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P52735

- VAV2_HUMAN

UniProt

P52735 - VAV2_HUMAN

Protein

Guanine nucleotide exchange factor VAV2

Gene

VAV2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 152 (01 Oct 2014)
      Sequence version 2 (22 Jul 2008)
      Previous versions | rss
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    Functioni

    Guanine nucleotide exchange factor for the Rho family of Ras-related 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.By similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri523 – 57250Phorbol-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: IntAct
    4. Rho guanyl-nucleotide exchange factor activity Source: InterPro

    GO - Biological processi

    1. angiogenesis Source: UniProtKB-KW
    2. apoptotic signaling pathway Source: Reactome
    3. axon guidance Source: Reactome
    4. blood coagulation Source: Reactome
    5. cell migration Source: Ensembl
    6. Fc-epsilon receptor signaling pathway Source: Reactome
    7. Fc-gamma receptor signaling pathway involved in phagocytosis Source: Reactome
    8. innate immune response Source: Reactome
    9. lamellipodium assembly Source: Ensembl
    10. neurotrophin TRK receptor signaling pathway Source: Reactome
    11. platelet activation Source: Reactome
    12. positive regulation of apoptotic process Source: Reactome
    13. positive regulation of GTPase activity Source: GOC
    14. positive regulation of phosphatidylinositol 3-kinase activity Source: Ensembl
    15. regulation of blood coagulation Source: UniProt
    16. regulation of gene expression Source: UniProt
    17. regulation of small GTPase mediated signal transduction Source: Reactome
    18. signal transduction Source: ProtInc
    19. small GTPase mediated signal transduction Source: Reactome

    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.
    REACT_22272. Signal transduction by L1.
    SignaLinkiP52735.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Guanine nucleotide exchange factor VAV2
    Short name:
    VAV-2
    Gene namesi
    Name:VAV2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 9

    Organism-specific databases

    HGNCiHGNC:12658. VAV2.

    Subcellular locationi

    GO - Cellular componenti

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

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA37281.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 878878Guanine nucleotide exchange factor VAV2PRO_0000080984Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei142 – 1421Phosphotyrosine; by EGFR2 Publications
    Modified residuei159 – 1591Phosphotyrosine; by EGFR2 Publications
    Modified residuei172 – 1721Phosphotyrosine; by EGFR2 Publications
    Modified residuei576 – 5761Phosphoserine2 Publications
    Modified residuei626 – 6261Phosphoserine2 Publications

    Post-translational modificationi

    Phosphorylated on tyrosine residues in response to FGR activation.4 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP52735.
    PaxDbiP52735.
    PRIDEiP52735.

    PTM databases

    PhosphoSiteiP52735.

    Expressioni

    Tissue specificityi

    Widely expressed.

    Gene expression databases

    BgeeiP52735.
    GenevestigatoriP52735.

    Organism-specific databases

    HPAiHPA003224.

    Interactioni

    Subunit structurei

    Interacts (via SH2 domains) with the phosphorylated form of EPHA2. Interacts with SSX2IP By similarity. Interacts with NEK3 and PRLR and this interaction is prolactin-dependent.By similarity1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ABI1Q8IZP02EBI-297549,EBI-375446
    ERBB2P046263EBI-297549,EBI-641062
    GAB1Q134802EBI-297549,EBI-517684
    NEK3P519563EBI-297549,EBI-476041
    SH3BP2P783144EBI-297549,EBI-727062
    TOM1L1O756742EBI-297549,EBI-712991

    Protein-protein interaction databases

    BioGridi113253. 61 interactions.
    DIPiDIP-33088N.
    IntActiP52735. 59 interactions.
    MINTiMINT-1494337.

    Structurei

    Secondary structure

    1
    878
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi661 – 6644
    Helixi668 – 6703
    Beta strandi674 – 6774
    Helixi680 – 68910
    Beta strandi694 – 6985
    Beta strandi707 – 7126
    Beta strandi714 – 72512
    Beta strandi728 – 7314
    Beta strandi737 – 7393
    Helixi740 – 7478
    Turni752 – 7554
    Beta strandi767 – 7693
    Beta strandi819 – 8257
    Beta strandi842 – 8443
    Beta strandi847 – 8548
    Beta strandi856 – 8605
    Beta strandi863 – 8675
    Beta strandi869 – 8746

