Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  E3 SUMO-protein ligase PIAS1  

UniProtKB / Swiss-Prot ID :  PIAS1_HUMAN

Gene Name (Synonyms) : 
PIAS1, DDXBP1  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Nucleus speckle. Note=Interaction with CSRP2 may induce a partial redistribution along the cytoskeleton. 

Protein Function :  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. 

Protein Sequence MADSAELKQMVMSLRVSELQVLLGYAGRNKHGRKHELLTKALHLLKAGCSPAVQMKIKELYRRRFPQKIM...
Predicted Secondary Structure CCCHHHHHHHHHHCCCHHHHHHHHHHCCCCCCCHHHHHHHHHHHHCCCCCHHHHHHHHHHHHHCCCCCCC...
Protein Variant -
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
90Phosphoserine (CHUK)PATLSPSTI
CCCCCCCCC
16.67HPRD
Link-
100Caspase cleavage aspartic acidQLTYDGHPA
CCCCCCCCC
43.63Phosphositeplus
Link-
303Asymmetric dimethylarginine; by PRMT1.AKGIRNPDH
HCCCCCHHH
58.24UniProtKB
Link-
303N2,N2-dimethylarginineAKGIRNPDH
HCCCCCHHH
58.24Phosphositeplus
Link-
466PhosphoserineLTIDSSSDE
CCCCCCCCC
28.08HPRD
Link-
466PhosphoserineLTIDSSSDE
CCCCCCCCC
28.08PhosphoELM
Link-
466PhosphoserineLTIDSSSDE
CCCCCCCCC
28.08Phosphositeplus
Link-
466PhosphoserineLTIDSSSDE
CCCCCCCCC
28.08SysPTM
Link-
466Phosphoserine.LTIDSSSDE
CCCCCCCCC
28.08UniProtKB
Link-
467PhosphoserineTIDSSSDEE
CCCCCCCCC
37.75HPRD
Link-
467PhosphoserineTIDSSSDEE
CCCCCCCCC
37.75PhosphoELM
Link-
467PhosphoserineTIDSSSDEE
CCCCCCCCC
37.75Phosphositeplus
Link-
467PhosphoserineTIDSSSDEE
CCCCCCCCC
37.75SysPTM
Link-
467Phosphoserine.TIDSSSDEE
CCCCCCCCC
37.75UniProtKB
Link-
468PhosphoserineIDSSSDEEE
CCCCCCCCC
53.66HPRD
Link-
468PhosphoserineIDSSSDEEE
CCCCCCCCC
53.66PhosphoELM
Link-
468PhosphoserineIDSSSDEEE
CCCCCCCCC
53.66Phosphositeplus
Link-
468PhosphoserineIDSSSDEEE
CCCCCCCCC
53.66SysPTM
Link-
468Phosphoserine.IDSSSDEEE
CCCCCCCCC
53.66UniProtKB
Link-
476PhosphoserineEEEPSAKRT
CCCCCCCCC
50.10Phosphositeplus
Link-
483PhosphoserineRTCPSLSPT
CCCCCCCCC
43.56PhosphoELM
Link-
483PhosphoserineRTCPSLSPT
CCCCCCCCC
43.56Phosphositeplus
Link-
485PhosphoserineCPSLSPTSP
CCCCCCCCC
30.39HPRD
Link-
485PhosphoserineCPSLSPTSP
CCCCCCCCC
30.39PhosphoELM
Link-
485PhosphoserineCPSLSPTSP
CCCCCCCCC
30.39Phosphositeplus
Link-
485PhosphoserineCPSLSPTSP
CCCCCCCCC
30.39SysPTM
Link-
487PhosphothreonineSLSPTSPLN
CCCCCCCCC
39.33HPRD
Link-
487PhosphothreonineSLSPTSPLN
CCCCCCCCC
39.33SysPTM
Link-
488PhosphoserineLSPTSPLNN
CCCCCCCCC
30.67HPRD
Link-
488PhosphoserineLSPTSPLNN
CCCCCCCCC
30.67PhosphoELM
Link-
488PhosphoserineLSPTSPLNN
CCCCCCCCC
30.67Phosphositeplus
Link-
488PhosphoserineLSPTSPLNN
CCCCCCCCC
30.67SysPTM
Link-
503PhosphoserinePHQASPVSR
