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UniProtKB - O75925 (PIAS1_HUMAN)

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Protein

E3 SUMO-protein ligase PIAS1

Gene

PIAS1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -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 pathway and the steroid hormone signaling pathway. In vitro, binds A/T-rich DNA. The effects of this transcriptional coregulation, transactivation or silencing, may vary depending upon the biological context. Together with PRMT1, may repress STAT1 transcriptional activity, in the late phase of interferon gamma (IFN-gamma) signaling. Sumoylates PML (at'Lys-65' and 'Lys-160') and PML-RAR and promotes their ubiquitin-mediated degradation. PIAS1-mediated sumoylation of PML promotes its interaction with CSNK2A1/CK2 which in turn promotes PML phosphorylation and degradation (By similarity). Enhances the sumoylation of MTA1 and may participate in its paralog-selective sumoylation. Plays a dynamic role in adipogenesis by promoting the SUMOylation and degradation of CEBPB (By similarity).By similarity3 Publications

Pathwayi: protein sumoylation

This protein is involved in the pathway protein sumoylation, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein sumoylation and in Protein modification.

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri320 – 397SP-RING-typePROSITE-ProRule annotationAdd BLAST78

GO - Molecular functioni

  • androgen receptor binding Source: UniProtKB
  • DNA binding Source: UniProtKB-KW
  • enzyme binding Source: UniProtKB
  • protein C-terminus binding Source: Ensembl
  • protein domain specific binding Source: Ensembl
  • SUMO ligase activity Source: BHF-UCL
  • SUMO transferase activity Source: Reactome
  • transcription coactivator activity Source: UniProtKB
  • transcription corepressor activity Source: ProtInc
  • ubiquitin protein ligase binding Source: Ensembl
  • zinc ion binding Source: InterPro
View the complete GO annotation on QuickGO ...

GO - Biological processi

View the complete GO annotation on QuickGO ...

Keywordsi

Molecular functionDNA-binding, Transferase
Biological processTranscription, Transcription regulation, Ubl conjugation pathway
LigandMetal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-HSA-3108214 SUMOylation of DNA damage response and repair proteins
R-HSA-3232118 SUMOylation of transcription factors
R-HSA-4551638 SUMOylation of chromatin organization proteins
R-HSA-5696395 Formation of Incision Complex in GG-NER
R-HSA-877312 Regulation of IFNG signaling
SignaLinkiO75925
SIGNORiO75925
UniPathwayiUPA00886

Names & Taxonomyi

Protein namesi
Recommended name:
E3 SUMO-protein ligase PIAS1 (EC:2.3.2.-)
Alternative name(s):
DEAD/H box-binding protein 1
E3 SUMO-protein transferase PIAS1Curated
Gu-binding protein
Short name:
GBP
Protein inhibitor of activated STAT protein 1
RNA helicase II-binding protein
Gene namesi
Name:PIAS1
Synonyms:DDXBP1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
Proteomesi
  • UP000005640 Componenti: Chromosome 15

Organism-specific databases

EuPathDBiHostDB:ENSG00000033800.13
HGNCiHGNC:2752 PIAS1
MIMi603566 gene
neXtProtiNX_O75925

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi303R → K: Partial loss of repression on STAT1 transcriptional activity. 1 Publication1
Mutagenesisi351C → A or S: Loss of UBE2I-binding; almost complete loss of promotion of TP53 sumoylation; no loss of SUMO1- and TP53-binding. 1 Publication1

Organism-specific databases

DisGeNETi8554
OpenTargetsiENSG00000033800
PharmGKBiPA33285

Polymorphism and mutation databases

BioMutaiPIAS1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources
ChainiPRO_00002189742 – 651E3 SUMO-protein ligase PIAS1Add BLAST650

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineCombined sources1
Cross-linki40Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki46Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki137Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki238Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei303Asymmetric dimethylarginine; by PRMT11 Publication1
Cross-linki453Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei467PhosphoserineCombined sources1
Modified residuei468PhosphoserineCombined sources1
Modified residuei483PhosphoserineBy similarity1
Modified residuei485PhosphoserineCombined sources1
Modified residuei487PhosphothreonineBy similarity1
Modified residuei488PhosphoserineCombined sources1
Cross-linki493Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei503PhosphoserineCombined sources1
Modified residuei510PhosphoserineCombined sources1
Modified residuei522PhosphoserineCombined sources1

Post-translational modificationi

Sumoylated.2 Publications
Dimethylated by PRMT1 at Arg-303 in the late phase of interferon gamma (IFN-gamma) signaling, leading to preferential interaction with STAT1 and thus resulting in release of STAT1 from its target gene.

