UniProtKB - P27870 (VAV_MOUSE)
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Protein
Proto-oncogene vav
Gene
Vav1
Organism
Mus musculus (Mouse)
Status
Functioni
Couples tyrosine kinase signals with the activation of the Rho/Rac GTPases, thus leading to cell differentiation and/or proliferation.
Regions
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| Zinc fingeri | 515 – 564 | Phorbol-ester/DAG-typePROSITE-ProRule annotationAdd BLAST | 50 |
GO - Molecular functioni
- guanyl-nucleotide exchange factor activity Source: MGI
- metal ion binding Source: UniProtKB-KW
- phosphotyrosine binding Source: MGI
- Rac guanyl-nucleotide exchange factor activity Source: MGI
- Rho guanyl-nucleotide exchange factor activity Source: MGI
GO - Biological processi
- G-protein coupled receptor signaling pathway Source: MGI
- immune response Source: MGI
- integrin-mediated signaling pathway Source: MGI
- intracellular signal transduction Source: MGI
- neutrophil chemotaxis Source: MGI
- phagocytosis Source: MGI
- platelet activation Source: Reactome
- positive regulation of cell adhesion Source: MGI
- positive regulation of GTPase activity Source: MGI
- positive regulation of natural killer cell mediated cytotoxicity Source: MGI
- reactive oxygen species metabolic process Source: MGI
- regulation of cell size Source: Ensembl
- regulation of GTPase activity Source: MGI
- regulation of Rho protein signal transduction Source: InterPro
- small GTPase mediated signal transduction Source: InterPro
- T cell activation Source: MGI
- T cell differentiation Source: MGI
- vascular endothelial growth factor receptor signaling pathway Source: Reactome
Keywordsi
| Molecular function | Guanine-nucleotide releasing factor |
| Ligand | Metal-binding, Zinc |
Enzyme and pathway databases
| Reactomei | R-MMU-114604. GPVI-mediated activation cascade. R-MMU-1257604. PIP3 activates AKT signaling. R-MMU-1433557. Signaling by SCF-KIT. R-MMU-193648. NRAGE signals death through JNK. R-MMU-194840. Rho GTPase cycle. R-MMU-2029482. Regulation of actin dynamics for phagocytic cup formation. R-MMU-2871796. FCERI mediated MAPK activation. R-MMU-2871809. FCERI mediated Ca+2 mobilization. R-MMU-389359. CD28 dependent Vav1 pathway. R-MMU-416482. G alpha (12/13) signalling events. R-MMU-4420097. VEGFA-VEGFR2 Pathway. R-MMU-512988. Interleukin-3, 5 and GM-CSF signaling. R-MMU-5218920. VEGFR2 mediated vascular permeability. R-MMU-6811558. PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling. R-MMU-912631. Regulation of signaling by CBL. R-MMU-983695. Antigen activates B Cell Receptor (BCR) leading to generation of second messengers. |
Names & Taxonomyi
| Protein namesi | Recommended name: Proto-oncogene vavAlternative name(s): p95vav |
| Gene namesi | Name:Vav1 Synonyms:Vav |
| Organismi | Mus musculus (Mouse) |
| Taxonomic identifieri | 10090 [NCBI] |
| Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Mus › Mus |
| Proteomesi |
|
Organism-specific databases
| MGIi | MGI:98923. Vav1. |
Pathology & Biotechi
Mutagenesis
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| Mutagenesisi | 529 | C → S: Abolishes transforming activity. 1 Publication | 1 | |
| Mutagenesisi | 532 | C → S: Abolishes transforming activity. 1 Publication | 1 | |
| Mutagenesisi | 554 | H → D: Abolishes transforming activity. 1 Publication | 1 |
Keywords - Diseasei
Proto-oncogenePTM / Processingi
Molecule processing
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| ChainiPRO_0000080981 | 1 – 845 | Proto-oncogene vavAdd BLAST | 845 |
Amino acid modifications
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| Modified residuei | 826 | PhosphotyrosineBy similarity | 1 | |
