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Q9UKW4

- VAV3_HUMAN

UniProt

Q9UKW4 - VAV3_HUMAN

Protein

Guanine nucleotide exchange factor VAV3

Gene

VAV3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 149 (01 Oct 2014)
      Sequence version 1 (01 May 2000)
      Previous versions | rss
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    Functioni

    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.By similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri513 – 56250Phorbol-ester/DAG-typePROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. GTPase activator activity Source: ProtInc
    2. guanyl-nucleotide exchange factor activity Source: Reactome
    3. metal ion binding Source: UniProtKB-KW
    4. protein binding Source: IntAct
    5. Rac guanyl-nucleotide exchange factor activity Source: Ensembl
    6. SH3/SH2 adaptor activity Source: ProtInc

    GO - Biological processi

    1. angiogenesis Source: UniProtKB-KW
    2. apoptotic signaling pathway Source: Reactome
    3. B cell receptor signaling pathway Source: UniProtKB
    4. blood coagulation Source: Reactome
    5. cell migration Source: Ensembl
    6. cellular response to DNA damage stimulus Source: UniProtKB
    7. Fc-epsilon receptor signaling pathway Source: Reactome
    8. Fc-gamma receptor signaling pathway involved in phagocytosis Source: Reactome
    9. innate immune response Source: Reactome
    10. integrin-mediated signaling pathway Source: Ensembl
    11. lamellipodium assembly Source: Ensembl
    12. neurotrophin TRK receptor signaling pathway Source: Reactome
    13. platelet activation Source: Reactome
    14. positive regulation of apoptotic process Source: Reactome
    15. positive regulation of B cell proliferation Source: UniProtKB
    16. positive regulation of cell adhesion Source: Ensembl
    17. positive regulation of GTPase activity Source: GOC
    18. positive regulation of phosphatidylinositol 3-kinase activity Source: Ensembl
    19. positive regulation of signal transduction Source: GOC
    20. regulation of small GTPase mediated signal transduction Source: Reactome
    21. response to drug Source: UniProtKB
    22. small GTPase mediated signal transduction Source: Reactome
    23. vesicle fusion Source: Ensembl

    Keywords - Molecular functioni

    Guanine-nucleotide releasing factor

    Keywords - Biological processi

    Angiogenesis

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_11051. Rho GTPase cycle.
    REACT_13638. NRAGE signals death through JNK.
    REACT_147814. DAP12 signaling.
    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.
    SignaLinkiQ9UKW4.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Guanine nucleotide exchange factor VAV3
    Short name:
    VAV-3
    Gene namesi
    Name:VAV3
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:12659. VAV3.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. extracellular vesicular exosome Source: UniProt
    3. plasma membrane Source: Ensembl

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA37282.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 847847Guanine nucleotide exchange factor VAV3PRO_0000080986Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei141 – 1411Phosphotyrosine2 Publications

    Post-translational modificationi

    Phosphorylated. Phosphorylation can be mediated by ROS1. In osteoclasts, undergoes tyrosine phosphorylation in response to CSF1 By similarity.By similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ9UKW4.
    PaxDbiQ9UKW4.
    PRIDEiQ9UKW4.

    PTM databases

    PhosphoSiteiQ9UKW4.

    Expressioni

    Tissue specificityi

    Isoform 1 and isoform 3 are widely expressed; both are expressed at very low levels in skeletal muscle. In keratinocytes, isoform 1 is less abundant than isoform 3. Isoform 3 is detected at very low levels, if any, in adrenal gland, bone marrow, spleen, fetal brain and spinal chord; in these tissues, isoform 1 is readily detectable.2 Publications

    Inductioni

    Down-regulated by EGF and TGF-beta.1 Publication

    Gene expression databases

    ArrayExpressiQ9UKW4.
    BgeeiQ9UKW4.
    CleanExiHS_VAV3.
    GenevestigatoriQ9UKW4.

    Organism-specific databases

    HPAiCAB002012.
    HPA028138.