Keywords - PTMi

Acetylation, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiO75925
MaxQBiO75925
PaxDbiO75925
PeptideAtlasiO75925
PRIDEiO75925
ProteomicsDBi50293

PTM databases

iPTMnetiO75925
PhosphoSitePlusiO75925

Miscellaneous databases

PMAP-CutDBiO75925

Expressioni

Tissue specificityi

Expressed in numerous tissues with highest level in testis.2 Publications

Gene expression databases

BgeeiENSG00000033800
CleanExiHS_PIAS1
ExpressionAtlasiO75925 baseline and differential
GenevisibleiO75925 HS

Organism-specific databases

HPAiCAB012304
HPA005743

Interactioni

Subunit structurei

Interacts with NCOA2 and AR. Interacts with NR2C1; the interaction promotes its sumoylation (By similarity). Interacts with DDX21, CSRP2, AXIN1, JUN, UBE2I, SUMO1, SATB2, PLAG1, TP53 and STAT1 (dimer), following IFNA1-stimulation. Interacts with SP3 (preferentially when SUMO-modified). Interacts with KLF8; the interaction results in SUMO ligation and repression of KLF8 transcriptional activity and of its cell cycle progression into G1 phase. Interacts with STAT1. Interacts with CHUK/IKKA; this interaction induces PIAS1 phosphorylation. Interacts with PTK2/FAK1; the interaction promotes its sumoylation. Interacts with DDX5. Interacts with PML (By similarity). Interacts with MTA1.By similarity16 Publications

Binary interactionsi

Show more details

GO - Molecular functioni

  • androgen receptor binding Source: UniProtKB
  • enzyme binding Source: UniProtKB
  • protein C-terminus binding Source: Ensembl
  • protein domain specific binding Source: Ensembl
  • ubiquitin protein ligase binding Source: Ensembl
View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGridi114124, 104 interactors
DIPiDIP-5970N
ELMiO75925
IntActiO75925, 51 interactors
MINTiO75925
STRINGi9606.ENSP00000249636

Structurei

Secondary structure

1651
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi6 – 11Combined sources6
Helixi16 – 24Combined sources9
Helixi34 – 46Combined sources13
Helixi51 – 63Combined sources13

3D structure databases

ProteinModelPortaliO75925
SMRiO75925
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO75925

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini11 – 45SAPPROSITE-ProRule annotationAdd BLAST35
Domaini124 – 288PINITPROSITE-ProRule annotationAdd BLAST165
Repeati520 – 52314
Repeati557 – 56024
Repeati598 – 6013; approximate4
Repeati612 – 6154; approximate4

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni462 – 473SUMO1-bindingBy similarityAdd BLAST12
Regioni520 – 6154 X 4 AA repeats of N-T-S-LAdd BLAST96

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi19 – 23LXXLL motif5
Motifi56 – 64Nuclear localization signalSequence analysis9
Motifi368 – 380Nuclear localization signalSequence analysisAdd BLAST13

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi577 – 634Ser-richAdd BLAST58

Domaini

The LXXLL motif is a transcriptional coregulator signature.
The SP-RING-type domain is required for promoting EKLF sumoylation.By similarity

Sequence similaritiesi

Belongs to the PIAS family.Curated

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri320 – 397SP-RING-typePROSITE-ProRule annotationAdd BLAST78

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiKOG2169 Eukaryota
ENOG410XQ2E LUCA
GeneTreeiENSGT00550000074410
HOGENOMiHOG000230594
HOVERGENiHBG053598
InParanoidiO75925
KOiK04706
OMAiGRTYSMA
OrthoDBiEOG091G08G5
PhylomeDBiO75925
TreeFamiTF323787

Family and domain databases

Gene3Di1.10.720.30, 1 hit
2.60.120.780, 1 hit
3.30.40.10, 1 hit
InterProiView protein in InterPro
IPR023321 PINIT
IPR038654 PINIT_sf
IPR003034 SAP_dom
IPR036361 SAP_dom_sf
IPR004181 Znf_MIZ
IPR013083 Znf_RING/FYVE/PHD
PfamiView protein in Pfam
PF14324 PINIT, 1 hit
PF02891 zf-MIZ, 1 hit
SMARTiView protein in SMART
SM00513 SAP, 1 hit
SUPFAMiSSF68906 SSF68906, 1 hit
PROSITEiView protein in PROSITE
PS51466 PINIT, 1 hit
PS50800 SAP, 1 hit
PS51044 ZF_SP_RING, 1 hit

