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Protein Page:
PIAS1 (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitination
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
PIAS1 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. Interacts with NCOA2 and AR. Interacts with NR2C1; the interaction promotes its sumoylation. 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 G(1) 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. Expressed in numerous tissues with highest level in testis. Belongs to the PIAS family. Note: This description may include information from UniProtKB.
Protein type: SUMO conjugating system; Transcription, coactivator/corepressor; EC 6.3.2.-; Nuclear receptor co-regulator
Cellular Component: nucleoplasm; PML body; nuclear speck; nucleus
Molecular Function: protein domain specific binding; protein binding; enzyme binding; androgen receptor binding; DNA binding; zinc ion binding; ubiquitin protein ligase binding; transcription coactivator activity; SUMO ligase activity; transcription corepressor activity
Biological Process: positive regulation of protein sumoylation; protein sumoylation; transcription, DNA-dependent; positive regulation of smooth muscle cell differentiation; positive regulation of transcription, DNA-dependent; positive regulation of proteasomal ubiquitin-dependent protein catabolic process; cytokine and chemokine mediated signaling pathway; androgen receptor signaling pathway; spermatogenesis; negative regulation of transcription from RNA polymerase II promoter; JAK-STAT cascade; protein-DNA complex assembly; regulation of cell proliferation
Reference #:  O75925 (UniProtKB)
Alt. Names/Synonyms: AR interacting protein; DDXBP1; DEAD/H (Asp-Glu-Ala-Asp/His) box binding protein 1; DEAD/H box-binding protein 1; E3 SUMO-protein ligase PIAS1; GBP; Gu-binding protein; GU/RH-II; MGC141878; MGC141879; PIAS1; Protein inhibitor of activated STAT protein 1; protein inhibitor of activated STAT, 1; protein inhibitor of activated STAT-1; RNA helicase II-binding protein; zinc finger, MIZ-type containing 3; ZMIZ3
Gene Symbols: PIAS1
Molecular weight: 71,836 Da
Basal Isoelectric point: 6.9  Predict pI for various phosphorylation states
CST Pathways:  Crosstalk between PTMs  |  IL6 Signaling
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

PIAS1

Protein Structure Not Found.


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Sites Implicated In
transcription, inhibited: S466‑p, S467‑p, S468‑p, S522‑p
enzymatic activity, induced: S522‑p
molecular association, regulation: S466‑p, S467‑p, S468‑p
sumoylation: S522‑p

Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

 
0 1 S50-p HLLKAGCsPAVQMKI
0 1 T71-p RFPQKIMtPADLSIP
1 1 S90 SPMPATLSPSTIPQL
0 1 D100-ca TIPQLTYdGHPASSP
0 1 S229 KVNTKPCSLPGYLPP
0 1 S289-p VYLVKQLsstVLLQR
0 1 S290-p YLVKQLsstVLLQRL
0 1 T291-p LVKQLsstVLLQRLR
1 0 R303-m2 RLRAKGIrNPDHSRA
2 3 S466-p VIDLTIDsssDEEEE
2 3 S467-p IDLTIDsssDEEEEE
2 4 S468-p DLTIDsssDEEEEEP
0 1 S476-p DEEEEEPsAKRtCPs
0 1 T480-p EEPsAKRtCPsLsPt
0 10 S483-p sAKRtCPsLsPtsPL
0 23 S485-p KRtCPsLsPtsPLNN
0 8 T487-p tCPsLsPtsPLNNKG
0 9 S488-p CPsLsPtsPLNNKGI
0 4 N491 LsPtsPLNNKGILsL
0 1 S497-p LNNKGILsLPHQAsP
0 27 S503-p LsLPHQAsPVsRtPs
0 2 S506-p PHQAsPVsRtPsLPA
0 1 T508-p QAsPVsRtPsLPAVD
0 1 S510-p sPVsRtPsLPAVDTS
1 1 S522-p DTSYINTsLIQDYRH
  mouse

 
S50 HLLKAGCSPAVQMKI
T71 RFPQKIMTPADLSIP
S90-p SPMPPTLsPSTIPQL
D100 TIPQLTYDGHPASSP
S229-p KVNTKPCsLPGYLPP
S289 VYLVKQLSSTVLLQR
S290 YLVKQLSSTVLLQRL
T291 LVKQLSSTVLLQRLR
R303 RLRAKGIRNPDHSRA
S466-p VIDLTIDsssDEEEE
S467-p IDLTIDsssDEEEEE
S468-p DLTIDsssDEEEEEP
P476 DEEEEEPPAKRtCPs
T480-p EEPPAKRtCPsLsPt
S483-p PAKRtCPsLsPtsPL
S485-p KRtCPsLsPtsPLsN
T487-p tCPsLsPtsPLsNKG
S488-p CPsLsPtsPLsNKGI
S491-p LsPtsPLsNKGILsL
S497-p LsNKGILsLPHQAsP
S503-p LsLPHQAsPVsRTPS
S506-p PHQAsPVsRTPSLPA
T508 QAsPVsRTPSLPAVD
S510 sPVsRTPSLPAVDTS
S522 DTSYINTSLIQDYRH
  rat

 
S50 HLLKAGCSPAVQMKI
T71 RFPQKIMTPADLSIP
S90 SPMPATLSPSTIPQL
D100 TIPQLTYDGHPASSP
S229 KVNTKPCSLPGYLPP
S289 VYLVKQLSSTVLLQR
S290 YLVKQLSSTVLLQRL
T291 LVKQLSSTVLLQRLR
R303 RLRAKGIRNPDHSRA
S466 VIDLTIDSSSDEEEE
S467 IDLTIDSSSDEEEEE
S468 DLTIDSSSDEEEEEP
P476 DEEEEEPPAKRTCPS
T480 EEPPAKRTCPSLsPt
S483 PAKRTCPSLsPtsPL
S485-p KRTCPSLsPtsPLSN
T487-p TCPSLsPtsPLSNKG
S488-p CPSLsPtsPLSNKGI
S491 LsPtsPLSNKGILSL
S497 LSNKGILSLPHQASP
S503 LSLPHQASPVSRTPS
S506 PHQASPVSRTPSLPA
T508 QASPVSRTPSLPAVD
S510 SPVSRTPSLPAVDTS
S522 DTSYINTSLIQDYRH
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