_032244
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 11
| Mm_GenLoc_start = 32196489
| Mm_GenLoc_end = 32197310
| Mm_Uniprot = Q61287
}}
}}
'''Hemoglobin, alpha 1''', also known as '''HBA1''', is a human [[gene]].
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = The human alpha globin gene cluster located on chromosome 16 spans about 30 kb and includes seven loci: 5'- zeta - pseudozeta - mu - pseudoalpha-1 - alpha-2 - alpha-1 - theta - 3'. The alpha-2 (HBA2) and alpha-1 (HBA1) coding sequences are identical. These genes differ slightly over the 5' untranslated regions and the introns, but they differ significantly over the 3' untranslated regions. Two alpha chains plus two beta chains constitute HbA, which in normal adult life comprises about 97% of the total hemoglobin; alpha chains combine with delta chains to constitute HbA-2, which with HbF (fetal hemoglobin) makes up the remaining 3% of adult hemoglobin. Alpha thalassemias result from deletions of each of the alpha genes as well as deletions of both HBA2 and HBA1; some nondeletion alpha thalassemias have also been reported.<ref>{{cite web | title = Entrez Gene: HBA1 hemoglobin, alpha 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3039| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Schillirò G, Russo-Mancuso G, Dibenedetto SP, ''et al.'' |title=Six rare hemoglobin variants found in Sicily. |journal=Hemoglobin |volume=15 |issue= 5 |pages= 431-7 |year= 1992 |pmid= 1802885 |doi= }}
*{{cite journal | author=Higgs DR, Vickers MA, Wilkie AO, ''et al.'' |title=A review of the molecular genetics of the human alpha-globin gene cluster. |journal=Blood |volume=73 |issue= 5 |pages= 1081-104 |year= 1989 |pmid= 2649166 |doi= }}
*{{cite journal | author=Giardina B, Messana I, Scatena R, Castagnola M |title=The multiple functions of hemoglobin. |journal=Crit. Rev. Biochem. Mol. Biol. |volume=30 |issue= 3 |pages= 165-96 |year= 1995 |pmid= 7555018 |doi= }}
*{{cite journal | author=Yalçin A, Avcu F, Beyan C, ''et al.'' |title=A case of HB J-Meerut (or Hb J-Birmingham) [alpha 120(H3)Ala-->Glu] |journal=Hemoglobin |volume=18 |issue= 6 |pages= 433-5 |year= 1995 |pmid= 7713747 |doi= }}
*{{cite journal | author=Turbpaiboon C, Svasti S, Sawangareetakul P, ''et al.'' |title=Hb Siam [alpha15(A13)Gly-->Arg (alpha1) (GGT-->CGT)] is a typical alpha chain hemoglobinopathy without an alpha-thalassemic effect. |journal=Hemoglobin |volume=26 |issue= 1 |pages= 77-81 |year= 2002 |pmid= 11939517 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on HBB... {October 3, 2007 10:18:20 PM PDT}
- AMBIGUITY: Did not locate an acceptable page to update. {October 3, 2007 10:18:35 PM PDT}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
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| update_summary = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB = {{PDB2|1a00}}, {{PDB2|1a01}}, {{PDB2|1a0u}}, {{PDB2|1a0z}}, {{PDB2|1a3n}}, {{PDB2|1a3o}}, {{PDB2|1abw}}, {{PDB2|1aby}}, {{PDB2|1aj9}}, {{PDB2|1b86}}, {{PDB2|1bab}}, {{PDB2|1bbb}}, {{PDB2|1bij}}, {{PDB2|1buw}}, {{PDB2|1bz0}}, {{PDB2|1bz1}}, {{PDB2|1bzz}}, {{PDB2|1c7b}}, {{PDB2|1c7c}}, {{PDB2|1c7d}}, {{PDB2|1cbl}}, {{PDB2|1cbm}}, {{PDB2|1cls}}, {{PDB2|1cmy}}, {{PDB2|1coh}}, {{PDB2|1dke}}, {{PDB2|1dxt}}, {{PDB2|1dxu}}, {{PDB2|1dxv}}, {{PDB2|1fn3}}, {{PDB2|1g9v}}, {{PDB2|1gbu}}, {{PDB2|1gbv}}, {{PDB2|1gli}}, {{PDB2|1gzx}}, {{PDB2|1hab}}, {{PDB2|1hac}}, {{PDB2|1hba}}, {{PDB2|1hbb}}, {{PDB2|1hbs}}, {{PDB2|1hco}}, {{PDB2|1hdb}}, {{PDB2|1hga}}, {{PDB2|1hgb}}, {{PDB2|1hgc}}, {{PDB2|1hho}}, {{PDB2|1ird}}, {{PDB2|1j3y}}, {{PDB2|1j3z}}, {{PDB2|1j40}}, {{PDB2|1j41}}, {{PDB2|1j7s}}, {{PDB2|1j7w}}, {{PDB2|1j7y}}, {{PDB2|1jy7}}, {{PDB2|1k0y}}, {{PDB2|1k1k}}, {{PDB2|1kd2}}, {{PDB2|1lfl}}, {{PDB2|1lfq}}, {{PDB2|1lft}}, {{PDB2|1lfv}}, {{PDB2|1lfy}}, {{PDB2|1lfz}}, {{PDB2|1ljw}}, {{PDB2|1m9p}}, {{PDB2|1mko}}, {{PDB2|1nej}}, {{PDB2|1nih}}, {{PDB2|1nqp}}, {{PDB2|1o1i}}, {{PDB2|1o1j}}, {{PDB2|1o1k}}, {{PDB2|1o1l}}, {{PDB2|1o1m}}, {{PDB2|1o1n}}, {{PDB2|1o1o}}, {{PDB2|1o1p}}, {{PDB2|1qi8}}, {{PDB2|1qsh}}, {{PDB2|1qsi}}, {{PDB2|1qxd}}, {{PDB2|1qxe}}, {{PDB2|1r1x}}, {{PDB2|1r1y}}, {{PDB2|1rps}}, {{PDB2|1rq3}}, {{PDB2|1rq4}}, {{PDB2|1rqa}}, {{PDB2|1rvw}}, {{PDB2|1sdk}}, {{PDB2|1sdl}}, {{PDB2|1shr}}, {{PDB2|1si4}}, {{PDB2|1thb}}, {{PDB2|1uiw}}, {{PDB2|1vwt}}, {{PDB2|1xxt}}, {{PDB2|1xy0}}, {{PDB2|1xye}}, {{PDB2|1xz2}}, {{PDB2|1xz4}}, {{PDB2|1xz5}}, {{PDB2|1xz7}}, {{PDB2|1xzu}}, {{PDB2|1xzv}}, {{PDB2|1y09}}, {{PDB2|1y0a}}, {{PDB2|1y0c}}, {{PDB2|1y0d}}, {{PDB2|1y0t}}, {{PDB2|1y0w}}, {{PDB2|1y22}}, {{PDB2|1y2z}}, {{PDB2|1y31}}, {{PDB2|1y35}}, {{PDB2|1y45}}, {{PDB2|1y46}}, {{PDB2|1y4b}}, {{PDB2|1y4f}}, {{PDB2|1y4g}}, {{PDB2|1y4p}}, {{PDB2|1y4q}}, {{PDB2|1y4r}}, {{PDB2|1y4v}}, {{PDB2|1y5f}}, {{PDB2|1y5j}}, {{PDB2|1y5k}}, {{PDB2|1y7c}}, {{PDB2|1y7d}}, {{PDB2|1y7g}}, {{PDB2|1y7z}}, {{PDB2|1y83}}, {{PDB2|1y85}}, {{PDB2|1y8w}}, {{PDB2|1ydz}}, {{PDB2|1ye0}}, {{PDB2|1ye1}}, {{PDB2|1ye2}}, {{PDB2|1yen}}, {{PDB2|1yeo}}, {{PDB2|1yeq}}, {{PDB2|1yeu}}, {{PDB2|1yev}}, {{PDB2|1yff}}, {{PDB2|1yg5}}, {{PDB2|1ygd}}, {{PDB2|1ygf}}, {{PDB2|1yh9}}, {{PDB2|1yhe}}, {{PDB2|1yhr}}, {{PDB2|1yie}}, {{PDB2|1yih}}, {{PDB2|1yvq}}, {{PDB2|1yvt}}, {{PDB2|1yzi}}, {{PDB2|2d5z}}, {{PDB2|2d60}}, {{PDB2|2dn1}}, {{PDB2|2dn2}}, {{PDB2|2dn3}}, {{PDB2|2h35}}, {{PDB2|2hbc}}, {{PDB2|2hbd}}, {{PDB2|2hbe}}, {{PDB2|2hbf}}, {{PDB2|2hbs}}, {{PDB2|2hco}}, {{PDB2|2hhb}}, {{PDB2|2hhd}}, {{PDB2|2hhe}}, {{PDB2|3hhb}}, {{PDB2|4hhb}}, {{PDB2|6hbw}}
| Name = Hemoglobin, beta
| HGNCid = 4827
| Symbol = HBB
| AltSymbols =; CD113t-C; HBD
| OMIM = 141900
| ECnumber =
| Homologene = 68066
| MGIid = 96022
<!-- The Following entry is a time stamp of the last bot update. It is typically hidden data -->
| DateOfBotUpdate = ~~~~~
| Function = {{GNF_GO|id=GO:0005344 |text = oxygen transporter activity}} {{GNF_GO|id=GO:0005506 |text = iron ion binding}} {{GNF_GO|id=GO:0008430 |text = selenium binding}} {{GNF_GO|id=GO:0019825 |text = oxygen binding}} {{GNF_GO|id=GO:0020037 |text = heme binding}} {{GNF_GO|id=GO:0030492 |text = hemoglobin binding}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}}
| Component = {{GNF_GO|id=GO:0005833 |text = hemoglobin complex}}
| Process = {{GNF_GO|id=GO:0006810 |text = transport}} {{GNF_GO|id=GO:0008150 |text = biological_process}} {{GNF_GO|id=GO:0015671 |text = oxygen transport}} {{GNF_GO|id=GO:0030185 |text = nitric oxide transport}} {{GNF_GO|id=GO:0045429 |text = positive regulation of nitric oxide biosynthetic process}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 3043
| Hs_Ensembl =
| Hs_RefseqProtein = NP_000509
| Hs_RefseqmRNA = NM_000518
| Hs_GenLoc_db =
| Hs_GenLoc_chr =
| Hs_GenLoc_start =
| Hs_GenLoc_end =
| Hs_Uniprot =
| Mm_EntrezGene = 15130
| Mm_Ensembl =
| Mm_RefseqmRNA = NM_016956
| Mm_RefseqProtein = NP_058652
| Mm_GenLoc_db =
| Mm_GenLoc_chr =
| Mm_GenLoc_start =
| Mm_GenLoc_end =
| Mm_Uniprot =
}}
}}
'''Hemoglobin, beta''', also known as '''HBB''', is a human [[gene]].
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = The alpha (HBA) and beta (HBB) loci determine the structure of the 2 types of polypeptide chains in adult hemoglobin, Hb A. The normal adult hemoglobin tetramer consists of two alpha chains and two beta chains. Mutant beta globin causes sickle cell anemia. Absence of beta chain causes beta-zero-thalassemia. Reduced amounts of detectable beta globin causes beta-plus-thalassemia. The order of the genes in the beta-globin cluster is 5'-epsilon -- gamma-G -- gamma-A -- delta -- beta--3'.<ref>{{cite web | title = Entrez Gene: HBB hemoglobin, beta| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3043| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Higgs DR, Vickers MA, Wilkie AO, ''et al.'' |title=A review of the molecular genetics of the human alpha-globin gene cluster. |journal=Blood |volume=73 |issue= 5 |pages= 1081-104 |year= 1989 |pmid= 2649166 |doi= }}
*{{cite journal | author=Giardina B, Messana I, Scatena R, Castagnola M |title=The multiple functions of hemoglobin. |journal=Crit. Rev. Biochem. Mol. Biol. |volume=30 |issue= 3 |pages= 165-96 |year= 1995 |pmid= 7555018 |doi= }}
*{{cite journal | author=Salzano AM, Carbone V, Pagano L, ''et al.'' |title=Hb Vila Real [beta36(C2)Pro-->His] in Italy: characterization of the amino acid substitution and the DNA mutation. |journal=Hemoglobin |volume=26 |issue= 1 |pages= 21-31 |year= 2002 |pmid= 11939509 |doi= }}
*{{cite journal | author=Frischknecht H, Dutly F |title=A 65 bp duplication/insertion in exon II of the beta globin gene causing beta0-thalassemia. |journal=Haematologica |volume=92 |issue= 3 |pages= 423-4 |year= 2007 |pmid= 17339197 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on HLA-A... {October 3, 2007 10:18:35 PM PDT}
- AMBIGUITY: Did not locate an acceptable page to update. {October 3, 2007 10:18:45 PM PDT}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB = {{PDB2|1akj}}, {{PDB2|1ao7}}, {{PDB2|1b0g}}, {{PDB2|1b0r}}, {{PDB2|1bd2}}, {{PDB2|1duy}}, {{PDB2|1duz}}, {{PDB2|1eey}}, {{PDB2|1eez}}, {{PDB2|1hhg}}, {{PDB2|1hhh}}, {{PDB2|1hhi}}, {{PDB2|1hhj}}, {{PDB2|1hhk}}, {{PDB2|1hla}}, {{PDB2|1hsb}}, {{PDB2|1i1f}}, {{PDB2|1i1y}}, {{PDB2|1i4f}}, {{PDB2|1i7r}}, {{PDB2|1i7t}}, {{PDB2|1i7u}}, {{PDB2|1im3}}, {{PDB2|1jf1}}, {{PDB2|1jht}}, {{PDB2|1lp9}}, {{PDB2|1oga}}, {{PDB2|1p7q}}, {{PDB2|1q94}}, {{PDB2|1qew}}, {{PDB2|1qr1}}, {{PDB2|1qrn}}, {{PDB2|1qse}}, {{PDB2|1qsf}}, {{PDB2|1qvo}}, {{PDB2|1s8d}}, {{PDB2|1s9w}}, {{PDB2|1s9x}}, {{PDB2|1s9y}}, {{PDB2|1t1w}}, {{PDB2|1t1x}}, {{PDB2|1t1y}}, {{PDB2|1t1z}}, {{PDB2|1t20}}, {{PDB2|1t21}}, {{PDB2|1t22}}, {{PDB2|1tmc}}, {{PDB2|1tvb}}, {{PDB2|1tvh}}, {{PDB2|1w72}}, {{PDB2|1x7q}}, {{PDB2|2av1}}, {{PDB2|2av7}}, {{PDB2|2bck}}, {{PDB2|2bnq}}, {{PDB2|2bnr}}, {{PDB2|2bsu}}, {{PDB2|2bsv}}, {{PDB2|2c7u}}, {{PDB2|2clr}}, {{PDB2|2f53}}, {{PDB2|2f54}}, {{PDB2|2git}}, {{PDB2|2gj6}}, {{PDB2|2hla}}, {{PDB2|2hn7}}, {{PDB2|3hla}}
| Name = Major histocompatibility complex, class I, A
| HGNCid = 4931
| Symbol = HLA-A
| AltSymbols =;
| OMIM = 142800
| ECnumber =
| Homologene = 74421
| MGIid = 95904
<!-- The Following entry is a time stamp of the last bot update. It is typically hidden data -->
| DateOfBotUpdate = ~~~~~
| Function = {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0032393 |text = MHC class I receptor activity}}
| Component = {{GNF_GO|id=GO:0005887 |text = integral to plasma membrane}} {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}} {{GNF_GO|id=GO:0042612 |text = MHC class I protein complex}}
| Process = {{GNF_GO|id=GO:0002474 |text = antigen processing and presentation of peptide antigen via MHC class I}} {{GNF_GO|id=GO:0006955 |text = immune response}} {{GNF_GO|id=GO:0019882 |text = antigen processing and presentation}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 3105
| Hs_Ensembl =
| Hs_RefseqProtein = NP_002107
| Hs_RefseqmRNA = NM_002116
| Hs_GenLoc_db =
| Hs_GenLoc_chr =
| Hs_GenLoc_start =
| Hs_GenLoc_end =
| Hs_Uniprot =
| Mm_EntrezGene = 14972
| Mm_Ensembl =
| Mm_RefseqmRNA = NM_001001892
| Mm_RefseqProtein = NP_001001892
| Mm_GenLoc_db =
| Mm_GenLoc_chr =
| Mm_GenLoc_start =
| Mm_GenLoc_end =
| Mm_Uniprot =
}}
}}
'''Major histocompatibility complex, class I, A''', also known as '''HLA-A''', is a human [[gene]].
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = HLA-A belongs to the HLA class I heavy chain paralogues. This class I molecule is a heterodimer consisting of a heavy chain and a light chain (beta-2 microglobulin). The heavy chain is anchored in the membrane. Class I molecules play a central role in the immune system by presenting peptides derived from the endoplasmic reticulum lumen. They are expressed in nearly all cells. The heavy chain is approximately 45 kDa and its gene contains 8 exons. Exon 1 encodes the leader peptide, exons 2 and 3 encode the alpha1 and alpha2 domains, which both bind the peptide, exon 4 encodes the alpha3 domain, exon 5 encodes the transmembrane region, and exons 6 and 7 encode the cytoplasmic tail. Polymorphisms within exon 2 and exon 3 are responsible for the peptide binding specificity of each class one molecule. Typing for these polymorphisms is routinely done for bone marrow and kidney transplantation. Hundreds of HLA-A alleles have been described.<ref>{{cite web | title = Entrez Gene: HLA-A major histocompatibility complex, class I, A| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3105| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Geyer M, Fackler OT, Peterlin BM |title=Structure--function relationships in HIV-1 Nef. |journal=EMBO Rep. |volume=2 |issue= 7 |pages= 580-5 |year= 2001 |pmid= 11463741 |doi= 10.1093/embo-reports/kve141 }}
*{{cite journal | author=Greenway AL, Holloway G, McPhee DA, ''et al.'' |title=HIV-1 Nef control of cell signalling molecules: multiple strategies to promote virus replication. |journal=J. Biosci. |volume=28 |issue= 3 |pages= 323-35 |year= 2004 |pmid= 12734410 |doi= }}
*{{cite journal | author=Scolari F |title=Inherited forms of IgA nephropathy. |journal=J. Nephrol. |volume=16 |issue= 2 |pages= 317-20 |year= 2003 |pmid= 12768083 |doi= }}
*{{cite journal | author=Bénichou S, Benmerah A |title=[The HIV nef and the Kaposi-sarcoma-associated virus K3/K5 proteins: "parasites"of the endocytosis pathway] |journal=Med Sci (Paris) |volume=19 |issue= 1 |pages= 100-6 |year= 2003 |pmid= 12836198 |doi= }}
*{{cite journal | author=Leavitt SA, SchOn A, Klein JC, ''et al.'' |title=Interactions of HIV-1 proteins gp120 and Nef with cellular partners define a novel allosteric paradigm. |journal=Curr. Protein Pept. Sci. |volume=5 |issue= 1 |pages= 1-8 |year= 2004 |pmid= 14965316 |doi= }}
*{{cite journal | author=Tolstrup M, Ostergaard L, Laursen AL, ''et al.'' |title=HIV/SIV escape from immune surveillance: focus on Nef. |journal=Curr. HIV Res. |volume=2 |issue= 2 |pages= 141-51 |year= 2004 |pmid= 15078178 |doi= }}
*{{cite journal | author=Joseph AM, Kumar M, Mitra D |title=Nef: "necessary and enforcing factor" in HIV infection. |journal=Curr. HIV Res. |volume=3 |issue= 1 |pages= 87-94 |year= 2005 |pmid= 15638726 |doi= }}
*{{cite journal | author=Anderson JL, Hope TJ |title=HIV accessory proteins and surviving the host cell. |journal=Current HIV/AIDS reports |volume=1 |issue= 1 |pages= 47-53 |year= 2005 |pmid= 16091223 |doi= }}
*{{cite journal | author=Li L, Li HS, Pauza CD, ''et al.'' |title=Roles of HIV-1 auxiliary proteins in viral pathogenesis and host-pathogen interactions. |journal=Cell Res. |volume=15 |issue= 11-12 |pages= 923-34 |year= 2006 |pmid= 16354571 |doi= 10.1038/sj.cr.7290370 }}
*{{cite journal | author=Stove V, Verhasselt B |title=Modelling thymic HIV-1 Nef effects. |journal=Curr. HIV Res. |volume=4 |issue= 1 |pages= 57-64 |year= 2006 |pmid= 16454711 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on HLA-DRB1... {October 3, 2007 10:18:46 PM PDT}
- AMBIGUITY: Did not locate an acceptable page to update. {October 3, 2007 10:19:43 PM PDT}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB = {{PDB2|1aqd}}, {{PDB2|1bx2}}, {{PDB2|1d5m}}, {{PDB2|1d5x}}, {{PDB2|1d5z}}, {{PDB2|1d6e}}, {{PDB2|1dlh}}, {{PDB2|1fv1}}, {{PDB2|1fyt}}, {{PDB2|1h15}}, {{PDB2|1hqr}}, {{PDB2|1hxy}}, {{PDB2|1j8h}}, {{PDB2|1jwm}}, {{PDB2|1jws}}, {{PDB2|1jwu}}, {{PDB2|1kg0}}, {{PDB2|1klg}}, {{PDB2|1klu}}, {{PDB2|1lo5}}, {{PDB2|1pyw}}, {{PDB2|1r5i}}, {{PDB2|1seb}}, {{PDB2|1sje}}, {{PDB2|1sjh}}, {{PDB2|1t5w}}, {{PDB2|1t5x}}, {{PDB2|1ymm}}, {{PDB2|1zgl}}, {{PDB2|2fse}}, {{PDB2|2g9h}}, {{PDB2|2iam}}, {{PDB2|2ian}}, {{PDB2|2icw}}, {{PDB2|2ipk}}, {{PDB2|2oje}}, {{PDB2|2seb}}
| Name = Major histocompatibility complex, class II, DR beta 1
| HGNCid = 4948
| Symbol = HLA-DRB1
| AltSymbols =; DRB1; HLA DRB1; HLA-DR1B
| OMIM = 142857
| ECnumber =
| Homologene = 85991
| MGIid = 95901
| GeneAtlas_image1 = PBB_GE_HLA-DRB1_209312_x_at_tn.png
| GeneAtlas_image2 = PBB_GE_HLA-DRB1_215193_x_at_tn.png
<!-- The Following entry is a time stamp of the last bot update. It is typically hidden data -->
| DateOfBotUpdate = ~~~~~
| Function = {{GNF_GO|id=GO:0032395 |text = MHC class II receptor activity}}
| Component = {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}} {{GNF_GO|id=GO:0042613 |text = MHC class II protein complex}}
| Process = {{GNF_GO|id=GO:0002504 |text = antigen processing and presentation of peptide or polysaccharide antigen via MHC class II}} {{GNF_GO|id=GO:0006955 |text = immune response}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 3123
| Hs_Ensembl = ENSG00000196126
| Hs_RefseqProtein = NP_002115
| Hs_RefseqmRNA = NM_002124
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 6
| Hs_GenLoc_start = 32654524
| Hs_GenLoc_end = 32665603
| Hs_Uniprot = P01911
| Mm_EntrezGene = 14969
| Mm_Ensembl = ENSMUSG00000060586
| Mm_RefseqmRNA = NM_010382
| Mm_RefseqProtein = NP_034512
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 17
| Mm_GenLoc_start = 33913591
| Mm_GenLoc_end = 33923315
| Mm_Uniprot = O19450
}}
}}
'''Major histocompatibility complex, class II, DR beta 1''', also known as '''HLA-DRB1''', is a human [[gene]].