| Modified residuei | 844 | PhosphotyrosineCombined sources | 1 |
Post-translational modificationi
Phosphorylated by FYN (By similarity). Phosphorylated on tyrosine residues by HCK in response to IFNG and bacterial lipopolysaccharide (LPS).By similarity3 Publications
Keywords - PTMi
PhosphoproteinProteomic databases
| EPDi | P27870. |
| PaxDbi | P27870. |
| PeptideAtlasi | P27870. |
| PRIDEi | P27870. |
PTM databases
| iPTMneti | P27870. |
| PhosphoSitePlusi | P27870. |
Expressioni
Tissue specificityi
Widely expressed in hematopoietic cells but not in other cell types. Found in the spleen and lung.1 Publication
Gene expression databases
| Bgeei | ENSMUSG00000034116. |
| CleanExi | MM_VAV1. |
| ExpressionAtlasi | P27870. baseline and differential. |
| Genevisiblei | P27870. MM. |
Interactioni
Subunit structurei
Interacts with SHB (By similarity). Interacts with APS, DOCK2, GRB2, GRB3, DOCK2, SLA, TEC and ZNF655/VIK. Interacts with SIAH2; without leading to its degradation. Associates with BLNK, PLCG1, GRB2 and NCK1 in a B-cell antigen receptor-dependent fashion. Interacts with CBLB; which inhibits tyrosine phosphorylation and down-regulates activity (PubMed:10646609, PubMed:10646608). May interact with CCPG1 (PubMed:17000758). Interacts with CLNK (PubMed:11463797). Interacts with THEMIS2 (PubMed:20644716). Interacts with NEK3 and this interaction is prolactin-dependent. Interacts with ITK. Interacts with PTK2B/PYK2 (By similarity). Interacts with HCK. Interacts with PTK2B/PYK2. Interacts (via SH2 domain) with SYK (By similarity). Interacts with ANKRD54 (PubMed:19064729). Interacts with CD6 (PubMed:24584089).By similarity9 Publications
GO - Molecular functioni
- phosphotyrosine binding Source: MGI
Protein-protein interaction databases
| BioGridi | 204500. 8 interactors. |
| DIPi | DIP-31010N. |
| IntActi | P27870. 12 interactors. |
| MINTi | MINT-85069. |
| STRINGi | 10090.ENSMUSP00000005889. |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| Helixi | 170 – 177 | Combined sources | 8 | |
| Turni | 178 – 180 | Combined sources | 3 | |
| Helixi | 191 – 219 | Combined sources | 29 | |
| Helixi | 221 – 224 | Combined sources | 4 | |
| Turni | 225 – 227 | Combined sources | 3 | |
| Helixi | 230 – 237 | Combined sources | 8 | |
| Helixi | 240 – 259 | Combined sources | 20 | |
| Helixi | 261 – 263 | Combined sources | 3 | |
| Helixi | 266 – 273 | Combined sources | 8 | |
| Helixi | 276 – 278 | Combined sources | 3 | |
| Helixi | 279 – 300 | Combined sources | 22 | |
| Helixi | 302 – 316 | Combined sources | 15 | |
| Helixi | 322 – 325 | Combined sources | 4 | |
| Helixi | 328 – 333 | Combined sources | 6 | |
| Helixi | 336 – 346 | Combined sources | 11 | |
| Helixi | 350 – 389 | Combined sources | 40 | |
| Beta strandi | 390 – 392 | Combined sources | 3 | |
| Helixi | 397 – 400 | Combined sources | 4 | |
| Beta strandi | 402 – 412 | Combined sources | 11 | |
| Beta strandi | 420 – 437 | Combined sources | 18 | |
| Beta strandi | 440 – 448 | Combined sources | 9 | |
| Turni | 449 – 451 | Combined sources | 3 | |
| Beta strandi | 452 – 455 | Combined sources | 4 | |
| Beta strandi | 469 – 475 | Combined sources | 7 | |
| Beta strandi | 481 – 488 | Combined sources | 8 | |
| Helixi | 489 – 506 | Combined sources | 18 | |
| Turni | 509 – 512 | Combined sources | 4 | |
| Helixi | 513 – 515 | Combined sources | 3 | |
| Beta strandi | 518 – 521 | Combined sources | 4 | |
| Turni | 530 – 532 | Combined sources | 3 | |
| Beta strandi | 538 – 541 | Combined sources | 4 | |
| Beta strandi | 543 – 546 | Combined sources | 4 | |
| Turni | 547 – 549 | Combined sources | 3 | |
