VAV2_HUMAN - dbPTM
VAV2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID VAV2_HUMAN
UniProt AC P52735
Protein Name Guanine nucleotide exchange factor VAV2
Gene Name VAV2
Organism Homo sapiens (Human).
Sequence Length 878
Subcellular Localization
Protein Description Guanine nucleotide exchange factor for the Rho family of Ras-related GTPases. Plays an important role in angiogenesis. Its recruitment by phosphorylated EPHA2 is critical for EFNA1-induced RAC1 GTPase activation and vascular endothelial cell migration and assembly (By similarity)..
Protein Sequence MEQWRQCGRWLIDCKVLPPNHRVVWPSAVVFDLAQALRDGVLLCQLLHNLSPGSIDLKDINFRPQMSQFLCLKNIRTFLKVCHDKFGLRNSELFDPFDLFDVRDFGKVISAVSRLSLHSIAQNKGIRPFPSEETTENDDDVYRSLEELADEHDLGEDIYDCVPCEDGGDDIYEDIIKVEVQQPMIRYMQKMGMTEDDKRNCCLLEIQETEAKYYRTLEDIEKNYMSPLRLVLSPADMAAVFINLEDLIKVHHSFLRAIDVSVMVGGSTLAKVFLDFKERLLIYGEYCSHMEHAQNTLNQLLASREDFRQKVEECTLKVQDGKFKLQDLLVVPMQRVLKYHLLLKELLSHSAERPERQQLKEALEAMQDLAMYINEVKRDKETLRKISEFQSSIENLQVKLEEFGRPKIDGELKVRSIVNHTKQDRYLFLFDKVVIVCKRKGYSYELKEIIELLFHKMTDDPMNNKDVKKSHGKMWSYGFYLIHLQGKQGFQFFCKTEDMKRKWMEQFEMAMSNIKPDKANANHHSFQMYTFDKTTNCKACKMFLRGTFYQGYMCTKCGVGAHKECLEVIPPCKFTSPADLDASGAGPGPKMVAMQNYHGNPAPPGKPVLTFQTGDVLELLRGDPESPWWEGRLVQTRKSGYFPSSSVKPCPVDGRPPISRPPSREIDYTAYPWFAGNMERQQTDNLLKSHASGTYLIRERPAEAERFAISIKFNDEVKHIKVVEKDNWIHITEAKKFDSLLELVEYYQCHSLKESFKQLDTTLKYPYKSRERSASRASSRSPASCASYNFSFLSPQGLSFASQGPSAPFWSVFTPRVIGTAVARYNFAARDMRELSLREGDVVRIYSRIGGDQGWWKGETNGRIGWFPSTYVEEEGIQ
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
54PhosphorylationLHNLSPGSIDLKDIN
HHHCCCCCCCHHHCC		19.1324961811
91PhosphorylationDKFGLRNSELFDPFD
HHHCCCCCCCCCCCC		29.2822617229
116O-linked_GlycosylationISAVSRLSLHSIAQN
HHHHHHHCHHHHHHC		23.9529237092
116PhosphorylationISAVSRLSLHSIAQN
HHHHHHHCHHHHHHC		23.9520873877
119O-linked_GlycosylationVSRLSLHSIAQNKGI
HHHHCHHHHHHCCCC		25.5529237092
119PhosphorylationVSRLSLHSIAQNKGI
HHHHCHHHHHHCCCC		25.5520873877
124UbiquitinationLHSIAQNKGIRPFPS
HHHHHHCCCCCCCCC		43.5729967540
142PhosphorylationTENDDDVYRSLEELA
CCCCHHHHHHHHHHH		11.0721082442
159PhosphorylationHDLGEDIYDCVPCED
CCCCCCCCCCCCCCC		18.6612454019
172PhosphorylationEDGGDDIYEDIIKVE
CCCCCCHHHHHHHHC		17.9712454019
187PhosphorylationVQQPMIRYMQKMGMT
CCHHHHHHHHHCCCC		7.9329759185
189 (in isoform 2)Phosphorylation-24.53-
189 (in isoform 3)Phosphorylation-24.53-
194PhosphorylationYMQKMGMTEDDKRNC
HHHHCCCCHHHCCCE		30.4529759185
