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Q8N2W9

- PIAS4_HUMAN

UniProt

Q8N2W9 - PIAS4_HUMAN

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Protein
E3 SUMO-protein ligase PIAS4
Gene
PIAS4, PIASG
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Functions as an E3-type small ubiquitin-like modifier (SUMO) ligase, stabilizing the interaction between UBE2I and the substrate, and as a SUMO-tethering factor. Plays a crucial role as a transcriptional coregulation in various cellular pathways, including the STAT pathway, the p53/TP53 pathway, the Wnt pathway and the steroid hormone signaling pathway. Involved in gene silencing. Mediates sumoylation of CEBPA, PARK7, HERC2, MYB, TCF4 and RNF168. In Wnt signaling, represses LEF1 and enhances TCF4 transcriptional activities through promoting their sumoylations.6 Publications

Pathwayi

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri311 – 38878SP-RING-type
Add
BLAST

GO - Molecular functioni

  1. DNA binding Source: UniProtKB-KW
  2. SUMO ligase activity Source: UniProtKB
  3. protein binding Source: UniProtKB
  4. ubiquitin protein ligase binding Source: BHF-UCL
  5. zinc ion binding Source: UniProtKB

GO - Biological processi

  1. Wnt signaling pathway Source: UniProtKB-KW
  2. negative regulation of NF-kappaB transcription factor activity Source: Ensembl
  3. negative regulation of transcription from RNA polymerase II promoter Source: Ensembl
  4. negative regulation of transcription, DNA-templated Source: UniProtKB
  5. positive regulation of intrinsic apoptotic signaling pathway in response to DNA damage Source: Ensembl
  6. positive regulation of keratinocyte apoptotic process Source: BHF-UCL
  7. positive regulation of protein sumoylation Source: UniProtKB
  8. protein sumoylation Source: UniProtKB
  9. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Ligase, Repressor

Keywords - Biological processi

Transcription, Transcription regulation, Ubl conjugation pathway, Wnt signaling pathway

Keywords - Ligandi

DNA-binding, Metal-binding, Zinc

Enzyme and pathway databases

SignaLinkiQ8N2W9.
UniPathwayiUPA00886.

Names & Taxonomyi

Protein namesi
Recommended name:
E3 SUMO-protein ligase PIAS4 (EC:6.3.2.-)
Alternative name(s):
PIASy
Protein inhibitor of activated STAT protein 4
Protein inhibitor of activated STAT protein gamma
Short name:
PIAS-gamma
Gene namesi
Name:PIAS4
Synonyms:PIASG
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 19

Organism-specific databases

HGNCiHGNC:17002. PIAS4.

Subcellular locationi

NucleusPML body
Note: Colocalizes with SUMO1 and TCF7L2/TCF4 and LEF1 in a subset of PML (promyelocytic leukemia) nuclear bodies.3 Publications

GO - Cellular componenti

  1. PML body Source: UniProtKB-SubCell
  2. cytoplasm Source: BHF-UCL
  3. nuclear matrix Source: Ensembl
  4. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi23 – 242LL → AA: Loss of repression of AR- and STAT1-induced transcription; no effect on AR- and STAT1-binding. 2 Publications
Mutagenesisi35 – 351K → R: Complete loss of sumoylation. No enhancement of TCF4 sumoylation. No effect on interaction with TCF4. Colocalizes with SUMO1 in nucleus but concentrated into nuclear granules. 4 Publications
Mutagenesisi128 – 1281K → R: Some loss of sumoylation. 4 Publications
Mutagenesisi342 – 3421C → A: Inhibits TCF4 sumoylation. Inhibits beta-catenin-mediated TCF7L2/TCF4 activity. No colocalization with TCF7L2/TCF4 in nuclear punctate structures; when associated with A-347. 2 Publications
Mutagenesisi347 – 3471C → A: Inhibits TCF4 sumoylation. Inhibits beta-catenin-mediated TCF7L2/TCF4 activity. No colocalization with TCF7L2/TCF4 in nuclear punctate structures; when associated with A-342. AR- and STAT1-binding. 2 Publications

Organism-specific databases

PharmGKBiPA134945903.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 510509E3 SUMO-protein ligase PIAS4
PRO_0000218982Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication
Cross-linki35 – 35Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)1 Publication
Modified residuei114 – 1141N6-acetyllysine1 Publication
Cross-linki128 – 128Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)1 Publication

Post-translational modificationi

Sumoylated. Lys-35 is the main site of sumoylation. Sumoylation is required for TCF4 sumoylation and transcriptional activation. Represses LEF1 transcriptional activity. SUMO1 is the preferred conjugate.1 Publication

Keywords - PTMi

Acetylation, Isopeptide bond, Ubl conjugation

Proteomic databases

MaxQBiQ8N2W9.
PaxDbiQ8N2W9.
PRIDEiQ8N2W9.

PTM databases

PhosphoSiteiQ8N2W9.

Expressioni

Tissue specificityi

Highly expressed in testis and, at lower levels, in spleen, prostate, ovary, colon and peripheral blood leukocytes.1 Publication

Gene expression databases

ArrayExpressiQ8N2W9.
BgeeiQ8N2W9.
CleanExiHS_PIAS4.
GenevestigatoriQ8N2W9.

Organism-specific databases

HPAiHPA010598.

Interactioni

Subunit structurei

Interacts with AR, AXIN1, GATA2, LEF1, TP53 and STAT1 (IFNG-induced). Binds to AT-rich DNA sequences, known as matrix or scaffold attachment regions (MARs/SARs) By similarity. Interacts with TICAM1. Interacts with KLF8; the interaction results in SUMO ligation and repression of KLF8 transcriptional activity and of its cell cycle progression into G1 phase.7 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
HIF1AQ166653EBI-473160,EBI-447269
HTTP428583EBI-473160,EBI-466029
PARP1P098745EBI-473160,EBI-355676
SUMO2P619563EBI-473160,EBI-473220
TADA3O755282EBI-473160,EBI-473249
TP53P046372EBI-473160,EBI-366083

Protein-protein interaction databases

BioGridi119624. 87 interactions.
IntActiQ8N2W9. 55 interactions.
MINTiMINT-1181821.
STRINGi9606.ENSP00000262971.

Structurei

3D structure databases

ProteinModelPortali