CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-004343
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Proto-oncogene vav 
Protein Synonyms/Alias
  
Gene Name
 VAV1 
Gene Synonyms/Alias
 VAV 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
73MSQFLCLKNIRTFLSubiquitination[1]
85FLSTCCEKFGLKRSEubiquitination[1]
188EPVSMPPKMTEYDKRubiquitination[1]
194PKMTEYDKRCCCLREacetylation[2]
194PKMTEYDKRCCCLREubiquitination[1]
208EIQQTEEKYTDTLGSubiquitination[1]
222SIQQHFLKPLQRFLKacetylation[2, 3]
222SIQQHFLKPLQRFLKubiquitination[1, 4, 5]
252RVHTHFLKEMKEALGacetylation[3]
272NLYQVFIKYKERFLVubiquitination[1]
292SQVESASKHLDRVAAubiquitination[1]
307AREDVQMKLEECSQRubiquitination[1, 6]
335VPMQRVLKYHLLLQEubiquitination[1, 6]
345LLLQELVKHTQEAMEubiquitination[1]
353HTQEAMEKENLRLALubiquitination[1, 6]
374AQCVNEVKRDNETLRubiquitination[1, 6]
404LAHYGRPKIDGELKIubiquitination[1]
410PKIDGELKITSVERRubiquitination[1, 6]
429RYAFLLDKALLICKRubiquitination[1]
435DKALLICKRRGDSYDubiquitination[1]
444RGDSYDLKDFVNLHSubiquitination[1, 6]
577DFPGTMKKDKLHRRAubiquitination[1]
629GDIVELTKAEAEQNWubiquitination[1]
700FLVRQRVKDAAEFAIubiquitination[1]
716IKYNVEVKHIKIMTAacetylation[3]
716IKYNVEVKHIKIMTAubiquitination[1]
751FYQQNSLKDCFKSLDubiquitination[1, 6, 7]
770FPFKEPEKRTISRPAubiquitination[1]
782RPAVGSTKYFGTAKAubiquitination[1, 7]
788TKYFGTAKARYDFCAubiquitination[1, 7]
804DRSELSLKEGDIIKIubiquitination[1]
810LKEGDIIKILNKKGQubiquitination[1]
815IIKILNKKGQQGWWRubiquitination[1, 7]
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] 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] 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]
 [5] 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]
 [6] 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]
 [7] 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
 Couples tyrosine kinase signals with the activation of the Rho/Rac GTPases, thus leading to cell differentiation and/or proliferation. 
Sequence Annotation
 DOMAIN 1 119 CH.
 DOMAIN 194 373 DH.
 DOMAIN 402 504 PH.
 DOMAIN 617 660 SH3 1.
 DOMAIN 671 765 SH2.
 DOMAIN 782 842 SH3 2.
 ZN_FING 515 564 Phorbol-ester/DAG-type.
 MOD_RES 826 826 Phosphotyrosine.
 MOD_RES 844 844 Phosphotyrosine (By similarity).  