CCCCCCCCC
21.18HPRD
Link-
503PhosphoserinePHQASPVSR
CCCCCCCCC
21.18PhosphoELM
Link-
503PhosphoserinePHQASPVSR
CCCCCCCCC
21.18Phosphositeplus
Link-
503PhosphoserinePHQASPVSR
CCCCCCCCC
21.18SysPTM
Link-
503Phosphoserine.PHQASPVSR
CCCCCCCCC
21.18UniProtKB
Link-
506PhosphoserineASPVSRTPS
CCCCCCCCC
33.54HPRD
Link-
506PhosphoserineASPVSRTPS
CCCCCCCCC
33.54PhosphoELM
Link-
506PhosphoserineASPVSRTPS
CCCCCCCCC
33.54Phosphositeplus
Link-
508PhosphothreoninePVSRTPSLP
CCCCCCCCC
15.10Phosphositeplus
Link-
510PhosphoserineSRTPSLPAV
CCCCCCCCC
46.50Phosphositeplus
Link-
510Phosphoserine.SRTPSLPAV
CCCCCCCCC
46.50UniProtKB
Link-
522PhosphoserineYINTSLIQD
CCCCCCCCC
20.98HPRD
Link-
522PhosphoserineYINTSLIQD
CCCCCCCCC
20.98PhosphoELM
Link-
522PhosphoserineYINTSLIQD
CCCCCCCCC
20.98Phosphositeplus
Link-
522PhosphoserineYINTSLIQD
CCCCCCCCC
20.98SysPTM
Link-
522Phosphoserine.YINTSLIQD
CCCCCCCCC
20.98UniProtKB
Link-
635PhosphothreonineNRSSTDTAS
CCCCCCCCE
38.32HPRD
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
SMAD7_HUMANphysical interactionMINT-61806MINT15231748
PR40A_HUMANphysical interactionMINT-61844MINT15231748
SKIL_HUMANphysical interactionMINT-61629MINT15231748
STAT1_HUMANphysical interactionMINT-14068MINT10805787
STAT1_HUMANphysical interactionMINT-15950MINT10805787
STAT1_HUMANphysical interactionMINT-15951MINT10805787
SMAD1_HUMANphysical interactionMINT-61985MINT15231748
SNIP1_HUMANphysical interactionMINT-62153MINT15231748
MBD1_HUMANphysical interactionMINT-3382891MINT17066076
MBD1_HUMANphysical interactionMINT-3382994MINT17066076
MBD1_HUMANdirect interactionMINT-3382909MINT17066076
PTN1_HUMANphysical interactionEBI-1267424
intact17159996
P53_HUMANdirect interaction
direct interaction
direct interaction
EBI-629447
EBI-629452
EBI-629
intact15133049
15133049
15133049
COT2_HUMANin vitro
yeast 2-hybrid
HPRD:16029HPRD15666827
15611122
ESR1_HUMANyeast 2-hybridHPRD:16029HPRD15666801
MDM2_HUMANin vitroHPRD:16029HPRD12393906
JUN_HUMANin vitroHPRD:16029HPRD11867732
TF65_HUMANin vitro
in vivo
HPRD:16029HPRD15657437
ANDR_HUMANin vitro
in vivo
HPRD:16029HPRD11877418
12177000
STF1_HUMANin vitro
in vivo
yeast 2-hybrid
HPRD:16029HPRD15192080
P53_HUMANin vitro
yeast 2-hybrid
HPRD:16029HPRD15133049
11867732
11788578
11583632
ZNF76_HUMANin vitro
yeast 2-hybrid
HPRD:16029HPRD15280358
SP3_HUMANin vitro
yeast 2-hybrid
HPRD:16029HPRD12356736
MCR_HUMANin vitro
in vivo
yeast 2-hybrid
HPRD:16029HPRD14500761
SMAD4_HUMANin vitro
yeast 2-hybrid
HPRD:16029HPRD15028714
15231748
STAT1_HUMANin vitro
in vivo
yeast 2-hybrid
HPRD:16029HPRD10805787
9724754
12855578
ELK3_HUMANin vitro
in vivo