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = HLA-DRB1 belongs to the HLA class II beta chain paralogues. The class II molecule is a heterodimer consisting of an alpha (DRA) and a beta chain (DRB), both anchored in the membrane. It plays a central role in the immune system by presenting peptides derived from extracellular proteins. Class II molecules are expressed in antigen presenting cells (APC: B lymphocytes, dendritic cells, macrophages). The beta chain is approximately 26-28 kDa. It is encoded by 6 exons, exon one encodes the leader peptide, exons 2 and 3 encode the two extracellular domains, exon 4 encodes the transmembrane domain and exon 5 encodes the cytoplasmic tail. Within the DR molecule the beta chain contains all the polymorphisms specifying the peptide binding specificities. Hundreds of DRB1 alleles have been described and typing for these polymorphisms is routinely done for bone marrow and kidney transplantation. DRB1 is expressed at a level five times higher than its paralogues DRB3, DRB4 and DRB5. DRB1 is present in all individuals. Allelic variants of DRB1 are linked with either none or one of the genes DRB3, DRB4 and DRB5. There are 4 related pseudogenes: DRB2, DRB6, DRB7, DRB8 and DRB9.<ref>{{cite web | title = Entrez Gene: HLA-DRB1 major histocompatibility complex, class II, DR beta 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3123| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Turesson C, Matteson EL |title=Genetics of rheumatoid arthritis. |journal=Mayo Clin. Proc. |volume=81 |issue= 1 |pages= 94-101 |year= 2006 |pmid= 16438485 |doi= }}
*{{cite journal | author=Ahmad T, Marshall SE, Jewell D |title=Genetics of inflammatory bowel disease: the role of the HLA complex. |journal=World J. Gastroenterol. |volume=12 |issue= 23 |pages= 3628-35 |year= 2006 |pmid= 16773677 |doi= }}
*{{cite journal | author=Schmidt H, Williamson D, Ashley-Koch A |title=HLA-DR15 haplotype and multiple sclerosis: a HuGE review. |journal=Am. J. Epidemiol. |volume=165 |issue= 10 |pages= 1097-109 |year= 2007 |pmid= 17329717 |doi= 10.1093/aje/kwk118 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on ICAM1... {October 3, 2007 10:19:43 PM PDT}
- AMBIGUITY: Did not locate an acceptable page to update. {October 3, 2007 10:21:13 PM PDT}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB = {{PDB2|1d3e}}, {{PDB2|1d3i}}, {{PDB2|1d3l}}, {{PDB2|1iam}}, {{PDB2|1ic1}}, {{PDB2|1mq8}}, {{PDB2|1p53}}, {{PDB2|1z7z}}
| Name = Intercellular adhesion molecule 1 (CD54), human rhinovirus receptor
| HGNCid = 5344
| Symbol = ICAM1
| AltSymbols =; BB2; CD54; P3.58
| OMIM = 147840
| ECnumber =
| Homologene = 168
| MGIid = 96392
| GeneAtlas_image1 = PBB_GE_ICAM1_202638_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_ICAM1_207194_s_at_tn.png
| GeneAtlas_image3 = PBB_GE_ICAM1_202637_s_at_tn.png
<!-- The Following entry is a time stamp of the last bot update. It is typically hidden data -->
| DateOfBotUpdate = ~~~~~
| Function = {{GNF_GO|id=GO:0004888 |text = transmembrane receptor activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}}
| Component = {{GNF_GO|id=GO:0005886 |text = plasma membrane}} {{GNF_GO|id=GO:0005887 |text = integral to plasma membrane}}
| Process = {{GNF_GO|id=GO:0016337 |text = cell-cell adhesion}} {{GNF_GO|id=GO:0030155 |text = regulation of cell adhesion}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 3383
| Hs_Ensembl = ENSG00000090339
| Hs_RefseqProtein = NP_000192
| Hs_RefseqmRNA = NM_000201
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 19
| Hs_GenLoc_start = 10242765
| Hs_GenLoc_end = 10258291
| Hs_Uniprot = P05362
| Mm_EntrezGene = 15894
| Mm_Ensembl = ENSMUSG00000037405
| Mm_RefseqmRNA = NM_010493
| Mm_RefseqProtein = NP_034623
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 9
| Mm_GenLoc_start = 20766362
| Mm_GenLoc_end = 20779199
| Mm_Uniprot = Q3TB10
}}
}}
'''Intercellular adhesion molecule 1 (CD54), human rhinovirus receptor''', also known as '''ICAM1''', is a human [[gene]].
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = ICAM1 (CD54) is typically expressed on endothelial cells and cells of the immune system. ICAM1 binds to integrins of type CD11a / CD18, or CD11b / CD18. ICAM1 is also exploited by Rhinovirus as a receptor.<ref>{{cite web | title = Entrez Gene: ICAM1 intercellular adhesion molecule 1 (CD54), human rhinovirus receptor| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3383| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Wahl SM, Greenwell-Wild T, Hale-Donze H, ''et al.'' |title=Permissive factors for HIV-1 infection of macrophages. |journal=J. Leukoc. Biol. |volume=68 |issue= 3 |pages= 303-10 |year= 2000 |pmid= 10985244 |doi= }}
*{{cite journal | author=Yonekawa K, Harlan JM |title=Targeting leukocyte integrins in human diseases. |journal=J. Leukoc. Biol. |volume=77 |issue= 2 |pages= 129-40 |year= 2005 |pmid= 15548573 |doi= 10.1189/jlb.0804460 }}
*{{cite journal | author=Chakravorty SJ, Craig A |title=The role of ICAM-1 in Plasmodium falciparum cytoadherence. |journal=Eur. J. Cell Biol. |volume=84 |issue= 1 |pages= 15-27 |year= 2005 |pmid= 15724813 |doi= }}
*{{cite journal | author=Lebedeva T, Dustin ML, Sykulev Y |title=ICAM-1 co-stimulates target cells to facilitate antigen presentation. |journal=Curr. Opin. Immunol. |volume=17 |issue= 3 |pages= 251-8 |year= 2005 |pmid= 15886114 |doi= 10.1016/j.coi.2005.04.008 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on IFNG... {October 3, 2007 10:21:13 PM PDT}
- AMBIGUITY: Did not locate an acceptable page to update. {October 3, 2007 10:21:55 PM PDT}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB = {{PDB2|1eku}}, {{PDB2|1fg9}}, {{PDB2|1fyh}}, {{PDB2|1hig}}
| Name = Interferon, gamma
| HGNCid = 5438
| Symbol = IFNG
| AltSymbols =; IFG; IFI
| OMIM = 147570
| ECnumber =
| Homologene = 55526
| MGIid = 107656
| GeneAtlas_image1 = PBB_GE_IFNG_210354_at_tn.png
<!-- The Following entry is a time stamp of the last bot update. It is typically hidden data -->
| DateOfBotUpdate = ~~~~~
| Function = {{GNF_GO|id=GO:0005125 |text = cytokine activity}} {{GNF_GO|id=GO:0005133 |text = interferon-gamma receptor binding}} {{GNF_GO|id=GO:0016563 |text = transcription activator activity}}
| Component = {{GNF_GO|id=GO:0005576 |text = extracellular region}} {{GNF_GO|id=GO:0005615 |text = extracellular space}}
| Process = {{GNF_GO|id=GO:0001558 |text = regulation of cell growth}} {{GNF_GO|id=GO:0001781 |text = neutrophil apoptosis}} {{GNF_GO|id=GO:0006925 |text = inflammatory cell apoptosis}} {{GNF_GO|id=GO:0006928 |text = cell motility}} {{GNF_GO|id=GO:0007166 |text = cell surface receptor linked signal transduction}} {{GNF_GO|id=GO:0007267 |text = cell-cell signaling}} {{GNF_GO|id=GO:0009615 |text = response to virus}} {{GNF_GO|id=GO:0019882 |text = antigen processing and presentation}} {{GNF_GO|id=GO:0030593 |text = neutrophil chemotaxis}} {{GNF_GO|id=GO:0030968 |text = unfolded protein response}} {{GNF_GO|id=GO:0031642 |text = negative regulation of myelination}} {{GNF_GO|id=GO:0042742 |text = defense response to bacterium}} {{GNF_GO|id=GO:0045080 |text = positive regulation of chemokine biosynthetic process}} {{GNF_GO|id=GO:0045084 |text = positive regulation of interleukin-12 biosynthetic process}} {{GNF_GO|id=GO:0045348 |text = positive regulation of MHC class II biosynthetic process}} {{GNF_GO|id=GO:0045410 |text = positive regulation of interleukin-6 biosynthetic process}} {{GNF_GO|id=GO:0045449 |text = regulation of transcription}} {{GNF_GO|id=GO:0045893 |text = positive regulation of transcription, DNA-dependent}} {{GNF_GO|id=GO:0048304 |text = positive regulation of isotype switching to IgG isotypes}} {{GNF_GO|id=GO:0050718 |text = positive regulation of interleukin-1 beta secretion}} {{GNF_GO|id=GO:0050776 |text = regulation of immune response}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 3458
| Hs_Ensembl = ENSG00000111537
| Hs_RefseqProtein = NP_000610
| Hs_RefseqmRNA = NM_000619
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 12
| Hs_GenLoc_start = 66834816
| Hs_GenLoc_end = 66839790
| Hs_Uniprot = P01579
| Mm_EntrezGene = 15978
| Mm_Ensembl = ENSMUSG00000055170
| Mm_RefseqmRNA = NM_008337
| Mm_RefseqProtein = NP_032363
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 10
| Mm_GenLoc_start = 117844040
| Mm_GenLoc_end = 117848885
| Mm_Uniprot = Q6TDH0
}}
}}
'''Interferon, gamma''', also known as '''IFNG''', is a human [[gene]].
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text =
}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Ikeda H, Old LJ, Schreiber RD |title=The roles of IFN gamma in protection against tumor development and cancer immunoediting. |journal=Cytokine Growth Factor Rev. |volume=13 |issue= 2 |pages= 95-109 |year= 2002 |pmid= 11900986 |doi= }}
*{{cite journal | author=Chesler DA, Reiss CS |title=The role of IFN-gamma in immune responses to viral infections of the central nervous system. |journal=Cytokine Growth Factor Rev. |volume=13 |issue= 6 |pages= 441-54 |year= 2003 |pmid= 12401479 |doi= }}
*{{cite journal | author=Dessein A, Kouriba B, Eboumbou C, ''et al.'' |title=Interleukin-13 in the skin and interferon-gamma in the liver are key players in immune protection in human schistosomiasis. |journal=Immunol. Rev. |volume=201 |issue= |pages= 180-90 |year= 2005 |pmid= 15361241 |doi= 10.1111/j.0105-2896.2004.00195.x }}
*{{cite journal | author=Joseph AM, Kumar M, Mitra D |title=Nef: "necessary and enforcing factor" in HIV infection. |journal=Curr. HIV Res. |volume=3 |issue= 1 |pages= 87-94 |year= 2005 |pmid= 15638726 |doi= }}
*{{cite journal | author=Copeland KF |title=Modulation of HIV-1 transcription by cytokines and chemokines. |journal=Mini reviews in medicinal chemistry |volume=5 |issue= 12 |pages= 1093-101 |year= 2006 |pmid= 16375755 |doi= }}
*{{cite journal | author=Chiba H, Kojima T, Osanai M, Sawada N |title=The significance of interferon-gamma-triggered internalization of tight-junction proteins in inflammatory bowel disease. |journal=Sci. STKE |volume=2006 |issue= 316 |pages= pe1 |year= 2006 |pmid= 16391178 |doi= 10.1126/stke.3162006pe1 }}
*{{cite journal | author=Tellides G, Pober JS |title=Interferon-gamma axis in graft arteriosclerosis. |journal=Circ. Res. |volume=100 |issue= 5 |pages= 622-32 |year= 2007 |pmid= 17363708 |doi= 10.1161/01.RES.0000258861.72279.29 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on INSR... {October 3, 2007 10:21:55 PM PDT}
- AMBIGUITY: Did not locate an acceptable page to update. {October 3, 2007 10:23:28 PM PDT}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
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| update_citations = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB = {{PDB2|1gag}}, {{PDB2|1i44}}, {{PDB2|1ir3}}, {{PDB2|1irk}}, {{PDB2|1p14}}, {{PDB2|1rqq}}, {{PDB2|2auh}}, {{PDB2|2b4s}}, {{PDB2|2dtg}}, {{PDB2|2hr7}}
| Name = Insulin receptor
| HGNCid = 6091
| Symbol = INSR
| AltSymbols =; CD220; HHF5
| OMIM = 147670
| ECnumber =
| Homologene = 20090
| MGIid = 96575
| GeneAtlas_image1 = PBB_GE_INSR_213792_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_INSR_207851_s_at_tn.png
<!-- The Following entry is a time stamp of the last bot update. It is typically hidden data -->
| DateOfBotUpdate = ~~~~~
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0004716 |text = receptor signaling protein tyrosine kinase activity}} {{GNF_GO|id=GO:0004872 |text = receptor activity}} {{GNF_GO|id=GO:0005006 |text = epidermal growth factor receptor activity}} {{GNF_GO|id=GO:0005009 |text = insulin receptor activity}} {{GNF_GO|id=GO:0005066 |text = transmembrane receptor protein tyrosine kinase signaling protein activity}} {{GNF_GO|id=GO:0005524 |text = ATP binding}} {{GNF_GO|id=GO:0016740 |text = transferase activity}} {{GNF_GO|id=GO:0042169 |text = SH2 domain binding}} {{GNF_GO|id=GO:0043548 |text = phosphoinositide 3-kinase binding}} {{GNF_GO|id=GO:0043559 |text = insulin binding}} {{GNF_GO|id=GO:0043560 |text = insulin receptor substrate binding}} {{GNF_GO|id=GO:0051425 |text = PTB domain binding}}
| Component = {{GNF_GO|id=GO:0005886 |text = plasma membrane}} {{GNF_GO|id=GO:0005887 |text = integral to plasma membrane}} {{GNF_GO|id=GO:0016020 |text = membrane}}
| Process = {{GNF_GO|id=GO:0005975 |text = carbohydrate metabolic process}} {{GNF_GO|id=GO:0006091 |text = generation of precursor metabolites and energy}} {{GNF_GO|id=GO:0006468 |text = protein amino acid phosphorylation}} {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0007169 |text = transmembrane receptor protein tyrosine kinase signaling pathway}} {{GNF_GO|id=GO:0008286 |text = insulin receptor signaling pathway}} {{GNF_GO|id=GO:0009887 |text = organ morphogenesis}} {{GNF_GO|id=GO:0030238 |text = male sex determination}} {{GNF_GO|id=GO:0046777 |text = protein amino acid autophosphorylation}} {{GNF_GO|id=GO:0051290 |text = protein heterotetramerization}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 3643
| Hs_Ensembl = ENSG00000171105
| Hs_RefseqProtein = NP_000199
| Hs_RefseqmRNA = NM_000208
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 19
| Hs_GenLoc_start = 7067049
| Hs_GenLoc_end = 7245045
| Hs_Uniprot = P06213
| Mm_EntrezGene = 16337
| Mm_Ensembl = ENSMUSG00000005534
| Mm_RefseqmRNA = XM_972939
| Mm_RefseqProtein = XP_978033
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 8
| Mm_GenLoc_start = 3155401
| Mm_GenLoc_end = 3279128
| Mm_Uniprot = O35466
}}
}}
'''Insulin receptor''', also known as '''INSR''', is a human [[gene]].
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = After removal of the precursor signal peptide, the insulin receptor precursor is post-translationally cleaved into two chains (alpha and beta) that are covalently linked. Binding of insulin to the insulin receptor (INSR) stimulates glucose uptake. Two transcript variants encoding different isoforms have been found for this gene.<ref>{{cite web | title = Entrez Gene: INSR insulin receptor| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3643| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Pearson RB, Kemp BE |title=Protein kinase phosphorylation site sequences and consensus specificity motifs: tabulations. |journal=Meth. Enzymol. |volume=200 |issue= |pages= 62-81 |year= 1991 |pmid= 1956339 |doi= }}
*{{cite journal | author=Joost HG |title=Structural and functional heterogeneity of insulin receptors. |journal=Cell. Signal. |volume=7 |issue= 2 |pages= 85-91 |year= 1995 |pmid= 7794689 |doi= }}
*{{cite journal | author=O'Dell SD, Day IN |title=Insulin-like growth factor II (IGF-II). |journal=Int. J. Biochem. Cell Biol. |volume=30 |issue= 7 |pages= 767-71 |year= 1998 |pmid= 9722981 |doi= }}
*{{cite journal | author=Lopaczynski W |title=Differential regulation of signaling pathways for insulin and insulin-like growth factor I. |journal=Acta Biochim. Pol. |volume=46 |issue= 1 |pages= 51-60 |year= 1999 |pmid= 10453981 |doi= }}
*{{cite journal | author=Sasaoka T, Kobayashi M |title=The functional significance of Shc in insulin signaling as a substrate of the insulin receptor. |journal=Endocr. J. |volume=47 |issue= 4 |pages= 373-81 |year= 2000 |pmid= 11075717 |doi= }}
*{{cite journal | author=Perz M, Torlińska T |title=Insulin receptor--structural and functional characteristics. |journal=Med. Sci. Monit. |volume=7 |issue= 1 |pages= 169-77 |year= 2001 |pmid= 11208515 |doi= }}
*{{cite journal | author=Benaim G, Villalobo A |title=Phosphorylation of calmodulin. Functional implications. |journal=Eur. J. Biochem. |volume=269 |issue= 15 |pages= 3619-31 |year= 2002 |pmid= 12153558 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on ITGB3... {October 3, 2007 10:23:28 PM PDT}
- AMBIGUITY: Did not locate an acceptable page to update. {October 3, 2007 10:24:57 PM PDT}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB = {{PDB2|1jv2}}, {{PDB2|1l5g}}, {{PDB2|1m1x}}, {{PDB2|1m8o}}, {{PDB2|1txv}}, {{PDB2|1ty3}}, {{PDB2|1ty5}}, {{PDB2|1ty6}}, {{PDB2|1ty7}}, {{PDB2|1tye}}, {{PDB2|1u8c}}
| Name = Integrin, beta 3 (platelet glycoprotein IIIa, antigen CD61)
| HGNCid = 6156
| Symbol = ITGB3
| AltSymbols =; CD61; GP3A; GPIIIa
| OMIM = 173470
| ECnumber =
| Homologene = 55444
| MGIid = 96612
| GeneAtlas_image1 = PBB_GE_ITGB3_204628_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_ITGB3_204625_s_at_tn.png
| GeneAtlas_image3 = PBB_GE_ITGB3_204626_s_at_tn.png
<!-- The Following entry is a time stamp of the last bot update. It is typically hidden data -->
| DateOfBotUpdate = ~~~~~
| Function = {{GNF_GO|id=GO:0004872 |text = receptor activity}} {{GNF_GO|id=GO:0005178 |text = integrin binding}} {{GNF_GO|id=GO:0042802 |text = identical protein binding}}
| Component = {{GNF_GO|id=GO:0008305 |text = integrin complex}} {{GNF_GO|id=GO:0009897 |text = external side of plasma membrane}} {{GNF_GO|id=GO:0016020 |text = membrane}}
| Process = {{GNF_GO|id=GO:0007044 |text = cell-substrate junction assembly}} {{GNF_GO|id=GO:0007155 |text = cell adhesion}} {{GNF_GO|id=GO:0007160 |text = cell-matrix adhesion}} {{GNF_GO|id=GO:0007229 |text = integrin-mediated signaling pathway}} {{GNF_GO|id=GO:0007275 |text = multicellular organismal development}} {{GNF_GO|id=GO:0007596 |text = blood coagulation}} {{GNF_GO|id=GO:0030334 |text = regulation of cell migration}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 3690
| Hs_Ensembl = ENSG00000056345
| Hs_RefseqProtein = NP_000203
| Hs_RefseqmRNA = NM_000212
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 17
| Hs_GenLoc_start = 42686207
| Hs_GenLoc_end = 42745076
| Hs_Uniprot = P05106
| Mm_EntrezGene = 16416
| Mm_Ensembl = ENSMUSG00000020689
| Mm_RefseqmRNA = NM_016780
| Mm_RefseqProtein = NP_058060
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 11
| Mm_GenLoc_start = 104424146
| Mm_GenLoc_end = 104483465
| Mm_Uniprot = P97483
}}
}}
'''Integrin, beta 3 (platelet glycoprotein IIIa, antigen CD61)''', also known as '''ITGB3''', is a human [[gene]].
