Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P27870

- VAV_MOUSE

UniProt

P27870 - VAV_MOUSE

Protein

Proto-oncogene vav

Gene

Vav1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 157 (01 Oct 2014)
      Sequence version 1 (01 Aug 1992)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Couples tyrosine kinase signals with the activation of the Rho/Rac GTPases, thus leading to cell differentiation and/or proliferation.

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri515 – 56450Phorbol-ester/DAG-typePROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. metal ion binding Source: UniProtKB-KW
    2. protein binding Source: MGI
    3. Rac guanyl-nucleotide exchange factor activity Source: MGI
    4. Rho guanyl-nucleotide exchange factor activity Source: MGI

    GO - Biological processi

    1. G-protein coupled receptor signaling pathway Source: MGI
    2. immune response Source: MGI
    3. integrin-mediated signaling pathway Source: MGI
    4. intracellular signal transduction Source: MGI
    5. neutrophil chemotaxis Source: MGI
    6. phagocytosis Source: MGI
    7. positive regulation of cell adhesion Source: MGI
    8. positive regulation of Rac GTPase activity Source: MGI
    9. reactive oxygen species metabolic process Source: MGI
    10. regulation of GTPase activity Source: MGI
    11. small GTPase mediated signal transduction Source: InterPro
    12. T cell activation Source: MGI
    13. T cell differentiation Source: MGI

    Keywords - Molecular functioni

    Guanine-nucleotide releasing factor

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_188194. Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
    REACT_188202. FCERI mediated Ca+2 mobilization.
    REACT_188530. FCERI mediated MAPK activation.
    REACT_188578. Signaling by SCF-KIT.
    REACT_196588. Constitutive PI3K/AKT Signaling in Cancer.
    REACT_198374. Regulation of actin dynamics for phagocytic cup formation.
    REACT_198634. Regulation of signaling by CBL.
    REACT_204733. G alpha (12/13) signalling events.
    REACT_209641. NRAGE signals death through JNK.
    REACT_210090. Rho GTPase cycle.
    REACT_220092. GPVI-mediated activation cascade.
    REACT_225836. Interleukin-3, 5 and GM-CSF signaling.
    REACT_226341. PIP3 activates AKT signaling.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Proto-oncogene vav
    Alternative name(s):
    p95vav
    Gene namesi
    Name:Vav1
    Synonyms:Vav
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 17

    Organism-specific databases

    MGIiMGI:98923. Vav1.

    Subcellular locationi

    GO - Cellular componenti

    1. cell-cell junction Source: MGI
    2. cytosol Source: Reactome

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi529 – 5291C → S: Abolishes transforming activity. 1 Publication
    Mutagenesisi532 – 5321C → S: Abolishes transforming activity. 1 Publication
    Mutagenesisi554 – 5541H → D: Abolishes transforming activity. 1 Publication

    Keywords - Diseasei

    Proto-oncogene

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 845845Proto-oncogene vavPRO_0000080981Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei826 – 8261PhosphotyrosineBy similarity
    Modified residuei844 – 8441Phosphotyrosine1 Publication

    Post-translational modificationi

    Phosphorylated by FYN By similarity. Phosphorylated on tyrosine residues by HCK in response to IFNG and bacterial lipopolysaccharide (LPS).By similarity4 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP27870.
    PaxDbiP27870.
    PRIDEiP27870.

    PTM databases

    PhosphoSiteiP27870.

    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

    ArrayExpressiP27870.
    BgeeiP27870.
    CleanExiMM_VAV1.
    GenevestigatoriP27870.

    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. May interact with CCPG1. Interacts with CLNK. Interacts with THEMIS2. 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.By similarity8 Publications

    Protein-protein interaction databases

    BioGridi204500. 8 interactions.
    DIPiDIP-31010N.
    IntActiP27870. 7 interactions.
    MINTiMINT-85069.

