CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-001294
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 E3 SUMO-protein ligase PIAS2 
Protein Synonyms/Alias
 Androgen receptor-interacting protein 3; ARIP3; DAB2-interacting protein; DIP; Msx-interacting zinc finger protein; Miz1; PIAS-NY protein; Protein inhibitor of activated STAT x; Protein inhibitor of activated STAT2 
Gene Name
 PIAS2 
Gene Synonyms/Alias
 PIASX 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
46MRALHLLKSGCSPAVubiquitination[1]
249PGYAPPPKNGIEQKRubiquitination[1, 2]
326SRALIKEKLTADPDSubiquitination[3, 4]
443VSSQPCTKIESSSVLubiquitination[1]
452ESSSVLSKPCSVTVAubiquitination[1]
464TVASEASKKKVDVIDubiquitination[1]
465VASEASKKKVDVIDLubiquitination[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]
 [2] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [3] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [4] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724
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 coregulator in various cellular pathways, including the STAT pathway, the p53 pathway and the steroid hormone signaling pathway. The effects of this transcriptional coregulation, transactivation or silencing may vary depending upon the biological context and the PIAS2 isoform studied. However, it seems to be mostly involved in gene silencing. Binds to sumoylated ELK1 and enhances its transcriptional activity by preventing recruitment of HDAC2 by ELK1, thus reversing SUMO-mediated repression of ELK1 transactivation activity. Isoform PIAS2-beta, but not isoform PIAS2-alpha, promotes MDM2 sumoylation. Isoform PIAS2-alpha promotes PARK7 sumoylation. Isoform PIAS2-beta promotes NCOA2 sumoylation more efficiently than isoform PIAS2- alpha. Isoform PIAS2-alpha sumoylates PML at'Lys-65' and 'Lys- 160'. 
Sequence Annotation
 DOMAIN 11 45 SAP.
 DOMAIN 134 299 PINIT.
 ZN_FING 331 408 SP-RING-type.
 REGION 467 473 SUMO1-binding.
 MOTIF 19 23 LXXLL motif.
 MOTIF 484 492 Nuclear localization signal (By
 MOD_RES 476 476 Phosphoserine.
 MOD_RES 477 477 Phosphoserine.
 MOD_RES 478 478 Phosphoserine.  
Keyword
 3D-structure; Alternative splicing; Complete proteome; DNA-binding; Ligase; Metal-binding; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Transcription; Transcription regulation; Ubl conjugation; Ubl conjugation pathway; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 621 AA 
Protein Sequence
MADFEELRNM VSSFRVSELQ VLLGFAGRNK SGRKHDLLMR ALHLLKSGCS PAVQIKIREL 60
YRRRYPRTLE GLSDLSTIKS SVFSLDGGSS PVEPDLAVAG IHSLPSTSVT PHSPSSPVGS 120
VLLQDTKPTF EMQQPSPPIP PVHPDVQLKN LPFYDVLDVL IKPTSLVQSS IQRFQEKFFI 180
FALTPQQVRE ICISRDFLPG GRRDYTVQVQ LRLCLAETSC PQEDNYPNSL CIKVNGKLFP 240
LPGYAPPPKN GIEQKRPGRP LNITSLVRLS SAVPNQISIS WASEIGKNYS MSVYLVRQLT 300
SAMLLQRLKM KGIRNPDHSR ALIKEKLTAD PDSEIATTSL RVSLMCPLGK MRLTIPCRAV 360
TCTHLQCFDA ALYLQMNEKK PTWICPVCDK KAAYESLILD GLFMEILNDC SDVDEIKFQE 420
DGSWCPMRPK KEAMKVSSQP CTKIESSSVL SKPCSVTVAS EASKKKVDVI DLTIESSSDE 480
EEDPPAKRKC IFMSETQSSP TKGVLMYQPS SVRVPSVTSV DPAAIPPSLT DYSVPFHHTP 540
ISSMSSDLPG LDFLSLIPVD PQYCPPMFLD SLTSPLTASS TSVTTTSSHE SSTHVSSSSS 600
RSETGVITSS GSNIPDIISL D 621 
Gene Ontology
 GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
 GO:0005634; C:nucleus; IDA:UniProtKB.
 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:0008270; F:zinc ion binding; TAS:ProtInc.
 GO:0030521; P:androgen receptor signaling pathway; NAS:UniProtKB.
 GO:0060766; P:negative regulation of androgen receptor signaling pathway; IDA:UniProtKB.
 GO:0045893; P:positive regulation of transcription, DNA-dependent; NAS:UniProtKB.
 GO:0016925; P:protein sumoylation; IDA:UniProtKB.
 GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW. 
Interpro
 IPR027228; PIAS2.
 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