CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-037480
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
  
Protein Name
 E3 SUMO-protein ligase PIAS3 
Protein Synonyms/Alias
  
Gene Name
 PIAS3 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
8MAELGELKHMVMSFRubiquitination[1]
253TAGTLLQKLRAKGIRubiquitination[1]
272SRALIKEKLTADPDSubiquitination[1, 2, 3]
337TCPVCDKKAPYESLIubiquitination[1]
407GGDPSENKKKVEVIDubiquitination[1, 4]
408GDPSENKKKVEVIDLubiquitination[1]
431EDLPPTKKHCSVTSAubiquitination[3]
447IPALPGSKGVLTSGHubiquitination[1, 3]
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] 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]
 [3] 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]
 [4] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094
Functional Description
  
Sequence Annotation
  
Keyword
 Complete proteome; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 593 AA 
Protein Sequence
MAELGELKHM VMSFRVSELQ VLLGFAGRNK SGRKHELLAK ALHLLKSSCA PSVQMKIKEL 60
YRRRFPRKTL GPSDLSLLSL PPGTSPPVHP DVTMKPLPFY EVYGELIRPT TLASTSSQRF 120
EEAHFTFALT PQQVQQILTS REVLPGAKCD YTIQVQLRFC LCETSCPQED YFPPNLFVKV 180
NGKLCPLPGY LPPTKNGAEP KRPSRPINIT PLARLSATVP NTIVVNWSSE FGRNYSLSVY 240
LVRQLTAGTL LQKLRAKGIR NPDHSRALIK EKLTADPDSE VATTSLRVSL MCPLGKMRLT 300
VPCRALTCAH LQSFDAALYL QMNEKKPTWT CPVCDKKAPY ESLIIDGLFM EILSSCSDCD 360
EIQFMEDGSW CPMKPKKEAS EVCPPPGYGL DGLQYSPVQG GDPSENKKKV EVIDLTIESS 420
SDEEDLPPTK KHCSVTSAAI PALPGSKGVL TSGHQPSSVL RSPAMGTLGG DFLSSLPLHE 480
YPPAFPLGAD IQGLDLFSFL QTESQHYGPS VITSLDEQDA LGHFFQYRGT PSHFLGPLAP 540
TLGSSHCSAT PAPPPGRVSS IVAPGGALRE GHGGPLPSGP SLTGCRSDII SLD 593 
Gene Ontology
 GO:0003676; F:nucleic acid binding; IEA:InterPro.
 GO:0019789; F:SUMO ligase activity; IEA:InterPro.
 GO:0008270; F:zinc ion binding; IEA:InterPro. 
Interpro
 IPR027226; PIAS3.
 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