    Structurei

    Secondary structure

    1
    845
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi170 – 1778
    Turni178 – 1803
    Helixi191 – 21929
    Helixi221 – 2244
    Turni225 – 2273
    Helixi230 – 2378
    Helixi240 – 25920
    Helixi261 – 2633
    Helixi266 – 2738
    Helixi276 – 2783
    Helixi279 – 30022
    Helixi302 – 31615
    Helixi322 – 3254
    Helixi328 – 3336
    Helixi336 – 34611
    Helixi350 – 38940
    Beta strandi390 – 3923
    Helixi397 – 4004
    Beta strandi402 – 41211
    Beta strandi420 – 43718
    Beta strandi440 – 4489
    Turni449 – 4513
    Beta strandi452 – 4554
    Beta strandi469 – 4757
    Beta strandi481 – 4888
    Helixi489 – 50618
    Turni509 – 5124
    Helixi513 – 5153
    Beta strandi518 – 5214
    Turni530 – 5323
    Beta strandi538 – 5414
    Beta strandi543 – 5464
    Turni547 – 5493
    Helixi555 – 5606
    Turni585 – 5873
    Beta strandi596 – 5994
    Beta strandi603 – 6075
    Helixi610 – 6123
    Beta strandi624 – 6296
    Beta strandi635 – 6417
    Turni642 – 6443
    Beta strandi647 – 6515
    Helixi652 – 6543
    Beta strandi655 – 6573
    Beta strandi786 – 7916
    Beta strandi796 – 8005
    Beta strandi808 – 8136
    Beta strandi817 – 8259
    Beta strandi828 – 8336
    Beta strandi836 – 8416

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1F5XNMR-A170-375[»]
    1GCPX-ray2.10A/B/C/D595-660[»]
    1GCQX-ray1.68C595-660[»]
    1K1ZNMR-A583-660[»]
    2KBTNMR-A784-844[»]
    2VRWX-ray1.85B170-575[»]
    ProteinModelPortaliP27870.
    SMRiP27870. Positions 2-565, 596-779, 784-844.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP27870.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1 – 119119CHPROSITE-ProRule annotationAdd
    BLAST
    Domaini194 – 373180DHPROSITE-ProRule annotationAdd
    BLAST
    Domaini402 – 504103PHPROSITE-ProRule annotationAdd
    BLAST
    Domaini617 – 66044SH3 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini671 – 76595SH2PROSITE-ProRule annotationAdd
    BLAST
    Domaini782 – 84261SH3 2PROSITE-ProRule annotationAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi33 – 9967Leu-richAdd
    BLAST

    Domaini

    The DH domain is involved in interaction with CCPG1.

    Sequence similaritiesi

    Contains 1 CH (calponin-homology) domain.PROSITE-ProRule annotation
    Contains 1 DH (DBL-homology) domain.PROSITE-ProRule annotation
    Contains 1 PH domain.PROSITE-ProRule annotation
    Contains 1 phorbol-ester/DAG-type zinc finger.PROSITE-ProRule annotation
    Contains 1 SH2 domain.PROSITE-ProRule annotation
    Contains 2 SH3 domains.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri515 – 56450Phorbol-ester/DAG-typePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Repeat, SH2 domain, SH3 domain, Zinc-finger

    Phylogenomic databases

    eggNOGiNOG326494.
    HOGENOMiHOG000234364.
    HOVERGENiHBG018066.
    InParanoidiP27870.
    KOiK05730.
    OMAiSHRVTWD.
    PhylomeDBiP27870.
    TreeFamiTF316171.