    Interactioni

    Subunit structurei

    Interacts with the PH domain of APS. Interacts (via SH2 domains) with the phosphorylated form of EPHA2. Interacts with ROS1; constitutive interaction that mediates VAV3 phosphorylation.3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    GAB1Q134806EBI-297568,EBI-517684
    GRB2P629935EBI-297568,EBI-401755
    METP085812EBI-297568,EBI-1039152
    PIK3R1P279862EBI-297568,EBI-79464

    Protein-protein interaction databases

    BioGridi115715. 15 interactions.
    IntActiQ9UKW4. 12 interactions.
    MINTiMINT-256977.
    STRINGi9606.ENSP00000359073.

    Structurei

    Secondary structure

    1
    847
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi3 – 1311
    Helixi30 – 389
    Helixi41 – 5010
    Helixi57 – 593
    Helixi68 – 8417
    Turni90 – 923
    Helixi96 – 1005
    Helixi106 – 11510
    Helixi121 – 1244

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2D86NMR-A1-130[»]
    ProteinModelPortaliQ9UKW4.
    SMRiQ9UKW4. Positions 1-563, 594-846.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9UKW4.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1 – 119119CHPROSITE-ProRule annotationAdd
    BLAST
    Domaini192 – 371180DHPROSITE-ProRule annotationAdd
    BLAST
    Domaini400 – 502103PHPROSITE-ProRule annotationAdd
    BLAST
    Domaini592 – 66069SH3 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini672 – 76695SH2PROSITE-ProRule annotationAdd
    BLAST
    Domaini788 – 84760SH3 2PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni560 – 847288Sufficient for interaction with ROS1Add
    BLAST

    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 fingeri513 – 56250Phorbol-ester/DAG-typePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Repeat, SH2 domain, SH3 domain, Zinc-finger

    Phylogenomic databases

    eggNOGiNOG326494.
    HOGENOMiHOG000049191.
    HOVERGENiHBG018066.
    InParanoidiQ9UKW4.
    KOiK05730.
    OMAiDPGLPKM.
    OrthoDBiEOG73FQKZ.
    PhylomeDBiQ9UKW4.
    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.
    IPR011511. SH3_2.
    IPR001452. SH3_domain.
    IPR003096. SM22_calponin.
    IPR028530. Vav.
    [Graphical view]
    PANTHERiPTHR22826:SF97. PTHR22826:SF97. 1 hit.
    PfamiPF00130. C1_1. 1 hit.
    PF00307. CH. 1 hit.
    PF00169. PH. 1 hit.
    PF00621. RhoGEF. 1 hit.
    PF00017. SH2. 1 hit.
    PF07653. SH3_2. 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. 2 hits.
    SSF55550. SSF55550. 2 hits.
    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 (4)i

    Sequence statusi: Complete.

    This entry describes 4 isoformsi produced by alternative promoter usage and alternative splicing. Align

    Isoform 1 (identifier: Q9UKW4-1) [UniParc]FASTAAdd to Basket

    Also known as: Alpha

    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

    MEPWKQCAQW LIHCKVLPTN HRVTWDSAQV FDLAQTLRDG VLLCQLLNNL    50
    RAHSINLKEI NLRPQMSQFL CLKNIRTFLT ACCETFGMRK SELFEAFDLF 100
    DVRDFGKVIE TLSRLSRTPI ALATGIRPFP TEESINDEDI YKGLPDLIDE 150
    TLVEDEEDLY DCVYGEDEGG EVYEDLMKAE EAHQPKCPEN DIRSCCLAEI 200
    KQTEEKYTET LESIEKYFMA PLKRFLTAAE FDSVFINIPE LVKLHRNLMQ 250
    EIHDSIVNKN DQNLYQVFIN YKERLVIYGQ YCSGVESAIS SLDYISKTKE 300
    DVKLKLEECS KRANNGKFTL RDLLVVPMQR VLKYHLLLQE LVKHTTDPTE 350
    KANLKLALDA MKDLAQYVNE VKRDNETLRE IKQFQLSIEN LNQPVLLFGR 400
    PQGDGEIRIT TLDKHTKQER HIFLFDLAVI VCKRKGDNYE MKEIIDLQQY 450
    KIANNPTTDK ENKKWSYGFY LIHTQGQNGL EFYCKTKDLK KKWLEQFEMA 500
    LSNIRPDYAD SNFHDFKMHT FTRVTSCKVC QMLLRGTFYQ GYLCFKCGAR 550
    AHKECLGRVD NCGRVNSGEQ GTLKLPEKRT NGLRRTPKQV DPGLPKMQVI 600
    RNYSGTPPPA LHEGPPLQLQ AGDTVELLKG DAHSLFWQGR NLASGEVGFF 650
    PSDAVKPCPC VPKPVDYSCQ PWYAGAMERL QAETELINRV NSTYLVRHRT 700
    KESGEYAISI KYNNEAKHIK ILTRDGFFHI AENRKFKSLM ELVEYYKHHS 750
    LKEGFRTLDT TLQFPYKEPE HSAGQRGNRA GNSLLSPKVL GIAIARYDFC 800
    ARDMRELSLL KGDVVKIYTK MSANGWWRGE VNGRVGWFPS TYVEEDE 847
    Length:847
    Mass (Da):97,776
    Last modified:May 1, 2000 - v1
    Checksum:iC1E29F0B094CB721
    GO
    Isoform 2 (identifier: Q9UKW4-2) [UniParc]FASTAAdd to Basket