Sequences (3)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: O75925-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MADSAELKQM VMSLRVSELQ VLLGYAGRNK HGRKHELLTK ALHLLKAGCS 
        60         70         80         90        100
PAVQMKIKEL YRRRFPQKIM TPADLSIPNV HSSPMPATLS PSTIPQLTYD 
       110        120        130        140        150
GHPASSPLLP VSLLGPKHEL ELPHLTSALH PVHPDIKLQK LPFYDLLDEL 
       160        170        180        190        200
IKPTSLASDN SQRFRETCFA FALTPQQVQQ ISSSMDISGT KCDFTVQVQL 
       210        220        230        240        250
RFCLSETSCP QEDHFPPNLC VKVNTKPCSL PGYLPPTKNG VEPKRPSRPI 
       260        270        280        290        300
NITSLVRLST TVPNTIVVSW TAEIGRNYSM AVYLVKQLSS TVLLQRLRAK 
       310        320        330        340        350
GIRNPDHSRA LIKEKLTADP DSEIATTSLR VSLLCPLGKM RLTIPCRALT 
       360        370        380        390        400
CSHLQCFDAT LYIQMNEKKP TWVCPVCDKK APYEHLIIDG LFMEILKYCT 
       410        420        430        440        450
DCDEIQFKED GTWAPMRSKK EVQEVSASYN GVDGCLSSTL EHQVASHHQS 
       460        470        480        490        500
SNKNKKVEVI DLTIDSSSDE EEEEPSAKRT CPSLSPTSPL NNKGILSLPH 
       510        520        530        540        550
QASPVSRTPS LPAVDTSYIN TSLIQDYRHP FHMTPMPYDL QGLDFFPFLS 
       560        570        580        590        600
GDNQHYNTSL LAAAAAAVSD DQDLLHSSRF FPYTSSQMFL DQLSAGGSTS 
       610        620        630        640        650
LPTTNGSSSG SNSSLVSSNS LRESHSHTVT NRSSTDTASI FGIIPDIISL 

D
Length:651
Mass (Da):71,836
Last modified:March 5, 2002 - v2
Checksum:iAA69338221124119
GO
Isoform 2 (identifier: O75925-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-7: MADSAEL → MFTLQDSYV

Note: No experimental confirmation available.
Show »
Length:653
Mass (Da):72,203
Checksum:i585370DA0FBDC926
GO
Isoform 3 (identifier: O75925-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     312-325: IKEKLTADPDSEIA → STYDKLISLIQLFC
     326-651: Missing.

Show »
Length:325
Mass (Da):36,204
Checksum:iF0A265377BDCADC2
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti119E → K in AAC36702 (PubMed:9724754).Curated1
Sequence conflicti266 – 268IVV → MC in AAC36702 (PubMed:9724754).Curated3
Sequence conflicti613S → T in AAB58488 (PubMed:15489334).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0562191 – 7MADSAEL → MFTLQDSYV in isoform 2. 1 Publication7
Alternative sequenceiVSP_057195312 – 325IKEKL…DSEIA → STYDKLISLIQLFC in isoform 3. 1 PublicationAdd BLAST14
Alternative sequenceiVSP_057196326 – 651Missing in isoform 3. 1 PublicationAdd BLAST326

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF077951 mRNA Translation: AAC36702.1
AF167160 mRNA Translation: AAD49722.1
FJ997900 mRNA Translation: ACR77525.1
AK094641 mRNA Translation: BAG52901.1
AK314515 mRNA Translation: BAG37114.1
AC107871 Genomic DNA No translation available.
AC135628 Genomic DNA No translation available.
BC118587 mRNA Translation: AAI18588.1
BC121797 mRNA Translation: AAI21798.1
U78524 mRNA Translation: AAB58488.1
CCDSiCCDS45290.1 [O75925-1]
CCDS81902.1 [O75925-2]
RefSeqiNP_001307616.1, NM_001320687.1 [O75925-2]
NP_057250.1, NM_016166.2 [O75925-1]
XP_016878177.1, XM_017022688.1 [O75925-2]
UniGeneiHs.162458
Hs.694796

Genome annotation databases

EnsembliENST00000249636; ENSP00000249636; ENSG00000033800 [O75925-1]
ENST00000545237; ENSP00000438574; ENSG00000033800 [O75925-2]
GeneIDi8554
KEGGihsa:8554
UCSCiuc002aqz.4 human [O75925-1]

Keywords - Coding sequence diversityi

Alternative splicing

Similar proteinsi

Entry informationi

Entry nameiPIAS1_HUMAN
AccessioniPrimary (citable) accession number: O75925
Secondary accession number(s): B2RB67
, B3KSY9, C5J4B4, Q147X4, Q99751, Q9UN02
Entry historyiIntegrated into UniProtKB/Swiss-Prot: March 5, 2002
Last sequence update: March 5, 2002
Last modified: June 20, 2018
This is version 182 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 15
    Human chromosome 15: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  5. SIMILARITY comments
    Index of protein domains and families

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