    Family and domain databases

    Gene3Di1.10.418.10. 1 hit.
    1.20.900.10. 1 hit.
    2.30.29.30. 1 hit.
    3.30.505.10. 1 hit.
    InterProiIPR022613. CAMSAP_CH.
    IPR001715. CH-domain.
    IPR000219. DH-domain.
    IPR001331. GDS_CDC24_CS.
    IPR001849. PH_domain.
    IPR011993. PH_like_dom.
    IPR002219. Prot_Kinase_C-like_PE/DAG-bd.
    IPR000980. SH2.
    IPR011511. SH3_2.
    IPR001452. SH3_domain.
    IPR003096. SM22_calponin.
    IPR028530. Vav.
    [Graphical view]
    PANTHERiPTHR22826:SF112. PTHR22826:SF112. 1 hit.
    PfamiPF00130. C1_1. 1 hit.
    PF11971. CAMSAP_CH. 1 hit.
    PF00169. PH. 1 hit.
    PF00621. RhoGEF. 1 hit.
    PF00017. SH2. 1 hit.
    PF00018. SH3_1. 1 hit.
    PF07653. SH3_2. 1 hit.
    [Graphical view]
    PRINTSiPR00401. SH2DOMAIN.
    PR00452. SH3DOMAIN.
    PR00888. SM22CALPONIN.
    SMARTiSM00109. C1. 1 hit.
    SM00033. CH. 1 hit.
    SM00233. PH. 1 hit.
    SM00325. RhoGEF. 1 hit.
    SM00252. SH2. 1 hit.
    SM00326. SH3. 2 hits.
    [Graphical view]
    SUPFAMiSSF47576. SSF47576. 1 hit.
    SSF48065. SSF48065. 1 hit.
    SSF50044. SSF50044. 1 hit.
    SSF55550. SSF55550. 1 hit.
    PROSITEiPS50021. 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.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P27870-1 [UniParc]FASTAAdd to Basket

    « Hide

    MELWRQCTHW LIQCRVLPPS HRVTWEGAQV CELAQALRDG VLLCQLLNNL    50
    LPQAINLREV NLRPQMSQFL CLKNIRTFLS TCCEKFGLKR SELFEAFDLF 100
    DVQDFGKVIY TLSALSWTPI AQNKGIMPFP TEDSALNDED IYSGLSDQID 150
    DTAEEDEDLY DCVENEEAEG DEIYEDLMRL ESVPTPPKMT EYDKRCCCLR 200
    EIQQTEEKYT DTLGSIQQHF MKPLQRFLKP QDMETIFVNI EELFSVHTHF 250
    LKELKDALAG PGATTLYQVF IKYKERFLVY GRYCSQVESA SKHLDQVATA 300
    REDVQMKLEE CSQRANNGRF TLRDLLMVPM QRVLKYHLLL QELVKHTQDA 350
    TEKENLRLAL DAMRDLAQCV NEVKRDNETL RQITNFQLSI ENLDQSLANY 400
    GRPKIDGELK ITSVERRSKT DRYAFLLDKA LLICKRRGDS YDLKASVNLH 450
    SFQVRDDSSG ERDNKKWSHM FLLIEDQGAQ GYELFFKTRE LKKKWMEQFE 500
    MAISNIYPEN ATANGHDFQM FSFEETTSCK ACQMLLRGTF YQGYRCYRCR 550
    APAHKECLGR VPPCGRHGQD FAGTMKKDKL HRRAQDKKRN ELGLPKMEVF 600
    QEYYGIPPPP GAFGPFLRLN PGDIVELTKA EAEHNWWEGR NTATNEVGWF 650
    PCNRVHPYVH GPPQDLSVHL WYAGPMERAG AEGILTNRSD GTYLVRQRVK 700
    DTAEFAISIK YNVEVKHIKI MTSEGLYRIT EKKAFRGLLE LVEFYQQNSL 750
    KDCFKSLDTT LQFPYKEPER RAISKPPAGS TKYFGTAKAR YDFCARDRSE 800
    LSLKEGDIIK ILNKKGQQGW WRGEIYGRIG WFPSNYVEED YSEYC 845
    Length:845
    Mass (Da):98,137
    Last modified:August 1, 1992 - v1
    Checksum:i3666DCCD1C5229DA
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti29 – 291Q → E in AAA63402. (PubMed:2005887)Curated
    Sequence conflicti226 – 2261R → L in BAC40436. (PubMed:16141072)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X64361 mRNA. Translation: CAA45713.1.
    AK088586 mRNA. Translation: BAC40436.1.
    M59833 mRNA. Translation: AAA63402.1.
    CCDSiCCDS28931.1.
    PIRiA61187. TVMSVV.
    RefSeqiNP_035821.3. NM_011691.4.
    UniGeneiMm.248172.

