VAV3_HUMAN - dbPTM
VAV3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID VAV3_HUMAN
UniProt AC Q9UKW4
Protein Name Guanine nucleotide exchange factor VAV3
Gene Name VAV3
Organism Homo sapiens (Human).
Sequence Length 847
Subcellular Localization
Protein Description Exchange factor for GTP-binding proteins RhoA, RhoG and, to a lesser extent, Rac1. Binds physically to the nucleotide-free states of those 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). May be important for integrin-mediated signaling, at least in some cell types. In osteoclasts, along with SYK tyrosine kinase, required for signaling through integrin alpha-v/beta-1 (ITAGV-ITGB1), a crucial event for osteoclast proper cytoskeleton organization and function. This signaling pathway involves RAC1, but not RHO, activation. Necessary for proper wound healing. In the course of wound healing, required for the phagocytotic cup formation preceding macrophage phagocytosis of apoptotic neutrophils. Responsible for integrin beta-2 (ITGB2)-mediated macrophage adhesion and, to a lesser extent, contributes to beta-3 (ITGB3)-mediated adhesion. Does not affect integrin beta-1 (ITGB1)-mediated adhesion (By similarity)..
Protein Sequence MEPWKQCAQWLIHCKVLPTNHRVTWDSAQVFDLAQTLRDGVLLCQLLNNLRAHSINLKEINLRPQMSQFLCLKNIRTFLTACCETFGMRKSELFEAFDLFDVRDFGKVIETLSRLSRTPIALATGIRPFPTEESINDEDIYKGLPDLIDETLVEDEEDLYDCVYGEDEGGEVYEDLMKAEEAHQPKCPENDIRSCCLAEIKQTEEKYTETLESIEKYFMAPLKRFLTAAEFDSVFINIPELVKLHRNLMQEIHDSIVNKNDQNLYQVFINYKERLVIYGQYCSGVESAISSLDYISKTKEDVKLKLEECSKRANNGKFTLRDLLVVPMQRVLKYHLLLQELVKHTTDPTEKANLKLALDAMKDLAQYVNEVKRDNETLREIKQFQLSIENLNQPVLLFGRPQGDGEIRITTLDKHTKQERHIFLFDLAVIVCKRKGDNYEMKEIIDLQQYKIANNPTTDKENKKWSYGFYLIHTQGQNGLEFYCKTKDLKKKWLEQFEMALSNIRPDYADSNFHDFKMHTFTRVTSCKVCQMLLRGTFYQGYLCFKCGARAHKECLGRVDNCGRVNSGEQGTLKLPEKRTNGLRRTPKQVDPGLPKMQVIRNYSGTPPPALHEGPPLQLQAGDTVELLKGDAHSLFWQGRNLASGEVGFFPSDAVKPCPCVPKPVDYSCQPWYAGAMERLQAETELINRVNSTYLVRHRTKESGEYAISIKYNNEAKHIKILTRDGFFHIAENRKFKSLMELVEYYKHHSLKEGFRTLDTTLQFPYKEPEHSAGQRGNRAGNSLLSPKVLGIAIARYDFCARDMRELSLLKGDVVKIYTKMSANGWWRGEVNGRVGWFPSTYVEEDE
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
28UbiquitinationHRVTWDSAQVFDLAQ
CCCCCCHHHHHHHHH		13.6929967540
77PhosphorylationLCLKNIRTFLTACCE
HHHHHHHHHHHHHHH		21.1426552605
80PhosphorylationKNIRTFLTACCETFG
HHHHHHHHHHHHHHC		17.2926552605
85PhosphorylationFLTACCETFGMRKSE
HHHHHHHHHCCCHHH		16.1526552605
96UbiquitinationRKSELFEAFDLFDVR
CHHHHHHHHCCCCHH		8.9129967540
107UbiquitinationFDVRDFGKVIETLSR
CCHHHHHHHHHHHHH		39.7824816145
131PhosphorylationTGIRPFPTEESINDE
CCCCCCCCCCCCCHH		53.4122817900
134PhosphorylationRPFPTEESINDEDIY
CCCCCCCCCCHHHHH		22.0622817900
141PhosphorylationSINDEDIYKGLPDLI
CCCHHHHHCCCHHHH		16.0114702039
157UbiquitinationETLVEDEEDLYDCVY
HHCCCCCHHHHHHHC		66.6829967540
160UbiquitinationVEDEEDLYDCVYGED
CCCCHHHHHHHCCCC		21.4429967540
160PhosphorylationVEDEEDLYDCVYGED
CCCCHHHHHHHCCCC		21.44-
164PhosphorylationEDLYDCVYGEDEGGE
HHHHHHHCCCCCCCC		22.56-
173PhosphorylationEDEGGEVYEDLMKAE
CCCCCCHHHHHHHHH		10.2211917103
