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P15498

- VAV_HUMAN

UniProt

P15498 - VAV_HUMAN

Protein

Proto-oncogene vav

Gene

VAV1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 177 (01 Oct 2014)
      Sequence version 4 (21 Feb 2001)
      Previous versions | rss
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    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. guanyl-nucleotide exchange factor activity Source: Reactome
    2. metal ion binding Source: UniProtKB-KW
    3. protein binding Source: UniProtKB
    4. Rac guanyl-nucleotide exchange factor activity Source: Ensembl
    5. sequence-specific DNA binding transcription factor activity Source: ProtInc

    GO - Biological processi

    1. apoptotic signaling pathway Source: Reactome
    2. blood coagulation Source: Reactome
    3. epidermal growth factor receptor signaling pathway Source: Reactome
    4. Fc-epsilon receptor signaling pathway Source: Reactome
    5. Fc-gamma receptor signaling pathway involved in phagocytosis Source: Reactome
    6. fibroblast growth factor receptor signaling pathway Source: Reactome
    7. innate immune response Source: Reactome
    8. integrin-mediated signaling pathway Source: Ensembl
    9. neurotrophin TRK receptor signaling pathway Source: Reactome
    10. phosphatidylinositol-mediated signaling Source: Reactome
    11. platelet activation Source: Reactome
    12. positive regulation of apoptotic process Source: Reactome
    13. positive regulation of cell adhesion Source: Ensembl
    14. positive regulation of GTPase activity Source: GOC
    15. regulation of small GTPase mediated signal transduction Source: Reactome
    16. regulation of transcription, DNA-templated Source: GOC
    17. small GTPase mediated signal transduction Source: Reactome
    18. T cell activation Source: Ensembl
    19. T cell costimulation Source: Reactome

    Keywords - Molecular functioni

    Guanine-nucleotide releasing factor

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_11051. Rho GTPase cycle.
    REACT_111040. Signaling by SCF-KIT.
    REACT_118700. Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
    REACT_13638. NRAGE signals death through JNK.
    REACT_147727. Constitutive PI3K/AKT Signaling in Cancer.
    REACT_160086. Regulation of actin dynamics for phagocytic cup formation.
    REACT_163701. FCERI mediated MAPK activation.
    REACT_163834. FCERI mediated Ca+2 mobilization.
    REACT_1695. GPVI-mediated activation cascade.
    REACT_18407. G alpha (12/13) signalling events.
    REACT_19238. CD28 dependent Vav1 pathway.
    REACT_23787. Regulation of signaling by CBL.
    REACT_23837. Interleukin-3, 5 and GM-CSF signaling.
    REACT_75829. PIP3 activates AKT signaling.
    SignaLinkiP15498.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Proto-oncogene vav
    Gene namesi
    Name:VAV1
    Synonyms:VAV
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 19

    Organism-specific databases

    HGNCiHGNC:12657. VAV1.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. plasma membrane Source: Reactome

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi529 – 5291C → R: Abolishes transforming activity. 1 Publication
    Mutagenesisi696 – 6961R → L: Loss of interaction with SYK. 1 Publication

    Keywords - Diseasei

    Proto-oncogene

    Organism-specific databases

    PharmGKBiPA37280.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 845845Proto-oncogene vavPRO_0000080980Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei826 – 8261Phosphotyrosine2 Publications
    Modified residuei844 – 8441PhosphotyrosineBy similarity

    Post-translational modificationi

    Phosphorylated on tyrosine residues by HCK in response to IFNG and bacterial lipopolysaccharide (LPS) By similarity. Phosphorylated by FYN.By similarity2 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP15498.
    PaxDbiP15498.
    PeptideAtlasiP15498.
    PRIDEiP15498.

    PTM databases

    PhosphoSiteiP15498.

    Miscellaneous databases

    PMAP-CutDBP15498.

    Expressioni

    Tissue specificityi

    Widely expressed in hematopoietic cells but not in other cell types.

    Gene expression databases

    ArrayExpressiP15498.
    BgeeiP15498.
    CleanExiHS_VAV1.
    GenevestigatoriP15498.

    Organism-specific databases

    HPAiHPA001864.

