VAV_MOUSE - dbPTM
VAV_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID VAV_MOUSE
UniProt AC P27870
Protein Name Proto-oncogene vav
Gene Name Vav1
Organism Mus musculus (Mouse).
Sequence Length 845
Subcellular Localization
Protein Description Couples tyrosine kinase signals with the activation of the Rho/Rac GTPases, thus leading to cell differentiation and/or proliferation..
Protein Sequence MELWRQCTHWLIQCRVLPPSHRVTWEGAQVCELAQALRDGVLLCQLLNNLLPQAINLREVNLRPQMSQFLCLKNIRTFLSTCCEKFGLKRSELFEAFDLFDVQDFGKVIYTLSALSWTPIAQNKGIMPFPTEDSALNDEDIYSGLSDQIDDTAEEDEDLYDCVENEEAEGDEIYEDLMRLESVPTPPKMTEYDKRCCCLREIQQTEEKYTDTLGSIQQHFMKPLQRFLKPQDMETIFVNIEELFSVHTHFLKELKDALAGPGATTLYQVFIKYKERFLVYGRYCSQVESASKHLDQVATAREDVQMKLEECSQRANNGRFTLRDLLMVPMQRVLKYHLLLQELVKHTQDATEKENLRLALDAMRDLAQCVNEVKRDNETLRQITNFQLSIENLDQSLANYGRPKIDGELKITSVERRSKTDRYAFLLDKALLICKRRGDSYDLKASVNLHSFQVRDDSSGERDNKKWSHMFLLIEDQGAQGYELFFKTRELKKKWMEQFEMAISNIYPENATANGHDFQMFSFEETTSCKACQMLLRGTFYQGYRCYRCRAPAHKECLGRVPPCGRHGQDFAGTMKKDKLHRRAQDKKRNELGLPKMEVFQEYYGIPPPPGAFGPFLRLNPGDIVELTKAEAEHNWWEGRNTATNEVGWFPCNRVHPYVHGPPQDLSVHLWYAGPMERAGAEGILTNRSDGTYLVRQRVKDTAEFAISIKYNVEVKHIKIMTSEGLYRITEKKAFRGLLELVEFYQQNSLKDCFKSLDTTLQFPYKEPERRAISKPPAGSTKYFGTAKARYDFCARDRSELSLKEGDIIKILNKKGQQGWWRGEIYGRIGWFPSNYVEEDYSEYC
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
110PhosphorylationQDFGKVIYTLSALSW
HHHHHHHHHHHHCCC
12.4825367039
111PhosphorylationDFGKVIYTLSALSWT
HHHHHHHHHHHCCCC
11.7825367039
142PhosphorylationALNDEDIYSGLSDQI
CCCCHHHHCCCHHHC
14.7010669745
160PhosphorylationAEEDEDLYDCVENEE
CCCCCCHHHHHHCCC
21.4410669745
174PhosphorylationEAEGDEIYEDLMRLE
CCCCCHHHHHHHCCC
11.0110669745
182PhosphorylationEDLMRLESVPTPPKM
HHHHCCCCCCCCCCC
37.6825159016
185PhosphorylationMRLESVPTPPKMTEY
HCCCCCCCCCCCCHH
50.4927180971
192PhosphorylationTPPKMTEYDKRCCCL
CCCCCCHHHHHHHHH
20.00-
245PhosphorylationVNIEELFSVHTHFLK
ECHHHHHHHHHHHHH
26.1328978645
265PhosphorylationLAGPGATTLYQVFIK
HCCCCCCCHHHHHHH
23.9625367039
267PhosphorylationGPGATTLYQVFIKYK
CCCCCCHHHHHHHHH
10.6722817900
283PhosphorylationRFLVYGRYCSQVESA
HHHHCCCHHHHHHHH
7.6530635358
285PhosphorylationLVYGRYCSQVESASK
HHCCCHHHHHHHHHH
28.4630635358
289PhosphorylationRYCSQVESASKHLDQ
CHHHHHHHHHHHHHH
38.7030635358
291PhosphorylationCSQVESASKHLDQVA
HHHHHHHHHHHHHHH
29.8630635358
321PhosphorylationRANNGRFTLRDLLMV
HHHCCCCCHHHHHHH
21.3724719451
423PhosphorylationRRSKTDRYAFLLDKA
CCCCCHHHHHHHHHH
12.43-
541PhosphorylationMLLRGTFYQGYRCYR
HHHHCCCCCCEEEEE
10.81-
544PhosphorylationRGTFYQGYRCYRCRA