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2DLZNMR-A663-767[»]
    2DM1NMR-A819-878[»]
    2LNWNMR-A659-771[»]
    2LNXNMR-A659-771[»]
    ProteinModelPortaliP52735.
    SMRiP52735. Positions 1-572, 589-878.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP52735.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1 – 119119CHPROSITE-ProRule annotationAdd
    BLAST
    Domaini198 – 376179DHPROSITE-ProRule annotationAdd
    BLAST
    Domaini405 – 512108PHPROSITE-ProRule annotationAdd
    BLAST
    Domaini586 – 65267SH3 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini673 – 76795SH2PROSITE-ProRule annotationAdd
    BLAST
    Domaini816 – 87762SH3 2PROSITE-ProRule annotationAdd
    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 fingeri523 – 57250Phorbol-ester/DAG-typePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Repeat, SH2 domain, SH3 domain, Zinc-finger

    Phylogenomic databases

    eggNOGiNOG326494.
    HOVERGENiHBG018066.
    InParanoidiP52735.
    KOiK05730.
    OMAiWFAGNME.
    OrthoDBiEOG73FQKZ.
    PhylomeDBiP52735.
    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.
    IPR028530. Vav.
    [Graphical view]
    PANTHERiPTHR22826:SF95. PTHR22826:SF95. 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.
    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 (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P52735-1) [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

    MEQWRQCGRW LIDCKVLPPN HRVVWPSAVV FDLAQALRDG VLLCQLLHNL    50
    SPGSIDLKDI NFRPQMSQFL CLKNIRTFLK VCHDKFGLRN SELFDPFDLF 100
    DVRDFGKVIS AVSRLSLHSI AQNKGIRPFP SEETTENDDD VYRSLEELAD 150
    EHDLGEDIYD CVPCEDGGDD IYEDIIKVEV QQPMIRYMQK MGMTEDDKRN 200
    CCLLEIQETE AKYYRTLEDI EKNYMSPLRL VLSPADMAAV FINLEDLIKV 250
    HHSFLRAIDV SVMVGGSTLA KVFLDFKERL LIYGEYCSHM EHAQNTLNQL 300
    LASREDFRQK VEECTLKVQD GKFKLQDLLV VPMQRVLKYH LLLKELLSHS 350
    AERPERQQLK EALEAMQDLA MYINEVKRDK ETLRKISEFQ SSIENLQVKL 400
    EEFGRPKIDG ELKVRSIVNH TKQDRYLFLF DKVVIVCKRK GYSYELKEII 450
    ELLFHKMTDD PMNNKDVKKS HGKMWSYGFY LIHLQGKQGF QFFCKTEDMK 500
    RKWMEQFEMA MSNIKPDKAN ANHHSFQMYT FDKTTNCKAC KMFLRGTFYQ 550
    GYMCTKCGVG AHKECLEVIP PCKFTSPADL DASGAGPGPK MVAMQNYHGN 600
    PAPPGKPVLT FQTGDVLELL RGDPESPWWE GRLVQTRKSG YFPSSSVKPC 650
    PVDGRPPISR PPSREIDYTA YPWFAGNMER QQTDNLLKSH ASGTYLIRER 700
    PAEAERFAIS IKFNDEVKHI KVVEKDNWIH ITEAKKFDSL LELVEYYQCH 750
    SLKESFKQLD TTLKYPYKSR ERSASRASSR SPASCASYNF SFLSPQGLSF 800
    ASQGPSAPFW SVFTPRVIGT AVARYNFAAR DMRELSLREG DVVRIYSRIG 850
    GDQGWWKGET NGRIGWFPST YVEEEGIQ 878
    Length:878
    Mass (Da):101,289
    Last modified:July 22, 2008 - v2
    Checksum:iC186911605FD5B73
    GO
    Isoform 2 (identifier: P52735-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         185-189: Missing.
         470-474: Missing.

    Show »
    Length:868
    Mass (Da):100,057
    Checksum:i6C67C472825D2DFD
    GO
    Isoform 3 (identifier: P52735-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         185-189: Missing.
         470-474: Missing.
         783-811: Missing.

    Note: Contains a phosphoserine at position 769.