    Also known as: Beta

    The sequence of this isoform differs from the canonical sequence as follows:
         1-107: MEPWKQCAQW...DLFDVRDFGK → MQLPDCPCRAHLP

    Show »
    Length:753
    Mass (Da):86,696
    Checksum:iA67868CBD2FFD9A7
    GO
    Isoform 3 (identifier: Q9UKW4-3) [UniParc]FASTAAdd to Basket

    Also known as: VAV3.1

    The sequence of this isoform differs from the canonical sequence as follows:
         1-560: Missing.
         561-568: NCGRVNSG → MPIFTFLS

    Note: May be produced by alternative promoter usage.

    Show »
    Length:287
    Mass (Da):32,604
    Checksum:iD23C21EBEF7F48CF
    GO
    Isoform 4 (identifier: Q9UKW4-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         783-784: SL → SSPSLFCGFSFVTPPDYSFVPPSSTPFWSV

    Note: No experimental confirmation available.

    Show »
    Length:875
    Mass (Da):100,828
    Checksum:iAD6B651338EEE812
    GO

    Sequence cautioni

    The sequence AAD03799.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti107 – 1071K → E in AAC79695. (PubMed:9705494)Curated
    Sequence conflicti217 – 2171Y → H in AAD20348. (PubMed:10523675)Curated
    Sequence conflicti429 – 4291V → A in AAD20348. (PubMed:10523675)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti139 – 1391D → N.
    Corresponds to variant rs34318889 [ dbSNP | Ensembl ].
    VAR_061800
    Natural varianti298 – 2981T → S.2 Publications
    Corresponds to variant rs7528153 [ dbSNP | Ensembl ].
    VAR_033522
    Natural varianti616 – 6161P → S.
    Corresponds to variant rs12410676 [ dbSNP | Ensembl ].
    VAR_051998
    Natural varianti618 – 6181Q → H.
    Corresponds to variant rs12403266 [ dbSNP | Ensembl ].
    VAR_033523

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 560560Missing in isoform 3. 2 PublicationsVSP_041360Add
    BLAST
    Alternative sequencei1 – 107107MEPWK…RDFGK → MQLPDCPCRAHLP in isoform 2. 1 PublicationVSP_001820Add
    BLAST
    Alternative sequencei561 – 5688NCGRVNSG → MPIFTFLS in isoform 3. 2 PublicationsVSP_041361
    Alternative sequencei783 – 7842SL → SSPSLFCGFSFVTPPDYSFV PPSSTPFWSV in isoform 4. 1 PublicationVSP_042359