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = The ITGB3 protein product is the integrin beta chain beta 3. Integrins are integral cell-surface proteins composed of an alpha chain and a beta chain. A given chain may combine with multiple partners resulting in different integrins. Integrin beta 3 is found along with the alpha IIb chain in platelets. Integrins are known to participate in cell adhesion as well as cell-surface mediated signalling.<ref>{{cite web | title = Entrez Gene: ITGB3 integrin, beta 3 (platelet glycoprotein IIIa, antigen CD61)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3690| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Bray PF |title=Inherited diseases of platelet glycoproteins: considerations for rapid molecular characterization. |journal=Thromb. Haemost. |volume=72 |issue= 4 |pages= 492-502 |year= 1995 |pmid= 7878622 |doi= }}
*{{cite journal | author=Bennett JS |title=Platelet-fibrinogen interactions. |journal=Ann. N. Y. Acad. Sci. |volume=936 |issue= |pages= 340-54 |year= 2001 |pmid= 11460491 |doi= }}
*{{cite journal | author=Sajid M, Stouffer GA |title=The role of alpha(v)beta3 integrins in vascular healing. |journal=Thromb. Haemost. |volume=87 |issue= 2 |pages= 187-93 |year= 2002 |pmid= 11858476 |doi= }}
*{{cite journal | author=Quinn MJ, Byzova TV, Qin J, ''et al.'' |title=Integrin alphaIIbbeta3 and its antagonism. |journal=Arterioscler. Thromb. Vasc. Biol. |volume=23 |issue= 6 |pages= 945-52 |year= 2004 |pmid= 12637342 |doi= 10.1161/01.ATV.0000066686.46338.F1 }}
*{{cite journal | author=Charakida M, Tousoulis D, Stefanadis C, Toutouzas P |title=The impact of platelet glycoprotein IIIa and Ia polymorphisms in cardiovascular thrombotic disease. |journal=Italian heart journal : official journal of the Italian Federation of Cardiology |volume=4 |issue= 1 |pages= 17-22 |year= 2003 |pmid= 12690916 |doi= }}
*{{cite journal | author=Smith FB, Connor JM, Lee AJ, ''et al.'' |title=Relationship of the platelet glycoprotein PlA and fibrinogen T/G+1689 polymorphisms with peripheral arterial disease and ischaemic heart disease. |journal=Thromb. Res. |volume=112 |issue= 4 |pages= 209-16 |year= 2004 |pmid= 14987913 |doi= 10.1016/j.thromres.2003.11.010 }}
*{{cite journal | author=Fullard JF |title=The role of the platelet glycoprotein IIb/IIIa in thrombosis and haemostasis. |journal=Curr. Pharm. Des. |volume=10 |issue= 14 |pages= 1567-76 |year= 2004 |pmid= 15134555 |doi= }}
*{{cite journal | author=Cacciari B, Spalluto G |title=Non peptidic alphavbeta3 antagonists: recent developments. |journal=Curr. Med. Chem. |volume=12 |issue= 1 |pages= 51-70 |year= 2005 |pmid= 15638730 |doi= }}
*{{cite journal | author=Watson SP, Auger JM, McCarty OJ, Pearce AC |title=GPVI and integrin alphaIIb beta3 signaling in platelets. |journal=J. Thromb. Haemost. |volume=3 |issue= 8 |pages= 1752-62 |year= 2005 |pmid= 16102042 |doi= 10.1111/j.1538-7836.2005.01429.x }}
*{{cite journal | author=Bennett JS |title=Structure and function of the platelet integrin alphaIIbbeta3. |journal=J. Clin. Invest. |volume=115 |issue= 12 |pages= 3363-9 |year= 2006 |pmid= 16322781 |doi= 10.1172/JCI26989 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on JAK2... {October 3, 2007 10:24:57 PM PDT}
- AMBIGUITY: Did not locate an acceptable page to update. {October 3, 2007 10:25:09 PM PDT}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB = {{PDB2|2b7a}}
| Name = Janus kinase 2 (a protein tyrosine kinase)
| HGNCid = 6192
| Symbol = JAK2
| AltSymbols =;
| OMIM = 147796
| ECnumber =
| Homologene = 21033
| MGIid = 96629
<!-- The Following entry is a time stamp of the last bot update. It is typically hidden data -->
| DateOfBotUpdate = ~~~~~
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0004713 |text = protein-tyrosine kinase activity}} {{GNF_GO|id=GO:0004718 |text = Janus kinase activity}} {{GNF_GO|id=GO:0005102 |text = receptor binding}} {{GNF_GO|id=GO:0005524 |text = ATP binding}} {{GNF_GO|id=GO:0016740 |text = transferase activity}} {{GNF_GO|id=GO:0042169 |text = SH2 domain binding}}
| Component = {{GNF_GO|id=GO:0005856 |text = cytoskeleton}}
| Process = {{GNF_GO|id=GO:0000074 |text = regulation of progression through cell cycle}} {{GNF_GO|id=GO:0006468 |text = protein amino acid phosphorylation}} {{GNF_GO|id=GO:0006915 |text = apoptosis}} {{GNF_GO|id=GO:0006928 |text = cell motility}} {{GNF_GO|id=GO:0007242 |text = intracellular signaling cascade}} {{GNF_GO|id=GO:0007260 |text = tyrosine phosphorylation of STAT protein}} {{GNF_GO|id=GO:0007262 |text = STAT protein nuclear translocation}} {{GNF_GO|id=GO:0007498 |text = mesoderm development}} {{GNF_GO|id=GO:0008285 |text = negative regulation of cell proliferation}} {{GNF_GO|id=GO:0030099 |text = myeloid cell differentiation}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 3717
| Hs_Ensembl = ENSG00000096968
| Hs_RefseqProtein = NP_004963
| Hs_RefseqmRNA = NM_004972
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 9
| Hs_GenLoc_start = 4975245
| Hs_GenLoc_end = 5118183
| Hs_Uniprot = O60674
| Mm_EntrezGene = 16452
| Mm_Ensembl = ENSMUSG00000024789
| Mm_RefseqmRNA = NM_001048177
| Mm_RefseqProtein = NP_001041642
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 19
| Mm_GenLoc_start = 29318438
| Mm_GenLoc_end = 29378334
| Mm_Uniprot = Q8CIN8
}}
}}
'''Janus kinase 2 (a protein tyrosine kinase)''', also known as '''JAK2''', is a human [[gene]].
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = This gene product is a protein tyrosine kinase involved in a specific subset of cytokine receptor signaling pathways. It has been found to be constituitively associated with the prolactin receptor and is required for responses to gamma interferon. Mice that do not express an active protein for this gene exhibit embryonic lethality associated with the absence of definitive erythropoiesis.<ref>{{cite web | title = Entrez Gene: JAK2 Janus kinase 2 (a protein tyrosine kinase)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3717| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Berger R |title=[A recurrent mutation of the JAK2 gene in chronic myeloproliferative disorders] |journal=Pathol. Biol. |volume=54 |issue= 4 |pages= 182-4 |year= 2006 |pmid= 16084028 |doi= 10.1016/j.patbio.2005.07.002 }}
*{{cite journal | author=Pargade V, Darnige L, Gaussem P |title=[Acquired mutation of JAK2 tyrosine kinase and polycythaemia vera] |journal=Ann. Biol. Clin. (Paris) |volume=64 |issue= 1 |pages= 3-9 |year= 2006 |pmid= 16420986 |doi= }}
*{{cite journal | author=Staerk J, Kallin A, Royer Y, ''et al.'' |title=JAK2, the JAK2 V617F mutant and cytokine receptors. |journal=Pathol. Biol. |volume=55 |issue= 2 |pages= 88-91 |year= 2007 |pmid= 16904848 |doi= 10.1016/j.patbio.2006.06.003 }}
*{{cite journal | author=Hsu HC |title=Pathogenetic role of JAK2 V617F mutation in chronic myeloproliferative disorders. |journal=Journal of the Chinese Medical Association : JCMA |volume=70 |issue= 3 |pages= 89-93 |year= 2007 |pmid= 17389152 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on JUN... {October 3, 2007 10:25:09 PM PDT}
- AMBIGUITY: Did not locate an acceptable page to update. {October 3, 2007 10:26:22 PM PDT}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB = {{PDB2|1a02}}, {{PDB2|1fos}}, {{PDB2|1jnm}}, {{PDB2|1jun}}, {{PDB2|1s9k}}, {{PDB2|1t2k}}
| Name = Jun oncogene
| HGNCid = 6204
| Symbol = JUN
| AltSymbols =; AP1; c-Jun
| OMIM = 165160
| ECnumber =
| Homologene = 1679
| MGIid = 96646
| GeneAtlas_image1 = PBB_GE_JUN_201464_x_at_tn.png
| GeneAtlas_image2 = PBB_GE_JUN_201465_s_at_tn.png
| GeneAtlas_image3 = PBB_GE_JUN_201466_s_at_tn.png
<!-- The Following entry is a time stamp of the last bot update. It is typically hidden data -->
| DateOfBotUpdate = ~~~~~
| Function = {{GNF_GO|id=GO:0003700 |text = transcription factor activity}} {{GNF_GO|id=GO:0003702 |text = RNA polymerase II transcription factor activity}} {{GNF_GO|id=GO:0043565 |text = sequence-specific DNA binding}} {{GNF_GO|id=GO:0046983 |text = protein dimerization activity}}
| Component = {{GNF_GO|id=GO:0000228 |text = nuclear chromosome}} {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005667 |text = transcription factor complex}}
| Process = {{GNF_GO|id=GO:0000074 |text = regulation of progression through cell cycle}} {{GNF_GO|id=GO:0006350 |text = transcription}} {{GNF_GO|id=GO:0006355 |text = regulation of transcription, DNA-dependent}} {{GNF_GO|id=GO:0035026 |text = leading edge cell differentiation}} {{GNF_GO|id=GO:0045944 |text = positive regulation of transcription from RNA polymerase II promoter}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 3725
| Hs_Ensembl = ENSG00000177606
| Hs_RefseqProtein = NP_002219
| Hs_RefseqmRNA = NM_002228
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 1
| Hs_GenLoc_start = 59019048
| Hs_GenLoc_end = 59022587
| Hs_Uniprot = P05412
| Mm_EntrezGene = 16476
| Mm_Ensembl = ENSMUSG00000052684
| Mm_RefseqmRNA = NM_010591
| Mm_RefseqProtein = NP_034721
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 4
| Mm_GenLoc_start = 94542255
| Mm_GenLoc_end = 94544189
| Mm_Uniprot = Q3US19
}}
}}
'''Jun oncogene''', also known as '''JUN''', is a human [[gene]].
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = This gene is the putative transforming gene of avian sarcoma virus 17. It encodes a protein which is highly similar to the viral protein, and which interacts directly with specific target DNA sequences to regulate gene expression. This gene is intronless and is mapped to 1p32-p31, a chromosomal region involved in both translocations and deletions in human malignancies.<ref>{{cite web | title = Entrez Gene: JUN jun oncogene| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3725| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Bohmann D, Bos TJ, Admon A, ''et al.'' |title=Human proto-oncogene c-jun encodes a DNA binding protein with structural and functional properties of transcription factor AP-1. |journal=Science |volume=238 |issue= 4832 |pages= 1386-92 |year= 1988 |pmid= 2825349 |doi= }}
*{{cite journal | author=Rahmsdorf HJ |title=Jun: transcription factor and oncoprotein. |journal=J. Mol. Med. |volume=74 |issue= 12 |pages= 725-47 |year= 1997 |pmid= 8974016 |doi= }}
*{{cite journal | author=Liu JL, Kung HJ |title=Marek's disease herpesvirus transforming protein MEQ: a c-Jun analogue with an alternative life style. |journal=Virus Genes |volume=21 |issue= 1-2 |pages= 51-64 |year= 2001 |pmid= 11022789 |doi= }}
*{{cite journal | author=Velazquez Torres A, Gariglio Vidal P |title=[Possible role of transcription factor AP1 in the tissue-specific regulation of human papillomavirus] |journal=Rev. Invest. Clin. |volume=54 |issue= 3 |pages= 231-42 |year= 2002 |pmid= 12183893 |doi= }}
*{{cite journal | author=Karamouzis MV, Konstantinopoulos PA, Papavassiliou AG |title=The activator protein-1 transcription factor in respiratory epithelium carcinogenesis. |journal=Mol. Cancer Res. |volume=5 |issue= 2 |pages= 109-20 |year= 2007 |pmid= 17314269 |doi= 10.1158/1541-7786.MCR-06-0311 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on LCK... {October 3, 2007 10:26:22 PM PDT}
- AMBIGUITY: Did not locate an acceptable page to update. {October 3, 2007 10:27:17 PM PDT}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB = {{PDB2|1bhf}}, {{PDB2|1bhh}}, {{PDB2|1cwd}}, {{PDB2|1cwe}}, {{PDB2|1fbz}}, {{PDB2|1h92}}, {{PDB2|1ijr}}, {{PDB2|1kik}}, {{PDB2|1lcj}}, {{PDB2|1lck}}, {{PDB2|1lkk}}, {{PDB2|1lkl}}, {{PDB2|1q68}}, {{PDB2|1q69}}, {{PDB2|1qpc}}, {{PDB2|1qpd}}, {{PDB2|1qpe}}, {{PDB2|1qpj}}, {{PDB2|1x27}}, {{PDB2|2iim}}, {{PDB2|2of2}}, {{PDB2|2of4}}, {{PDB2|2ofu}}, {{PDB2|2ofv}}, {{PDB2|2og8}}, {{PDB2|3lck}}
| Name = Lymphocyte-specific protein tyrosine kinase
| HGNCid = 6524
| Symbol = LCK
| AltSymbols =; YT16; p56lck; pp58lck
| OMIM = 153390
| ECnumber =
| Homologene = 3911
| MGIid = 96756
| GeneAtlas_image1 = PBB_GE_LCK_204891_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_LCK_204890_s_at_tn.png
<!-- The Following entry is a time stamp of the last bot update. It is typically hidden data -->
| DateOfBotUpdate = ~~~~~
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0001948 |text = glycoprotein binding}} {{GNF_GO|id=GO:0004713 |text = protein-tyrosine kinase activity}} {{GNF_GO|id=GO:0004722 |text = protein serine/threonine phosphatase activity}} {{GNF_GO|id=GO:0005524 |text = ATP binding}} {{GNF_GO|id=GO:0008022 |text = protein C-terminus binding}} {{GNF_GO|id=GO:0016740 |text = transferase activity}} {{GNF_GO|id=GO:0019901 |text = protein kinase binding}} {{GNF_GO|id=GO:0042169 |text = SH2 domain binding}} {{GNF_GO|id=GO:0042609 |text = CD4 receptor binding}} {{GNF_GO|id=GO:0042610 |text = CD8 receptor binding}} {{GNF_GO|id=GO:0043548 |text = phosphoinositide 3-kinase binding}} {{GNF_GO|id=GO:0051117 |text = ATPase binding}}
| Component = {{GNF_GO|id=GO:0000242 |text = pericentriolar material}} {{GNF_GO|id=GO:0005886 |text = plasma membrane}} {{GNF_GO|id=GO:0045121 |text = lipid raft}}
| Process = {{GNF_GO|id=GO:0000074 |text = regulation of progression through cell cycle}} {{GNF_GO|id=GO:0006468 |text = protein amino acid phosphorylation}} {{GNF_GO|id=GO:0006882 |text = cellular zinc ion homeostasis}} {{GNF_GO|id=GO:0006917 |text = induction of apoptosis}} {{GNF_GO|id=GO:0006919 |text = caspase activation}} {{GNF_GO|id=GO:0007242 |text = intracellular signaling cascade}} {{GNF_GO|id=GO:0007265 |text = Ras protein signal transduction}} {{GNF_GO|id=GO:0030097 |text = hemopoiesis}} {{GNF_GO|id=GO:0030217 |text = T cell differentiation}} {{GNF_GO|id=GO:0042493 |text = response to drug}} {{GNF_GO|id=GO:0050862 |text = positive regulation of T cell receptor signaling pathway}} {{GNF_GO|id=GO:0050870 |text = positive regulation of T cell activation}} {{GNF_GO|id=GO:0051209 |text = release of sequestered calcium ion into cytosol}} {{GNF_GO|id=GO:0051249 |text = regulation of lymphocyte activation}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 3932
| Hs_Ensembl = ENSG00000182866
| Hs_RefseqProtein = NP_001036236
| Hs_RefseqmRNA = NM_001042771
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 1
| Hs_GenLoc_start = 32489480
| Hs_GenLoc_end = 32524353
| Hs_Uniprot = P06239
| Mm_EntrezGene = 16818
| Mm_Ensembl =
| Mm_RefseqmRNA = XM_992422
| Mm_RefseqProtein = XP_997516
| Mm_GenLoc_db =
| Mm_GenLoc_chr =
| Mm_GenLoc_start =
| Mm_GenLoc_end =
| Mm_Uniprot =
}}
}}
'''Lymphocyte-specific protein tyrosine kinase''', also known as '''LCK''', is a human [[gene]].
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = This gene is a member of the Src family of protein tyrosine kinases (PTKs). The encoded protein is a key signaling molecule in the selection and maturation of developing T-cells. It contains N-terminal sites for myristylation and palmitylation, a PTK domain, and SH2 and SH3 domains which are involved in mediating protein-protein interactions with phosphotyrosine-containing and proline-rich motifs, respectively. The protein localizes to the plasma membrane and pericentrosomal vesicles, and binds to cell surface receptors, including CD4 and CD8, and other signaling molecules. Multiple alternatively spliced variants, encoding the same protein, have been described.<ref>{{cite web | title = Entrez Gene: LCK lymphocyte-specific protein tyrosine kinase| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3932| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Sasaoka T, Kobayashi M |title=The functional significance of Shc in insulin signaling as a substrate of the insulin receptor. |journal=Endocr. J. |volume=47 |issue= 4 |pages= 373-81 |year= 2000 |pmid= 11075717 |doi= }}
*{{cite journal | author=Goldmann WH |title=p56(lck) Controls phosphorylation of filamin (ABP-280) and regulates focal adhesion kinase (pp125(FAK)). |journal=Cell Biol. Int. |volume=26 |issue= 6 |pages= 567-71 |year= 2003 |pmid= 12171035 |doi= }}
*{{cite journal | author=Mustelin T, Taskén K |title=Positive and negative regulation of T-cell activation through kinases and phosphatases. |journal=Biochem. J. |volume=371 |issue= Pt 1 |pages= 15-27 |year= 2003 |pmid= 12485116 |doi= 10.1042/BJ20021637 }}
*{{cite journal | author=Zamoyska R, Basson A, Filby A, ''et al.'' |title=The influence of the src-family kinases, Lck and Fyn, on T cell differentiation, survival and activation. |journal=Immunol. Rev. |volume=191 |issue= |pages= 107-18 |year= 2003 |pmid= 12614355 |doi= }}
*{{cite journal | author=Summy JM, Gallick GE |title=Src family kinases in tumor progression and metastasis. |journal=Cancer Metastasis Rev. |volume=22 |issue= 4 |pages= 337-58 |year= 2004 |pmid= 12884910 |doi= }}
*{{cite journal | author=Leavitt SA, SchOn A, Klein JC, ''et al.'' |title=Interactions of HIV-1 proteins gp120 and Nef with cellular partners define a novel allosteric paradigm. |journal=Curr. Protein Pept. Sci. |volume=5 |issue= 1 |pages= 1-8 |year= 2004 |pmid= 14965316 |doi= }}
*{{cite journal | author=Tolstrup M, Ostergaard L, Laursen AL, ''et al.'' |title=HIV/SIV escape from immune surveillance: focus on Nef. |journal=Curr. HIV Res. |volume=2 |issue= 2 |pages= 141-51 |year= 2004 |pmid= 15078178 |doi= }}
*{{cite journal | author=Palacios EH, Weiss A |title=Function of the Src-family kinases, Lck and Fyn, in T-cell development and activation. |journal=Oncogene |volume=23 |issue= 48 |pages= 7990-8000 |year= 2004 |pmid= 15489916 |doi= 10.1038/sj.onc.1208074 }}
*{{cite journal | author=Joseph AM, Kumar M, Mitra D |title=Nef: "necessary and enforcing factor" in HIV infection. |journal=Curr. HIV Res. |volume=3 |issue= 1 |pages= 87-94 |year= 2005 |pmid= 15638726 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on LEP... {October 3, 2007 10:27:17 PM PDT}
- AMBIGUITY: Did not locate an acceptable page to update. {October 3, 2007 10:27:53 PM PDT}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB = {{PDB2|1ax8}}
| Name = Leptin (obesity homolog, mouse)
| HGNCid = 6553
| Symbol = LEP
| AltSymbols =; OB; OBS
| OMIM = 164160
| ECnumber =
| Homologene = 193
| MGIid = 104663
| GeneAtlas_image1 = PBB_GE_LEP_207092_at_tn.png
<!-- The Following entry is a time stamp of the last bot update. It is typically hidden data -->
| DateOfBotUpdate = ~~~~~
| Function = {{GNF_GO|id=GO:0005179 |text = hormone activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0008083 |text = growth factor activity}}
| Component = {{GNF_GO|id=GO:0005576 |text = extracellular region}} {{GNF_GO|id=GO:0005615 |text = extracellular space}}
| Process = {{GNF_GO|id=GO:0006006 |text = glucose metabolic process}} {{GNF_GO|id=GO:0006112 |text = energy reserve metabolic process}} {{GNF_GO|id=GO:0006629 |text = lipid metabolic process}} {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0007267 |text = cell-cell signaling}} {{GNF_GO|id=GO:0008206 |text = bile acid metabolic process}} {{GNF_GO|id=GO:0008343 |text = adult feeding behavior}} {{GNF_GO|id=GO:0030300 |text = regulation of cholesterol absorption}} {{GNF_GO|id=GO:0032099 |text = negative regulation of appetite}} {{GNF_GO|id=GO:0042755 |text = eating behavior}} {{GNF_GO|id=GO:0045639 |text = positive regulation of myeloid cell differentiation}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 3952
| Hs_Ensembl = ENSG00000174697
| Hs_RefseqProtein = NP_000221
| Hs_RefseqmRNA = NM_000230
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 7
| Hs_GenLoc_start = 127668567
| Hs_GenLoc_end = 127684917
| Hs_Uniprot = P41159
| Mm_EntrezGene = 16846
| Mm_Ensembl = ENSMUSG00000059201
| Mm_RefseqmRNA = NM_008493
| Mm_RefseqProtein = NP_032519
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 6
| Mm_GenLoc_start = 29010231
| Mm_GenLoc_end = 29023886
| Mm_Uniprot = Q544U0
}}
}}
'''Leptin (obesity homolog, mouse)''', also known as '''LEP''', is a human [[gene]].