yeast 2-hybrid
HPRD:16029HPRD15580297
CEBPE_HUMANin vitro
yeast 2-hybrid
HPRD:16029HPRD15588942
FAK1_HUMANin vitro
in vivo
yeast 2-hybrid
HPRD:16029HPRD14500712
DNM3A_HUMANin vitro
in vivo
yeast 2-hybrid
HPRD:16029HPRD14752048
DYN1_HUMANin vitro
yeast 2-hybrid
HPRD:16029HPRD15123615
CSRP2_HUMANin vitro
in vivo
yeast 2-hybrid
HPRD:16029HPRD11672422
AXN1_HUMANyeast 2-hybridHPRD:16029HPRD12223491
SUMO1_HUMANin vitro
yeast 2-hybrid
HPRD:16029HPRD11583632
P73_HUMANin vitroHPRD:16029HPRD15572666
SUFU_HUMANyeast 2-hybridHPRD:16029HPRD14611647
DCR1A_HUMANin vitro
yeast 2-hybrid
HPRD:16029HPRD15572677
GATA4_HUMANin vitroHPRD:16029HPRD15337742
UBC9_HUMANyeast 2-hybridHPRD:16029HPRD12177000
PIAS4_HUMANin vitroHPRD:16029HPRD11877418
PIAS2_HUMANin vitro
yeast 2-hybrid
HPRD:16029HPRD11877418
SATB2_HUMANin vitro
in vivo
HPRD:16029HPRD14701874
DDX21_HUMANin vitro
in vivo
HPRD:16029HPRD9177271
PIAS1_HUMANyeast 2-hybridHPRD:16029HPRD14611647
SKIL_HUMANyeast 2-hybridHPRD:16029HPRD15231748
SMAD7_HUMANyeast 2-hybridHPRD:16029HPRD15231748
PR40A_HUMANyeast 2-hybridHPRD:16029HPRD15231748
SMAD1_HUMANyeast 2-hybridHPRD:16029HPRD15231748
SNIP1_HUMANyeast 2-hybridHPRD:16029HPRD15231748
ESR1_HUMANENSP00000249636STRING
SKIL_HUMANENSP00000249636STRING
SATB2_HUMANENSP00000249636STRING
SUMO1_HUMANENSP00000249636STRING
STAT3_HUMANENSP00000249636STRING
P53_HUMANENSP00000249636STRING
MSX1_HUMANENSP00000249636STRING
COT1_HUMANENSP00000249636STRING
FAK1_HUMANENSP00000249636STRING
SMAD4_HUMANENSP00000249636STRING
UBC9_HUMANENSP00000249636STRING
STAT1_HUMANENSP00000249636STRING
STAT1_HUMANENSP00000249636STRING
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Disease Reference
Kegg disease
There are no disease associations of PTM sites.
Drug Reference
There are no disease associations of PTM sites.
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Related Literatures of Post-Translational Modification
Methylation
ReferencePubMed
"PRMT1-mediated arginine methylation of PIAS1 regulates STAT1signaling.";
Weber S., Maass F., Schuemann M., Krause E., Suske G., Bauer U.M.;
Genes Dev. 23:118-132(2009).
Cited for: FUNCTION, INTERACTION WITH STAT1, METHYLATION AT ARG-303 BY PRMT1,MASS SPECTROMETRY, SUBCELLULAR LOCATION, AND MUTAGENESIS OF ARG-303.
Phosphorylation
ReferencePubMed
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-466; SER-467 ANDSER-468, AND MASS SPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-503 AND SER-522, ANDMASS SPECTROMETRY.
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-503 AND SER-510, ANDMASS SPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures