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Protein

E3 SUMO-protein ligase PIAS1

Gene

PIAS1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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 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
  • ligase activity Source: UniProtKB-KW
  • SUMO ligase activity Source: BHF-UCL
  • SUMO transferase activity Source: Reactome
  • transcription coactivator activity Source: UniProtKB
  • transcription corepressor activity Source: ProtInc
  • zinc ion binding Source: InterPro

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Transcription, Transcription regulation, Ubl conjugation pathway

Keywords - Ligandi

DNA-binding, Metal-binding, Zinc

Enzyme and pathway databases

BioCyciZFISH:ENSG00000033800-MONOMER.
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:6.3.2.-)
Alternative name(s):
DEAD/H box-binding protein 1
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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 15

Organism-specific databases

HGNCiHGNC:2752. PIAS1.

Subcellular locationi

GO - Cellular componenti

  • nuclear speck Source: UniProtKB-SubCell
  • nucleoplasm Source: Reactome
  • nucleus Source: UniProtKB
  • PML body Source: UniProtKB-SubCell
Complete GO annotation...

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-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
Modified residuei467PhosphoserineCombined sources1
Modified residuei468PhosphoserineCombined sources1
Modified residuei483PhosphoserineBy similarity1
Modified residuei485PhosphoserineCombined sources1
Modified residuei487PhosphothreonineBy similarity1
Modified residuei488PhosphoserineCombined sources1
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.

PTM databases

iPTMnetiO75925.
PhosphoSitePlusiO75925.

Miscellaneous databases

PMAP-CutDBO75925.

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

WithEntry#Exp.IntActNotes
P299913EBI-629434,EBI-8826488From a different organism.
CASP8AP2Q9UKL34EBI-629434,EBI-2339650
MBD1Q9UIS93EBI-629434,EBI-867196
PRDM1O756262EBI-629434,EBI-948789
TP53P046374EBI-629434,EBI-366083

GO - Molecular functioni

  • androgen receptor binding Source: UniProtKB
  • enzyme binding Source: UniProtKB

Protein-protein interaction databases

BioGridi114124. 101 interactors.
DIPiDIP-5970N.
IntActiO75925. 46 interactors.
MINTiMINT-132657.
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

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1V66NMR-A1-65[»]
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
Contains 1 PINIT domain.PROSITE-ProRule annotation
Contains 1 SAP domain.PROSITE-ProRule annotation
Contains 1 SP-RING-type zinc finger.PROSITE-ProRule annotation

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.
InterProiIPR027227. PIAS1.
IPR023321. PINIT.
IPR003034. SAP_dom.
IPR004181. Znf_MIZ.
[Graphical view]
PANTHERiPTHR10782:SF11. PTHR10782:SF11. 1 hit.
PfamiPF14324. PINIT. 1 hit.
PF02891. zf-MIZ. 1 hit.
[Graphical view]
SMARTiSM00513. SAP. 1 hit.
[Graphical view]
PROSITEiPS51466. PINIT. 1 hit.
PS50800. SAP. 1 hit.
PS51044. ZF_SP_RING. 1 hit.
[Graphical view]

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

Cross-referencesi

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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1V66NMR-A1-65[»]
ProteinModelPortaliO75925.
SMRiO75925.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114124. 101 interactors.
DIPiDIP-5970N.
IntActiO75925. 46 interactors.
MINTiMINT-132657.
STRINGi9606.ENSP00000249636.

PTM databases

iPTMnetiO75925.
PhosphoSitePlusiO75925.

Polymorphism and mutation databases

BioMutaiPIAS1.

Proteomic databases

EPDiO75925.
MaxQBiO75925.
PaxDbiO75925.
PeptideAtlasiO75925.
PRIDEiO75925.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi8554.
DisGeNETi8554.
GeneCardsiPIAS1.
HGNCiHGNC:2752. PIAS1.
HPAiCAB012304.
HPA005743.
MIMi603566. gene.
neXtProtiNX_O75925.
OpenTargetsiENSG00000033800.
PharmGKBiPA33285.
GenAtlasiSearch...

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayiUPA00886.
BioCyciZFISH:ENSG00000033800-MONOMER.
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.

Miscellaneous databases

ChiTaRSiPIAS1. human.
EvolutionaryTraceiO75925.
GeneWikiiPIAS1.
GenomeRNAii8554.
PMAP-CutDBO75925.
PROiO75925.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000033800.
CleanExiHS_PIAS1.
ExpressionAtlasiO75925. baseline and differential.
GenevisibleiO75925. HS.

Family and domain databases

Gene3Di1.10.720.30. 1 hit.
InterProiIPR027227. PIAS1.
IPR023321. PINIT.
IPR003034. SAP_dom.
IPR004181. Znf_MIZ.
[Graphical view]
PANTHERiPTHR10782:SF11. PTHR10782:SF11. 1 hit.
PfamiPF14324. PINIT. 1 hit.
PF02891. zf-MIZ. 1 hit.
[Graphical view]
SMARTiSM00513. SAP. 1 hit.
[Graphical view]
PROSITEiPS51466. PINIT. 1 hit.
PS50800. SAP. 1 hit.
PS51044. ZF_SP_RING. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPIAS1_HUMAN
AccessioniPrimary (citable) accession number: O75925
Secondary accession number(s): B2RB67
, B3KSY9, C5J4B4, Q147X4, Q99751, Q9UN02
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 5, 2002
Last sequence update: March 5, 2002
Last modified: November 30, 2016
This is version 169 of the entry and version 2 of the sequence. [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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.