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = This gene is similar to the mouse obesity gene (ob). The protein encoded by this gene is secreted by white adipocytes. In the mouse study, mutations in this gene are linked to severe and morbid obesity.<ref>{{cite web | title = Entrez Gene: LEP leptin (obesity homolog, mouse)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3952| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Friedman JM, Halaas JL |title=Leptin and the regulation of body weight in mammals. |journal=Nature |volume=395 |issue= 6704 |pages= 763-70 |year= 1998 |pmid= 9796811 |doi= 10.1038/27376 }}
*{{cite journal | author=Prolo P, Wong ML, Licinio J |title=Leptin. |journal=Int. J. Biochem. Cell Biol. |volume=30 |issue= 12 |pages= 1285-90 |year= 1999 |pmid= 9924798 |doi= }}
*{{cite journal | author=Heshka JT, Jones PJ |title=A role for dietary fat in leptin receptor, OB-Rb, function. |journal=Life Sci. |volume=69 |issue= 9 |pages= 987-1003 |year= 2001 |pmid= 11508653 |doi= }}
*{{cite journal | author=Janeckova R |title=The role of leptin in human physiology and pathophysiology. |journal=Physiological research / Academia Scientiarum Bohemoslovaca |volume=50 |issue= 5 |pages= 443-59 |year= 2002 |pmid= 11702849 |doi= }}
*{{cite journal | author=Lee DW, Leinung MC, Rozhavskaya-Arena M, Grasso P |title=Leptin and the treatment of obesity: its current status. |journal=Eur. J. Pharmacol. |volume=440 |issue= 2-3 |pages= 129-39 |year= 2002 |pmid= 12007531 |doi= }}
*{{cite journal | author=Al-Daghri N, Bartlett WA, Jones AF, Kumar S |title=Role of leptin in glucose metabolism in type 2 diabetes. |journal=Diabetes, obesity & metabolism |volume=4 |issue= 3 |pages= 147-55 |year= 2002 |pmid= 12047393 |doi= }}
*{{cite journal | author=Sabath Silva EF |title=[Leptin] |journal=Rev. Invest. Clin. |volume=54 |issue= 2 |pages= 161-5 |year= 2002 |pmid= 12053815 |doi= }}
*{{cite journal | author=Thomas T, Burguera B |title=Is leptin the link between fat and bone mass? |journal=J. Bone Miner. Res. |volume=17 |issue= 9 |pages= 1563-9 |year= 2003 |pmid= 12211425 |doi= }}
*{{cite journal | author=Kraemer RR, Chu H, Castracane VD |title=Leptin and exercise. |journal=Exp. Biol. Med. (Maywood) |volume=227 |issue= 9 |pages= 701-8 |year= 2002 |pmid= 12324651 |doi= }}
*{{cite journal | author=Waelput W, Brouckaert P, Broekaert D, Tavernier J |title=A role for leptin in the systemic inflammatory response syndrome (SIRS) and in immune response. |journal=Current drug targets. Inflammation and allergy |volume=1 |issue= 3 |pages= 277-89 |year= 2003 |pmid= 14561193 |doi= }}
*{{cite journal | author=Stenvinkel P, Pecoits-Filho R, Lindholm B |title=Leptin, ghrelin, and proinflammatory cytokines: compounds with nutritional impact in chronic kidney disease? |journal=Advances in renal replacement therapy |volume=10 |issue= 4 |pages= 332-45 |year= 2004 |pmid= 14681862 |doi= }}
*{{cite journal | author=Cohen P, Ntambi JM, Friedman JM |title=Stearoyl-CoA desaturase-1 and the metabolic syndrome. |journal=Curr. Drug Targets Immune Endocr. Metabol. Disord. |volume=3 |issue= 4 |pages= 271-80 |year= 2004 |pmid= 14683458 |doi= }}
*{{cite journal | author=Sahu A |title=Leptin signaling in the hypothalamus: emphasis on energy homeostasis and leptin resistance. |journal=Frontiers in neuroendocrinology |volume=24 |issue= 4 |pages= 225-53 |year= 2004 |pmid= 14726256 |doi= }}
*{{cite journal | author=Elefteriou F, Karsenty G |title=[Bone mass regulation by leptin: a hypothalamic control of bone formation] |journal=Pathol. Biol. |volume=52 |issue= 3 |pages= 148-53 |year= 2004 |pmid= 15063934 |doi= 10.1016/j.patbio.2003.05.006 }}
*{{cite journal | author=Blüher S, Mantzoros CS |title=The role of leptin in regulating neuroendocrine function in humans. |journal=J. Nutr. |volume=134 |issue= 9 |pages= 2469S-2474S |year= 2004 |pmid= 15333744 |doi= }}
*{{cite journal | author=Farooqi S, O'Rahilly S |title=Genetics of obesity in humans. |journal=Endocr. Rev. |volume=27 |issue= 7 |pages= 710-18 |year= 2007 |pmid= 17122358 |doi= 10.1210/er.2006-0040 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on MAPK3... {October 3, 2007 10:36:48 PM PDT}
- AMBIGUITY: Did not locate an acceptable page to update. {October 3, 2007 10:37:34 PM PDT}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Mitogen-activated protein kinase 3
| HGNCid = 6877
| Symbol = MAPK3
| AltSymbols =; ERK1; HS44KDAP; HUMKER1A; MGC20180; P44ERK1; P44MAPK; PRKM3
| OMIM = 601795
| ECnumber =
| Homologene = 55682
| MGIid = 1346859
| GeneAtlas_image1 = PBB_GE_MAPK3_212046_x_at_tn.png
<!-- The Following entry is a time stamp of the last bot update. It is typically hidden data -->
| DateOfBotUpdate = ~~~~~
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0001784 |text = phosphotyrosine binding}} {{GNF_GO|id=GO:0004672 |text = protein kinase activity}} {{GNF_GO|id=GO:0004674 |text = protein serine/threonine kinase activity}} {{GNF_GO|id=GO:0004707 |text = MAP kinase activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0005524 |text = ATP binding}} {{GNF_GO|id=GO:0016740 |text = transferase activity}}
| Component = {{GNF_GO|id=GO:0005575 |text = cellular_component}} {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005737 |text = cytoplasm}}
| Process = {{GNF_GO|id=GO:0000074 |text = regulation of progression through cell cycle}} {{GNF_GO|id=GO:0006468 |text = protein amino acid phosphorylation}} {{GNF_GO|id=GO:0006974 |text = response to DNA damage stimulus}} {{GNF_GO|id=GO:0007049 |text = cell cycle}} {{GNF_GO|id=GO:0009887 |text = organ morphogenesis}} {{GNF_GO|id=GO:0019233 |text = sensory perception of pain}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 5595
| Hs_Ensembl = ENSG00000102882
| Hs_RefseqProtein = NP_001035145
| Hs_RefseqmRNA = NM_001040056
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 16
| Hs_GenLoc_start = 30032951
| Hs_GenLoc_end = 30042116
| Hs_Uniprot = P27361
| Mm_EntrezGene = 26417
| Mm_Ensembl = ENSMUSG00000063065
| Mm_RefseqmRNA = NM_011952
| Mm_RefseqProtein = NP_036082
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 7
| Mm_GenLoc_start = 126550780
| Mm_GenLoc_end = 126556964
| Mm_Uniprot = Q63844
}}
}}
'''Mitogen-activated protein kinase 3''', also known as '''MAPK3''', is a human [[gene]].
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = The protein encoded by this gene is a member of the MAP kinase family. MAP kinases, also known as extracellular signal-regulated kinases (ERKs), act in a signaling cascade that regulates various cellular processes such as proliferation, differentiation, and cell cycle progression in response to a variety of extracellular signals. This kinase is activated by upstream kinases, resulting in its translocation to the nucleus where it phosphorylates nuclear targets. Alternatively spliced transcript variants encoding different protein isoforms have been described.<ref>{{cite web | title = Entrez Gene: MAPK3 mitogen-activated protein kinase 3| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5595| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Peruzzi F, Gordon J, Darbinian N, Amini S |title=Tat-induced deregulation of neuronal differentiation and survival by nerve growth factor pathway. |journal=J. Neurovirol. |volume=8 Suppl 2 |issue= |pages= 91-6 |year= 2003 |pmid= 12491158 |doi= 10.1080/13550280290167885 }}
*{{cite journal | author=Meloche S, Pouysségur J |title=The ERK1/2 mitogen-activated protein kinase pathway as a master regulator of the G1- to S-phase transition. |journal=Oncogene |volume=26 |issue= 22 |pages= 3227-39 |year= 2007 |pmid= 17496918 |doi= 10.1038/sj.onc.1210414 }}
*{{cite journal | author=Ruscica M, Dozio E, Motta M, Magni P |title=Modulatory actions of neuropeptide Y on prostate cancer growth: role of MAP kinase/ERK 1/2 activation. |journal=Adv. Exp. Med. Biol. |volume=604 |issue= |pages= 96-100 |year= 2007 |pmid= 17695723 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on MDM2... {October 3, 2007 10:27:53 PM PDT}
- AMBIGUITY: Did not locate an acceptable page to update. {October 3, 2007 10:29:31 PM PDT}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB = {{PDB2|1rv1}}, {{PDB2|1t4e}}, {{PDB2|1t4f}}, {{PDB2|1ycr}}, {{PDB2|1z1m}}, {{PDB2|2axi}}, {{PDB2|2c6a}}, {{PDB2|2c6b}}, {{PDB2|2gv2}}, {{PDB2|2hdp}}
| Name = Mdm2, transformed 3T3 cell double minute 2, p53 binding protein (mouse)
| HGNCid = 6973
| Symbol = MDM2
| AltSymbols =; HDMX; MGC71221; hdm2
| OMIM = 164785
| ECnumber =
| Homologene = 1793
| MGIid = 96952
| GeneAtlas_image1 = PBB_GE_MDM2_205386_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_MDM2_211832_s_at_tn.png
| GeneAtlas_image3 = PBB_GE_MDM2_217373_x_at_tn.png
<!-- The Following entry is a time stamp of the last bot update. It is typically hidden data -->
| DateOfBotUpdate = ~~~~~
| Function = {{GNF_GO|id=GO:0004842 |text = ubiquitin-protein ligase activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0008270 |text = zinc ion binding}} {{GNF_GO|id=GO:0016874 |text = ligase activity}} {{GNF_GO|id=GO:0017163 |text = negative regulator of basal transcription activity}} {{GNF_GO|id=GO:0019899 |text = enzyme binding}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}}
| Component = {{GNF_GO|id=GO:0005622 |text = intracellular}} {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005654 |text = nucleoplasm}} {{GNF_GO|id=GO:0005730 |text = nucleolus}} {{GNF_GO|id=GO:0005737 |text = cytoplasm}}
| Process = {{GNF_GO|id=GO:0000074 |text = regulation of progression through cell cycle}} {{GNF_GO|id=GO:0000122 |text = negative regulation of transcription from RNA polymerase II promoter}} {{GNF_GO|id=GO:0006461 |text = protein complex assembly}} {{GNF_GO|id=GO:0006512 |text = ubiquitin cycle}} {{GNF_GO|id=GO:0007089 |text = traversing start control point of mitotic cell cycle}} {{GNF_GO|id=GO:0008285 |text = negative regulation of cell proliferation}} {{GNF_GO|id=GO:0016567 |text = protein ubiquitination}} {{GNF_GO|id=GO:0042176 |text = regulation of protein catabolic process}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 4193
| Hs_Ensembl = ENSG00000135679
| Hs_RefseqProtein = NP_002383
| Hs_RefseqmRNA = NM_002392
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 12
| Hs_GenLoc_start = 67488247
| Hs_GenLoc_end = 67520481
| Hs_Uniprot = Q00987
| Mm_EntrezGene = 17246
| Mm_Ensembl = ENSMUSG00000020184
| Mm_RefseqmRNA = NM_010786
| Mm_RefseqProtein = NP_034916
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 10
| Mm_GenLoc_start = 117091888
| Mm_GenLoc_end = 117113704
| Mm_Uniprot = Q2L9A9
}}
}}
'''Mdm2, transformed 3T3 cell double minute 2, p53 binding protein (mouse)''', also known as '''MDM2''', is a human [[gene]].
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = This gene is a target gene of the transcription factor tumor protein p53. The encoded protein is a nuclear phosphoprotein that binds and inhibits transactivation by tumor protein p53, as part of an autoregulatory negative feedback loop. Overexpression of this gene can result in excessive inactivation of tumor protein p53, diminishing its tumor suppressor function. This protein has E3 ubiquitin ligase activity, which targets tumor protein p53 for proteasomal degradation. This protein also affects the cell cycle, apoptosis, and tumorigenesis through interactions with other proteins, including retinoblastoma 1 and ribosomal protein L5. More than 40 different alternatively spliced transcript variants have been isolated from both tumor and normal tissues.<ref>{{cite web | title = Entrez Gene: MDM2 Mdm2, transformed 3T3 cell double minute 2, p53 binding protein (mouse)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4193| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Momand J, Wu HH, Dasgupta G |title=MDM2--master regulator of the p53 tumor suppressor protein. |journal=Gene |volume=242 |issue= 1-2 |pages= 15-29 |year= 2000 |pmid= 10721693 |doi= }}
*{{cite journal | author=Deb SP |title=Function and dysfunction of the human oncoprotein MDM2. |journal=Front. Biosci. |volume=7 |issue= |pages= d235-43 |year= 2002 |pmid= 11779693 |doi= }}
*{{cite journal | author=Alarcon-Vargas D, Ronai Z |title=p53-Mdm2--the affair that never ends. |journal=Carcinogenesis |volume=23 |issue= 4 |pages= 541-7 |year= 2002 |pmid= 11960904 |doi= }}
*{{cite journal | author=Bartel F, Taubert H, Harris LC |title=Alternative and aberrant splicing of MDM2 mRNA in human cancer. |journal=Cancer Cell |volume=2 |issue= 1 |pages= 9-15 |year= 2003 |pmid= 12150820 |doi= }}
*{{cite journal | author=Michael D, Oren M |title=The p53-Mdm2 module and the ubiquitin system. |journal=Semin. Cancer Biol. |volume=13 |issue= 1 |pages= 49-58 |year= 2003 |pmid= 12507556 |doi= }}
*{{cite journal | author=Vargas DA, Takahashi S, Ronai Z |title=Mdm2: A regulator of cell growth and death. |journal=Adv. Cancer Res. |volume=89 |issue= |pages= 1-34 |year= 2003 |pmid= 14587869 |doi= }}
*{{cite journal | author=Bartel F, Harris LC, Würl P, Taubert H |title=MDM2 and its splice variant messenger RNAs: expression in tumors and down-regulation using antisense oligonucleotides. |journal=Mol. Cancer Res. |volume=2 |issue= 1 |pages= 29-35 |year= 2004 |pmid= 14757843 |doi= }}
*{{cite journal | author=Jain S, Khuri FR, Shin DM |title=Prevention of head and neck cancer: current status and future prospects. |journal=Current problems in cancer |volume=28 |issue= 5 |pages= 265-86 |year= 2004 |pmid= 15375804 |doi= }}
*{{cite journal | author=Bond GL, Hu W, Levine AJ |title=MDM2 is a central node in the p53 pathway: 12 years and counting. |journal=Current cancer drug targets |volume=5 |issue= 1 |pages= 3-8 |year= 2005 |pmid= 15720184 |doi= }}
*{{cite journal | author=Zhang Z, Zhang R |title=p53-independent activities of MDM2 and their relevance to cancer therapy. |journal=Current cancer drug targets |volume=5 |issue= 1 |pages= 9-20 |year= 2005 |pmid= 15720185 |doi= }}
*{{cite journal | author=Harris LC |title=MDM2 splice variants and their therapeutic implications. |journal=Current cancer drug targets |volume=5 |issue= 1 |pages= 21-6 |year= 2005 |pmid= 15720186 |doi= }}
*{{cite journal | author=Rayburn E, Zhang R, He J, Wang H |title=MDM2 and human malignancies: expression, clinical pathology, prognostic markers, and implications for chemotherapy. |journal=Current cancer drug targets |volume=5 |issue= 1 |pages= 27-41 |year= 2005 |pmid= 15720187 |doi= }}
*{{cite journal | author=Meulmeester E, Pereg Y, Shiloh Y, Jochemsen AG |title=ATM-mediated phosphorylations inhibit Mdmx/Mdm2 stabilization by HAUSP in favor of p53 activation. |journal=Cell Cycle |volume=4 |issue= 9 |pages= 1166-70 |year= 2006 |pmid= 16082221 |doi= }}
*{{cite journal | author=Zhang Z, Wang H, Li M, ''et al.'' |title=Novel MDM2 p53-independent functions identified through RNA silencing technologies. |journal=Ann. N. Y. Acad. Sci. |volume=1058 |issue= |pages= 205-14 |year= 2006 |pmid= 16394138 |doi= 10.1196/annals.1359.030 }}
*{{cite journal | author=Harms KL, Chen X |title=p19ras brings a new twist to the regulation of p73 by Mdm2. |journal=Sci. STKE |volume=2006 |issue= 337 |pages= pe24 |year= 2006 |pmid= 16738062 |doi= 10.1126/stke.3372006pe24 }}
*{{cite journal | author=Gilkes DM, Chen J |title=Distinct roles of MDMX in the regulation of p53 response to ribosomal stress. |journal=Cell Cycle |volume=6 |issue= 2 |pages= 151-5 |year= 2007 |pmid= 17327702 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on MMP2... {October 3, 2007 10:29:32 PM PDT}
- AMBIGUITY: Did not locate an acceptable page to update. {October 3, 2007 10:32:30 PM PDT}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB = {{PDB2|1ck7}}, {{PDB2|1cxw}}, {{PDB2|1eak}}, {{PDB2|1gen}}, {{PDB2|1gxd}}, {{PDB2|1j7m}}, {{PDB2|1ks0}}, {{PDB2|1rtg}}
| Name = Matrix metallopeptidase 2 (gelatinase A, 72kDa gelatinase, 72kDa type IV collagenase)
| HGNCid = 7166
| Symbol = MMP2
| AltSymbols =; CLG4; CLG4A; MMP-II; MONA; TBE-1
| OMIM = 120360
| ECnumber =
| Homologene = 3329
| MGIid = 97009
| GeneAtlas_image1 = PBB_GE_MMP2_201069_at_tn.png
<!-- The Following entry is a time stamp of the last bot update. It is typically hidden data -->
| DateOfBotUpdate = ~~~~~
| Function = {{GNF_GO|id=GO:0004228 |text = gelatinase A activity}} {{GNF_GO|id=GO:0005509 |text = calcium ion binding}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0008270 |text = zinc ion binding}}
| Component = {{GNF_GO|id=GO:0005578 |text = proteinaceous extracellular matrix}} {{GNF_GO|id=GO:0005615 |text = extracellular space}}
| Process = {{GNF_GO|id=GO:0000270 |text = peptidoglycan metabolic process}} {{GNF_GO|id=GO:0001955 |text = blood vessel maturation}} {{GNF_GO|id=GO:0006508 |text = proteolysis}} {{GNF_GO|id=GO:0030574 |text = collagen catabolic process}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 4313
| Hs_Ensembl = ENSG00000087245
| Hs_RefseqProtein = NP_004521
| Hs_RefseqmRNA = NM_004530
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 16
| Hs_GenLoc_start = 54070589
| Hs_GenLoc_end = 54098101
| Hs_Uniprot = P08253
| Mm_EntrezGene = 17390
| Mm_Ensembl = ENSMUSG00000031740
| Mm_RefseqmRNA = NM_008610
| Mm_RefseqProtein = NP_032636
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 8
| Mm_GenLoc_start = 95716456
| Mm_GenLoc_end = 95742548
| Mm_Uniprot = Q3UG07
}}
}}
'''Matrix metallopeptidase 2 (gelatinase A, 72kDa gelatinase, 72kDa type IV collagenase)''', also known as '''MMP2''', is a human [[gene]].
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = Proteins of the matrix metalloproteinase (MMP) family are involved in the breakdown of extracellular matrix in normal physiological processes, such as embryonic development, reproduction, and tissue remodeling, as well as in disease processes, such as arthritis and metastasis. Most MMP's are secreted as inactive proproteins which are activated when cleaved by extracellular proteinases. This gene encodes an enzyme which degrades type IV collagen, the major structural component of basement membranes. The enzyme plays a role in endometrial menstrual breakdown, regulation of vascularization and the inflammatory response. Mutations in this gene have been associated with Winchester syndrome and Nodulosis-Arthropathy-Osteolysis (NAO) syndrome.<ref>{{cite web | title = Entrez Gene: MMP2 matrix metallopeptidase 2 (gelatinase A, 72kDa gelatinase, 72kDa type IV collagenase)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4313| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Massova I, Kotra LP, Fridman R, Mobashery S |title=Matrix metalloproteinases: structures, evolution, and diversification. |journal=FASEB J. |volume=12 |issue= 12 |pages= 1075-95 |year= 1998 |pmid= 9737711 |doi= }}
*{{cite journal | author=Nagase H, Woessner JF |title=Matrix metalloproteinases. |journal=J. Biol. Chem. |volume=274 |issue= 31 |pages= 21491-4 |year= 1999 |pmid= 10419448 |doi= }}
*{{cite journal | author=Goffin F, Frankenne F, Béliard A, ''et al.'' |title=Human endometrial epithelial cells modulate the activation of gelatinase a by stromal cells. |journal=Gynecol. Obstet. Invest. |volume=53 |issue= 2 |pages= 105-11 |year= 2002 |pmid= 11961384 |doi= }}
*{{cite journal | author=Hrabec E, Naduk J, Strek M, Hrabec Z |title=[Type IV collagenases (MMP-2 and MMP-9) and their substrates--intracellular proteins, hormones, cytokines, chemokines and their receptors] |journal=Postepy Biochem. |volume=53 |issue= 1 |pages= 37-45 |year= 2007 |pmid= 17718386 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on MYC... {October 3, 2007 10:32:30 PM PDT}
- AMBIGUITY: Did not locate an acceptable page to update. {October 3, 2007 10:32:42 PM PDT}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB = {{PDB2|1nkp}}
| Name = V-myc myelocytomatosis viral oncogene homolog (avian)
| HGNCid = 7553
| Symbol = MYC
| AltSymbols =; c-Myc
| OMIM = 190080
| ECnumber =
| Homologene = 31092
| MGIid = 97250
<!-- The Following entry is a time stamp of the last bot update. It is typically hidden data -->
| DateOfBotUpdate = ~~~~~
| Function = {{GNF_GO|id=GO:0003700 |text = transcription factor activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005819 |text = spindle}}
| Process = {{GNF_GO|id=GO:0001836 |text = release of cytochrome c from mitochondria}} {{GNF_GO|id=GO:0006309 |text = DNA fragmentation during apoptosis}} {{GNF_GO|id=GO:0006355 |text = regulation of transcription, DNA-dependent}} {{GNF_GO|id=GO:0006357 |text = regulation of transcription from RNA polymerase II promoter}} {{GNF_GO|id=GO:0006879 |text = cellular iron ion homeostasis}} {{GNF_GO|id=GO:0006919 |text = caspase activation}} {{GNF_GO|id=GO:0007050 |text = cell cycle arrest}} {{GNF_GO|id=GO:0008284 |text = positive regulation of cell proliferation}} {{GNF_GO|id=GO:0008629 |text = induction of apoptosis by intracellular signals}} {{GNF_GO|id=GO:0008633 |text = activation of pro-apoptotic gene products}} {{GNF_GO|id=GO:0008634 |text = negative regulation of survival gene product activity}} {{GNF_GO|id=GO:0009314 |text = response to radiation}} {{GNF_GO|id=GO:0042981 |text = regulation of apoptosis}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 4609
| Hs_Ensembl =
| Hs_RefseqProtein = XP_001129632
| Hs_RefseqmRNA = XM_001129632
| Hs_GenLoc_db =
| Hs_GenLoc_chr =
| Hs_GenLoc_start =
| Hs_GenLoc_end =
| Hs_Uniprot =
| Mm_EntrezGene = 17869
| Mm_Ensembl = ENSMUSG00000022346
| Mm_RefseqmRNA = NM_010849
| Mm_RefseqProtein = NP_034979
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 15
| Mm_GenLoc_start = 61815052
| Mm_GenLoc_end = 61820027
| Mm_Uniprot = O88594
}}
}}
'''V-myc myelocytomatosis viral oncogene homolog (avian)''', also known as '''MYC''', is a human [[gene]].
