Members of the PIAS family act as SUMO ligases for c-Jun and p53 and repress p53 activity - Test2 - elhamkhani - TriplyDB

Members of the PIAS family act as SUMO ligases for c-Jun and p53 and repress p53 activity

Members of the PIAS family act as SUMO ligases for c-Jun and p53 and repress p53 activity

http://www.wikidata.org/entity/Q24531180

about

NMR structure of the N-terminal domain of SUMO ligase PIAS1 and its interaction with tumor suppressor p53 and A/T-rich DNA oligomers PIASy stimulates HIF1α SUMOylation and negatively regulates HIF1α activity in response to hypoxia The SUMO system controls nucleolar partitioning of a novel mammalian ribosome biogenesis complex Sumoylation delays the ATF7 transcription factor subcellular localization and inhibits its transcriptional activity The interaction of Piasy with Trim32, an E3-ubiquitin ligase mutated in limb-girdle muscular dystrophy type 2H, promotes Piasy degradation and regulates UVB-induced keratinocyte apoptosis through NFkappaB Modification of de novo DNA methyltransferase 3a (Dnmt3a) by SUMO-1 modulates its interaction with histone deacetylases (HDACs) and its capacity to repress transcription The SUMO E3-ligase PIAS1 regulates the tumor suppressor PML and its oncogenic counterpart PML-RARA The cell death regulator GRIM-19 is an inhibitor of signal transducer and activator of transcription 3 Small ubiquitin-like modifier-2 modification of retinoic acid receptor-alpha regulates its subcellular localization and transcriptional activity The nucleolar SUMO-specific protease SENP3 reverses SUMO modification of nucleophosmin and is required for rRNA processing Impaired endocytosis of the ion channel TRPM4 is associated with human progressive familial heart block type I MDA5 is SUMOylated by PIAS2β in the upregulation of type I interferon signaling Regulation of MEF2 by histone deacetylase 4- and SIRT1 deacetylase-mediated lysine modifications.Sumoylation of the zinc finger protein ZXDC enhances the function of its transcriptional activation domain Down-regulation of c-Fos/c-Jun AP-1 dimer activity by sumoylation.The negative regulator of Gli, Suppressor of fused (Sufu), interacts with SAP18, Galectin3 and other nuclear proteins Modification with SUMO. A role in transcriptional regulation Physical and functional interactions of histone deacetylase 3 with TFII-I family proteins and PIASxbeta.PIAS-1 is a checkpoint regulator which affects exit from G1 and G2 by sumoylation of p73 Protein inhibitor of activated STAT Y (PIASy) and a splice variant lacking exon 6 enhance sumoylation but are not essential for embryogenesis and adult life Interaction of protein inhibitor of activated STAT (PIAS) proteins with the TATA-binding protein, TBP SUMO modification of a novel MAR-binding protein, SATB2, modulates immunoglobulin mu gene expression PIAS3 promotes homology‑directed repair and distal non‑homologous end joining Activation of Smad transcriptional activity by protein inhibitor of activated STAT3 (PIAS3)hZimp10 is an androgen receptor co-activator and forms a complex with SUMO-1 at replication foci Structure of the Siz/PIAS SUMO E3 ligase Siz1 and determinants required for SUMO modification of PCNA Sumoylation is involved in beta-catenin-dependent activation of Tcf-4 Nuclear translocation of an ICA512 cytosolic fragment couples granule exocytosis and insulin expression in {beta}-cells The novel PIAS-like protein hZimp10 is a transcriptional co-activator of the p53 tumor suppressor Phosphorylation of serine 303 is a prerequisite for the stress-inducible SUMO modification of heat shock factor 1 Mapping the SUMOylated landscape The genetics of the p53 pathway, apoptosis and cancer therapy.Mechanisms, regulation and consequences of protein SUMOylation p14 Arf promotes small ubiquitin-like modifier conjugation of Werners helicase Synergy of glucose and growth hormone signalling in islet cells through ICA512 and STAT5 Sumoylation of MITF and its related family members TFE3 and TFEB MDM2 promotes SUMO-2/3 modification of p53 to modulate transcriptional activity The RanBP2 SUMO E3 ligase is neither HECT- nor RING-type Characterization of human constitutive photomorphogenesis protein 1, a RING finger ubiquitin ligase that interacts with Jun transcription factors and modulates their transcriptional activity The 'PINIT' motif, of a newly identified conserved domain of the PIAS protein family, is essential for nuclear retention of PIAS3L