    Show »
    Length:839
    Mass (Da):97,032
    Checksum:i21910D516F4A211D
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti241 – 2411F → L in CAE45861. (PubMed:17974005)Curated
    Sequence conflicti254 – 2541F → L in CAE45861. (PubMed:17974005)Curated
    Sequence conflicti877 – 8771I → T in CAE45861. (PubMed:17974005)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti594 – 5941M → V.2 Publications
    Corresponds to variant rs602990 [ dbSNP | Ensembl ].
    VAR_045690

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei185 – 1895Missing in isoform 2 and isoform 3. 2 PublicationsVSP_034900
    Alternative sequencei470 – 4745Missing in isoform 2 and isoform 3. 2 PublicationsVSP_034901
    Alternative sequencei783 – 81129Missing in isoform 3. 2 PublicationsVSP_034902Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    S76992 mRNA. Translation: AAB34377.1.
    AL590710, AL357934, AL445931 Genomic DNA. Translation: CAI12279.1.
    AL445931, AL357934, AL590710 Genomic DNA. Translation: CAI13722.1.
    AL357934, AL445931, AL590710 Genomic DNA. Translation: CAI15783.1.
    AL590710, AL357934, AL445931 Genomic DNA. Translation: CAI12278.1.
    AL445931, AL357934, AL590710 Genomic DNA. Translation: CAI13723.1.
    AL357934, AL445931, AL590710 Genomic DNA. Translation: CAI15781.1.
    AL590710, AL357934, AL445931 Genomic DNA. Translation: CAI12280.1.
    AL445931, AL357934, AL590710 Genomic DNA. Translation: CAI13724.1.
    AL357934, AL445931, AL590710 Genomic DNA. Translation: CAI15782.1.
    CH471090 Genomic DNA. Translation: EAW88108.1.
    BC033187 mRNA. Translation: AAH33187.1.
    BC132965 mRNA. Translation: AAI32966.1.
    BC132967 mRNA. Translation: AAI32968.1.
    BX640754 mRNA. Translation: CAE45861.1.
    AY563001 mRNA. Translation: AAS75591.1.
    CCDSiCCDS48053.1. [P52735-1]
    CCDS6979.1. [P52735-3]
    PIRiI51940.
    RefSeqiNP_001127870.1. NM_001134398.1. [P52735-1]
    NP_003362.2. NM_003371.3. [P52735-3]
    XP_005272270.1. XM_005272213.1. [P52735-2]
    UniGeneiHs.369921.
    Hs.689325.

    Genome annotation databases

    EnsembliENST00000371850; ENSP00000360916; ENSG00000160293. [P52735-1]
    ENST00000371851; ENSP00000360917; ENSG00000160293. [P52735-2]
    ENST00000406606; ENSP00000385362; ENSG00000160293. [P52735-3]
    GeneIDi7410.
    KEGGihsa:7410.
    UCSCiuc004cer.3. human. [P52735-3]
    uc004ces.3. human. [P52735-1]

    Polymorphism databases

    DMDMi212287930.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    S76992 mRNA. Translation: AAB34377.1 .
    AL590710 , AL357934 , AL445931 Genomic DNA. Translation: CAI12279.1 .
    AL445931 , AL357934 , AL590710 Genomic DNA. Translation: CAI13722.1 .
    AL357934 , AL445931 , AL590710 Genomic DNA. Translation: CAI15783.1 .
    AL590710 , AL357934 , AL445931 Genomic DNA. Translation: CAI12278.1 .
    AL445931 , AL357934 , AL590710 Genomic DNA. Translation: CAI13723.1 .
    AL357934 , AL445931 , AL590710 Genomic DNA. Translation: CAI15781.1 .
    AL590710 , AL357934 , AL445931 Genomic DNA. Translation: CAI12280.1 .
    AL445931 , AL357934 , AL590710 Genomic DNA. Translation: CAI13724.1 .
    AL357934 , AL445931 , AL590710 Genomic DNA. Translation: CAI15782.1 .
    CH471090 Genomic DNA. Translation: EAW88108.1 .
    BC033187 mRNA. Translation: AAH33187.1 .
    BC132965 mRNA. Translation: AAI32966.1 .
    BC132967 mRNA. Translation: AAI32968.1 .
    BX640754 mRNA. Translation: CAE45861.1 .
    AY563001 mRNA. Translation: AAS75591.1 .
    CCDSi CCDS48053.1. [P52735-1 ]
    CCDS6979.1. [P52735-3 ]
    PIRi I51940.
    RefSeqi NP_001127870.1. NM_001134398.1. [P52735-1 ]
    NP_003362.2. NM_003371.3. [P52735-3 ]
    XP_005272270.1. XM_005272213.1. [P52735-2 ]
    UniGenei Hs.369921.
    Hs.689325.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2DLZ NMR - A 663-767 [» ]
    2DM1 NMR - A 819-878 [» ]
    2LNW NMR - A 659-771 [» ]
    2LNX NMR - A 659-771 [» ]
    ProteinModelPortali P52735.
    SMRi P52735. Positions 1-572, 589-878.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 113253. 61 interactions.
    DIPi DIP-33088N.
    IntActi P52735. 59 interactions.
    MINTi MINT-1494337.