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = The protein encoded by this gene is a multifunctional, nuclear phosphoprotein that plays a role in cell cycle progression, apoptosis and cellular transformation. It functions as a transcription factor that regulates transcription of specific target genes. Mutations, overexpression, rearrangement and translocation of this gene have been associated with a variety of hematopoietic tumors, leukemias and lymphomas, including Burkitt lymphoma. There is evidence to show that alternative translation initiations from an upstream, in-frame non-AUG (CUG) and a downstream AUG start site result in the production of two isoforms with distinct N-termini. The synthesis of non-AUG initiated protein is suppressed in Burkitt's lymphomas, suggesting its importance in the normal function of this gene.<ref>{{cite web | title = Entrez Gene: MYC v-myc myelocytomatosis viral oncogene homolog (avian)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4609| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Ruf IK, Rhyne PW, Yang H, ''et al.'' |title=EBV regulates c-MYC, apoptosis, and tumorigenicity in Burkitt's lymphoma. |journal=Curr. Top. Microbiol. Immunol. |volume=258 |issue= |pages= 153-60 |year= 2002 |pmid= 11443860 |doi= }}
*{{cite journal | author=Lüscher B |title=Function and regulation of the transcription factors of the Myc/Max/Mad network. |journal=Gene |volume=277 |issue= 1-2 |pages= 1-14 |year= 2001 |pmid= 11602341 |doi= }}
*{{cite journal | author=Hoffman B, Amanullah A, Shafarenko M, Liebermann DA |title=The proto-oncogene c-myc in hematopoietic development and leukemogenesis. |journal=Oncogene |volume=21 |issue= 21 |pages= 3414-21 |year= 2002 |pmid= 12032779 |doi= 10.1038/sj.onc.1205400 }}
*{{cite journal | author=Pelengaris S, Khan M, Evan G |title=c-MYC: more than just a matter of life and death. |journal=Nat. Rev. Cancer |volume=2 |issue= 10 |pages= 764-76 |year= 2002 |pmid= 12360279 |doi= 10.1038/nrc904 }}
*{{cite journal | author=Nilsson JA, Cleveland JL |title=Myc pathways provoking cell suicide and cancer. |journal=Oncogene |volume=22 |issue= 56 |pages= 9007-21 |year= 2004 |pmid= 14663479 |doi= 10.1038/sj.onc.1207261 }}
*{{cite journal | author=Dang CV, O'donnell KA, Juopperi T |title=The great MYC escape in tumorigenesis. |journal=Cancer Cell |volume=8 |issue= 3 |pages= 177-8 |year= 2005 |pmid= 16169462 |doi= 10.1016/j.ccr.2005.08.005 }}
*{{cite journal | author=Dang CV, Li F, Lee LA |title=Could MYC induction of mitochondrial biogenesis be linked to ROS production and genomic instability? |journal=Cell Cycle |volume=4 |issue= 11 |pages= 1465-6 |year= 2007 |pmid= 16205115 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on NOS3... {October 3, 2007 10:32:42 PM PDT}
- AMBIGUITY: Did not locate an acceptable page to update. {October 3, 2007 10:33:34 PM PDT}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB = {{PDB2|1d0c}}, {{PDB2|1d0o}}, {{PDB2|1d1v}}, {{PDB2|1d1w}}, {{PDB2|1d1x}}, {{PDB2|1d1y}}, {{PDB2|1dm6}}, {{PDB2|1dm7}}, {{PDB2|1dm8}}, {{PDB2|1dmi}}, {{PDB2|1dmj}}, {{PDB2|1dmk}}, {{PDB2|1ed4}}, {{PDB2|1ed5}}, {{PDB2|1ed6}}, {{PDB2|1foi}}, {{PDB2|1foj}}, {{PDB2|1fol}}, {{PDB2|1foo}}, {{PDB2|1fop}}, {{PDB2|1i83}}, {{PDB2|1m9j}}, {{PDB2|1m9k}}, {{PDB2|1m9m}}, {{PDB2|1m9q}}, {{PDB2|1m9r}}, {{PDB2|1nse}}, {{PDB2|1p6l}}, {{PDB2|1p6m}}, {{PDB2|1p6n}}, {{PDB2|1q2o}}, {{PDB2|1rs8}}, {{PDB2|1rs9}}, {{PDB2|1zzs}}, {{PDB2|1zzt}}, {{PDB2|2g6o}}, {{PDB2|2hx2}}, {{PDB2|2nse}}, {{PDB2|3nos}}, {{PDB2|3nse}}, {{PDB2|4nse}}, {{PDB2|5nse}}, {{PDB2|6nse}}, {{PDB2|7nse}}, {{PDB2|8nse}}, {{PDB2|9nse}}
| Name = Nitric oxide synthase 3 (endothelial cell)
| HGNCid = 7876
| Symbol = NOS3
| AltSymbols =; ECNOS; NOS III; eNOS
| OMIM = 163729
| ECnumber =
| Homologene = 504
| MGIid = 97362
| GeneAtlas_image1 = PBB_GE_NOS3_205581_s_at_tn.png
<!-- The Following entry is a time stamp of the last bot update. It is typically hidden data -->
| DateOfBotUpdate = ~~~~~
| Function = {{GNF_GO|id=GO:0004517 |text = nitric-oxide synthase activity}} {{GNF_GO|id=GO:0005506 |text = iron ion binding}} {{GNF_GO|id=GO:0005509 |text = calcium ion binding}} {{GNF_GO|id=GO:0005516 |text = calmodulin binding}} {{GNF_GO|id=GO:0008270 |text = zinc ion binding}} {{GNF_GO|id=GO:0009055 |text = electron carrier activity}} {{GNF_GO|id=GO:0010181 |text = FMN binding}} {{GNF_GO|id=GO:0020037 |text = heme binding}} {{GNF_GO|id=GO:0050660 |text = FAD binding}} {{GNF_GO|id=GO:0050661 |text = NADP binding}}
| Component = {{GNF_GO|id=GO:0005737 |text = cytoplasm}}
| Process = {{GNF_GO|id=GO:0001542 |text = ovulation (sensu Mammalia)}} {{GNF_GO|id=GO:0006118 |text = electron transport}} {{GNF_GO|id=GO:0006520 |text = amino acid metabolic process}} {{GNF_GO|id=GO:0006809 |text = nitric oxide biosynthetic process}} {{GNF_GO|id=GO:0006928 |text = cell motility}} {{GNF_GO|id=GO:0007612 |text = learning}} {{GNF_GO|id=GO:0031663 |text = lipopolysaccharide-mediated signaling pathway}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 4846
| Hs_Ensembl = ENSG00000164867
| Hs_RefseqProtein = NP_000594
| Hs_RefseqmRNA = NM_000603
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 7
| Hs_GenLoc_start = 150319080
| Hs_GenLoc_end = 150342608
| Hs_Uniprot = P29474
| Mm_EntrezGene = 18127
| Mm_Ensembl = ENSMUSG00000028978
| Mm_RefseqmRNA = NM_008713
| Mm_RefseqProtein = NP_032739
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 5
| Mm_GenLoc_start = 23874884
| Mm_GenLoc_end = 23894536
| Mm_Uniprot = Q7TSV7
}}
}}
'''Nitric oxide synthase 3 (endothelial cell)''', also known as '''NOS3''', is a human [[gene]].
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text =
}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=de la Monte SM, Lu BX, Sohn YK, ''et al.'' |title=Aberrant expression of nitric oxide synthase III in Alzheimer's disease: relevance to cerebral vasculopathy and neurodegeneration. |journal=Neurobiol. Aging |volume=21 |issue= 2 |pages= 309-19 |year= 2000 |pmid= 10867216 |doi= }}
*{{cite journal | author=Shaul PW |title=Regulation of endothelial nitric oxide synthase: location, location, location. |journal=Annu. Rev. Physiol. |volume=64 |issue= |pages= 749-74 |year= 2002 |pmid= 11826287 |doi= 10.1146/annurev.physiol.64.081501.155952 }}
*{{cite journal | author=Wu KK |title=Regulation of endothelial nitric oxide synthase activity and gene expression. |journal=Ann. N. Y. Acad. Sci. |volume=962 |issue= |pages= 122-30 |year= 2002 |pmid= 12076969 |doi= }}
*{{cite journal | author=Alp NJ, Channon KM |title=Regulation of endothelial nitric oxide synthase by tetrahydrobiopterin in vascular disease. |journal=Arterioscler. Thromb. Vasc. Biol. |volume=24 |issue= 3 |pages= 413-20 |year= 2005 |pmid= 14656731 |doi= 10.1161/01.ATV.0000110785.96039.f6 }}
*{{cite journal | author=Tai SC, Robb GB, Marsden PA |title=Endothelial nitric oxide synthase: a new paradigm for gene regulation in the injured blood vessel. |journal=Arterioscler. Thromb. Vasc. Biol. |volume=24 |issue= 3 |pages= 405-12 |year= 2005 |pmid= 14656742 |doi= 10.1161/01.ATV.0000109171.50229.33 }}
*{{cite journal | author=Kawashima S, Yokoyama M |title=Dysfunction of endothelial nitric oxide synthase and atherosclerosis. |journal=Arterioscler. Thromb. Vasc. Biol. |volume=24 |issue= 6 |pages= 998-1005 |year= 2004 |pmid= 15001455 |doi= 10.1161/01.ATV.0000125114.88079.96 }}
*{{cite journal | author=Duda DG, Fukumura D, Jain RK |title=Role of eNOS in neovascularization: NO for endothelial progenitor cells. |journal=Trends in molecular medicine |volume=10 |issue= 4 |pages= 143-5 |year= 2004 |pmid= 15162796 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on NR3C1... {October 3, 2007 10:16:27 PM PDT}
- AMBIGUITY: Did not locate an acceptable page to update. {October 3, 2007 10:18:02 PM PDT}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB = {{PDB2|1gdc}}, {{PDB2|1glu}}, {{PDB2|1m2z}}, {{PDB2|1nhz}}, {{PDB2|1p93}}, {{PDB2|1r4o}}, {{PDB2|1r4r}}, {{PDB2|1rgd}}, {{PDB2|2gda}}
| Name = Nuclear receptor subfamily 3, group C, member 1 (glucocorticoid receptor)
| HGNCid = 7978
| Symbol = NR3C1
| AltSymbols =; GCCR; GCR; GR; GRL
| OMIM = 138040
| ECnumber =
| Homologene = 30960
| MGIid = 95824
| GeneAtlas_image1 = PBB_GE_NR3C1_216321_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_NR3C1_201865_x_at_tn.png
| GeneAtlas_image3 = PBB_GE_NR3C1_201866_s_at_tn.png
<!-- The Following entry is a time stamp of the last bot update. It is typically hidden data -->
| DateOfBotUpdate = ~~~~~
| Function = {{GNF_GO|id=GO:0003700 |text = transcription factor activity}} {{GNF_GO|id=GO:0004883 |text = glucocorticoid receptor activity}} {{GNF_GO|id=GO:0005496 |text = steroid binding}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0008270 |text = zinc ion binding}} {{GNF_GO|id=GO:0008289 |text = lipid binding}} {{GNF_GO|id=GO:0043565 |text = sequence-specific DNA binding}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005737 |text = cytoplasm}} {{GNF_GO|id=GO:0005759 |text = mitochondrial matrix}}
| Process = {{GNF_GO|id=GO:0006355 |text = regulation of transcription, DNA-dependent}} {{GNF_GO|id=GO:0006366 |text = transcription from RNA polymerase II promoter}} {{GNF_GO|id=GO:0006954 |text = inflammatory response}} {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0007530 |text = sex determination}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 2908
| Hs_Ensembl = ENSG00000113580
| Hs_RefseqProtein = NP_000167
| Hs_RefseqmRNA = NM_000176
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 5
| Hs_GenLoc_start = 142637689
| Hs_GenLoc_end = 142795270
| Hs_Uniprot = P04150
| Mm_EntrezGene = 14815
| Mm_Ensembl = ENSMUSG00000024431
| Mm_RefseqmRNA = NM_008173
| Mm_RefseqProtein = NP_032199
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 18
| Mm_GenLoc_start = 39537961
| Mm_GenLoc_end = 39615759
| Mm_Uniprot = Q05DD1
}}
}}
'''Nuclear receptor subfamily 3, group C, member 1 (glucocorticoid receptor)''', also known as '''NR3C1''', is a human [[gene]].
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = The protein encoded by this gene is a receptor for glucocorticoids that can act as both a transcription factor and as a regulator of other transcription factors. This protein can also be found in heteromeric cytoplasmic complexes along with heat shock factors and immunophilins. The protein is typically found in the cytoplasm until it binds a ligand, which induces transport into the nucleus. Mutations in this gene are a cause of glucocorticoid resistance, or cortisol, resistance. Alternate splicing, the use of at least three different promoters, and alternate translation initiation sites result in several transcript variants encoding the same protein or different isoforms, but the full-length nature of some variants has not been determined.<ref>{{cite web | title = Entrez Gene: NR3C1 nuclear receptor subfamily 3, group C, member 1 (glucocorticoid receptor)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2908| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Adcock IM, Ito K |title=Molecular mechanisms of corticosteroid actions. |journal=Monaldi archives for chest disease = Archivio Monaldi per le malattie del torace / Fondazione clinica del lavoro, IRCCS [and] Istituto di clinica tisiologica e malattie apparato respiratorio, Università di Napoli, Secondo ateneo |volume=55 |issue= 3 |pages= 256-66 |year= 2000 |pmid= 10948677 |doi= }}
*{{cite journal | author=Chikanza IC |title=Mechanisms of corticosteroid resistance in rheumatoid arthritis: a putative role for the corticosteroid receptor beta isoform. |journal=Ann. N. Y. Acad. Sci. |volume=966 |issue= |pages= 39-48 |year= 2002 |pmid= 12114257 |doi= }}
*{{cite journal | author=Neeck G, Kluter A, Dotzlaw H, Eggert M |title=Involvement of the glucocorticoid receptor in the pathogenesis of rheumatoid arthritis. |journal=Ann. N. Y. Acad. Sci. |volume=966 |issue= |pages= 491-5 |year= 2002 |pmid= 12114309 |doi= }}
*{{cite journal | author=Yudt MR, Cidlowski JA |title=The glucocorticoid receptor: coding a diversity of proteins and responses through a single gene. |journal=Mol. Endocrinol. |volume=16 |issue= 8 |pages= 1719-26 |year= 2003 |pmid= 12145329 |doi= }}
*{{cite journal | author=Torrego A, Pujols L, Picado C |title=[Response to glucocorticoid treatment in asthma. The role of alpha and beta isoforms of the glucocorticoid receptor] |journal=Arch. Bronconeumol. |volume=38 |issue= 9 |pages= 436-40 |year= 2003 |pmid= 12237016 |doi= }}
*{{cite journal | author=Bray PJ, Cotton RG |title=Variations of the human glucocorticoid receptor gene (NR3C1): pathological and in vitro mutations and polymorphisms. |journal=Hum. Mutat. |volume=21 |issue= 6 |pages= 557-68 |year= 2003 |pmid= 12754700 |doi= 10.1002/humu.10213 }}
*{{cite journal | author=Kino T, Pavlakis GN |title=Partner molecules of accessory protein Vpr of the human immunodeficiency virus type 1. |journal=DNA Cell Biol. |volume=23 |issue= 4 |pages= 193-205 |year= 2004 |pmid= 15142377 |doi= 10.1089/104454904773819789 }}
*{{cite journal | author=Lu NZ, Cidlowski JA |title=The origin and functions of multiple human glucocorticoid receptor isoforms. |journal=Ann. N. Y. Acad. Sci. |volume=1024 |issue= |pages= 102-23 |year= 2004 |pmid= 15265776 |doi= 10.1196/annals.1321.008 }}
*{{cite journal | author=Kino T, Chrousos GP |title=Human immunodeficiency virus type-1 accessory protein Vpr: a causative agent of the AIDS-related insulin resistance/lipodystrophy syndrome? |journal=Ann. N. Y. Acad. Sci. |volume=1024 |issue= |pages= 153-67 |year= 2004 |pmid= 15265780 |doi= 10.1196/annals.1321.013 }}
*{{cite journal | author=Andersen JL, Planelles V |title=The role of Vpr in HIV-1 pathogenesis. |journal=Curr. HIV Res. |volume=3 |issue= 1 |pages= 43-51 |year= 2005 |pmid= 15638722 |doi= }}
*{{cite journal | author=Le Rouzic E, Benichou S |title=The Vpr protein from HIV-1: distinct roles along the viral life cycle. |journal=Retrovirology |volume=2 |issue= |pages= 11 |year= 2006 |pmid= 15725353 |doi= 10.1186/1742-4690-2-11 }}
*{{cite journal | author=Muthumani K, Choo AY, Premkumar A, ''et al.'' |title=Human immunodeficiency virus type 1 (HIV-1) Vpr-regulated cell death: insights into mechanism. |journal=Cell Death Differ. |volume=12 Suppl 1 |issue= |pages= 962-70 |year= 2006 |pmid= 15832179 |doi= 10.1038/sj.cdd.4401583 }}
*{{cite journal | author=Zhou J, Cidlowski JA |title=The human glucocorticoid receptor: one gene, multiple proteins and diverse responses. |journal=Steroids |volume=70 |issue= 5-7 |pages= 407-17 |year= 2005 |pmid= 15862824 |doi= 10.1016/j.steroids.2005.02.006 }}
*{{cite journal | author=Chrousos GP, Kino T |title=Intracellular glucocorticoid signaling: a formerly simple system turns stochastic. |journal=Sci. STKE |volume=2005 |issue= 304 |pages= pe48 |year= 2006 |pmid= 16204701 |doi= 10.1126/stke.3042005pe48 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on PRKACA... {October 3, 2007 10:35:54 PM PDT}
- AMBIGUITY: Did not locate an acceptable page to update. {October 3, 2007 10:36:12 PM PDT}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB = {{PDB2|1apm}}, {{PDB2|1atp}}, {{PDB2|1bkx}}, {{PDB2|1bx6}}, {{PDB2|1cdk}}, {{PDB2|1cmk}}, {{PDB2|1ctp}}, {{PDB2|1fmo}}, {{PDB2|1j3h}}, {{PDB2|1jbp}}, {{PDB2|1jlu}}, {{PDB2|1l3r}}, {{PDB2|1q24}}, {{PDB2|1q61}}, {{PDB2|1q62}}, {{PDB2|1q8t}}, {{PDB2|1q8u}}, {{PDB2|1q8w}}, {{PDB2|1rdq}}, {{PDB2|1re8}}, {{PDB2|1rej}}, {{PDB2|1rek}}, {{PDB2|1smh}}, {{PDB2|1stc}}, {{PDB2|1sve}}, {{PDB2|1svg}}, {{PDB2|1svh}}, {{PDB2|1syk}}, {{PDB2|1szm}}, {{PDB2|1u7e}}, {{PDB2|1veb}}, {{PDB2|1xh4}}, {{PDB2|1xh5}}, {{PDB2|1xh6}}, {{PDB2|1xh7}}, {{PDB2|1xh8}}, {{PDB2|1xh9}}, {{PDB2|1xha}}, {{PDB2|1ydr}}, {{PDB2|1yds}}, {{PDB2|1ydt}}, {{PDB2|2c1a}}, {{PDB2|2c1b}}, {{PDB2|2cpk}}, {{PDB2|2erz}}, {{PDB2|2f7e}}, {{PDB2|2f7x}}, {{PDB2|2f7z}}, {{PDB2|2gfc}}, {{PDB2|2gnf}}, {{PDB2|2gng}}, {{PDB2|2gnh}}, {{PDB2|2gni}}, {{PDB2|2gnj}}, {{PDB2|2gnl}}, {{PDB2|2gu8}}, {{PDB2|2jds}}, {{PDB2|2jdt}}, {{PDB2|2jdv}}, {{PDB2|2oh0}}, {{PDB2|2ojf}}, {{PDB2|2uvx}}, {{PDB2|2uvy}}, {{PDB2|2uvz}}, {{PDB2|2uw0}}, {{PDB2|2uw3}}, {{PDB2|2uw4}}, {{PDB2|2uw5}}, {{PDB2|2uw6}}, {{PDB2|2uw7}}, {{PDB2|2uw8}}, {{PDB2|2uzt}}, {{PDB2|2uzu}}, {{PDB2|2uzv}}, {{PDB2|2uzw}}
| Name = Protein kinase, cAMP-dependent, catalytic, alpha
| HGNCid = 9380
| Symbol = PRKACA
| AltSymbols =; MGC102831; MGC48865; PKACA
| OMIM = 601639
| ECnumber =
| Homologene = 68129
| MGIid = 97592
<!-- The Following entry is a time stamp of the last bot update. It is typically hidden data -->
| DateOfBotUpdate = ~~~~~
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0004674 |text = protein serine/threonine kinase activity}} {{GNF_GO|id=GO:0004691 |text = cAMP-dependent protein kinase activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0005524 |text = ATP binding}} {{GNF_GO|id=GO:0016740 |text = transferase activity}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005952 |text = cAMP-dependent protein kinase complex}}
| Process = {{GNF_GO|id=GO:0006468 |text = protein amino acid phosphorylation}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 5566
| Hs_Ensembl =
| Hs_RefseqProtein = NP_002721
| Hs_RefseqmRNA = NM_002730
| Hs_GenLoc_db =
| Hs_GenLoc_chr =
| Hs_GenLoc_start =
| Hs_GenLoc_end =
| Hs_Uniprot =
| Mm_EntrezGene = 18747
| Mm_Ensembl =
| Mm_RefseqmRNA = NM_008854
| Mm_RefseqProtein = NP_032880
| Mm_GenLoc_db =
| Mm_GenLoc_chr =
| Mm_GenLoc_start =
| Mm_GenLoc_end =
| Mm_Uniprot =
}}
}}
'''Protein kinase, cAMP-dependent, catalytic, alpha''', also known as '''PRKACA''', is a human [[gene]].
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = cAMP is a signaling molecule important for a variety of cellular functions. cAMP exerts its effects by activating the cAMP-dependent protein kinase (AMPK), which transduces the signal through phosphorylation of different target proteins. The inactive holoenzyme of AMPK is a tetramer composed of two regulatory and two catalytic subunits. cAMP causes the dissociation of the inactive holoenzyme into a dimer of regulatory subunits bound to four cAMP and two free monomeric catalytic subunits. Four different regulatory subunits and three catalytic subunits of AMPK have been identified in humans. The protein encoded by this gene is a member of the Ser/Thr protein kinase family and is a catalytic subunit of AMPK. Alternatively spliced transcript variants encoding distinct isoforms have been observed.<ref>{{cite web | title = Entrez Gene: PRKACA protein kinase, cAMP-dependent, catalytic, alpha| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5566| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Morishima-Kawashima M, Hasegawa M, Takio K, ''et al.'' |title=Hyperphosphorylation of tau in PHF. |journal=Neurobiol. Aging |volume=16 |issue= 3 |pages= 365-71; discussion 371-80 |year= 1995 |pmid= 7566346 |doi= }}
*{{cite journal | author=Deng X, Kornblau SM, Ruvolo PP, May WS |title=Regulation of Bcl2 phosphorylation and potential significance for leukemic cell chemoresistance. |journal=J. Natl. Cancer Inst. Monographs |volume= |issue= 28 |pages= 30-7 |year= 2003 |pmid= 11158204 |doi= }}
*{{cite journal | author=Ali A, Hoeflich KP, Woodgett JR |title=Glycogen synthase kinase-3: properties, functions, and regulation. |journal=Chem. Rev. |volume=101 |issue= 8 |pages= 2527-40 |year= 2002 |pmid= 11749387 |doi= }}
*{{cite journal | author=Holm C |title=Molecular mechanisms regulating hormone-sensitive lipase and lipolysis. |journal=Biochem. Soc. Trans. |volume=31 |issue= Pt 6 |pages= 1120-4 |year= 2004 |pmid= 14641008 |doi= 10.1042/ }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on PRKCD... {October 3, 2007 10:36:12 PM PDT}
- AMBIGUITY: Did not locate an acceptable page to update. {October 3, 2007 10:36:48 PM PDT}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB = {{PDB2|1bdy}}, {{PDB2|1ptq}}, {{PDB2|1ptr}}, {{PDB2|1yrk}}
| Name = Protein kinase C, delta
| HGNCid = 9399
| Symbol = PRKCD
| AltSymbols =; MAY1; MGC49908; nPKC-delta
| OMIM = 176977
| ECnumber =
| Homologene = 55963
| MGIid = 97598
| GeneAtlas_image1 = PBB_GE_PRKCD_202545_at_tn.png
<!-- The Following entry is a time stamp of the last bot update. It is typically hidden data -->
| DateOfBotUpdate = ~~~~~
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0004674 |text = protein serine/threonine kinase activity}} {{GNF_GO|id=GO:0004701 |text = diacylglycerol-activated phospholipid-dependent protein kinase C activity}} {{GNF_GO|id=GO:0005524 |text = ATP binding}} {{GNF_GO|id=GO:0008022 |text = protein C-terminus binding}} {{GNF_GO|id=GO:0008047 |text = enzyme activator activity}} {{GNF_GO|id=GO:0008270 |text = zinc ion binding}} {{GNF_GO|id=GO:0016740 |text = transferase activity}} {{GNF_GO|id=GO:0019899 |text = enzyme binding}} {{GNF_GO|id=GO:0019992 |text = diacylglycerol binding}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005737 |text = cytoplasm}} {{GNF_GO|id=GO:0016020 |text = membrane}}
| Process = {{GNF_GO|id=GO:0006468 |text = protein amino acid phosphorylation}} {{GNF_GO|id=GO:0007242 |text = intracellular signaling cascade}} {{GNF_GO|id=GO:0016064 |text = immunoglobulin mediated immune response}} {{GNF_GO|id=GO:0042100 |text = B cell proliferation}} {{GNF_GO|id=GO:0050821 |text = protein stabilization}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 5580
| Hs_Ensembl = ENSG00000163932
| Hs_RefseqProtein = NP_006245
| Hs_RefseqmRNA = NM_006254
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 3
| Hs_GenLoc_start = 53170263
| Hs_GenLoc_end = 53201771
| Hs_Uniprot = Q05655
| Mm_EntrezGene = 18753
| Mm_Ensembl = ENSMUSG00000021948
| Mm_RefseqmRNA = NM_011103
| Mm_RefseqProtein = NP_035233
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 14
| Mm_GenLoc_start = 29424378
| Mm_GenLoc_end = 29439321
| Mm_Uniprot = Q1MX41
}}
}}
'''Protein kinase C, delta''', also known as '''PRKCD''', is a human [[gene]].
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = Protein kinase C (PKC) is a family of serine- and threonine-specific protein kinases that can be activated by calcium and the second messenger diacylglycerol. PKC family members phosphorylate a wide variety of protein targets and are known to be involved in diverse cellular signaling pathways. PKC family members also serve as major receptors for phorbol esters, a class of tumor promoters. Each member of the PKC family has a specific expression profile and is believed to play distinct roles in cells. The protein encoded by this gene is one of the PKC family members. Studies both in human and mice demonstrate that this kinase is involved in B cell signaling and in the regulation of growth, apoptosis, and differentiation of a variety of cell types. Alternatively spliced transcript variants encoding the same protein have been observed.<ref>{{cite web | title = Entrez Gene: PRKCD protein kinase C, delta| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5580| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Ali A, Hoeflich KP, Woodgett JR |title=Glycogen synthase kinase-3: properties, functions, and regulation. |journal=Chem. Rev. |volume=101 |issue= 8 |pages= 2527-40 |year= 2002 |pmid= 11749387 |doi= }}
*{{cite journal | author=Slater SJ, Ho C, Stubbs CD |title=The use of fluorescent phorbol esters in studies of protein kinase C-membrane interactions. |journal=Chem. Phys. Lipids |volume=116 |issue= 1-2 |pages= 75-91 |year= 2003 |pmid= 12093536 |doi= }}
*{{cite journal | author=Brodie C, Blumberg PM |title=Regulation of cell apoptosis by protein kinase c delta. |journal=Apoptosis |volume=8 |issue= 1 |pages= 19-27 |year= 2003 |pmid= 12510148 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on PSEN1... {October 3, 2007 10:37:34 PM PDT}
- AMBIGUITY: Did not locate an acceptable page to update. {October 3, 2007 10:38:34 PM PDT}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Presenilin 1 (Alzheimer disease 3)
| HGNCid = 9508
| Symbol = PSEN1
| AltSymbols =; FAD; AD3; PS1; S182
| OMIM = 104311
| ECnumber =
| Homologene = 7186
| MGIid = 1202717
| GeneAtlas_image1 = PBB_GE_PSEN1_203460_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_PSEN1_207782_s_at_tn.png
<!-- The Following entry is a time stamp of the last bot update. It is typically hidden data -->
| DateOfBotUpdate = ~~~~~
| Function = {{GNF_GO|id=GO:0004175 |text = endopeptidase activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}}
| Component = {{GNF_GO|id=GO:0000776 |text = kinetochore}} {{GNF_GO|id=GO:0005622 |text = intracellular}} {{GNF_GO|id=GO:0005624 |text = membrane fraction}} {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005639 |text = integral to nuclear inner membrane}} {{GNF_GO|id=GO:0005739 |text = mitochondrion}} {{GNF_GO|id=GO:0005783 |text = endoplasmic reticulum}} {{GNF_GO|id=GO:0005794 |text = Golgi apparatus}} {{GNF_GO|id=GO:0005887 |text = integral to plasma membrane}} {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0030424 |text = axon}} {{GNF_GO|id=GO:0030425 |text = dendrite}} {{GNF_GO|id=GO:0031410 |text = cytoplasmic vesicle}} {{GNF_GO|id=GO:0035253 |text = ciliary rootlet}} {{GNF_GO|id=GO:0043025 |text = cell soma}}
| Process = {{GNF_GO|id=GO:0001568 |text = blood vessel development}} {{GNF_GO|id=GO:0001708 |text = cell fate specification}} {{GNF_GO|id=GO:0001764 |text = neuron migration}} {{GNF_GO|id=GO:0006509 |text = membrane protein ectodomain proteolysis}} {{GNF_GO|id=GO:0006874 |text = cellular calcium ion homeostasis}} {{GNF_GO|id=GO:0006915 |text = apoptosis}} {{GNF_GO|id=GO:0006916 |text = anti-apoptosis}} {{GNF_GO|id=GO:0007001 |text = chromosome organization and biogenesis (sensu Eukaryota)}} {{GNF_GO|id=GO:0007059 |text = chromosome segregation}} {{GNF_GO|id=GO:0007155 |text = cell adhesion}} {{GNF_GO|id=GO:0007220 |text = Notch receptor processing}} {{GNF_GO|id=GO:0007242 |text = intracellular signaling cascade}} {{GNF_GO|id=GO:0007507 |text = heart development}} {{GNF_GO|id=GO:0007613 |text = memory}} {{GNF_GO|id=GO:0016485 |text = protein processing}} {{GNF_GO|id=GO:0030326 |text = embryonic limb morphogenesis}} {{GNF_GO|id=GO:0042325 |text = regulation of phosphorylation}} {{GNF_GO|id=GO:0042640 |text = anagen}} {{GNF_GO|id=GO:0042987 |text = amyloid precursor protein catabolic process}} {{GNF_GO|id=GO:0043065 |text = positive regulation of apoptosis}} {{GNF_GO|id=GO:0043085 |text = positive regulation of enzyme activity}} {{GNF_GO|id=GO:0045860 |text = positive regulation of protein kinase activity}} {{GNF_GO|id=GO:0051563 |text = smooth endoplasmic reticulum calcium ion homeostasis}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 5663
| Hs_Ensembl = ENSG00000080815
| Hs_RefseqProtein = NP_000012
| Hs_RefseqmRNA = NM_000021
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 14
| Hs_GenLoc_start = 72672915
| Hs_GenLoc_end = 72756862
| Hs_Uniprot = P49768
| Mm_EntrezGene = 19164
| Mm_Ensembl = ENSMUSG00000019969
| Mm_RefseqmRNA = NM_008943
| Mm_RefseqProtein = NP_032969
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 12
| Mm_GenLoc_start = 84577950
| Mm_GenLoc_end = 84624947
| Mm_Uniprot = Q3TDW2
}}
}}
'''Presenilin 1 (Alzheimer disease 3)''', also known as '''PSEN1''', is a human [[gene]].
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = Alzheimer's disease (AD) patients with an inherited form of the disease carry mutations in the presenilin proteins (PSEN1; PSEN2) or in the amyloid precursor protein (APP). These disease-linked mutations result in increased production of the longer form of amyloid-beta (main component of amyloid deposits found in AD brains). Presenilins are postulated to regulate APP processing through their effects on gamma-secretase, an enzyme that cleaves APP. Also, it is thought that the presenilins are involved in the cleavage of the Notch receptor, such that they either directly regulate gamma-secretase activity or themselves are protease enzymes. Multiple alternatively spliced transcript variants have been identified for this gene, the full-length natures of only some have been determined.<ref>{{cite web | title = Entrez Gene: PSEN1 presenilin 1 (Alzheimer disease 3)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5663| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Cruts M, Hendriks L, Van Broeckhoven C |title=The presenilin genes: a new gene family involved in Alzheimer disease pathology. |journal=Hum. Mol. Genet. |volume=5 Spec No |issue= |pages= 1449-55 |year= 1997 |pmid= 8875251 |doi= }}
*{{cite journal | author=Cruts M, Van Broeckhoven C |title=Presenilin mutations in Alzheimer's disease. |journal=Hum. Mutat. |volume=11 |issue= 3 |pages= 183-90 |year= 1998 |pmid= 9521418 |doi= 10.1002/(SICI)1098-1004(1998)11:3<183::AID-HUMU1>3.0.CO;2-J }}
*{{cite journal | author=Larner AJ, Doran M |title=Clinical phenotypic heterogeneity of Alzheimer's disease associated with mutations of the presenilin-1 gene. |journal=J. Neurol. |volume=253 |issue= 2 |pages= 139-58 |year= 2006 |pmid= 16267640 |doi= 10.1007/s00415-005-0019-5 }}
*{{cite journal | author=Wolfe MS |title=When loss is gain: reduced presenilin proteolytic function leads to increased Abeta42/Abeta40. Talking Point on the role of presenilin mutations in Alzheimer disease. |journal=EMBO Rep. |volume=8 |issue= 2 |pages= 136-40 |year= 2007 |pmid= 17268504 |doi= 10.1038/sj.embor.7400896 }}
*{{cite journal | author=De Strooper B |title=Loss-of-function presenilin mutations in Alzheimer disease. Talking Point on the role of presenilin mutations in Alzheimer disease. |journal=EMBO Rep. |volume=8 |issue= 2 |pages= 141-6 |year= 2007 |pmid= 17268505 |doi= 10.1038/sj.embor.7400897 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on PTEN... {October 3, 2007 10:38:34 PM PDT}
- AMBIGUITY: Did not locate an acceptable page to update. {October 3, 2007 10:38:59 PM PDT}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB = {{PDB2|1d5r}}
| Name = Phosphatase and tensin homolog (mutated in multiple advanced cancers 1)
| HGNCid = 9588
| Symbol = PTEN
| AltSymbols =; BZS; MGC11227; MHAM; MMAC1; PTEN1; TEP1
| OMIM = 601728
| ECnumber =
| Homologene = 265
| MGIid = 109583
<!-- The Following entry is a time stamp of the last bot update. It is typically hidden data -->
| DateOfBotUpdate = ~~~~~
| Function = {{GNF_GO|id=GO:0004438 |text = phosphatidylinositol-3-phosphatase activity}} {{GNF_GO|id=GO:0004722 |text = protein serine/threonine phosphatase activity}} {{GNF_GO|id=GO:0004725 |text = protein tyrosine phosphatase activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0008138 |text = protein tyrosine/serine/threonine phosphatase activity}} {{GNF_GO|id=GO:0008289 |text = lipid binding}} {{GNF_GO|id=GO:0016314 |text = phosphatidylinositol-3,4,5-trisphosphate 3-phosphatase activity}} {{GNF_GO|id=GO:0016787 |text = hydrolase activity}} {{GNF_GO|id=GO:0030165 |text = PDZ domain binding}} {{GNF_GO|id=GO:0051717 |text = inositol-1,3,4,5-tetrakisphosphate 3-phosphatase activity}} {{GNF_GO|id=GO:0051800 |text = phosphatidylinositol-3,4-bisphosphate 3-phosphatase activity}}
| Component = {{GNF_GO|id=GO:0005737 |text = cytoplasm}}
| Process = {{GNF_GO|id=GO:0000079 |text = regulation of cyclin-dependent protein kinase activity}} {{GNF_GO|id=GO:0006470 |text = protein amino acid dephosphorylation}} {{GNF_GO|id=GO:0006629 |text = lipid metabolic process}} {{GNF_GO|id=GO:0006917 |text = induction of apoptosis}} {{GNF_GO|id=GO:0007049 |text = cell cycle}} {{GNF_GO|id=GO:0007417 |text = central nervous system development}} {{GNF_GO|id=GO:0007507 |text = heart development}} {{GNF_GO|id=GO:0008283 |text = cell proliferation}} {{GNF_GO|id=GO:0008285 |text = negative regulation of cell proliferation}} {{GNF_GO|id=GO:0016477 |text = cell migration}} {{GNF_GO|id=GO:0030336 |text = negative regulation of cell migration}} {{GNF_GO|id=GO:0031647 |text = regulation of protein stability}} {{GNF_GO|id=GO:0043066 |text = negative regulation of apoptosis}} {{GNF_GO|id=GO:0045786 |text = negative regulation of progression through cell cycle}} {{GNF_GO|id=GO:0046855 |text = inositol phosphate dephosphorylation}} {{GNF_GO|id=GO:0046856 |text = phosphoinositide dephosphorylation}} {{GNF_GO|id=GO:0051895 |text = negative regulation of focal adhesion formation}} {{GNF_GO|id=GO:0051898 |text = negative regulation of protein kinase B signaling cascade}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 5728
| Hs_Ensembl =
| Hs_RefseqProtein = NP_000305
| Hs_RefseqmRNA = NM_000314
| Hs_GenLoc_db =
| Hs_GenLoc_chr =
| Hs_GenLoc_start =
| Hs_GenLoc_end =
| Hs_Uniprot =
| Mm_EntrezGene = 19211
| Mm_Ensembl = ENSMUSG00000013663
| Mm_RefseqmRNA = NM_008960
| Mm_RefseqProtein = NP_032986
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 19
| Mm_GenLoc_start = 32823574
| Mm_GenLoc_end = 32892157
| Mm_Uniprot = Q3UFB0
}}
}}
'''Phosphatase and tensin homolog (mutated in multiple advanced cancers 1)''', also known as '''PTEN''', is a human [[gene]].
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = This gene was identified as a tumor suppressor that is mutated in a large number of cancers at high frequency. The protein encoded this gene is a phosphatidylinositol-3,4,5-trisphosphate 3-phosphatase. It contains a tensin like domain as well as a catalytic domain similar to that of the dual specificity protein tyrosine phosphatases. Unlike most of the protein tyrosine phosphatases, this protein preferentially dephosphorylates phosphoinositide substrates. It negatively regulates intracellular levels of phosphatidylinositol-3,4,5-trisphosphate in cells and functions as a tumor suppressor by negatively regulating AKT/PKB signaling pathway.<ref>{{cite web | title = Entrez Gene: PTEN phosphatase and tensin homolog (mutated in multiple advanced cancers 1)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5728| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Waite KA, Eng C |title=Protean PTEN: form and function. |journal=Am. J. Hum. Genet. |volume=70 |issue= 4 |pages= 829-44 |year= 2002 |pmid= 11875759 |doi= }}
*{{cite journal | author=Knobbe CB, Merlo A, Reifenberger G |title=Pten signaling in gliomas. |journal=Neuro-oncology |volume=4 |issue= 3 |pages= 196-211 |year= 2002 |pmid= 12084351 |doi= }}
*{{cite journal | author=Eng C |title=Role of PTEN, a lipid phosphatase upstream effector of protein kinase B, in epithelial thyroid carcinogenesis. |journal=Ann. N. Y. Acad. Sci. |volume=968 |issue= |pages= 213-21 |year= 2002 |pmid= 12119278 |doi= }}
*{{cite journal | author=Backman S, Stambolic V, Mak T |title=PTEN function in mammalian cell size regulation. |journal=Curr. Opin. Neurobiol. |volume=12 |issue= 5 |pages= 516-22 |year= 2002 |pmid= 12367630 |doi= }}
*{{cite journal | author=Wishart MJ, Dixon JE |title=PTEN and myotubularin phosphatases: from 3-phosphoinositide dephosphorylation to disease. |journal=Trends Cell Biol. |volume=12 |issue= 12 |pages= 579-85 |year= 2003 |pmid= 12495846 |doi= }}
*{{cite journal | author=Deocampo ND, Huang H, Tindall DJ |title=The role of PTEN in the progression and survival of prostate cancer. |journal=Minerva Endocrinol. |volume=28 |issue= 2 |pages= 145-53 |year= 2003 |pmid= 12717346 |doi= }}
*{{cite journal | author=Downes CP, Walker S, McConnachie G, ''et al.'' |title=Acute regulation of the tumour suppressor phosphatase, PTEN, by anionic lipids and reactive oxygen species. |journal=Biochem. Soc. Trans. |volume=32 |issue= Pt 2 |pages= 338-42 |year= 2004 |pmid= 15046604 |doi= 10.1042/ }}
*{{cite journal | author=Maehama T, Okahara F, Kanaho Y |title=The tumour suppressor PTEN: involvement of a tumour suppressor candidate protein in PTEN turnover. |journal=Biochem. Soc. Trans. |volume=32 |issue= Pt 2 |pages= 343-7 |year= 2004 |pmid= 15046605 |doi= 10.1042/ }}
*{{cite journal | author=Parsons R |title=Human cancer, PTEN and the PI-3 kinase pathway. |journal=Semin. Cell Dev. Biol. |volume=15 |issue= 2 |pages= 171-6 |year= 2004 |pmid= 15209376 |doi= }}
*{{cite journal | author=Steelman LS, Bertrand FE, McCubrey JA |title=The complexity of PTEN: mutation, marker and potential target for therapeutic intervention. |journal=Expert Opin. Ther. Targets |volume=8 |issue= 6 |pages= 537-50 |year= 2005 |pmid= 15584861 |doi= 10.1517/14728222.8.6.537 }}
*{{cite journal | author=Mulholland DJ, Dedhar S, Wu H, Nelson CC |title=PTEN and GSK3beta: key regulators of progression to androgen-independent prostate cancer. |journal=Oncogene |volume=25 |issue= 3 |pages= 329-37 |year= 2006 |pmid= 16421604 |doi= 10.1038/sj.onc.1209020 }}
*{{cite journal | author=Vazquez F, Devreotes P |title=Regulation of PTEN function as a PIP3 gatekeeper through membrane interaction. |journal=Cell Cycle |volume=5 |issue= 14 |pages= 1523-7 |year= 2006 |pmid= 16861931 |doi= }}
*{{cite journal | author=Mellinghoff IK, Cloughesy TF, Mischel PS |title=PTEN-mediated resistance to epidermal growth factor receptor kinase inhibitors. |journal=Clin. Cancer Res. |volume=13 |issue= 2 Pt 1 |pages= 378-81 |year= 2007 |pmid= 17255257 |doi= 10.1158/1078-0432.CCR-06-1992 }}
*{{cite journal | author=Shen MM, Abate-Shen C |title=Pten inactivation and the emergence of androgen-independent prostate cancer. |journal=Cancer Res. |volume=67 |issue= 14 |pages= 6535-8 |year= 2007 |pmid= 17638861 |doi= 10.1158/0008-5472.CAN-07-1271 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on RAC1... {October 3, 2007 10:39:00 PM PDT}
- CREATE: Found no pages, creating new page. {October 3, 2007 10:40:05 PM PDT}
- UPLOAD: Added new Image to wikiCreated new protein page: <a href=http://en.wikipedia.org/w/index.php?title=RAC1>RAC1</a> {October 3, 2007 10:40:12 PM PDT}
- CREATED: Created new protein page: RAC1 {October 3, 2007 10:40:25 PM PDT}
- INFO: Beginning work on RELA... {October 3, 2007 10:40:25 PM PDT}
- CREATE: Found no pages, creating new page. {October 3, 2007 10:41:19 PM PDT}
- UPLOAD: Added new Image to wikiCreated new protein page: <a href=http://en.wikipedia.org/w/index.php?title=RELA>RELA</a> {October 3, 2007 10:41:31 PM PDT}
- CREATED: Created new protein page: RELA {October 3, 2007 10:41:45 PM PDT}
- INFO: Beginning work on RET... {October 3, 2007 10:41:45 PM PDT}
- AMBIGUITY: Did not locate an acceptable page to update. {October 3, 2007 10:43:11 PM PDT}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB = {{PDB2|2ivs}}, {{PDB2|2ivt}}, {{PDB2|2ivu}}, {{PDB2|2ivv}}
| Name = Ret proto-oncogene
| HGNCid = 9967
| Symbol = RET
| AltSymbols =; PTC; CDHF12; HSCR1; MEN2A; MEN2B; MTC1; RET-ELE1; RET51
| OMIM = 164761
| ECnumber =
| Homologene = 7517
| MGIid = 97902
| GeneAtlas_image1 = PBB_GE_RET_211421_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_RET_205879_x_at_tn.png
| GeneAtlas_image3 = PBB_GE_RET_215771_x_at_tn.png
<!-- The Following entry is a time stamp of the last bot update. It is typically hidden data -->
| DateOfBotUpdate = ~~~~~
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0004674 |text = protein serine/threonine kinase activity}} {{GNF_GO|id=GO:0004713 |text = protein-tyrosine kinase activity}} {{GNF_GO|id=GO:0004872 |text = receptor activity}} {{GNF_GO|id=GO:0005509 |text = calcium ion binding}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0005524 |text = ATP binding}} {{GNF_GO|id=GO:0016301 |text = kinase activity}} {{GNF_GO|id=GO:0016740 |text = transferase activity}}
| Component = {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}}
| Process = {{GNF_GO|id=GO:0000165 |text = MAPKKK cascade}} {{GNF_GO|id=GO:0001657 |text = ureteric bud development}} {{GNF_GO|id=GO:0001755 |text = neural crest cell migration}} {{GNF_GO|id=GO:0001838 |text = embryonic epithelial tube formation}} {{GNF_GO|id=GO:0006468 |text = protein amino acid phosphorylation}} {{GNF_GO|id=GO:0007156 |text = homophilic cell adhesion}} {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0007166 |text = cell surface receptor linked signal transduction}} {{GNF_GO|id=GO:0007399 |text = nervous system development}} {{GNF_GO|id=GO:0007497 |text = posterior midgut development}} {{GNF_GO|id=GO:0042551 |text = neuron maturation}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 5979
| Hs_Ensembl = ENSG00000165731
| Hs_RefseqProtein = NP_065681
| Hs_RefseqmRNA = NM_020630
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 10
| Hs_GenLoc_start = 42892528
| Hs_GenLoc_end = 42945805
| Hs_Uniprot = P07949
| Mm_EntrezGene = 19713
| Mm_Ensembl = ENSMUSG00000030110
| Mm_RefseqmRNA = NM_001080780
| Mm_RefseqProtein = NP_001074249
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 6
| Mm_GenLoc_start = 118119472
| Mm_GenLoc_end = 118163337
| Mm_Uniprot = P35546
}}
}}
'''Ret proto-oncogene''', also known as '''RET''', is a human [[gene]].