187UbiquitinationEEAHQPKCPENDIRS
HHHHCCCCCHHHHHH		6.9529967540
192UbiquitinationPKCPENDIRSCCLAE
CCCCHHHHHHHHHHH		5.4229967540
201UbiquitinationSCCLAEIKQTEEKYT
HHHHHHHHHCHHHHH		42.5529967540
206UbiquitinationEIKQTEEKYTETLES
HHHHCHHHHHHHHHH		51.7629967540
207UbiquitinationIKQTEEKYTETLESI
HHHCHHHHHHHHHHH		17.0629967540
207PhosphorylationIKQTEEKYTETLESI
HHHCHHHHHHHHHHH		17.0624275569
208PhosphorylationKQTEEKYTETLESIE
HHCHHHHHHHHHHHH		33.30-
210PhosphorylationTEEKYTETLESIEKY
CHHHHHHHHHHHHHH		28.2024275569
213PhosphorylationKYTETLESIEKYFMA
HHHHHHHHHHHHHHH		38.88-
217PhosphorylationTLESIEKYFMAPLKR
HHHHHHHHHHHHHHH		5.94-
223AcetylationKYFMAPLKRFLTAAE
HHHHHHHHHHHHHHH		39.7925953088
237UbiquitinationEFDSVFINIPELVKL
HCCEEEECHHHHHHH		32.0922817900
239 (in isoform 2)Ubiquitination-25.1221906983
239UbiquitinationDSVFINIPELVKLHR
CEEEECHHHHHHHHH		25.1222817900
251UbiquitinationLHRNLMQEIHDSIVN
HHHHHHHHHHHHHHC		28.4629967540
256UbiquitinationMQEIHDSIVNKNDQN
HHHHHHHHHCCCCCC		5.0129967540
265PhosphorylationNKNDQNLYQVFINYK
CCCCCCEEHHCCCCH		15.3527174698
271PhosphorylationLYQVFINYKERLVIY
EEHHCCCCHHEEEEE		14.9227174698
278PhosphorylationYKERLVIYGQYCSGV
CHHEEEEEEECCCHH		7.2427174698
281PhosphorylationRLVIYGQYCSGVESA
EEEEEEECCCHHHHH		5.5727174698
283PhosphorylationVIYGQYCSGVESAIS
EEEEECCCHHHHHHH		40.7227174698
287PhosphorylationQYCSGVESAISSLDY
ECCCHHHHHHHHCHH		28.6127174698
290PhosphorylationSGVESAISSLDYISK
CHHHHHHHHCHHHHC		25.2727174698
291PhosphorylationGVESAISSLDYISKT
HHHHHHHHCHHHHCC		21.1027174698
294PhosphorylationSAISSLDYISKTKED
HHHHHCHHHHCCHHH		16.6427174698
296PhosphorylationISSLDYISKTKEDVK
HHHCHHHHCCHHHHC		28.2227174698
298PhosphorylationSLDYISKTKEDVKLK
HCHHHHCCHHHHCHH		32.64-
305AcetylationTKEDVKLKLEECSKR
CHHHHCHHHHHHHHH		48.4025953088
311UbiquitinationLKLEECSKRANNGKF
HHHHHHHHHCCCCCC		68.1629967540
317UbiquitinationSKRANNGKFTLRDLL
HHHCCCCCCCHHHHH		36.98-
319PhosphorylationRANNGKFTLRDLLVV
HCCCCCCCHHHHHHH		25.1124719451
321UbiquitinationNNGKFTLRDLLVVPM
CCCCCCHHHHHHHHH		29.4924816145
323UbiquitinationGKFTLRDLLVVPMQR
CCCCHHHHHHHHHHH		2.9424816145
333UbiquitinationVPMQRVLKYHLLLQE
HHHHHHHHHHHHHHH		27.9722817900
333 (in isoform 1)Ubiquitination-27.9721906983
343UbiquitinationLLLQELVKHTTDPTE
HHHHHHHHCCCCHHH		48.1029967540
351UbiquitinationHTTDPTEKANLKLAL
CCCCHHHHHHHHHHH		45.0829967540
355UbiquitinationPTEKANLKLALDAMK
HHHHHHHHHHHHHHH		31.3629967540
355AcetylationPTEKANLKLALDAMK
HHHHHHHHHHHHHHH		31.3625953088
362UbiquitinationKLALDAMKDLAQYVN
HHHHHHHHHHHHHHH		51.8429967540
372UbiquitinationAQYVNEVKRDNETLR
HHHHHHHHCCCHHHH		48.1029967540
414UbiquitinationIRITTLDKHTKQERH
EEEEEECCCCCCCEE		57.1829967540
417UbiquitinationTTLDKHTKQERHIFL
EEECCCCCCCEEEEE		50.2924816145
435UbiquitinationAVIVCKRKGDNYEMK
EEEECCCCCCCCEEE		56.9929967540
442UbiquitinationKGDNYEMKEIIDLQQ
CCCCCEEEEHHHHHH		33.5529967540
451UbiquitinationIIDLQQYKIANNPTT
HHHHHHHEECCCCCC		30.8829967540
508PhosphorylationLSNIRPDYADSNFHD
HHHCCCCCCCCCCCC		18.2622115753
511PhosphorylationIRPDYADSNFHDFKM
CCCCCCCCCCCCCCE		32.9722817900
528UbiquitinationFTRVTSCKVCQMLLR