    Interactioni

    Subunit structurei

    May interact with CCPG1 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. Interacts with SHB and CLNK By similarity. Interacts with THEMIS2. Interacts with HCK By similarity. Interacts with NEK3 and this interaction is prolactin-dependent. Interacts with ITK. Interacts with PTK2B/PYK2. Interacts (via SH2 domain) with SYK. Interacts with ANKRD54 By similarity.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ABI1Q8IZP02EBI-625518,EBI-375446
    ABL1P005195EBI-625518,EBI-375543
    GAB1Q134802EBI-625518,EBI-517684
    GRB2P629932EBI-625518,EBI-401755
    KHDRBS1Q076663EBI-625518,EBI-1364
    LCP2Q130949EBI-625518,EBI-346946
    PLCG1P084874EBI-625518,EBI-8013886From a different organism.
    RAC1P630002EBI-625518,EBI-413628
    SH3BP2P783148EBI-625518,EBI-727062
    ZNF655Q8N7205EBI-625518,EBI-625509

    Protein-protein interaction databases

    BioGridi113252. 68 interactions.
    DIPiDIP-1061N.
    IntActiP15498. 26 interactions.
    MINTiMINT-1211643.
    STRINGi9606.ENSP00000302269.

    Structurei

    Secondary structure

    1
    845
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi3 – 1311
    Turni22 – 243
    Helixi30 – 378
    Helixi41 – 5010
    Helixi57 – 593
    Helixi68 – 8417
    Helixi96 – 1005
    Helixi105 – 11713
    Turni119 – 1213
    Helixi122 – 1243
    Helixi145 – 1495
    Helixi159 – 1624
    Helixi168 – 17811
    Helixi191 – 21828
    Helixi221 – 2244
    Turni225 – 2273
    Helixi230 – 2378
    Helixi240 – 25920
    Turni260 – 2623
    Helixi267 – 2737
    Helixi276 – 2783
    Helixi279 – 30022
    Helixi302 – 31615
    Beta strandi317 – 3193
    Helixi322 – 3265
    Helixi328 – 3336
    Helixi336 – 3449
    Helixi351 – 38838
    Helixi397 – 4004
    Beta strandi403 – 41210
    Beta strandi420 – 43516
    Beta strandi442 – 4487
    Helixi449 – 4513
    Beta strandi452 – 4565
    Beta strandi469 – 47911
    Beta strandi481 – 4888
    Helixi489 – 50618
    Turni509 – 5124
    Helixi513 – 5153
    Beta strandi518 – 5214
    Turni530 – 5323
    Beta strandi538 – 5403
    Beta strandi543 – 5464
    Turni547 – 5493
    Helixi555 – 5606
    Helixi666 – 6683
    Beta strandi669 – 6724
    Helixi678 – 6847
    Turni685 – 6873
    Beta strandi692 – 6965
    Beta strandi700 – 7023
    Beta strandi706 – 7116
    Beta strandi714 – 7196
    Beta strandi721 – 7233
    Beta strandi726 – 7305
    Beta strandi735 – 7373
    Helixi738 – 7458
    Helixi750 – 7523
    Beta strandi754 – 7563
    Beta strandi763 – 7664

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2CRHNMR-A629-775[»]
    2LCTNMR-A664-767[»]
    2MC1NMR-A664-767[»]
    2RORNMR-A629-775[»]
    3BJIX-ray2.60A/B189-565[»]
    3KY9X-ray2.73A/B2-584[»]
    ProteinModelPortaliP15498.
    SMRiP15498. Positions 2-565, 583-780, 784-844.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP15498.