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = This gene, a member of the cadherin superfamily, encodes one of the receptor tyrosine kinases, which are cell-surface molecules that transduce signals for cell growth and differentiation. This gene plays a crucial role in neural crest development, and it can undergo oncogenic activation in vivo and in vitro by cytogenetic rearrangement. Mutations in this gene are associated with the disorders multiple endocrine neoplasia, type IIA, multiple endocrine neoplasia, type IIB, Hirschsprung disease, and medullary thyroid carcinoma. Two transcript variants encoding different isoforms have been found for this gene. Additional transcript variants have been described but their biological validity has not been confirmed.<ref>{{cite web | title = Entrez Gene: RET ret proto-oncogene| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5979| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Eng C, Mulligan LM |title=Mutations of the RET proto-oncogene in the multiple endocrine neoplasia type 2 syndromes, related sporadic tumours, and hirschsprung disease. |journal=Hum. Mutat. |volume=9 |issue= 2 |pages= 97-109 |year= 1997 |pmid= 9067749 |doi= 10.1002/(SICI)1098-1004(1997)9:2<97::AID-HUMU1>3.0.CO;2-M }}
*{{cite journal | author=Hofstra RM, Osinga J, Buys CH |title=Mutations in Hirschsprung disease: when does a mutation contribute to the phenotype. |journal=Eur. J. Hum. Genet. |volume=5 |issue= 4 |pages= 180-5 |year= 1998 |pmid= 9359036 |doi= }}
*{{cite journal | author=Nikiforov YE |title=RET/PTC rearrangement in thyroid tumors. |journal=Endocr. Pathol. |volume=13 |issue= 1 |pages= 3-16 |year= 2002 |pmid= 12114746 |doi= }}
*{{cite journal | author=Santoro M, Melillo RM, Carlomagno F, ''et al.'' |title=Minireview: RET: normal and abnormal functions. |journal=Endocrinology |volume=145 |issue= 12 |pages= 5448-51 |year= 2004 |pmid= 15331579 |doi= 10.1210/en.2004-0922 }}
*{{cite journal | author=Santoro M, Carlomagno F, Melillo RM, Fusco A |title=Dysfunction of the RET receptor in human cancer. |journal=Cell. Mol. Life Sci. |volume=61 |issue= 23 |pages= 2954-64 |year= 2005 |pmid= 15583857 |doi= 10.1007/s00018-004-4276-8 }}
*{{cite journal | author=Niccoli-Sire P, Conte-Devolx B, |title=[RET mutations and preventive treatment of medullary thyroid cancer] |journal=Ann. Endocrinol. (Paris) |volume=66 |issue= 3 |pages= 168-75 |year= 2005 |pmid= 15988377 |doi= }}
*{{cite journal | author=Lantieri F, Griseri P, Ceccherini I |title=Molecular mechanisms of RET-induced Hirschsprung pathogenesis. |journal=Ann. Med. |volume=38 |issue= 1 |pages= 11-9 |year= 2006 |pmid= 16448984 |doi= 10.1080/07853890500442758 }}
*{{cite journal | author=Ciampi R, Nikiforov YE |title=RET/PTC rearrangements and BRAF mutations in thyroid tumorigenesis. |journal=Endocrinology |volume=148 |issue= 3 |pages= 936-41 |year= 2007 |pmid= 16946010 |doi= 10.1210/en.2006-0921 }}
*{{cite journal | author=Plaza-Menacho I, Burzynski GM, de Groot JW, ''et al.'' |title=Current concepts in RET-related genetics, signaling and therapeutics. |journal=Trends Genet. |volume=22 |issue= 11 |pages= 627-36 |year= 2007 |pmid= 16979782 |doi= 10.1016/j.tig.2006.09.005 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on SERPINE1... {October 3, 2007 10:33:34 PM PDT}
- AMBIGUITY: Did not locate an acceptable page to update. {October 3, 2007 10:34:32 PM PDT}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB = {{PDB2|1a7c}}, {{PDB2|1b3k}}, {{PDB2|1c5g}}, {{PDB2|1db2}}, {{PDB2|1dvm}}, {{PDB2|1dvn}}, {{PDB2|1lj5}}, {{PDB2|1oc0}}, {{PDB2|9pai}}
| Name = Serpin peptidase inhibitor, clade E (nexin, plasminogen activator inhibitor type 1), member 1
| HGNCid = 8583
| Symbol = SERPINE1
| AltSymbols =; PAI; PAI-1; PAI1; PLANH1
| OMIM = 173360
| ECnumber =
| Homologene = 68070
| MGIid = 97608
| GeneAtlas_image1 = PBB_GE_SERPINE1_202627_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_SERPINE1_202628_s_at_tn.png
<!-- The Following entry is a time stamp of the last bot update. It is typically hidden data -->
| DateOfBotUpdate = ~~~~~
| Function = {{GNF_GO|id=GO:0002020 |text = protease binding}} {{GNF_GO|id=GO:0004867 |text = serine-type endopeptidase inhibitor activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0008243 |text = plasminogen activator activity}}
| Component = {{GNF_GO|id=GO:0005576 |text = extracellular region}}
| Process = {{GNF_GO|id=GO:0007596 |text = blood coagulation}} {{GNF_GO|id=GO:0042730 |text = fibrinolysis}} {{GNF_GO|id=GO:0045765 |text = regulation of angiogenesis}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 5054
| Hs_Ensembl = ENSG00000106366
| Hs_RefseqProtein = NP_000593
| Hs_RefseqmRNA = NM_000602
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 7
| Hs_GenLoc_start = 100557172
| Hs_GenLoc_end = 100569026
| Hs_Uniprot = P05121
| Mm_EntrezGene = 18787
| Mm_Ensembl = ENSMUSG00000037411
| Mm_RefseqmRNA = NM_008871
| Mm_RefseqProtein = NP_032897
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 5
| Mm_GenLoc_start = 137346135
| Mm_GenLoc_end = 137356886
| Mm_Uniprot = Q7TPE9
}}
}}
'''Serpin peptidase inhibitor, clade E (nexin, plasminogen activator inhibitor type 1), member 1''', also known as '''SERPINE1''', is a human [[gene]].
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text =
}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Mimuro J |title=[Type 1 plasminogen activator inhibitor: its role in biological reactions] |journal=Rinsho Ketsueki |volume=32 |issue= 5 |pages= 487-9 |year= 1991 |pmid= 1870265 |doi= }}
*{{cite journal | author=Binder BR, Christ G, Gruber F, ''et al.'' |title=Plasminogen activator inhibitor 1: physiological and pathophysiological roles. |journal=News Physiol. Sci. |volume=17 |issue= |pages= 56-61 |year= 2002 |pmid= 11909993 |doi= }}
*{{cite journal | author=Eddy AA |title=Plasminogen activator inhibitor-1 and the kidney. |journal=Am. J. Physiol. Renal Physiol. |volume=283 |issue= 2 |pages= F209-20 |year= 2002 |pmid= 12110504 |doi= 10.1152/ajprenal.00032.2002 }}
*{{cite journal | author=Schroeck F, Arroyo de Prada N, Sperl S, ''et al.'' |title=Interaction of plasminogen activator inhibitor type-1 (PAI-1) with vitronectin (Vn): mapping the binding sites on PAI-1 and Vn. |journal=Biol. Chem. |volume=383 |issue= 7-8 |pages= 1143-9 |year= 2003 |pmid= 12437099 |doi= }}
*{{cite journal | author=Gils A, Declerck PJ |title=The structural basis for the pathophysiological relevance of PAI-I in cardiovascular diseases and the development of potential PAI-I inhibitors. |journal=Thromb. Haemost. |volume=91 |issue= 3 |pages= 425-37 |year= 2004 |pmid= 14983217 |doi= 10.1160/TH03-12-0764 }}
*{{cite journal | author=Durand MK, Bødker JS, Christensen A, ''et al.'' |title=Plasminogen activator inhibitor-I and tumour growth, invasion, and metastasis. |journal=Thromb. Haemost. |volume=91 |issue= 3 |pages= 438-49 |year= 2004 |pmid= 14983218 |doi= 10.1160/TH03-12-0784 }}
*{{cite journal | author=Harbeck N, Kates RE, Gauger K, ''et al.'' |title=Urokinase-type plasminogen activator (uPA) and its inhibitor PAI-I: novel tumor-derived factors with a high prognostic and predictive impact in breast cancer. |journal=Thromb. Haemost. |volume=91 |issue= 3 |pages= 450-6 |year= 2004 |pmid= 14983219 |doi= 10.1160/TH03-12-0798 }}
*{{cite journal | author=Hertig A, Rondeau E |title=Plasminogen activator inhibitor type 1: the two faces of the same coin. |journal=Curr. Opin. Nephrol. Hypertens. |volume=13 |issue= 1 |pages= 39-44 |year= 2004 |pmid= 15090858 |doi= }}
*{{cite journal | author=Hoekstra T, Geleijnse JM, Schouten EG, Kluft C |title=Plasminogen activator inhibitor-type 1: its plasma determinants and relation with cardiovascular risk. |journal=Thromb. Haemost. |volume=91 |issue= 5 |pages= 861-72 |year= 2004 |pmid= 15116245 |doi= 10.1267/THRO04050861 }}
*{{cite journal | author=Lijnen HR |title=Pleiotropic functions of plasminogen activator inhibitor-1. |journal=J. Thromb. Haemost. |volume=3 |issue= 1 |pages= 35-45 |year= 2005 |pmid= 15634264 |doi= 10.1111/j.1538-7836.2004.00827.x }}
*{{cite journal | author=De Taeye B, Smith LH, Vaughan DE |title=Plasminogen activator inhibitor-1: a common denominator in obesity, diabetes and cardiovascular disease. |journal=Current opinion in pharmacology |volume=5 |issue= 2 |pages= 149-54 |year= 2005 |pmid= 15780823 |doi= 10.1016/j.coph.2005.01.007 }}
*{{cite journal | author=Dellas C, Loskutoff DJ |title=Historical analysis of PAI-1 from its discovery to its potential role in cell motility and disease. |journal=Thromb. Haemost. |volume=93 |issue= 4 |pages= 631-40 |year= 2005 |pmid= 15841306 |doi= 10.1267/THRO05040631 }}
*{{cite journal | author=Könsgen D, Mustea A, Lichtenegger W, Sehouli J |title=[Role of PAI-1 in gynaecological malignancies] |journal=Zentralblatt für Gynäkologie |volume=127 |issue= 3 |pages= 125-31 |year= 2005 |pmid= 15915389 |doi= 10.1055/s-2005-836407 }}
*{{cite journal | author=Vaughan DE |title=PAI-1 and atherothrombosis. |journal=J. Thromb. Haemost. |volume=3 |issue= 8 |pages= 1879-83 |year= 2005 |pmid= 16102055 |doi= 10.1111/j.1538-7836.2005.01420.x }}
*{{cite journal | author=Hermans PW, Hazelzet JA |title=Plasminogen activator inhibitor type 1 gene polymorphism and sepsis. |journal=Clin. Infect. Dis. |volume=41 Suppl 7 |issue= |pages= S453-8 |year= 2007 |pmid= 16237647 |doi= 10.1086/431996 }}
*{{cite journal | author=Alessi MC, Poggi M, Juhan-Vague I |title=Plasminogen activator inhibitor-1, adipose tissue and insulin resistance. |journal=Curr. Opin. Lipidol. |volume=18 |issue= 3 |pages= 240-5 |year= 2007 |pmid= 17495595 |doi= 10.1097/MOL.0b013e32814e6d29 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on SNCA... {October 3, 2007 10:44:00 PM PDT}
- AMBIGUITY: Did not locate an acceptable page to update. {October 3, 2007 10:45:01 PM PDT}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
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| update_citations = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB = {{PDB2|1xq8}}
| Name = Synuclein, alpha (non A4 component of amyloid precursor)
| HGNCid = 11138
| Symbol = SNCA
| AltSymbols =; PD1; MGC110988; NACP; PARK1; PARK4
| OMIM = 163890
| ECnumber =
| Homologene = 293
| MGIid = 1277151
| GeneAtlas_image1 = PBB_GE_SNCA_204466_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_SNCA_204467_s_at_tn.png
<!-- The Following entry is a time stamp of the last bot update. It is typically hidden data -->
| DateOfBotUpdate = ~~~~~
| Function = {{GNF_GO|id=GO:0042802 |text = identical protein binding}}
| Component = {{GNF_GO|id=GO:0005737 |text = cytoplasm}} {{GNF_GO|id=GO:0019717 |text = synaptosome}}
| Process = {{GNF_GO|id=GO:0001956 |text = positive regulation of neurotransmitter secretion}} {{GNF_GO|id=GO:0001963 |text = synaptic transmission, dopaminergic}} {{GNF_GO|id=GO:0006644 |text = phospholipid metabolic process}} {{GNF_GO|id=GO:0006916 |text = anti-apoptosis}} {{GNF_GO|id=GO:0007417 |text = central nervous system development}} {{GNF_GO|id=GO:0040012 |text = regulation of locomotion}} {{GNF_GO|id=GO:0042416 |text = dopamine biosynthetic process}} {{GNF_GO|id=GO:0042493 |text = response to drug}} {{GNF_GO|id=GO:0048169 |text = regulation of long-term neuronal synaptic plasticity}} {{GNF_GO|id=GO:0048489 |text = synaptic vesicle transport}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 6622
| Hs_Ensembl = ENSG00000145335
| Hs_RefseqProtein = NP_000336
| Hs_RefseqmRNA = NM_000345
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 4
| Hs_GenLoc_start = 90866479
| Hs_GenLoc_end = 90978470
| Hs_Uniprot = P37840
| Mm_EntrezGene = 20617
| Mm_Ensembl = ENSMUSG00000025889
| Mm_RefseqmRNA = NM_001042451
| Mm_RefseqProtein = NP_001035916
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 6
| Mm_GenLoc_start = 60661224
| Mm_GenLoc_end = 60759433
| Mm_Uniprot = Q3U130
}}
}}
'''Synuclein, alpha (non A4 component of amyloid precursor)''', also known as '''SNCA''', is a human [[gene]].
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = Alpha-synuclein is a member of the synuclein family, which also includes beta- and gamma-synuclein. Synucleins are abundantly expressed in the brain and alpha- and beta-synuclein inhibit phospholipase D2 selectively. SNCA may serve to integrate presynaptic signaling and membrane trafficking. Defects in SNCA have been implicated in the pathogenesis of Parkinson disease. SNCA peptides are a major component of amyloid plaques in the brains of patients with Alzheimer's disease. Two alternatively spliced transcripts of SNCA have been identified. Additional splicing may be present but the full-length nature of these variants has not been determined.<ref>{{cite web | title = Entrez Gene: SNCA synuclein, alpha (non A4 component of amyloid precursor)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6622| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Lavedan C |title=The synuclein family. |journal=Genome Res. |volume=8 |issue= 9 |pages= 871-80 |year= 1998 |pmid= 9750188 |doi= }}
*{{cite journal | author=Ozawa T, Wakabayashi K, Oyanagi K |title=[Recent progress in the research of multiple system atrophy with special references to alpha-synuclein and suprachiasmatic nucleus] |journal=No To Shinkei |volume=54 |issue= 2 |pages= 111-7 |year= 2002 |pmid= 11889756 |doi= }}
*{{cite journal | author=Cole NB, Murphy DD |title=The cell biology of alpha-synuclein: a sticky problem? |journal=Neuromolecular Med. |volume=1 |issue= 2 |pages= 95-109 |year= 2002 |pmid= 12025860 |doi= }}
*{{cite journal | author=Iwatsubo T |title=[alpha-synuclein and Parkinson's disease] |journal=Seikagaku |volume=74 |issue= 6 |pages= 477-82 |year= 2002 |pmid= 12138709 |doi= }}
*{{cite journal | author=Trojanowski JQ, Lee VM |title=Parkinson's disease and related synucleinopathies are a new class of nervous system amyloidoses. |journal=Neurotoxicology |volume=23 |issue= 4-5 |pages= 457-60 |year= 2002 |pmid= 12428717 |doi= }}
*{{cite journal | author=Alves da Costa C |title=Recent advances on alpha-synuclein cell biology: functions and dysfunctions. |journal=Curr. Mol. Med. |volume=3 |issue= 1 |pages= 17-24 |year= 2003 |pmid= 12558071 |doi= }}
*{{cite journal | author=Di Rosa G, Puzzo D, Sant'Angelo A, ''et al.'' |title=Alpha-synuclein: between synaptic function and dysfunction. |journal=Histol. Histopathol. |volume=18 |issue= 4 |pages= 1257-66 |year= 2004 |pmid= 12973692 |doi= }}
*{{cite journal | author=Baptista MJ, Cookson MR, Miller DW |title=Parkin and alpha-synuclein: opponent actions in the pathogenesis of Parkinson's disease. |journal=The Neuroscientist : a review journal bringing neurobiology, neurology and psychiatry |volume=10 |issue= 1 |pages= 63-72 |year= 2004 |pmid= 14987449 |doi= 10.1177/1073858403260392 }}
*{{cite journal | author=Kim S, Seo JH, Suh YH |title=Alpha-synuclein, Parkinson's disease, and Alzheimer's disease. |journal=Parkinsonism Relat. Disord. |volume=10 Suppl 1 |issue= |pages= S9-13 |year= 2004 |pmid= 15109581 |doi= 10.1016/j.parkreldis.2003.11.005 }}
*{{cite journal | author=Sidhu A, Wersinger C, Vernier P |title=alpha-Synuclein regulation of the dopaminergic transporter: a possible role in the pathogenesis of Parkinson's disease. |journal=FEBS Lett. |volume=565 |issue= 1-3 |pages= 1-5 |year= 2004 |pmid= 15135042 |doi= 10.1016/j.febslet.2004.03.063 }}
*{{cite journal | author=Vekrellis K, Rideout HJ, Stefanis L |title=Neurobiology of alpha-synuclein. |journal=Mol. Neurobiol. |volume=30 |issue= 1 |pages= 1-21 |year= 2004 |pmid= 15247485 |doi= }}
*{{cite journal | author=Chiba-Falek O, Nussbaum RL |title=Regulation of alpha-synuclein expression: implications for Parkinson's disease. |journal=Cold Spring Harb. Symp. Quant. Biol. |volume=68 |issue= |pages= 409-15 |year= 2004 |pmid= 15338643 |doi= }}
*{{cite journal | author=Pankratz N, Foroud T |title=Genetics of Parkinson disease. |journal=NeuroRx : the journal of the American Society for Experimental NeuroTherapeutics |volume=1 |issue= 2 |pages= 235-42 |year= 2005 |pmid= 15717024 |doi= }}
*{{cite journal | author=Singleton AB |title=Altered alpha-synuclein homeostasis causing Parkinson's disease: the potential roles of dardarin. |journal=Trends Neurosci. |volume=28 |issue= 8 |pages= 416-21 |year= 2005 |pmid= 15955578 |doi= 10.1016/j.tins.2005.05.009 }}
*{{cite journal | author=Lee HG, Zhu X, Takeda A, ''et al.'' |title=Emerging evidence for the neuroprotective role of alpha-synuclein. |journal=Exp. Neurol. |volume=200 |issue= 1 |pages= 1-7 |year= 2006 |pmid= 16780837 |doi= 10.1016/j.expneurol.2006.04.024 }}
*{{cite journal | author=Giorgi FS, Bandettini di Poggio A, Battaglia G, ''et al.'' |title=A short overview on the role of alpha-synuclein and proteasome in experimental models of Parkinson's disease. |journal=J. Neural Transm. Suppl. |volume= |issue= 70 |pages= 105-9 |year= 2006 |pmid= 17017516 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on SOD1... {October 3, 2007 10:45:01 PM PDT}
- AMBIGUITY: Did not locate an acceptable page to update. {October 3, 2007 10:45:55 PM PDT}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB = {{PDB2|1azv}}, {{PDB2|1ba9}}, {{PDB2|1dsw}}, {{PDB2|1fun}}, {{PDB2|1hl4}}, {{PDB2|1hl5}}, {{PDB2|1kmg}}, {{PDB2|1l3n}}, {{PDB2|1mfm}}, {{PDB2|1n18}}, {{PDB2|1n19}}, {{PDB2|1oez}}, {{PDB2|1ozt}}, {{PDB2|1ozu}}, {{PDB2|1p1v}}, {{PDB2|1ptz}}, {{PDB2|1pu0}}, {{PDB2|1rk7}}, {{PDB2|1sos}}, {{PDB2|1spd}}, {{PDB2|1uxl}}, {{PDB2|1uxm}}, {{PDB2|2af2}}, {{PDB2|2c9s}}, {{PDB2|2c9u}}, {{PDB2|2c9v}}, {{PDB2|2gbt}}, {{PDB2|2gbu}}, {{PDB2|2gbv}}, {{PDB2|2nnx}}
| Name = Superoxide dismutase 1, soluble (amyotrophic lateral sclerosis 1 (adult))
| HGNCid = 11179
| Symbol = SOD1
| AltSymbols =; ALS; ALS1; IPOA; SOD; homodimer
| OMIM = 147450
| ECnumber =
| Homologene = 392
| MGIid = 98351
| GeneAtlas_image1 = PBB_GE_SOD1_200642_at_tn.png
<!-- The Following entry is a time stamp of the last bot update. It is typically hidden data -->
| DateOfBotUpdate = ~~~~~
| Function = {{GNF_GO|id=GO:0004785 |text = copper, zinc superoxide dismutase activity}} {{GNF_GO|id=GO:0005507 |text = copper ion binding}} {{GNF_GO|id=GO:0008270 |text = zinc ion binding}} {{GNF_GO|id=GO:0016209 |text = antioxidant activity}} {{GNF_GO|id=GO:0016491 |text = oxidoreductase activity}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}}
| Component = {{GNF_GO|id=GO:0005737 |text = cytoplasm}}
| Process = {{GNF_GO|id=GO:0006801 |text = superoxide metabolic process}} {{GNF_GO|id=GO:0006979 |text = response to oxidative stress}} {{GNF_GO|id=GO:0007399 |text = nervous system development}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 6647
| Hs_Ensembl = ENSG00000142168
| Hs_RefseqProtein = NP_000445
| Hs_RefseqmRNA = NM_000454
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 21
| Hs_GenLoc_start = 31953954
| Hs_GenLoc_end = 31963001
| Hs_Uniprot = P00441
| Mm_EntrezGene = 20655
| Mm_Ensembl =
| Mm_RefseqmRNA = NM_011434
| Mm_RefseqProtein = NP_035564
| Mm_GenLoc_db =
| Mm_GenLoc_chr =
| Mm_GenLoc_start =
| Mm_GenLoc_end =
| Mm_Uniprot =
}}
}}
'''Superoxide dismutase 1, soluble (amyotrophic lateral sclerosis 1 (adult))''', also known as '''SOD1''', is a human [[gene]].