EEHHHHHHHHHHHHC		45.90-
539PhosphorylationMLLRGTFYQGYLCFK
HHHCCCCCCCEEHHH		10.81-
567PhosphorylationDNCGRVNSGEQGTLK
CCCCCCCCCCCCCCC		40.6327251275
572PhosphorylationVNSGEQGTLKLPEKR
CCCCCCCCCCCCCCC		22.0328387310
574UbiquitinationSGEQGTLKLPEKRTN
CCCCCCCCCCCCCCC		62.9329967540
580PhosphorylationLKLPEKRTNGLRRTP
CCCCCCCCCCCCCCC		44.7130576142
588UbiquitinationNGLRRTPKQVDPGLP
CCCCCCCCCCCCCCC		63.4429967540
603PhosphorylationKMQVIRNYSGTPPPA
CCCCHHCCCCCCCCC		9.9128450419
604PhosphorylationMQVIRNYSGTPPPAL
CCCHHCCCCCCCCCC		39.4828464451
606PhosphorylationVIRNYSGTPPPALHE
CHHCCCCCCCCCCCC		27.0425159151
624PhosphorylationLQLQAGDTVELLKGD
EECCCCCCEEEECCC		18.2428464451
656UbiquitinationFFPSDAVKPCPCVPK
CCCCCCCCCCCCCCC		42.4929967540
667PhosphorylationCVPKPVDYSCQPWYA
CCCCCCCCCCCHHHH		16.16-
700PhosphorylationTYLVRHRTKESGEYA
EEEEEEEECCCCCEE		32.7927690223
703PhosphorylationVRHRTKESGEYAISI
EEEEECCCCCEEEEE		38.1827690223
706PhosphorylationRTKESGEYAISIKYN
EECCCCCEEEEEEEC		16.8627690223
717UbiquitinationIKYNNEAKHIKILTR
EEECCCCCEEEEEEC		39.4229967540
720UbiquitinationNNEAKHIKILTRDGF
CCCCCEEEEEECCCC		31.2329967540
735"N6,N6-dimethyllysine"FHIAENRKFKSLMEL
CHHHHCCHHHHHHHH		69.59-
735MethylationFHIAENRKFKSLMEL
CHHHHCCHHHHHHHH		69.5923644510
737MethylationIAENRKFKSLMELVE
HHHCCHHHHHHHHHH		45.7923644510
737"N6,N6-dimethyllysine"IAENRKFKSLMELVE
HHHCCHHHHHHHHHH		45.79-
738PhosphorylationAENRKFKSLMELVEY
HHCCHHHHHHHHHHH		35.7624719451
747UbiquitinationMELVEYYKHHSLKEG
HHHHHHHHHCCHHHC		33.6629967540
750PhosphorylationVEYYKHHSLKEGFRT
HHHHHHCCHHHCCCC		40.6424719451
752UbiquitinationYYKHHSLKEGFRTLD
HHHHCCHHHCCCCCC		59.8229967540
767UbiquitinationTTLQFPYKEPEHSAG
EEEECCCCCCCCCCC		68.0129967540
783PhosphorylationRGNRAGNSLLSPKVL
CCCCCCCCCCCHHHH		29.7523403867
786PhosphorylationRAGNSLLSPKVLGIA
CCCCCCCCHHHHHHH		28.1525159151
788UbiquitinationGNSLLSPKVLGIAIA
CCCCCCHHHHHHHHH		46.87-
797PhosphorylationLGIAIARYDFCARDM
HHHHHHHCHHHHCCH		12.3522817900
808PhosphorylationARDMRELSLLKGDVV
HCCHHHHHCCCCCEE		27.2324719451
811UbiquitinationMRELSLLKGDVVKIY
HHHHHCCCCCEEEEE		59.3629967540
816UbiquitinationLLKGDVVKIYTKMSA
CCCCCEEEEEEECCC		29.8229967540
818PhosphorylationKGDVVKIYTKMSANG
CCCEEEEEEECCCCC		8.45-
820UbiquitinationDVVKIYTKMSANGWW
CEEEEEEECCCCCEE		17.56-
840PhosphorylationGRVGWFPSTYVEEDE
CEEEEECCCCEECCC		23.93-
842PhosphorylationVGWFPSTYVEEDE--
EEEECCCCEECCC--		15.36-
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
173YPhosphorylationKinaseSRCP12931
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of VAV3_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 VAV3_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PGFRB_HUMANPDGFRBphysical
10938113
EGFR_HUMANEGFRphysical
10938113
IGF1R_HUMANIGF1Rphysical
11094073
ESR1_HUMANESR1physical
18518979
TRAF6_HUMANTRAF6physical
27507811
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 VAV3_HUMAN

loading...

Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-141 AND SER-786, ANDMASS SPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory