(Q34333425)

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The tumor suppressor protein p16(INK4a) and the human papillomavirus oncoprotein-58 E7 are naturally occurring lysine-less proteins that are degraded by the ubiquitin system. Direct evidence for ubiquitination at the N-terminal residue

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Europe PubMed Central

PubMed publication ID

1 August 2017

The tumor suppressor protein p16(INK4a) and the human papillomavirus oncoprotein-58 E7 are naturally occurring lysine-less proteins that are degraded by the ubiquitin system. Direct evidence for ubiquitination at the N-terminal residue (English)

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Europe PubMed Central

PubMed publication ID

1 August 2017

protein ubiquitination

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based on heuristic

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Aaron Ciechanover

6

object named as

Aaron Ciechanover

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Europe PubMed Central

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1 August 2017

author name string

Ronen Ben-Saadon

1

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Europe PubMed Central

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1 August 2017

Ifat Fajerman

2

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Europe PubMed Central

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1 August 2017

Tamar Ziv

3

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Europe PubMed Central

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1 August 2017

Ulf Hellman

4

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Europe PubMed Central

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1 August 2017

Alan L Schwartz

5

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1 August 2017

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publication date

14 July 2004

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Europe PubMed Central

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1 August 2017

Journal of Biological Chemistry

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1 August 2017

279

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Europe PubMed Central

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1 August 2017

40

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Europe PubMed Central

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1 August 2017

41414-41421

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Europe PubMed Central

PubMed publication ID

1 August 2017

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A novel site for ubiquitination: the N-terminal residue, and not internal lysines of MyoD, is essential for conjugation and degradation of the protein.

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Degradation of the epstein-barr virus latent membrane protein 1 (LMP1) by the ubiquitin-proteasome pathway. Targeting via ubiquitination of the N-terminal residue

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Isopeptide linkage between nonhistone and histone 2A polypeptides of chromosomal conjugate-protein A24

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Ubiquitin-Proteasome-mediated degradation of Id1 is modulated by MyoD.

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Principles of tumor suppression

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Ubiquitin/proteasome-mediated degradation of p19INK4d determines its periodic expression during the cell cycle

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Lysine-independent ubiquitination of Epstein-Barr virus LMP2A.

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Opposite regulation of the expression of cyclin-dependent kinase inhibitors during contact inhibition

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Phosphorylation of p16INK4A correlates with Cdk4 association

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Control of Smad7 stability by competition between acetylation and ubiquitination

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Direct binding of CDC20 protein family members activates the anaphase-promoting complex in mitosis and G1

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p16INK4 mediates contact-inhibition of growth

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N-Terminal ubiquitination of extracellular signal-regulated kinase 3 and p21 directs their degradation by the proteasome

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Degradation of the E7 human papillomavirus oncoprotein by the ubiquitin-proteasome system: targeting via ubiquitination of the N-terminal residue

1 reference

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Papillomaviruses and cancer: from basic studies to clinical application

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p53 mediates density-dependent growth arrest.

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N-terminal ubiquitination: more protein substrates join in.

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Proteasome-mediated degradation of p21 via N-terminal ubiquitinylation.

1 reference

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A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding

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Proteasomal turnover of p21Cip1 does not require p21Cip1 ubiquitination

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Identifiers

10.1074/JBC.M407201200

1 reference

Europe PubMed Central

PubMed publication ID

1 August 2017

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

1 August 2017

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