    Genome annotation databases

    EnsembliENSMUST00000005889; ENSMUSP00000005889; ENSMUSG00000034116.
    GeneIDi22324.
    KEGGimmu:22324.
    UCSCiuc008dep.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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. Positions 2-565, 596-779, 784-844.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 204500. 8 interactions.
    DIPi DIP-31010N.
    IntActi P27870. 7 interactions.
    MINTi MINT-85069.

    PTM databases

    PhosphoSitei P27870.

    Proteomic databases

    MaxQBi P27870.
    PaxDbi P27870.
    PRIDEi P27870.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000005889 ; ENSMUSP00000005889 ; ENSMUSG00000034116 .
    GeneIDi 22324.
    KEGGi mmu:22324.
    UCSCi uc008dep.2. mouse.

    Organism-specific databases

    CTDi 7409.
    MGIi MGI:98923. Vav1.

    Phylogenomic databases

    eggNOGi NOG326494.
    HOGENOMi HOG000234364.
    HOVERGENi HBG018066.
    InParanoidi P27870.
    KOi K05730.
    OMAi SHRVTWD.
    PhylomeDBi P27870.
    TreeFami TF316171.

    Enzyme and pathway databases

    Reactomei REACT_188194. Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
    REACT_188202. FCERI mediated Ca+2 mobilization.
    REACT_188530. FCERI mediated MAPK activation.
    REACT_188578. Signaling by SCF-KIT.
    REACT_196588. Constitutive PI3K/AKT Signaling in Cancer.
    REACT_198374. Regulation of actin dynamics for phagocytic cup formation.
    REACT_198634. Regulation of signaling by CBL.
    REACT_204733. G alpha (12/13) signalling events.
    REACT_209641. NRAGE signals death through JNK.
    REACT_210090. Rho GTPase cycle.
    REACT_220092. GPVI-mediated activation cascade.
    REACT_225836. Interleukin-3, 5 and GM-CSF signaling.
    REACT_226341. PIP3 activates AKT signaling.

    Miscellaneous databases

    EvolutionaryTracei P27870.
    NextBioi 302549.
    PROi P27870.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P27870.
    Bgeei P27870.
    CleanExi MM_VAV1.
    Genevestigatori P27870.

    Family and domain databases

    Gene3Di 1.10.418.10. 1 hit.
    1.20.900.10. 1 hit.
    2.30.29.30. 1 hit.
    3.30.505.10. 1 hit.
    InterProi IPR022613. CAMSAP_CH.
    IPR001715. CH-domain.
    IPR000219. DH-domain.
    IPR001331. GDS_CDC24_CS.
    IPR001849. PH_domain.
    IPR011993. PH_like_dom.
    IPR002219. Prot_Kinase_C-like_PE/DAG-bd.
    IPR000980. SH2.
    IPR011511. SH3_2.
    IPR001452. SH3_domain.
    IPR003096. SM22_calponin.
    IPR028530. Vav.
    [Graphical view ]
    PANTHERi PTHR22826:SF112. PTHR22826:SF112. 1 hit.
    Pfami 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. 1 hit.
    PF07653. SH3_2. 1 hit.
    [Graphical view ]
    PRINTSi PR00401. SH2DOMAIN.
    PR00452. SH3DOMAIN.
    PR00888. SM22CALPONIN.
    SMARTi SM00109. C1. 1 hit.
    SM00033. CH. 1 hit.
    SM00233. PH. 1 hit.
    SM00325. RhoGEF. 1 hit.
    SM00252. SH2. 1 hit.
    SM00326. SH3. 2 hits.
    [Graphical view ]
    SUPFAMi SSF47576. SSF47576. 1 hit.
    SSF48065. SSF48065. 1 hit.
    SSF50044. SSF50044. 1 hit.
    SSF55550. SSF55550. 1 hit.
    PROSITEi 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.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Mechanism of activation of the vav protooncogene."
      Coppola J., Bryant S., Koda T., Conway D., Barbacid M.
      Cell Growth Differ. 2:95-105(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, MUTAGENESIS OF CYS-529; CYS-532 AND HIS-554.
    2. "The hematopoietically expressed vav proto-oncogene shares homology with the dbl GDP-GTP exchange factor, the bcr gene and a yeast gene (CDC24) involved in cytoskeletal organization."
      Adams J.M., Houston H., Allen J., Lints T., Harvey R.
      Oncogene 7:611-618(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    3. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: NOD.
      Tissue: Thymus.
    4. "Loss of the amino-terminal helix-loop-helix domain of the vav proto-oncogene activates its transforming potential."
      Katzav S., Cleveland J.L., Heslop H.E., Pulido D.
      Mol. Cell. Biol. 11:1912-1920(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-93.
    5. "Tec protein tyrosine kinase is involved in the signaling mechanism of granulocyte colony-stimulating factor receptor."
      Miyazato A., Yamashita Y., Hatake K., Miura Y., Ozawa K., Mano H.
      Cell Growth Differ. 7:1135-1139(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TEC.
    6. "Bacterial LPS and IFN-gamma trigger the tyrosine phosphorylation of vav in macrophages: evidence for involvement of the hck tyrosine kinase."
      English B.K., Orlicek S.L., Mei Z., Meals E.A.
      J. Leukoc. Biol. 62:859-864(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HCK, PHOSPHORYLATION.
    7. "Src-like adaptor protein (SLAP) is a negative regulator of T cell receptor signaling."
      Sosinowski T., Pandey A., Dixit V.M., Weiss A.
      J. Exp. Med. 191:463-474(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SLA.
    8. Cited for: PHOSPHORYLATION, INTERACTION WITH CBLB.
    9. Cited for: PHOSPHORYLATION, INTERACTION WITH CBLB.
    10. "MIST functions through distinct domains in immunoreceptor signaling in the presence and absence of LAT."
      Goitsuka R., Tatsuno A., Ishiai M., Kurosaki T., Kitamura D.
      J. Biol. Chem. 276:36043-36050(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CLNK.
    11. "Ccpg1, a novel scaffold protein that regulates the activity of the Rho guanine nucleotide exchange factor Dbs."
      Kostenko E.V., Olabisi O.O., Sahay S., Rodriguez P.L., Whitehead I.P.
      Mol. Cell. Biol. 26:8964-8975(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: POSSIBLE INTERACTION WITH CCPG1.
    12. "Quantitative time-resolved phosphoproteomic analysis of mast cell signaling."
      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) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-844, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Mast cell.
    13. "Liar, a novel Lyn-binding nuclear/cytoplasmic shuttling protein that influences erythropoietin-induced differentiation."
      Samuels A.L., Klinken S.P., Ingley E.
      Blood 113:3845-3856(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ANKRD54.
    14. "Themis2/ICB1 is a signaling scaffold that selectively regulates macrophage Toll-like receptor signaling and cytokine production."
      Peirce M.J., Brook M., Morrice N., Snelgrove R., Begum S., Lanfrancotti A., Notley C., Hussell T., Cope A.P., Wait R.
      PLoS ONE 5:E11465-E11465(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH THEMIS2.

    Entry informationi

    Entry nameiVAV_MOUSE
    AccessioniPrimary (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: October 1, 2014
    This is version 157 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3