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF035442 mRNA. Translation: AAD03799.1. Different initiation.
    AF067817 mRNA. Translation: AAC79695.1.
    AF118887 mRNA. Translation: AAD20349.1.
    AF118886 mRNA. Translation: AAD20348.1.
    AK304088 mRNA. Translation: BAG64994.1.
    AK316295 mRNA. Translation: BAH14666.1.
    AL391235
    , AC114491, AL353892, AL513206, AL591042 Genomic DNA. Translation: CAH72458.1.
    AL513206
    , AC114491, AL353892, AL391235, AL591042 Genomic DNA. Translation: CAH73195.1.
    AL513206, AC114491, AL591042 Genomic DNA. Translation: CAH73196.1.
    AL591042
    , AC114491, AL353892, AL391235, AL513206 Genomic DNA. Translation: CAI14457.1.
    AL591042, AC114491, AL513206 Genomic DNA. Translation: CAI14458.1.
    AL353892
    , AC114491, AL391235, AL513206, AL591042 Genomic DNA. Translation: CAI21786.1.
    CH471156 Genomic DNA. Translation: EAW51252.1.
    BC143969 mRNA. Translation: AAI43970.1.
    CCDSiCCDS44181.1. [Q9UKW4-3]
    CCDS785.1. [Q9UKW4-1]
    RefSeqiNP_001073343.1. NM_001079874.1. [Q9UKW4-3]
    NP_006104.4. NM_006113.4. [Q9UKW4-1]
    XP_005270417.1. XM_005270360.1. [Q9UKW4-2]
    UniGeneiHs.267659.

    Genome annotation databases

    EnsembliENST00000370056; ENSP00000359073; ENSG00000134215. [Q9UKW4-1]
    ENST00000415432; ENSP00000394897; ENSG00000134215. [Q9UKW4-3]
    ENST00000527011; ENSP00000432540; ENSG00000134215. [Q9UKW4-4]
    GeneIDi10451.
    KEGGihsa:10451.
    UCSCiuc001dvj.1. human. [Q9UKW4-3]
    uc001dvk.1. human. [Q9UKW4-1]
    uc010ouw.1. human. [Q9UKW4-4]

    Polymorphism databases

    DMDMi12643372.

    Keywords - Coding sequence diversityi

    Alternative promoter usage, 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
    AF035442 mRNA. Translation: AAD03799.1 . Different initiation.
    AF067817 mRNA. Translation: AAC79695.1 .
    AF118887 mRNA. Translation: AAD20349.1 .
    AF118886 mRNA. Translation: AAD20348.1 .
    AK304088 mRNA. Translation: BAG64994.1 .
    AK316295 mRNA. Translation: BAH14666.1 .
    AL391235
    , AC114491 , AL353892 , AL513206 , AL591042 Genomic DNA. Translation: CAH72458.1 .
    AL513206
    , AC114491 , AL353892 , AL391235 , AL591042 Genomic DNA. Translation: CAH73195.1 .
    AL513206 , AC114491 , AL591042 Genomic DNA. Translation: CAH73196.1 .
    AL591042
    , AC114491 , AL353892 , AL391235 , AL513206 Genomic DNA. Translation: CAI14457.1 .
    AL591042 , AC114491 , AL513206 Genomic DNA. Translation: CAI14458.1 .
    AL353892
    , AC114491 , AL391235 , AL513206 , AL591042 Genomic DNA. Translation: CAI21786.1 .
    CH471156 Genomic DNA. Translation: EAW51252.1 .
    BC143969 mRNA. Translation: AAI43970.1 .
    CCDSi CCDS44181.1. [Q9UKW4-3 ]
    CCDS785.1. [Q9UKW4-1 ]
    RefSeqi NP_001073343.1. NM_001079874.1. [Q9UKW4-3 ]
    NP_006104.4. NM_006113.4. [Q9UKW4-1 ]
    XP_005270417.1. XM_005270360.1. [Q9UKW4-2 ]
    UniGenei Hs.267659.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2D86 NMR - A 1-130 [» ]
    ProteinModelPortali Q9UKW4.
    SMRi Q9UKW4. Positions 1-563, 594-846.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115715. 15 interactions.
    IntActi Q9UKW4. 12 interactions.
    MINTi MINT-256977.
    STRINGi 9606.ENSP00000359073.

    PTM databases

    PhosphoSitei Q9UKW4.

    Polymorphism databases

    DMDMi 12643372.

    Proteomic databases

    MaxQBi Q9UKW4.
    PaxDbi Q9UKW4.
    PRIDEi Q9UKW4.