    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.By similarity

    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.
    InParanoidiP15498.
    KOiK05730.
    OMAiSHRVTWD.
    OrthoDBiEOG73FQKZ.
    PhylomeDBiP15498.
    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.
    InterProiIPR001715. 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.
    IPR001452. SH3_domain.
    IPR003096. SM22_calponin.
    IPR028530. Vav.
    [Graphical view]
    PANTHERiPTHR22826:SF112. PTHR22826:SF112. 1 hit.
    PfamiPF00130. C1_1. 1 hit.
    PF00307. CH. 1 hit.
    PF00169. PH. 1 hit.
    PF00621. RhoGEF. 1 hit.
    PF00017. SH2. 1 hit.
    PF00018. SH3_1. 2 hits.
    [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]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P15498-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MELWRQCTHW LIQCRVLPPS HRVTWDGAQV CELAQALRDG VLLCQLLNNL    50
    LPHAINLREV NLRPQMSQFL CLKNIRTFLS TCCEKFGLKR SELFEAFDLF 100
    DVQDFGKVIY TLSALSWTPI AQNRGIMPFP TEEESVGDED IYSGLSDQID 150
    DTVEEDEDLY DCVENEEAEG DEIYEDLMRS EPVSMPPKMT EYDKRCCCLR 200
    EIQQTEEKYT DTLGSIQQHF LKPLQRFLKP QDIEIIFINI EDLLRVHTHF 250
    LKEMKEALGT PGAANLYQVF IKYKERFLVY GRYCSQVESA SKHLDRVAAA 300
    REDVQMKLEE CSQRANNGRF TLRDLLMVPM QRVLKYHLLL QELVKHTQEA 350
    MEKENLRLAL DAMRDLAQCV NEVKRDNETL RQITNFQLSI ENLDQSLAHY 400
    GRPKIDGELK ITSVERRSKM DRYAFLLDKA LLICKRRGDS YDLKDFVNLH 450
    SFQVRDDSSG DRDNKKWSHM FLLIEDQGAQ GYELFFKTRE LKKKWMEQFE 500
    MAISNIYPEN ATANGHDFQM FSFEETTSCK ACQMLLRGTF YQGYRCHRCR 550
    ASAHKECLGR VPPCGRHGQD FPGTMKKDKL HRRAQDKKRN ELGLPKMEVF 600
    QEYYGLPPPP GAIGPFLRLN PGDIVELTKA EAEQNWWEGR NTSTNEIGWF 650
    PCNRVKPYVH GPPQDLSVHL WYAGPMERAG AESILANRSD GTFLVRQRVK 700
    DAAEFAISIK YNVEVKHIKI MTAEGLYRIT EKKAFRGLTE LVEFYQQNSL 750
    KDCFKSLDTT LQFPFKEPEK RTISRPAVGS TKYFGTAKAR YDFCARDRSE 800
    LSLKEGDIIK ILNKKGQQGW WRGEIYGRVG WFPANYVEED YSEYC 845
    Length:845
    Mass (Da):98,314
    Last modified:February 21, 2001 - v4
    Checksum:iAC3BC9736FD2F138
    GO
    Isoform 2 (identifier: P15498-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         187-218: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:813
    Mass (Da):94,493
    Checksum:i2DD711DA5E0A8403
    GO

    Sequence cautioni

    The sequence CAA34383.1 differs from that shown. Reason: Frameshift at positions 322 and 355.
    The sequence BAG62721.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti264 – 2641A → P in CAA34383. (PubMed:2477241)Curated
    Sequence conflicti368 – 3681Q → R in BAG62721. (PubMed:14702039)Curated
    Sequence conflicti718 – 7181I → TV(PubMed:2477241)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti739 – 7391T → M.
    Corresponds to variant rs36097961 [ dbSNP | Ensembl ].
    VAR_051997

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei187 – 21832Missing in isoform 2. 1 PublicationVSP_047563Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF030227
    , AF030201, AF030202, AF030203, AF030204, AF030205, AF030206, AF030207, AF030208, AF030209, AF030210, AF030211, AF030212, AF030213, AF030214, AF030215, AF030216, AF030217, AF030218, AF030219, AF030220, AF030221, AF030222, AF030223, AF030224, AF030225, AF030226 Genomic DNA. Translation: AAC25011.1.
    AC010647 Genomic DNA. No translation available.
    AC020895 Genomic DNA. No translation available.
    AC020954 Genomic DNA. No translation available.
    AC022156 Genomic DNA. No translation available.
    M59834 Genomic DNA. Translation: AAA63267.1.
    AK301128 mRNA. Translation: BAG62721.1. Different initiation.
    X16316 mRNA. Translation: CAA34383.1. Frameshift.
    X83931 mRNA. Translation: CAA58783.1.
    CCDSiCCDS12174.1. [P15498-1]
    CCDS59342.1. [P15498-2]
    PIRiB39576. TVHUVV.
    RefSeqiNP_001245136.1. NM_001258207.1. [P15498-2]
    NP_005419.2. NM_005428.3. [P15498-1]
    UniGeneiHs.116237.

    Genome annotation databases

    EnsembliENST00000596764; ENSP00000469450; ENSG00000141968. [P15498-2]
    ENST00000602142; ENSP00000472929; ENSG00000141968. [P15498-1]
    GeneIDi7409.
    KEGGihsa:7409.
    UCSCiuc002mfu.2. human. [P15498-1]