HCCCCCCEEEEEECC
5.08-
547PhosphorylationFYQGYRCYRCRAPAH
CCCCEEEEEECCCCC
12.07-
574PhosphorylationHGQDFAGTMKKDKLH
CCCCCCHHHCHHHHH
23.5326824392
587AcetylationLHRRAQDKKRNELGL
HHHHHHHHHHHHCCC
41.377923493
588AcetylationHRRAQDKKRNELGLP
HHHHHHHHHHHCCCC
69.607923503
658PhosphorylationPCNRVHPYVHGPPQD
ECCCCCCCCCCCCCC
7.09-
692PhosphorylationLTNRSDGTYLVRQRV
EECCCCCCEEEEEEE
20.7629176673
745PhosphorylationLLELVEFYQQNSLKD
HHHHHHHHHHCCHHH
8.83-
756PhosphorylationSLKDCFKSLDTTLQF
CHHHHHHHCCCCCCC
15.9529472430
759PhosphorylationDCFKSLDTTLQFPYK
HHHHHCCCCCCCCCC
34.4029472430
760PhosphorylationCFKSLDTTLQFPYKE
HHHHCCCCCCCCCCC
20.4429472430
780PhosphorylationISKPPAGSTKYFGTA
CCCCCCCCCCEEEEH
24.6725266776
781PhosphorylationSKPPAGSTKYFGTAK
CCCCCCCCCEEEEHH
28.9229472430
791PhosphorylationFGTAKARYDFCARDR
EEEHHHHEEECCCCC
20.45-
802PhosphorylationARDRSELSLKEGDII
CCCCCCCCCCCCCEE
33.0922817900
826PhosphorylationGWWRGEIYGRIGWFP
CEECCEEEEECCCCH
8.9629899451
834PhosphorylationGRIGWFPSNYVEEDY
EECCCCHHHHCCCCH
31.1725367039
836PhosphorylationIGWFPSNYVEEDYSE
CCCCHHHHCCCCHHH
17.3625159016
841PhosphorylationSNYVEEDYSEYC---
HHHCCCCHHHCC---
13.4925159016
842PhosphorylationNYVEEDYSEYC----
HHCCCCHHHCC----
34.1225159016
844PhosphorylationVEEDYSEYC------
CCCCHHHCC------
9.492069873

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
142YPhosphorylationKinaseLCKP06239
PSP
142YPhosphorylationKinaseLCKP06240
PhosphoELM
160YPhosphorylationKinaseLCKP06239
PSP
160YPhosphorylationKinaseLCKP06240
PhosphoELM
174YPhosphorylationKinaseLCKP06239
PSP
174YPhosphorylationKinaseLCKP06240
PhosphoELM
174YPhosphorylationKinaseSRCP12931
PSP
-KUbiquitinationE3 ubiquitin ligaseCblP22682
PMID:22199232

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of VAV_MOUSE !!

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 VAV_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ITK_MOUSEItkgenetic
19009524
MK14_MOUSEMapk14physical
9064344
CD3Z_MOUSECd247physical
9064344
CD3E_MOUSECd3ephysical
9064344
ZAP70_MOUSEZap70physical
26936881

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of VAV_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative time-resolved phosphoproteomic analysis of mast cellsignaling.";
Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,Kawakami T., Salomon A.R.;
J. Immunol. 179:5864-5876(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-844, AND MASSSPECTROMETRY.

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