    Protocols and materials databases

    DNASUi 10451.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000370056 ; ENSP00000359073 ; ENSG00000134215 . [Q9UKW4-1 ]
    ENST00000415432 ; ENSP00000394897 ; ENSG00000134215 . [Q9UKW4-3 ]
    ENST00000527011 ; ENSP00000432540 ; ENSG00000134215 . [Q9UKW4-4 ]
    GeneIDi 10451.
    KEGGi hsa:10451.
    UCSCi uc001dvj.1. human. [Q9UKW4-3 ]
    uc001dvk.1. human. [Q9UKW4-1 ]
    uc010ouw.1. human. [Q9UKW4-4 ]

    Organism-specific databases

    CTDi 10451.
    GeneCardsi GC01M108113.
    HGNCi HGNC:12659. VAV3.
    HPAi CAB002012.
    HPA028138.
    MIMi 605541. gene.
    neXtProti NX_Q9UKW4.
    PharmGKBi PA37282.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG326494.
    HOGENOMi HOG000049191.
    HOVERGENi HBG018066.
    InParanoidi Q9UKW4.
    KOi K05730.
    OMAi DPGLPKM.
    OrthoDBi EOG73FQKZ.
    PhylomeDBi Q9UKW4.
    TreeFami TF316171.

    Enzyme and pathway databases

    Reactomei REACT_11051. Rho GTPase cycle.
    REACT_13638. NRAGE signals death through JNK.
    REACT_147814. DAP12 signaling.
    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.
    SignaLinki Q9UKW4.

    Miscellaneous databases

    ChiTaRSi VAV3. human.
    EvolutionaryTracei Q9UKW4.
    GeneWikii VAV3.
    GenomeRNAii 10451.
    NextBioi 39617.
    PROi Q9UKW4.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9UKW4.
    Bgeei Q9UKW4.
    CleanExi HS_VAV3.
    Genevestigatori Q9UKW4.

    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.
    IPR011511. SH3_2.
    IPR001452. SH3_domain.
    IPR003096. SM22_calponin.
    IPR028530. Vav.
    [Graphical view ]
    PANTHERi PTHR22826:SF97. PTHR22826:SF97. 1 hit.
    Pfami PF00130. C1_1. 1 hit.
    PF00307. CH. 1 hit.
    PF00169. PH. 1 hit.
    PF00621. RhoGEF. 1 hit.
    PF00017. SH2. 1 hit.
    PF07653. SH3_2. 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. 2 hits.
    SSF55550. SSF55550. 2 hits.
    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. "Non-stoichiometric reduced complexity probes for cDNA arrays."
      Trenkle T., Welsh J., Jung B., Mathieu-Daude F., McClelland M.
      Nucleic Acids Res. 26:3883-3891(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), NUCLEOTIDE SEQUENCE [MRNA] OF 1-692 (ISOFORM 3), ALTERNATIVE PROMOTER USAGE, TISSUE SPECIFICITY, INDUCTION, VARIANT SER-298.
      Tissue: Keratinocyte.
    2. "Biological and regulatory properties of Vav-3, a new member of the Vav family of oncoproteins."
      Movilla N., Bustelo X.R.
      Mol. Cell. Biol. 19:7870-7885(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), ALTERNATIVE SPLICING.
    3. "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] (ISOFORM 3).
      Tissue: Trachea.
    4. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), VARIANT SER-298.
    7. "Vav3 mediates receptor protein tyrosine kinase signaling, regulates GTPase activity, modulates cell morphology, and induces cell transformation."
      Zeng L., Sachdev P., Yan L., Chan J.L., Trenkle T., McClelland M., Welsh J., Wang L.H.
      Mol. Cell. Biol. 20:9212-9224(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ROS1, PHOSPHORYLATION, TISSUE SPECIFICITY.
    8. "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.
    9. "Essential role of Vav family guanine nucleotide exchange factors in EphA receptor-mediated angiogenesis."
      Hunter S.G., Zhuang G., Brantley-Sieders D.M., Swat W., Cowan C.W., Chen J.
      Mol. Cell. Biol. 26:4830-4842(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH EPHA2.
    10. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals 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) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-141, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    11. "Solution structure of the CH domain from human VAV-3 protein."
      RIKEN structural genomics initiative (RSGI)
      Submitted (DEC-2006) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 1-134.

    Entry informationi

    Entry nameiVAV3_HUMAN
    AccessioniPrimary (citable) accession number: Q9UKW4
    Secondary accession number(s): B1AMM0
    , B1APV5, B4E232, B7ZLR1, E9PQ97, O60498, O95230, Q9Y5X8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 24, 2001
    Last sequence update: May 1, 2000
    Last modified: October 1, 2014
    This is version 149 of the entry and version 1 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

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: 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