    Polymorphism databases

    DMDMi13124807.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF030227
    , AF030201 , AF030202 , AF030203 , AF030204 , AF030205 , AF030206 , AF030207 , AF030208 , AF030209 , AF030210 , AF030211 , AF030212 , AF030213 , AF030214 , AF030215 , AF030216 , AF030217 , AF030218 , AF030219 , AF030220 , AF030221 , AF030222 , AF030223 , AF030224 , AF030225 , AF030226 Genomic DNA. Translation: AAC25011.1 .
    AC010647 Genomic DNA. No translation available.
    AC020895 Genomic DNA. No translation available.
    AC020954 Genomic DNA. No translation available.
    AC022156 Genomic DNA. No translation available.
    M59834 Genomic DNA. Translation: AAA63267.1 .
    AK301128 mRNA. Translation: BAG62721.1 . Different initiation.
    X16316 mRNA. Translation: CAA34383.1 . Frameshift.
    X83931 mRNA. Translation: CAA58783.1 .
    CCDSi CCDS12174.1. [P15498-1 ]
    CCDS59342.1. [P15498-2 ]
    PIRi B39576. TVHUVV.
    RefSeqi NP_001245136.1. NM_001258207.1. [P15498-2 ]
    NP_005419.2. NM_005428.3. [P15498-1 ]
    UniGenei Hs.116237.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2CRH NMR - A 629-775 [» ]
    2LCT NMR - A 664-767 [» ]
    2MC1 NMR - A 664-767 [» ]
    2ROR NMR - A 629-775 [» ]
    3BJI X-ray 2.60 A/B 189-565 [» ]
    3KY9 X-ray 2.73 A/B 2-584 [» ]
    ProteinModelPortali P15498.
    SMRi P15498. Positions 2-565, 583-780, 784-844.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 113252. 68 interactions.
    DIPi DIP-1061N.
    IntActi P15498. 26 interactions.
    MINTi MINT-1211643.
    STRINGi 9606.ENSP00000302269.

    PTM databases

    PhosphoSitei P15498.

    Polymorphism databases

    DMDMi 13124807.

    Proteomic databases

    MaxQBi P15498.
    PaxDbi P15498.
    PeptideAtlasi P15498.
    PRIDEi P15498.

    Protocols and materials databases

    DNASUi 7409.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000596764 ; ENSP00000469450 ; ENSG00000141968 . [P15498-2 ]
    ENST00000602142 ; ENSP00000472929 ; ENSG00000141968 . [P15498-1 ]
    GeneIDi 7409.
    KEGGi hsa:7409.
    UCSCi uc002mfu.2. human. [P15498-1 ]

    Organism-specific databases

    CTDi 7409.
    GeneCardsi GC19P006772.
    H-InvDB HIX0202828.
    HGNCi HGNC:12657. VAV1.
    HPAi HPA001864.
    MIMi 164875. gene.
    neXtProti NX_P15498.
    PharmGKBi PA37280.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG326494.
    HOGENOMi HOG000234364.
    HOVERGENi HBG018066.
    InParanoidi P15498.
    KOi K05730.
    OMAi SHRVTWD.
    OrthoDBi EOG73FQKZ.
    PhylomeDBi P15498.
    TreeFami TF316171.

    Enzyme and pathway databases

    Reactomei REACT_11051. Rho GTPase cycle.
    REACT_111040. Signaling by SCF-KIT.
    REACT_118700. Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
    REACT_13638. NRAGE signals death through JNK.
    REACT_147727. Constitutive PI3K/AKT Signaling in Cancer.
    REACT_160086. Regulation of actin dynamics for phagocytic cup formation.
    REACT_163701. FCERI mediated MAPK activation.
    REACT_163834. FCERI mediated Ca+2 mobilization.
    REACT_1695. GPVI-mediated activation cascade.
    REACT_18407. G alpha (12/13) signalling events.
    REACT_19238. CD28 dependent Vav1 pathway.
    REACT_23787. Regulation of signaling by CBL.
    REACT_23837. Interleukin-3, 5 and GM-CSF signaling.
    REACT_75829. PIP3 activates AKT signaling.
    SignaLinki P15498.

    Miscellaneous databases

    EvolutionaryTracei P15498.
    GenomeRNAii 7409.
    NextBioi 29008.
    PMAP-CutDB P15498.
    PROi P15498.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P15498.
    Bgeei P15498.
    CleanExi HS_VAV1.
    Genevestigatori P15498.