207UbiquitinationNCCLLEIQETEAKYY
CEEEEEEEHHHHHHH		42.0329967540
212UbiquitinationEIQETEAKYYRTLED
EEEHHHHHHHCCHHH		36.2629967540
213PhosphorylationIQETEAKYYRTLEDI
EEHHHHHHHCCHHHH		12.7725627689
214PhosphorylationQETEAKYYRTLEDIE
EHHHHHHHCCHHHHH		9.0925627689
216PhosphorylationTEAKYYRTLEDIEKN
HHHHHHCCHHHHHHH		20.5529496907
224PhosphorylationLEDIEKNYMSPLRLV
HHHHHHHCCCCCEEE		15.2729496907
226PhosphorylationDIEKNYMSPLRLVLS
HHHHHCCCCCEEEEC		15.4924719451
283PhosphorylationFKERLLIYGEYCSHM
HHHHHHHHHHHHHHH		12.1329496907
286PhosphorylationRLLIYGEYCSHMEHA
HHHHHHHHHHHHHHH		8.5529496907
312UbiquitinationEDFRQKVEECTLKVQ
HHHHHHHHHCEEEEE		55.1633845483
317UbiquitinationKVEECTLKVQDGKFK
HHHHCEEEEECCCEE		21.5033845483
333UbiquitinationQDLLVVPMQRVLKYH
EEEEEHHHHHHHHHH		2.4122817900
338UbiquitinationVPMQRVLKYHLLLKE
HHHHHHHHHHHHHHH		27.9722817900
372UbiquitinationAMQDLAMYINEVKRD
HHHHHHHHHHHHHCC		8.5932015554
377UbiquitinationAMYINEVKRDKETLR
HHHHHHHHCCHHHHH		49.0232015554
380UbiquitinationINEVKRDKETLRKIS
HHHHHCCHHHHHHHH		57.5429967540
385UbiquitinationRDKETLRKISEFQSS
CCHHHHHHHHHHHHH		54.4129967540
387PhosphorylationKETLRKISEFQSSIE
HHHHHHHHHHHHHHH		35.0825850435
391PhosphorylationRKISEFQSSIENLQV
HHHHHHHHHHHHHHH		38.3124719451
392PhosphorylationKISEFQSSIENLQVK
HHHHHHHHHHHHHHH		24.1225850435
394UbiquitinationSEFQSSIENLQVKLE
HHHHHHHHHHHHHHH		54.5629967540
399UbiquitinationSIENLQVKLEEFGRP
HHHHHHHHHHHHCCC		36.9029967540
402UbiquitinationNLQVKLEEFGRPKID
HHHHHHHHHCCCCCC		64.9329967540
407UbiquitinationLEEFGRPKIDGELKV
HHHHCCCCCCCEEEE		52.6629967540
408UbiquitinationEEFGRPKIDGELKVR
HHHCCCCCCCEEEEE		10.2329967540
413UbiquitinationPKIDGELKVRSIVNH
CCCCCEEEEEEEECC		31.1629967540
426PhosphorylationNHTKQDRYLFLFDKV
CCCCCCEEEEEECEE		15.30-
443PhosphorylationVCKRKGYSYELKEII
EECCCCCCCCHHHHH		22.3129496907
515AcetylationEMAMSNIKPDKANAN
HHHHHCCCCCCCCCC		51.957683641
549PhosphorylationMFLRGTFYQGYMCTK
HHHCCCCCCCCCCCC		10.8129496907
563UbiquitinationKCGVGAHKECLEVIP
CCCCCCCHHHCHHCC		49.9829967540
573UbiquitinationLEVIPPCKFTSPADL
CHHCCCCCCCCHHHC		58.4129967540
575PhosphorylationVIPPCKFTSPADLDA
HCCCCCCCCHHHCCC		21.2129255136
576PhosphorylationIPPCKFTSPADLDAS
CCCCCCCCHHHCCCC		22.6329255136
583PhosphorylationSPADLDASGAGPGPK
CHHHCCCCCCCCCCC		28.9225159151
626PhosphorylationLLRGDPESPWWEGRL
HHCCCCCCCCCCCEE		31.0725159151
639PhosphorylationRLVQTRKSGYFPSSS
EEEEEECCCCCCCCC		35.1225159151