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = The protein encoded by this gene binds copper and zinc ions and is one of two isozymes responsible for destroying free superoxide radicals in the body. The encoded isozyme is a soluble cytoplasmic protein, acting as a homodimer to convert naturally-occuring but harmful superoxide radicals to molecular oxygen and hydrogen peroxide. The other isozyme is a mitochondrial protein. Mutations in this gene have been implicated as causes of familial amyotrophic lateral sclerosis. Rare transcript variants have been reported for this gene.<ref>{{cite web | title = Entrez Gene: SOD1 superoxide dismutase 1, soluble (amyotrophic lateral sclerosis 1 (adult))| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6647| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=de Belleroche J, Orrell R, King A |title=Familial amyotrophic lateral sclerosis/motor neurone disease (FALS): a review of current developments. |journal=J. Med. Genet. |volume=32 |issue= 11 |pages= 841-7 |year= 1996 |pmid= 8592323 |doi= }}
*{{cite journal | author=Ceroni M, Curti D, Alimonti D |title=Amyotrophic lateral sclerosis and SOD1 gene: an overview. |journal=Funct. Neurol. |volume=16 |issue= 4 Suppl |pages= 171-80 |year= 2002 |pmid= 11996514 |doi= }}
*{{cite journal | author=Zelko IN, Mariani TJ, Folz RJ |title=Superoxide dismutase multigene family: a comparison of the CuZn-SOD (SOD1), Mn-SOD (SOD2), and EC-SOD (SOD3) gene structures, evolution, and expression. |journal=Free Radic. Biol. Med. |volume=33 |issue= 3 |pages= 337-49 |year= 2003 |pmid= 12126755 |doi= }}
*{{cite journal | author=Hadano S |title=[Causative genes for familial amyotrophic lateral sclerosis] |journal=Seikagaku |volume=74 |issue= 6 |pages= 483-9 |year= 2002 |pmid= 12138710 |doi= }}
*{{cite journal | author=Noor R, Mittal S, Iqbal J |title=Superoxide dismutase--applications and relevance to human diseases. |journal=Med. Sci. Monit. |volume=8 |issue= 9 |pages= RA210-5 |year= 2003 |pmid= 12218958 |doi= }}
*{{cite journal | author=Potter SZ, Valentine JS |title=The perplexing role of copper-zinc superoxide dismutase in amyotrophic lateral sclerosis (Lou Gehrig's disease). |journal=J. Biol. Inorg. Chem. |volume=8 |issue= 4 |pages= 373-80 |year= 2004 |pmid= 12644909 |doi= 10.1007/s00775-003-0447-6 }}
*{{cite journal | author=Rotilio G, Aquilano K, Ciriolo MR |title=Interplay of Cu,Zn superoxide dismutase and nitric oxide synthase in neurodegenerative processes. |journal=IUBMB Life |volume=55 |issue= 10-11 |pages= 629-34 |year= 2004 |pmid= 14711010 |doi= }}
*{{cite journal | author=Jafari-Schluep HF, Khoris J, Mayeux-Portas V, ''et al.'' |title=[Superoxyde dismutase 1 gene abnormalities in familial amyotrophic lateral sclerosis: phenotype/genotype correlations. The French experience and review of the literature] |journal=Rev. Neurol. (Paris) |volume=160 |issue= 1 |pages= 44-50 |year= 2004 |pmid= 14978393 |doi= }}
*{{cite journal | author=Faraci FM, Didion SP |title=Vascular protection: superoxide dismutase isoforms in the vessel wall. |journal=Arterioscler. Thromb. Vasc. Biol. |volume=24 |issue= 8 |pages= 1367-73 |year= 2005 |pmid= 15166009 |doi= 10.1161/01.ATV.0000133604.20182.cf }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on SP1... {October 3, 2007 10:45:55 PM PDT}
- AMBIGUITY: Did not locate an acceptable page to update. {October 3, 2007 10:46:35 PM PDT}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB = {{PDB2|1sp1}}, {{PDB2|1sp2}}, {{PDB2|1va1}}, {{PDB2|1va2}}, {{PDB2|1va3}}
| Name = Sp1 transcription factor
| HGNCid = 11205
| Symbol = SP1
| AltSymbols =;
| OMIM = 189906
| ECnumber =
| Homologene = 8276
| MGIid = 98372
| GeneAtlas_image1 = PBB_GE_SP1_214732_at_tn.png
<!-- The Following entry is a time stamp of the last bot update. It is typically hidden data -->
| DateOfBotUpdate = ~~~~~
| Function = {{GNF_GO|id=GO:0003690 |text = double-stranded DNA binding}} {{GNF_GO|id=GO:0003700 |text = transcription factor activity}} {{GNF_GO|id=GO:0003702 |text = RNA polymerase II transcription factor activity}} {{GNF_GO|id=GO:0008022 |text = protein C-terminus binding}} {{GNF_GO|id=GO:0008270 |text = zinc ion binding}} {{GNF_GO|id=GO:0016563 |text = transcription activator activity}} {{GNF_GO|id=GO:0042803 |text = protein homodimerization activity}} {{GNF_GO|id=GO:0043565 |text = sequence-specific DNA binding}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}}
| Component = {{GNF_GO|id=GO:0005622 |text = intracellular}} {{GNF_GO|id=GO:0005634 |text = nucleus}}
| Process = {{GNF_GO|id=GO:0006350 |text = transcription}} {{GNF_GO|id=GO:0045817 |text = positive regulation of global transcription from RNA polymerase II promoter}} {{GNF_GO|id=GO:0045893 |text = positive regulation of transcription, DNA-dependent}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 6667
| Hs_Ensembl = ENSG00000185591
| Hs_RefseqProtein = NP_612482
| Hs_RefseqmRNA = NM_138473
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 12
| Hs_GenLoc_start = 52060246
| Hs_GenLoc_end = 52096488
| Hs_Uniprot = P08047
| Mm_EntrezGene = 20683
| Mm_Ensembl = ENSMUSG00000001280
| Mm_RefseqmRNA = NM_013672
| Mm_RefseqProtein = NP_038700
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 15
| Mm_GenLoc_start = 102234414
| Mm_GenLoc_end = 102260419
| Mm_Uniprot = O89090
}}
}}
'''Sp1 transcription factor''', also known as '''SP1''', is a human [[gene]].
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text =
}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Tseng L, Gao J, Mazella J, ''et al.'' |title=Differentiation-dependent and cell-specific regulation of the hIGFBP-1 gene in human endometrium. |journal=Ann. N. Y. Acad. Sci. |volume=828 |issue= |pages= 27-37 |year= 1997 |pmid= 9329821 |doi= }}
*{{cite journal | author=Dyson N |title=The regulation of E2F by pRB-family proteins. |journal=Genes Dev. |volume=12 |issue= 15 |pages= 2245-62 |year= 1998 |pmid= 9694791 |doi= }}
*{{cite journal | author=Zhang Y, Dufau ML |title=Dual mechanisms of regulation of transcription of luteinizing hormone receptor gene by nuclear orphan receptors and histone deacetylase complexes. |journal=J. Steroid Biochem. Mol. Biol. |volume=85 |issue= 2-5 |pages= 401-14 |year= 2003 |pmid= 12943729 |doi= }}
*{{cite journal | author=Kino T, Pavlakis GN |title=Partner molecules of accessory protein Vpr of the human immunodeficiency virus type 1. |journal=DNA Cell Biol. |volume=23 |issue= 4 |pages= 193-205 |year= 2004 |pmid= 15142377 |doi= 10.1089/104454904773819789 }}
*{{cite journal | author=Seelamgari A, Maddukuri A, Berro R, ''et al.'' |title=Role of viral regulatory and accessory proteins in HIV-1 replication. |journal=Front. Biosci. |volume=9 |issue= |pages= 2388-413 |year= 2006 |pmid= 15353294 |doi= }}
*{{cite journal | author=Le Rouzic E, Benichou S |title=The Vpr protein from HIV-1: distinct roles along the viral life cycle. |journal=Retrovirology |volume=2 |issue= |pages= 11 |year= 2006 |pmid= 15725353 |doi= 10.1186/1742-4690-2-11 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on TERT... {October 3, 2007 10:46:35 PM PDT}
- AMBIGUITY: Did not locate an acceptable page to update. {October 3, 2007 10:47:16 PM PDT}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Telomerase reverse transcriptase
| HGNCid = 11730
| Symbol = TERT
| AltSymbols =; EST2; TCS1; TP2; TRT; hEST2
| OMIM = 187270
| ECnumber =
| Homologene = 31141
| MGIid = 1202709
| GeneAtlas_image1 = PBB_GE_TERT_207199_at_tn.png
<!-- The Following entry is a time stamp of the last bot update. It is typically hidden data -->
| DateOfBotUpdate = ~~~~~
| Function = {{GNF_GO|id=GO:0003677 |text = DNA binding}} {{GNF_GO|id=GO:0003721 |text = telomeric template RNA reverse transcriptase activity}} {{GNF_GO|id=GO:0003723 |text = RNA binding}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0016740 |text = transferase activity}} {{GNF_GO|id=GO:0042162 |text = telomeric DNA binding}}
| Component = {{GNF_GO|id=GO:0000781 |text = chromosome, telomeric region}} {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005694 |text = chromosome}} {{GNF_GO|id=GO:0005697 |text = telomerase holoenzyme complex}}
| Process = {{GNF_GO|id=GO:0000723 |text = telomere maintenance}} {{GNF_GO|id=GO:0006278 |text = RNA-dependent DNA replication}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 7015
| Hs_Ensembl = ENSG00000164362
| Hs_RefseqProtein = NP_937983
| Hs_RefseqmRNA = NM_198253
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 5
| Hs_GenLoc_start = 1306282
| Hs_GenLoc_end = 1348162
| Hs_Uniprot = O14746
| Mm_EntrezGene = 21752
| Mm_Ensembl = ENSMUSG00000021611
| Mm_RefseqmRNA = NM_009354
| Mm_RefseqProtein = NP_033380
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 13
| Mm_GenLoc_start = 74092992
| Mm_GenLoc_end = 74115843
| Mm_Uniprot = A0JNY9
}}
}}
'''Telomerase reverse transcriptase''', also known as '''TERT''', is a human [[gene]].
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = Telomerase is a ribonucleoprotein polymerase that maintains telomere ends by addition of the telomere repeat TTAGGG. The enzyme consists of a protein component with reverse transcriptase activity, encoded by this gene, and an RNA component which serves as a template for the telomere repeat. Telomerase expression plays a role in cellular senescence, as it is normally repressed in postnatal somatic cells resulting in progressive shortening of telomeres. Deregulation of telomerase expression in somatic cells may be involved in oncogenesis. Studies in mouse suggest that telomerase also participates in chromosomal repair, since de novo synthesis of telomere repeats may occur at double-stranded breaks. Alternatively spliced variants encoding different isoforms of telomerase reverse transcriptase have been identified; the full-length sequence of some variants has not been determined. Alternative splicing at this locus is thought to be one mechanism of regulation of telomerase activity.<ref>{{cite web | title = Entrez Gene: TERT telomerase reverse transcriptase| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7015| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Mattson MP, Fu W, Zhang P |title=Emerging roles for telomerase in regulating cell differentiation and survival: a neuroscientist's perspective. |journal=Mech. Ageing Dev. |volume=122 |issue= 7 |pages= 659-71 |year= 2001 |pmid= 11322991 |doi= }}
*{{cite journal | author=Castillo Ureta H, Barrera Saldaña HA, Martínez Rodríguez HG |title=[Telomerase: an enzyme with multiple applications in cancer research] |journal=Rev. Invest. Clin. |volume=54 |issue= 4 |pages= 342-8 |year= 2003 |pmid= 12415959 |doi= }}
*{{cite journal | author=Janknecht R |title=On the road to immortality: hTERT upregulation in cancer cells. |journal=FEBS Lett. |volume=564 |issue= 1-2 |pages= 9-13 |year= 2004 |pmid= 15094035 |doi= 10.1016/S0014-5793(04)00356-4 }}
*{{cite journal | author=Cristofari G, Sikora K, Lingner J |title=Telomerase unplugged. |journal=ACS Chem. Biol. |volume=2 |issue= 3 |pages= 155-8 |year= 2007 |pmid= 17373762 |doi= 10.1021/cb700037c }}
*{{cite journal | author=Beliveau A, Yaswen P |title=Soothing the watchman: telomerase reduces the p53-dependent cellular stress response. |journal=Cell Cycle |volume=6 |issue= 11 |pages= 1284-7 |year= 2007 |pmid= 17534147 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on TLR4... {October 3, 2007 10:47:16 PM PDT}
- AMBIGUITY: Did not locate an acceptable page to update. {October 3, 2007 10:47:56 PM PDT}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Toll-like receptor 4
| HGNCid = 11850
| Symbol = TLR4
| AltSymbols =; CD284; TOLL; hToll
| OMIM = 603030
| ECnumber =
| Homologene = 41317
| MGIid = 96824
| GeneAtlas_image1 = PBB_GE_TLR4_221060_s_at_tn.png
<!-- The Following entry is a time stamp of the last bot update. It is typically hidden data -->
| DateOfBotUpdate = ~~~~~
| Function = {{GNF_GO|id=GO:0001530 |text = lipopolysaccharide binding}} {{GNF_GO|id=GO:0004888 |text = transmembrane receptor activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}}
| Component = {{GNF_GO|id=GO:0005887 |text = integral to plasma membrane}} {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0046696 |text = lipopolysaccharide receptor complex}}
| Process = {{GNF_GO|id=GO:0006954 |text = inflammatory response}} {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0007250 |text = activation of NF-kappaB-inducing kinase}} {{GNF_GO|id=GO:0009617 |text = response to bacterium}} {{GNF_GO|id=GO:0016046 |text = detection of fungus}} {{GNF_GO|id=GO:0042088 |text = T-helper 1 type immune response}} {{GNF_GO|id=GO:0042116 |text = macrophage activation}} {{GNF_GO|id=GO:0043123 |text = positive regulation of I-kappaB kinase/NF-kappaB cascade}} {{GNF_GO|id=GO:0045084 |text = positive regulation of interleukin-12 biosynthetic process}} {{GNF_GO|id=GO:0045087 |text = innate immune response}} {{GNF_GO|id=GO:0045362 |text = positive regulation of interleukin-1 biosynthetic process}} {{GNF_GO|id=GO:0045368 |text = positive regulation of interleukin-13 biosynthetic process}} {{GNF_GO|id=GO:0045410 |text = positive regulation of interleukin-6 biosynthetic process}} {{GNF_GO|id=GO:0045576 |text = mast cell activation}} {{GNF_GO|id=GO:0045671 |text = negative regulation of osteoclast differentiation}} {{GNF_GO|id=GO:0046330 |text = positive regulation of JNK cascade}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 7099
| Hs_Ensembl = ENSG00000136869
| Hs_RefseqProtein = NP_612564
| Hs_RefseqmRNA = NM_138554
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 9
| Hs_GenLoc_start = 119506405
| Hs_GenLoc_end = 119518970
| Hs_Uniprot = O00206
| Mm_EntrezGene = 21898
| Mm_Ensembl = ENSMUSG00000039005
| Mm_RefseqmRNA = NM_021297
| Mm_RefseqProtein = NP_067272
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 4
| Mm_GenLoc_start = 66313972
| Mm_GenLoc_end = 66328954
| Mm_Uniprot = Q3U4D4
}}
}}
'''Toll-like receptor 4''', also known as '''TLR4''', is a human [[gene]].
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = The protein encoded by this gene is a member of the Toll-like receptor (TLR) family which plays a fundamental role in pathogen recognition and activation of innate immunity. TLRs are highly conserved from Drosophila to humans and share structural and functional similarities. They recognize pathogen-associated molecular patterns (PAMPs) that are expressed on infectious agents, and mediate the production of cytokines necessary for the development of effective immunity. The various TLRs exhibit different patterns of expression. This receptor is most abundantly expressed in placenta, and in myelomonocytic subpopulation of the leukocytes. It has been implicated in signal transduction events induced by lipopolysaccharide (LPS) found in most gram-negative bacteria. Mutations in this gene have been associated with differences in LPS responsiveness. Also, several transcript variants of this gene have been found, but the protein coding potential of most of them is uncertain.<ref>{{cite web | title = Entrez Gene: TLR4 toll-like receptor 4| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7099| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Lien E, Ingalls RR |title=Toll-like receptors. |journal=Crit. Care Med. |volume=30 |issue= 1 Suppl |pages= S1-11 |year= 2002 |pmid= 11782555 |doi= }}
*{{cite journal | author=Raetz CR, Whitfield C |title=Lipopolysaccharide endotoxins. |journal=Annu. Rev. Biochem. |volume=71 |issue= |pages= 635-700 |year= 2002 |pmid= 12045108 |doi= 10.1146/annurev.biochem.71.110601.135414 }}
*{{cite journal | author=Lin WJ, Yeh WC |title=Implication of Toll-like receptor and tumor necrosis factor alpha signaling in septic shock. |journal=Shock |volume=24 |issue= 3 |pages= 206-9 |year= 2005 |pmid= 16135957 |doi= }}
*{{cite journal | author=Lorenz E |title=TLR2 and TLR4 expression during bacterial infections. |journal=Curr. Pharm. Des. |volume=12 |issue= 32 |pages= 4185-93 |year= 2007 |pmid= 17100621 |doi= }}
*{{cite journal | author=Stoll LL, Denning GM, Weintraub NL |title=Endotoxin, TLR4 signaling and vascular inflammation: potential therapeutic targets in cardiovascular disease. |journal=Curr. Pharm. Des. |volume=12 |issue= 32 |pages= 4229-45 |year= 2007 |pmid= 17100625 |doi= }}
*{{cite journal | author=Rousseaux C, Desreumaux P |title=[The peroxisome-proliferator-activated gamma receptor and chronic inflammatory bowel disease (PPARgamma and IBD)] |journal=J. Soc. Biol. |volume=200 |issue= 2 |pages= 121-31 |year= 2007 |pmid= 17151549 |doi= }}
*{{cite journal | author=Szabo G, Dolganiuc A, Dai Q, Pruett SB |title=TLR4, ethanol, and lipid rafts: a new mechanism of ethanol action with implications for other receptor-mediated effects. |journal=J. Immunol. |volume=178 |issue= 3 |pages= 1243-9 |year= 2007 |pmid= 17237368 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on VWF... {October 3, 2007 10:47:56 PM PDT}
- AMBIGUITY: Did not locate an acceptable page to update. {October 3, 2007 10:48:36 PM PDT}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB = {{PDB2|1ao3}}, {{PDB2|1atz}}, {{PDB2|1auq}}, {{PDB2|1fe8}}, {{PDB2|1fns}}, {{PDB2|1ijb}}, {{PDB2|1ijk}}, {{PDB2|1m10}}, {{PDB2|1oak}}, {{PDB2|1sq0}}, {{PDB2|1u0n}}, {{PDB2|1uex}}, {{PDB2|2adf}}
| Name = Von Willebrand factor
| HGNCid = 12726
| Symbol = VWF
| AltSymbols =; F8VWF; VWD
| OMIM = 193400
| ECnumber =
| Homologene = 466
| MGIid = 98941
| GeneAtlas_image1 = PBB_GE_VWF_202112_at_tn.png
<!-- The Following entry is a time stamp of the last bot update. It is typically hidden data -->
| DateOfBotUpdate = ~~~~~
| Function = {{GNF_GO|id=GO:0002020 |text = protease binding}} {{GNF_GO|id=GO:0005515 |text = protein binding}}
| Component = {{GNF_GO|id=GO:0005576 |text = extracellular region}} {{GNF_GO|id=GO:0005578 |text = proteinaceous extracellular matrix}}
| Process = {{GNF_GO|id=GO:0007155 |text = cell adhesion}} {{GNF_GO|id=GO:0009611 |text = response to wounding}} {{GNF_GO|id=GO:0030168 |text = platelet activation}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 7450
| Hs_Ensembl = ENSG00000110799
| Hs_RefseqProtein = NP_000543
| Hs_RefseqmRNA = NM_000552
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 12
| Hs_GenLoc_start = 5928308
| Hs_GenLoc_end = 6104097
| Hs_Uniprot = P04275
| Mm_EntrezGene = 22371
| Mm_Ensembl = ENSMUSG00000001930
| Mm_RefseqmRNA = NM_011708
| Mm_RefseqProtein = NP_035838
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 6
| Mm_GenLoc_start = 125512595
| Mm_GenLoc_end = 125652158
| Mm_Uniprot = Q2I0J7
}}
}}
'''Von Willebrand factor''', also known as '''VWF''', is a human [[gene]].
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = The glycoprotein encoded by this gene functions as both an antihemophilic factor carrier and a platelet-vessel wall mediator in the blood coagulation system. It is crucial to the hemostasis process. Mutations in this gene or deficiencies in this protein result in von Willebrand's disease. An unprocessed pseudogene has been found on chromosome 22.<ref>{{cite web | title = Entrez Gene: VWF von Willebrand factor| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7450| accessdate = }}</ref>
}}
==References==
{{reflist}}
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
}}
{{refend}}
{{protein-stub}}
end log.