| Helixi | 555 – 560 | Combined sources | 6 | |
| Turni | 585 – 587 | Combined sources | 3 | |
| Beta strandi | 596 – 599 | Combined sources | 4 | |
| Beta strandi | 603 – 607 | Combined sources | 5 | |
| Helixi | 610 – 612 | Combined sources | 3 | |
| Beta strandi | 624 – 629 | Combined sources | 6 | |
| Beta strandi | 635 – 641 | Combined sources | 7 | |
| Turni | 642 – 644 | Combined sources | 3 | |
| Beta strandi | 647 – 651 | Combined sources | 5 | |
| Helixi | 652 – 654 | Combined sources | 3 | |
| Beta strandi | 655 – 657 | Combined sources | 3 |
3D structure databases
| Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
| 1F5X | NMR | - | A | 170-375 | [»] | |
| 1GCP | X-ray | 2.10 | A/B/C/D | 595-660 | [»] | |
| 1GCQ | X-ray | 1.68 | C | 595-660 | [»] | |
| 1K1Z | NMR | - | A | 583-660 | [»] | |
| 2KBT | NMR | - | A | 784-844 | [»] | |
| 2VRW | X-ray | 1.85 | B | 170-575 | [»] | |
| ProteinModelPortali | P27870. | |||||
| SMRi | P27870. | |||||
| ModBasei | Search... | |||||
| MobiDBi | Search... | |||||
Miscellaneous databases
| EvolutionaryTracei | P27870. |
Family & Domainsi
Domains and Repeats
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| Domaini | 1 – 119 | Calponin-homologyPROSITE-ProRule annotationAdd BLAST | 119 | |
| Domaini | 194 – 373 | DHPROSITE-ProRule annotationAdd BLAST | 180 | |
| Domaini | 402 – 504 | PHPROSITE-ProRule annotationAdd BLAST | 103 | |
| Domaini | 617 – 660 | SH3 1PROSITE-ProRule annotationAdd BLAST | 44 | |
| Domaini | 671 – 765 | SH2PROSITE-ProRule annotationAdd BLAST | 95 | |
| Domaini | 782 – 842 | SH3 2PROSITE-ProRule annotationAdd BLAST | 61 |
Compositional bias
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| Compositional biasi | 33 – 99 | Leu-richAdd BLAST | 67 |
Domaini
The DH domain is involved in interaction with CCPG1.
Zinc finger
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| Zinc fingeri | 515 – 564 | Phorbol-ester/DAG-typePROSITE-ProRule annotationAdd BLAST | 50 |
Keywords - Domaini
Repeat, SH2 domain, SH3 domain, Zinc-fingerPhylogenomic databases
| eggNOGi | KOG2996. Eukaryota. ENOG410XPH6. LUCA. |
| GeneTreei | ENSGT00880000137925. |
| HOGENOMi | HOG000234364. |
| HOVERGENi | HBG018066. |
| InParanoidi | P27870. |
| KOi | K05730. |
| OMAi | EKDNKKW. |
| OrthoDBi | EOG091G01O3. |
| PhylomeDBi | P27870. |
| TreeFami | TF316171. |
Family and domain databases
| CDDi | cd00029. C1. 1 hit. |
| Gene3Di | 1.10.418.10. 1 hit. 2.30.29.30. 1 hit. 3.30.505.10. 1 hit. |
| InterProi | View protein in InterPro IPR022613. CAMSAP_CH. IPR001715. CH-domain. IPR000219. DH-domain. IPR001331. GDS_CDC24_CS. IPR002219. PE/DAG-bd. IPR011993. PH_dom-like. IPR001849. PH_domain. IPR000980. SH2. IPR001452. SH3_domain. IPR003096. SM22_calponin. IPR028530. Vav. |
| PANTHERi | PTHR22826:SF178. PTHR22826:SF178. 1 hit. |
| Pfami | View protein in Pfam PF00130. C1_1. 1 hit. PF11971. CAMSAP_CH. 1 hit. PF00169. PH. 1 hit. PF00621. RhoGEF. 1 hit. PF00017. SH2. 1 hit. PF00018. SH3_1. 2 hits. |
| PRINTSi | PR00401. SH2DOMAIN. PR00452. SH3DOMAIN. PR00888. SM22CALPONIN. |
| SMARTi | View protein in SMART SM00109. C1. 1 hit. SM00033. CH. 1 hit. SM00233. PH. 1 hit. SM00325. RhoGEF. 1 hit. SM00252. SH2. 1 hit. SM00326. SH3. 2 hits. |
| SUPFAMi | SSF47576. SSF47576. 1 hit. SSF48065. SSF48065. 1 hit. SSF50044. SSF50044. 1 hit. SSF50729. SSF50729. 1 hit. SSF55550. SSF55550. 1 hit. |
| PROSITEi | View protein in PROSITE PS50021. CH. 1 hit. PS00741. DH_1. 1 hit. PS50010. DH_2. 1 hit. PS50003. PH_DOMAIN. 1 hit. PS50001. SH2. 1 hit. PS50002. SH3. 2 hits. PS00479. ZF_DAG_PE_1. 1 hit. PS50081. ZF_DAG_PE_2. 1 hit. |
Sequencei
Sequence statusi: Complete.