641PhosphorylationVQTRKSGYFPSSSVK
EEEECCCCCCCCCCC		21.2927080861
644PhosphorylationRKSGYFPSSSVKPCP
ECCCCCCCCCCCCCC		25.9127080861
645PhosphorylationKSGYFPSSSVKPCPV
CCCCCCCCCCCCCCC		39.1127080861
646PhosphorylationSGYFPSSSVKPCPVD
CCCCCCCCCCCCCCC		38.2027080861
659PhosphorylationVDGRPPISRPPSREI
CCCCCCCCCCCCCCC		44.5028985074
663PhosphorylationPPISRPPSREIDYTA
CCCCCCCCCCCCCCC		45.2725849741
692PhosphorylationNLLKSHASGTYLIRE
HHHHHHCCCCEEEEE		26.6628857561
694PhosphorylationLKSHASGTYLIRERP
HHHHCCCCEEEEECC		16.8028857561
695PhosphorylationKSHASGTYLIRERPA
HHHCCCCEEEEECCC		12.0323312004
708UbiquitinationPAEAERFAISIKFND
CCCCCEEEEEEECCC		10.8029967540
718UbiquitinationIKFNDEVKHIKVVEK
EECCCCCCEEEEEEC		37.2529967540
747UbiquitinationLLELVEYYQCHSLKE
HHHHHHHHHHHCHHH		7.3729967540
757UbiquitinationHSLKESFKQLDTTLK
HCHHHHHHHHHCCCC		60.2629967540
761PhosphorylationESFKQLDTTLKYPYK
HHHHHHHCCCCCCCH		42.4928152594
762PhosphorylationSFKQLDTTLKYPYKS
HHHHHHCCCCCCCHH		22.4028152594
763 (in isoform 3)Phosphorylation-5.6323090842
765PhosphorylationQLDTTLKYPYKSRER
HHHCCCCCCCHHCCC		18.2028152594
765 (in isoform 3)Phosphorylation-18.2023090842
767PhosphorylationDTTLKYPYKSRERSA
HCCCCCCCHHCCCCC		20.6428152594
768 (in isoform 3)Phosphorylation-38.2330266825
769 (in isoform 3)Phosphorylation-33.2722167270
769PhosphorylationTLKYPYKSRERSASR
CCCCCCHHCCCCCCC		33.2718691976
771 (in isoform 3)Phosphorylation-59.0622167270
773PhosphorylationPYKSRERSASRASSR
CCHHCCCCCCCCCCC		26.3325137130
775PhosphorylationKSRERSASRASSRSP
HHCCCCCCCCCCCCC		29.6225137130
775 (in isoform 3)Phosphorylation-29.6230266825
778PhosphorylationERSASRASSRSPASC
CCCCCCCCCCCCCHH		25.77-
779PhosphorylationRSASRASSRSPASCA
CCCCCCCCCCCCHHH		35.4718669648
781PhosphorylationASRASSRSPASCASY
CCCCCCCCCCHHHCC		27.1118669648
814PhosphorylationAPFWSVFTPRVIGTA
CCCHHCCCHHHHHHH		14.1824719451
836PhosphorylationARDMRELSLREGDVV
HHHHHHHHCCCCCEE		22.1924719451
847PhosphorylationGDVVRIYSRIGGDQG
CCEEEEEEEECCCCC		18.3024719451
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources
142YPhosphorylationKinaseEGFRP00533
Uniprot
142YPhosphorylationKinaseLCKP06239
PhosphoELM
159YPhosphorylationKinaseEGFRP00533
Uniprot
159YPhosphorylationKinaseLCKP06239
PhosphoELM
172YPhosphorylationKinaseEGFRP00533
Uniprot
172YPhosphorylationKinaseLCKP06239
PhosphoELM
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of VAV2_HUMAN !!