P2860

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P2860

Members of the PIAS family act as SUMO ligases for c-Jun and p53 and repress p53 activity

http://www.wikidata.org/entity/Q24531180

description

2002 nî lūn-bûn

@nan

2002 թուականի Փետրուարին հրատարակուած գիտական յօդուած

@hyw

2002 թվականի փետրվարին հրատարակված գիտական հոդված

@hy

2002年の論文

@ja

2002年論文

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2002年論文

@zh-hant

2002年論文

@zh-hk

2002年論文

@zh-mo

2002年論文

@zh-tw

2002年论文

@wuu

name

Members of the PIAS family act as SUMO ligases for c-Jun and p53 and repress p53 activity

@ast

Members of the PIAS family act as SUMO ligases for c-Jun and p53 and repress p53 activity

@en

Members of the PIAS family act as SUMO ligases for c-Jun and p53 and repress p53 activity

@en-gb

Members of the PIAS family act as SUMO ligases for c-Jun and p53 and repress p53 activity

@nl

type

label

Members of the PIAS family act as SUMO ligases for c-Jun and p53 and repress p53 activity

@ast

Members of the PIAS family act as SUMO ligases for c-Jun and p53 and repress p53 activity

@en

Members of the PIAS family act as SUMO ligases for c-Jun and p53 and repress p53 activity

@en-gb

Members of the PIAS family act as SUMO ligases for c-Jun and p53 and repress p53 activity

@nl

prefLabel

Members of the PIAS family act as SUMO ligases for c-Jun and p53 and repress p53 activity

@ast

Members of the PIAS family act as SUMO ligases for c-Jun and p53 and repress p53 activity

@en

Members of the PIAS family act as SUMO ligases for c-Jun and p53 and repress p53 activity

@en-gb

Members of the PIAS family act as SUMO ligases for c-Jun and p53 and repress p53 activity

@nl

P1433

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P2860

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P1433

Proceedings of the National Academy of Sciences of the United States of America

P1476

Members of the PIAS family act as SUMO ligases for c-Jun and p53 and repress p53 activity

@en

P2093

Darja Schmidt

http://www.w3.org/2001/XMLSchema#string

Stefan Müller

http://www.w3.org/2001/XMLSchema#string

P2860

The zinc finger protein Gfi-1 can enhance STAT3 signaling by interacting with the STAT3 inhibitor PIAS3

A putative protein inhibitor of activated STAT (PIASy) interacts with p53 and inhibits p53-mediated transactivation but not apoptosis

Inhibition of Stat1-mediated gene activation by PIAS1

SUMO-1 modification activates the transcriptional response of p53

A novel factor required for the SUMO1/Smt3 conjugation of yeast septins.

Yeast Ull1/Siz1 is a novel SUMO1/Smt3 ligase for septin components and functions as an adaptor between conjugating enzyme and substrates.

Miz1, a novel zinc finger transcription factor that interacts with Msx2 and enhances its affinity for DNA

Activation of p53 by conjugation to the ubiquitin-like protein SUMO-1.

MBP1: a novel mutant p53-specific protein partner with oncogenic properties

RING finger proteins: mediators of ubiquitin ligase activity

P304

2872-2877

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scholarly article

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10.1073/PNAS.052559499

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P433

5

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P478

99

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2002-02-26T00:00:00Z

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11493949

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P698

11867732

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122440

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