CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-001293
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 E3 SUMO-protein ligase PIAS1 
Protein Synonyms/Alias
 DEAD/H box-binding protein 1; Gu-binding protein; GBP; Protein inhibitor of activated STAT protein 1; RNA helicase II-binding protein 
Gene Name
 PIAS1 
Gene Synonyms/Alias
 DDXBP1 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
8MADSAELKQMVMSLRubiquitination[1]
46TKALHLLKAGCSPAVubiquitination[1]
56CSPAVQMKIKELYRRubiquitination[1]
58PAVQMKIKELYRRRFubiquitination[1]
140HPDIKLQKLPFYDLLubiquitination[1]
226LCVKVNTKPCSLPGYubiquitination[1]
238PGYLPPTKNGVEPKRubiquitination[1]
315SRALIKEKLTADPDSubiquitination[1]
339SLLCPLGKMRLTIPCubiquitination[1]
408DCDEIQFKEDGTWAPubiquitination[1]
419TWAPMRSKKEVQEVSubiquitination[1]
453SHHQSSNKNKKVEVIubiquitination[1]
455HQSSNKNKKVEVIDLubiquitination[1]
456QSSNKNKKVEVIDLTubiquitination[1]
493PTSPLNNKGILSLPHubiquitination[1]
Reference
 [1] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961] 
Functional Description
 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). 
Sequence Annotation
 DOMAIN 11 45 SAP.
 DOMAIN 124 288 PINIT.
 REPEAT 520 523 1.
 REPEAT 557 560 2.
 REPEAT 598 601 3; approximate.
 REPEAT 612 615 4; approximate.
 ZN_FING 320 397 SP-RING-type.
 REGION 462 473 SUMO1-binding (By similarity).
 REGION 520 615 4 X 4 AA repeats of N-T-S-L.
 MOTIF 19 23 LXXLL motif.
 MOTIF 56 64 Nuclear localization signal (Potential).
 MOTIF 368 380 Nuclear localization signal (Potential).
 MOD_RES 303 303 Asymmetric dimethylarginine; by PRMT1.
 MOD_RES 483 483 Phosphoserine (By similarity).
 MOD_RES 485 485 Phosphoserine (By similarity).
 MOD_RES 487 487 Phosphothreonine (By similarity).
 MOD_RES 503 503 Phosphoserine.
 MOD_RES 510 510 Phosphoserine.
 MOD_RES 522 522 Phosphoserine.  
Keyword
 3D-structure; Complete proteome; DNA-binding; Ligase; Metal-binding; Methylation; Nucleus; Phosphoprotein; Reference proteome; Repeat; Transcription; Transcription regulation; Ubl conjugation; Ubl conjugation pathway; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 651 AA 
Protein Sequence
MADSAELKQM VMSLRVSELQ VLLGYAGRNK HGRKHELLTK ALHLLKAGCS PAVQMKIKEL 60
YRRRFPQKIM TPADLSIPNV HSSPMPATLS PSTIPQLTYD GHPASSPLLP VSLLGPKHEL 120
ELPHLTSALH PVHPDIKLQK LPFYDLLDEL IKPTSLASDN SQRFRETCFA FALTPQQVQQ 180
ISSSMDISGT KCDFTVQVQL RFCLSETSCP QEDHFPPNLC VKVNTKPCSL PGYLPPTKNG 240
VEPKRPSRPI NITSLVRLST TVPNTIVVSW TAEIGRNYSM AVYLVKQLSS TVLLQRLRAK 300
GIRNPDHSRA LIKEKLTADP DSEIATTSLR VSLLCPLGKM RLTIPCRALT CSHLQCFDAT 360
LYIQMNEKKP TWVCPVCDKK APYEHLIIDG LFMEILKYCT DCDEIQFKED GTWAPMRSKK 420
EVQEVSASYN GVDGCLSSTL EHQVASHHQS SNKNKKVEVI DLTIDSSSDE EEEEPSAKRT 480
CPSLSPTSPL NNKGILSLPH QASPVSRTPS LPAVDTSYIN TSLIQDYRHP FHMTPMPYDL 540
QGLDFFPFLS GDNQHYNTSL LAAAAAAVSD DQDLLHSSRF FPYTSSQMFL DQLSAGGSTS 600
LPTTNGSSSG SNSSLVSSNS LRESHSHTVT NRSSTDTASI FGIIPDIISL D 651 
Gene Ontology
 GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
 GO:0005654; C:nucleoplasm; TAS:Reactome.
 GO:0016605; C:PML body; IEA:UniProtKB-SubCell.
 GO:0050681; F:androgen receptor binding; NAS:UniProtKB.
 GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
 GO:0019789; F:SUMO ligase activity; IDA:BHF-UCL.
 GO:0003713; F:transcription coactivator activity; NAS:UniProtKB.
 GO:0003714; F:transcription corepressor activity; TAS:ProtInc.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0030521; P:androgen receptor signaling pathway; NAS:UniProtKB.
 GO:0060333; P:interferon-gamma-mediated signaling pathway; TAS:Reactome.
 GO:0007259; P:JAK-STAT cascade; TAS:ProtInc.
 GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IEA:Compara.
 GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
 GO:0033235; P:positive regulation of protein sumoylation; IDA:UniProtKB.
 GO:0051152; P:positive regulation of smooth muscle cell differentiation; IEA:Compara.
 GO:0045893; P:positive regulation of transcription, DNA-dependent; NAS:UniProtKB.
 GO:0016925; P:protein sumoylation; ISS:UniProtKB.
 GO:0065004; P:protein-DNA complex assembly; IEA:Compara.
 GO:0042127; P:regulation of cell proliferation; ISS:UniProtKB.
 GO:0060334; P:regulation of interferon-gamma-mediated signaling pathway; TAS:Reactome.
 GO:0007283; P:spermatogenesis; IEA:Compara.
 GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW. 
Interpro
 IPR027227; PIAS1.
 IPR023321; PINIT.
 IPR003034; SAP_dom.
 IPR004181; Znf_MIZ. 
Pfam
 PF14324; PINIT
 PF02891; zf-MIZ 
SMART
 SM00513; SAP 
PROSITE
 PS51466; PINIT
 PS50800; SAP
 PS51044; ZF_SP_RING 
PRINTS