    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 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.
    IPR001452. SH3_domain.
    IPR003096. SM22_calponin.
    IPR028530. Vav.
    [Graphical view ]
    PANTHERi PTHR22826:SF112. PTHR22826:SF112. 1 hit.
    Pfami PF00130. C1_1. 1 hit.
    PF00307. CH. 1 hit.
    PF00169. PH. 1 hit.
    PF00621. RhoGEF. 1 hit.
    PF00017. SH2. 1 hit.
    PF00018. SH3_1. 2 hits.
    [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] (ISOFORM 1), MUTAGENESIS OF CYS-529.
    2. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "The DNA sequence and biology of human chromosome 19."
      Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V.
      , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
      Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    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 [GENOMIC DNA] OF 1-61.
    5. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 51-813 (ISOFORM 2).
      Tissue: Spleen.
    6. "vav, a novel human oncogene derived from a locus ubiquitously expressed in hematopoietic cells."
      Katzav S., Martin-Zanca D., Barbacid M.
      EMBO J. 8:2283-2290(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 68-845 (ISOFORM 1).
    7. Romero F.
      Submitted (JAN-1995) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 299-837 (ISOFORM 1).
    8. "The proline-rich region of Vav binds to Grb2 and Grb3-3."
      Ramos-Morales F., Romero F., Schweighoffer F., Bismuth G., Camonis J., Tortolero M., Fischer S.
      Oncogene 11:1665-1669(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 299-334 (ISOFORM 1).
    9. "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: SIMILARITY TO CDC24 FAMILY.
    10. "Functional and physical interactions of Syk family kinases with the Vav proto-oncogene product."
      Deckert M., Tartare-Deckert S., Couture C., Mustelin T., Altman A.
      Immunity 5:591-604(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SYK, MUTAGENESIS OF ARG-696.
    11. "Cbl-b, a member of the Sli-1/c-Cbl protein family, inhibits Vav-mediated c-Jun N-terminal kinase activation."
      Bustelo X.R., Crespo P., Lopez-Barahona M., Gutkind J.S., Barbacid M.
      Oncogene 15:2511-2520(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CBLB.
    12. "BLNK: a central linker protein in B cell activation."
      Fu C., Turck C.W., Kurosaki T., Chan A.C.
      Immunity 9:93-103(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH BLNK; PLCG1; GRB2 AND NCK1.
    13. "hSiah2 is a new Vav binding protein which inhibits Vav-mediated signaling pathways."
      Germani A., Romero F., Houlard M., Camonis J., Gisselbrecht S., Fischer S., Varin-Blank N.
      Mol. Cell. Biol. 19:3798-3807(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SIAH2.
    14. "T-cell receptor antagonists induce Vav phosphorylation by selective activation of Fyn kinase."
      Huang J., Tilly D., Altman A., Sugie K., Grey H.M.
      Proc. Natl. Acad. Sci. U.S.A. 97:10923-10929(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION BY FYN.
    15. "DOCK2 associates with CrkL and regulates Rac1 in human leukemia cell lines."
      Nishihara H., Maeda M., Oda A., Tsuda M., Sawa H., Nagashima K., Tanaka S.
      Blood 100:3968-3974(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH DOCK2.
    16. "Shb links SLP-76 and Vav with the CD3 complex in Jurkat T cells."
      Lindholm C.K., Henriksson M.L., Hallberg B., Welsh M.
      Eur. J. Biochem. 269:3279-3288(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SHB.
    17. "Adaptor protein APS binds the NH2-terminal autoinhibitory domain of guanine nucleotide exchange factor Vav3 and augments its activity."
      Yabana N., Shibuya M.
      Oncogene 21:7720-7729(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH APS.
    18. "Kinase-independent functions for Itk in TCR-induced regulation of Vav and the actin cytoskeleton."
      Dombroski D., Houghtling R.A., Labno C.M., Precht P., Takesono A., Caplen N.J., Billadeau D.D., Wange R.L., Burkhardt J.K., Schwartzberg P.L.
      J. Immunol. 174:1385-1392(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ITK.
    19. "Novel association of Vav2 and Nek3 modulates signaling through the human prolactin receptor."
      Miller S.L., DeMaria J.E., Freier D.O., Riegel A.M., Clevenger C.V.
      Mol. Endocrinol. 19:939-949(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NEK3.
    20. "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
      Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
      Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-826, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    21. Cited for: INTERACTION WITH ZNF655/VIK.
    22. "A Pyk2-Vav1 complex is recruited to beta3-adhesion sites to initiate Rho activation."
      Gao C., Blystone S.D.
      Biochem. J. 420:49-56(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PTK2B/PYK2.
    23. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    24. "Solution structure of the SH2 domain of human proto-oncogene protein VAV1."
      RIKEN structural genomics initiative (RSGI)
      Submitted (NOV-2005) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 661-775.

    Entry informationi

    Entry nameiVAV_HUMAN
    AccessioniPrimary (citable) accession number: P15498
    Secondary accession number(s): B4DVK9, M0QXX6, Q15860
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1990
    Last sequence update: February 21, 2001
    Last modified: October 1, 2014
    This is version 177 of the entry and version 4 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Miscellaneous

    'Vav' stands for the sixth letter of the Hebrew alphabet.

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 19
      Human chromosome 19: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3