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of VAV2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PGFRB_HUMANPDGFRBphysical
10938113
EGFR_HUMANEGFRphysical
10938113
CD19_HUMANCD19physical
11080163
EGFR_HUMANEGFRphysical
20940296
CBL_HUMANCBLphysical
20940296
CCNO_HUMANCCNOphysical
18654987
BRDT_HUMANBRDTphysical
18654987
IF4G3_HUMANEIF4G3physical
18654987
RBBP6_HUMANRBBP6physical
18654987
F10A1_HUMANST13physical
18654987
TM1L1_HUMANTOM1L1physical
18654987
VCIP1_HUMANVCPIP1physical
18654987
PNMA1_HUMANPNMA1physical
18654987
BD1L1_HUMANBOD1L1physical
18654987
SRRT_HUMANSRRTphysical
18654987
FNTA_HUMANFNTAphysical
18654987
TCP11_HUMANTCP11physical
18654987
MARH7_HUMANMARCH7physical
18654987
HS105_HUMANHSPH1physical
18654987
BZW1_HUMANBZW1physical
18654987
PAIRB_HUMANSERBP1physical
18654987
UBP38_HUMANUSP38physical
18654987
UBE4B_HUMANUBE4Bphysical
18654987
GAPD1_HUMANGAPVD1physical
18654987
POGZ_HUMANPOGZphysical
18654987
MRGBP_HUMANMRGBPphysical
18654987
TRBP2_HUMANTARBP2physical
18654987
SF3A3_HUMANSF3A3physical
18654987
SNW1_HUMANSNW1physical
18654987
IPO4_HUMANIPO4physical
18654987
FUCO_HUMANFUCA1physical
18654987
CHMP3_HUMANCHMP3physical
18654987
NCKP5_HUMANNCKAP5physical
18654987
CE170_HUMANCEP170physical
18654987
MED21_HUMANMED21physical
18654987
RD23A_HUMANRAD23Aphysical
18654987
HNRPF_HUMANHNRNPFphysical
18654987
DJC21_HUMANDNAJC21physical
18654987
TITIN_HUMANTTNphysical
18654987
TCPG_HUMANCCT3physical
18654987
DCNL4_HUMANDCUN1D4physical
18654987
STK24_HUMANSTK24physical
18654987
PHF10_HUMANPHF10physical
18654987
PPM1B_HUMANPPM1Bphysical
18654987
ARI1_HUMANARIH1physical
18654987
BIRC6_HUMANBIRC6physical
18654987
SRPK2_HUMANSRPK2physical
18654987
TCPB_HUMANCCT2physical
18654987
RPC9_HUMANCRCPphysical
18654987
CBL_HUMANCBLphysical
11262396
CBLB_HUMANCBLBphysical
9399639
CAV1_HUMANCAV1physical
20808760
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of VAV2_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-576, AND MASSSPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-576 AND SER-626, ANDMASS SPECTROMETRY.
"Multiple reaction monitoring for robust quantitative proteomicanalysis of cellular signaling networks.";
Wolf-Yadlin A., Hautaniemi S., Lauffenburger D.A., White F.M.;
Proc. Natl. Acad. Sci. U.S.A. 104:5860-5865(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-142, AND MASSSPECTROMETRY.
"Mechanism of epidermal growth factor regulation of Vav2, a guaninenucleotide exchange factor for Rac.";
Tamas P., Solti Z., Bauer P., Illes A., Sipeki S., Bauer A.,Farago A., Downward J., Buday L.;
J. Biol. Chem. 278:5163-5171(2003).
Cited for: PHOSPHORYLATION AT TYR-142; TYR-159 AND TYR-172 BY EGFR.

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