Keyword
 3D-structure; Alternative splicing; Complete proteome; Guanine-nucleotide releasing factor; Metal-binding; Phosphoprotein; Polymorphism; Proto-oncogene; Reference proteome; Repeat; SH2 domain; SH3 domain; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 845 AA 
Protein Sequence
MELWRQCTHW LIQCRVLPPS HRVTWDGAQV CELAQALRDG VLLCQLLNNL LPHAINLREV 60
NLRPQMSQFL CLKNIRTFLS TCCEKFGLKR SELFEAFDLF DVQDFGKVIY TLSALSWTPI 120
AQNRGIMPFP TEEESVGDED IYSGLSDQID DTVEEDEDLY DCVENEEAEG DEIYEDLMRS 180
EPVSMPPKMT EYDKRCCCLR EIQQTEEKYT DTLGSIQQHF LKPLQRFLKP QDIEIIFINI 240
EDLLRVHTHF LKEMKEALGT PGAANLYQVF IKYKERFLVY GRYCSQVESA SKHLDRVAAA 300
REDVQMKLEE CSQRANNGRF TLRDLLMVPM QRVLKYHLLL QELVKHTQEA MEKENLRLAL 360
DAMRDLAQCV NEVKRDNETL RQITNFQLSI ENLDQSLAHY GRPKIDGELK ITSVERRSKM 420
DRYAFLLDKA LLICKRRGDS YDLKDFVNLH SFQVRDDSSG DRDNKKWSHM FLLIEDQGAQ 480
GYELFFKTRE LKKKWMEQFE MAISNIYPEN ATANGHDFQM FSFEETTSCK ACQMLLRGTF 540
YQGYRCHRCR ASAHKECLGR VPPCGRHGQD FPGTMKKDKL HRRAQDKKRN ELGLPKMEVF 600
QEYYGLPPPP GAIGPFLRLN PGDIVELTKA EAEQNWWEGR NTSTNEIGWF PCNRVKPYVH 660
GPPQDLSVHL WYAGPMERAG AESILANRSD GTFLVRQRVK DAAEFAISIK YNVEVKHIKI 720
MTAEGLYRIT EKKAFRGLTE LVEFYQQNSL KDCFKSLDTT LQFPFKEPEK RTISRPAVGS 780
TKYFGTAKAR YDFCARDRSE LSLKEGDIIK ILNKKGQQGW WRGEIYGRVG WFPANYVEED 840
YSEYC 845 
Gene Ontology
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0005886; C:plasma membrane; TAS:Reactome.
 GO:0005085; F:guanyl-nucleotide exchange factor activity; EXP:Reactome.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0005543; F:phospholipid binding; IEA:InterPro.
 GO:0005089; F:Rho guanyl-nucleotide exchange factor activity; IEA:InterPro.
 GO:0003700; F:sequence-specific DNA binding transcription factor activity; TAS:ProtInc.
 GO:0097190; P:apoptotic signaling pathway; TAS:Reactome.
 GO:0007173; P:epidermal growth factor receptor signaling pathway; TAS:Reactome.
 GO:0038096; P:Fc-gamma receptor signaling pathway involved in phagocytosis; TAS:Reactome.
 GO:0008543; P:fibroblast growth factor receptor signaling pathway; TAS:Reactome.
 GO:0045087; P:innate immune response; TAS:Reactome.
 GO:0048011; P:neurotrophin TRK receptor signaling pathway; TAS:Reactome.
 GO:0048015; P:phosphatidylinositol-mediated signaling; TAS:Reactome.
 GO:0030168; P:platelet activation; TAS:Reactome.
 GO:0035023; P:regulation of Rho protein signal transduction; IEA:InterPro.
 GO:0051056; P:regulation of small GTPase mediated signal transduction; TAS:Reactome.
 GO:0007264; P:small GTPase mediated signal transduction; TAS:Reactome.
 GO:0031295; P:T cell costimulation; TAS:Reactome. 
Interpro
 IPR001715; CH-domain.
 IPR000219; DH-domain.
 IPR001331; GDS_CDC24_CS.
 IPR011993; PH_like_dom.
 IPR001849; Pleckstrin_homology.
 IPR002219; Prot_Kinase_C-like_PE/DAG-bd.
 IPR000980; SH2.
 IPR001452; SH3_domain.
 IPR003096; SM22_calponin. 
Pfam
 PF00130; C1_1
 PF00307; CH
 PF00169; PH
 PF00621; RhoGEF
 PF00017; SH2
 PF00018; SH3_1 
SMART
 SM00109; C1
 SM00033; CH
 SM00233; PH
 SM00325; RhoGEF
 SM00252; SH2
 SM00326; SH3 
PROSITE
 PS50021; CH
 PS00741; DH_1
 PS50010; DH_2
 PS50003; PH_DOMAIN
 PS50001; SH2
 PS50002; SH3
 PS00479; ZF_DAG_PE_1
 PS50081; ZF_DAG_PE_2 
PRINTS
 PR00401; SH2DOMAIN.
 PR00452; SH3DOMAIN.
 PR00888; SM22CALPONIN.