CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-008516
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Signal transducer and activator of transcription 2 
Protein Synonyms/Alias
 p113 
Gene Name
 STAT2 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
161AMMEKLVKSISQLKDubiquitination[1]
182FRYKIQAKGKTPSLDacetylation[2]
184YKIQAKGKTPSLDPHacetylation[2]
194SLDPHQTKEQKILQEacetylation[2]
197PHQTKEQKILQETLNacetylation[2]
239LPKLEEWKAQQQKACubiquitination[1]
295YQDDPLTKGVDLRNAubiquitination[1]
375PQLQGFRKFNILTSNacetylation[3]
375PQLQGFRKFNILTSNubiquitination[1]
384NILTSNQKTLTPEKGacetylation[2, 4]
384NILTSNQKTLTPEKGubiquitination[5, 6, 7]
390QKTLTPEKGQSQGLIacetylation[2]
415QRSGGSGKGSNKGPLacetylation[2]
419GSGKGSNKGPLGVTEacetylation[2]
523QLSMLRNKLFGQNCRubiquitination[1]
543LSWADFTKRESPPGKubiquitination[1, 8]
592QERRLLKKTMSGTFLacetylation[2]
681FGCYYQEKVNLQERRubiquitination[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] Acetylation-dependent signal transduction for type I interferon receptor.
 Tang X, Gao JS, Guan YJ, McLane KE, Yuan ZL, Ramratnam B, Chin YE.
 Cell. 2007 Oct 5;131(1):93-105. [PMID: 17923090]
 [3] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [4] Regulation of cellular metabolism by protein lysine acetylation.
 Zhao S, Xu W, Jiang W, Yu W, Lin Y, Zhang T, Yao J, Zhou L, Zeng Y, Li H, Li Y, Shi J, An W, Hancock SM, He F, Qin L, Chin J, Yang P, Chen X, Lei Q, Xiong Y, Guan KL.
 Science. 2010 Feb 19;327(5968):1000-4. [PMID: 20167786]
 [5] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [6] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [7] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [8] 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] 
Functional Description
 Signal transducer and activator of transcription that mediates signaling by type I IFNs (IFN-alpha and IFN-beta). Following type I IFN binding to cell surface receptors, Jak kinases (TYK2 and JAK1) are activated, leading to tyrosine phosphorylation of STAT1 and STAT2. The phosphorylated STATs dimerize, associate with ISGF3G/IRF-9 to form a complex termed ISGF3 transcription factor, that enters the nucleus. ISGF3 binds to the IFN stimulated response element (ISRE) to activate the transcription of interferon stimulated genes, which drive the cell in an antiviral state. 
Sequence Annotation
 DOMAIN 572 667 SH2.
 MOD_RES 283 283 Phosphoserine.
 MOD_RES 287 287 Phosphoserine.
 MOD_RES 294 294 Phosphothreonine.
 MOD_RES 690 690 Phosphotyrosine; by JAK.  
Keyword
 3D-structure; Activator; Alternative splicing; Antiviral defense; Complete proteome; Cytoplasm; Direct protein sequencing; DNA-binding; Host-virus interaction; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; SH2 domain; Transcription; Transcription regulation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 851 AA 
Protein Sequence
MAQWEMLQNL DSPFQDQLHQ LYSHSLLPVD IRQYLAVWIE DQNWQEAALG SDDSKATMLF 60
FHFLDQLNYE CGRCSQDPES LLLQHNLRKF CRDIQPFSQD PTQLAEMIFN LLLEEKRILI 120
QAQRAQLEQG EPVLETPVES QQHEIESRIL DLRAMMEKLV KSISQLKDQQ DVFCFRYKIQ 180
AKGKTPSLDP HQTKEQKILQ ETLNELDKRR KEVLDASKAL LGRLTTLIEL LLPKLEEWKA 240
QQQKACIRAP IDHGLEQLET WFTAGAKLLF HLRQLLKELK GLSCLVSYQD DPLTKGVDLR 300
NAQVTELLQR LLHRAFVVET QPCMPQTPHR PLILKTGSKF TVRTRLLVRL QEGNESLTVE 360
VSIDRNPPQL QGFRKFNILT SNQKTLTPEK GQSQGLIWDF GYLTLVEQRS GGSGKGSNKG 420
PLGVTEELHI ISFTVKYTYQ GLKQELKTDT LPVVIISNMN QLSIAWASVL WFNLLSPNLQ 480
NQQFFSNPPK APWSLLGPAL SWQFSSYVGR GLNSDQLSML RNKLFGQNCR TEDPLLSWAD 540
FTKRESPPGK LPFWTWLDKI LELVHDHLKD LWNDGRIMGF VSRSQERRLL KKTMSGTFLL 600
RFSESSEGGI TCSWVEHQDD DKVLIYSVQP YTKEVLQSLP LTEIIRHYQL LTEENIPENP 660
LRFLYPRIPR DEAFGCYYQE KVNLQERRKY LKHRLIVVSN RQVDELQQPL ELKPEPELES 720
LELELGLVPE PELSLDLEPL LKAGLDLGPE LESVLESTLE PVIEPTLCMV SQTVPEPDQG 780
PVSQPVPEPD LPCDLRHLNT EPMEIFRNCV KIEEIMPNGD PLLAGQNTVD EVYVSRPSHF 840
YTDGPLMPSD F 851 
Gene Ontology
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0005654; C:nucleoplasm; TAS:Reactome.
 GO:0005886; C:plasma membrane; IDA:HPA.
 GO:0005509; F:calcium ion binding; IEA:InterPro.
 GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
 GO:0003700; F:sequence-specific DNA binding transcription factor activity; IEA:InterPro.
 GO:0004871; F:signal transducer activity; TAS:ProtInc.
 GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
 GO:0007259; P:JAK-STAT cascade; TAS:ProtInc.
 GO:0006357; P:regulation of transcription from RNA polymerase II promoter; TAS:ProtInc.
 GO:0060338; P:regulation of type I interferon-mediated signaling pathway; TAS:Reactome.
 GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW.
 GO:0060337; P:type I interferon-mediated signaling pathway; TAS:Reactome.
 GO:0019048; P:virus-host interaction; IEA:UniProtKB-KW. 
Interpro
 IPR011992; EF-hand-like_dom.
 IPR008967; p53-like_TF_DNA-bd.
 IPR000980; SH2.
 IPR022756; STAT2_C.
 IPR013800; STAT_TF_alpha.
 IPR015988; STAT_TF_coiled-coil.
 IPR001217; STAT_TF_core.
 IPR013801; STAT_TF_DNA-bd.
 IPR012345; STAT_TF_DNA-bd_sub.
 IPR013799; STAT_TF_prot_interaction. 
Pfam
 PF00017; SH2
 PF12188; STAT2_C
 PF01017; STAT_alpha
 PF02864; STAT_bind
 PF02865; STAT_int 
SMART
 SM00252; SH2
 SM00964; STAT_int 
PROSITE
 PS50001; SH2 
PRINTS