P27870-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MELWRQCTHW LIQCRVLPPS HRVTWEGAQV CELAQALRDG VLLCQLLNNL
60 70 80 90 100
LPQAINLREV NLRPQMSQFL CLKNIRTFLS TCCEKFGLKR SELFEAFDLF
110 120 130 140 150
DVQDFGKVIY TLSALSWTPI AQNKGIMPFP TEDSALNDED IYSGLSDQID
160 170 180 190 200
DTAEEDEDLY DCVENEEAEG DEIYEDLMRL ESVPTPPKMT EYDKRCCCLR
210 220 230 240 250
EIQQTEEKYT DTLGSIQQHF MKPLQRFLKP QDMETIFVNI EELFSVHTHF
260 270 280 290 300
LKELKDALAG PGATTLYQVF IKYKERFLVY GRYCSQVESA SKHLDQVATA
310 320 330 340 350
REDVQMKLEE CSQRANNGRF TLRDLLMVPM QRVLKYHLLL QELVKHTQDA
360 370 380 390 400
TEKENLRLAL DAMRDLAQCV NEVKRDNETL RQITNFQLSI ENLDQSLANY
410 420 430 440 450
GRPKIDGELK ITSVERRSKT DRYAFLLDKA LLICKRRGDS YDLKASVNLH
460 470 480 490 500
SFQVRDDSSG ERDNKKWSHM FLLIEDQGAQ GYELFFKTRE LKKKWMEQFE
510 520 530 540 550
MAISNIYPEN ATANGHDFQM FSFEETTSCK ACQMLLRGTF YQGYRCYRCR
560 570 580 590 600
APAHKECLGR VPPCGRHGQD FAGTMKKDKL HRRAQDKKRN ELGLPKMEVF
610 620 630 640 650
QEYYGIPPPP GAFGPFLRLN PGDIVELTKA EAEHNWWEGR NTATNEVGWF
660 670 680 690 700
PCNRVHPYVH GPPQDLSVHL WYAGPMERAG AEGILTNRSD GTYLVRQRVK
710 720 730 740 750
DTAEFAISIK YNVEVKHIKI MTSEGLYRIT EKKAFRGLLE LVEFYQQNSL
760 770 780 790 800
KDCFKSLDTT LQFPYKEPER RAISKPPAGS TKYFGTAKAR YDFCARDRSE
810 820 830 840
LSLKEGDIIK ILNKKGQQGW WRGEIYGRIG WFPSNYVEED YSEYC
Experimental Info
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| Sequence conflicti | 29 | Q → E in AAA63402 (PubMed:2005887).Curated | 1 | |
| Sequence conflicti | 226 | R → L in BAC40436 (PubMed:16141072).Curated | 1 |
Sequence databases
| Select the link destinations: EMBLi GenBanki DDBJi Links Updated | X64361 mRNA. Translation: CAA45713.1. AK088586 mRNA. Translation: BAC40436.1. M59833 mRNA. Translation: AAA63402.1. |
| CCDSi | CCDS28931.1. |
| PIRi | A61187. TVMSVV. |
| RefSeqi | NP_035821.3. NM_011691.4. |
| UniGenei | Mm.248172. |
Genome annotation databases
| Ensembli | ENSMUST00000005889; ENSMUSP00000005889; ENSMUSG00000034116. |
| GeneIDi | 22324. |
| KEGGi | mmu:22324. |
| UCSCi | uc008dep.2. mouse. |
Similar proteinsi
Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:| 100% | UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry. |
| 90% | UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence). |
| 50% | UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster. |
Entry informationi
| Entry namei | VAV_MOUSE | |
| Accessioni | P27870Primary (citable) accession number: P27870 Secondary accession number(s): Q8BTV7 | |
| Entry historyi | Integrated into UniProtKB/Swiss-Prot: | August 1, 1992 |
| Last sequence update: | August 1, 1992 | |
| Last modified: | July 5, 2017 | |
| This is version 186 of the entry and version 1 of the sequence. See complete history. | ||
| Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
| Annotation program | Chordata Protein Annotation Program | |
Miscellaneousi
Keywords - Technical termi
3D-structure, Complete proteome, Reference proteomeDocuments
- MGD cross-references
Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot - PDB cross-references
Index of Protein Data Bank (PDB) cross-references