    PTM databases

    PhosphoSitei P52735.

    Polymorphism databases

    DMDMi 212287930.

    Proteomic databases

    MaxQBi P52735.
    PaxDbi P52735.
    PRIDEi P52735.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000371850 ; ENSP00000360916 ; ENSG00000160293 . [P52735-1 ]
    ENST00000371851 ; ENSP00000360917 ; ENSG00000160293 . [P52735-2 ]
    ENST00000406606 ; ENSP00000385362 ; ENSG00000160293 . [P52735-3 ]
    GeneIDi 7410.
    KEGGi hsa:7410.
    UCSCi uc004cer.3. human. [P52735-3 ]
    uc004ces.3. human. [P52735-1 ]

    Organism-specific databases

    CTDi 7410.
    GeneCardsi GC09M136627.
    HGNCi HGNC:12658. VAV2.
    HPAi HPA003224.
    MIMi 600428. gene.
    neXtProti NX_P52735.
    PharmGKBi PA37281.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG326494.
    HOVERGENi HBG018066.
    InParanoidi P52735.
    KOi K05730.
    OMAi WFAGNME.
    OrthoDBi EOG73FQKZ.
    PhylomeDBi P52735.
    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.
    REACT_22272. Signal transduction by L1.
    SignaLinki P52735.

    Miscellaneous databases

    ChiTaRSi VAV2. human.
    EvolutionaryTracei P52735.
    GeneWikii VAV2.
    GenomeRNAii 7410.
    NextBioi 29012.
    PROi P52735.
    SOURCEi Search...

    Gene expression databases

    Bgeei P52735.
    Genevestigatori P52735.

    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.
    IPR028530. Vav.
    [Graphical view ]
    PANTHERi PTHR22826:SF95. PTHR22826:SF95. 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.
    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. "Identification of VAV2 on 9q34 and its exclusion as the tuberous sclerosis gene TSC1."
      Henske E.P., Short M.P., Jozwiak S., Bovey C.M., Ramlakhan S., Haines J.L., Kwiatkowski D.J.
      Ann. Hum. Genet. 59:25-37(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT VAL-594.
      Tissue: Brain.
    2. "DNA sequence and analysis of human chromosome 9."
      Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
      , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
      Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "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 3), VARIANT VAL-594.
      Tissue: Kidney.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 39-878 (ISOFORM 3).
      Tissue: Rectum tumor.
    6. "Transcript variant of VAV2 gene in tumoral cell lines (FaDu, HEp2, HeLa and SiHa)."
      Mancini U.M., Tajara E.H.
      Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 453-506 (ISOFORMS 2/3).
    7. "Mechanism of epidermal growth factor regulation of Vav2, a guanine nucleotide exchange factor for Rac."
      Tamas P., Solti Z., Bauer P., Illes A., Sipeki S., Bauer A., Farago A., Downward J., Buday L.
      J. Biol. Chem. 278:5163-5171(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT TYR-142; TYR-159 AND TYR-172 BY EGFR.
    8. "The proto-oncogene Fgr regulates cell migration and this requires its plasma membrane localization."
      Continolo S., Baruzzi A., Majeed M., Caveggion E., Fumagalli L., Lowell C.A., Berton G.
      Exp. Cell Res. 302:253-269(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION.
    9. "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 AND PRLR.
    10. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
      Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
      Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
      Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
      Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-626, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-769 (ISOFORM 3), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-576, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. "Solution structure of the SH2 domain and of the second SH3 domain of human protein VAV-2."
      RIKEN structural genomics initiative (RSGI)
      Submitted (APR-2007) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 663-878.

    Entry informationi

    Entry nameiVAV2_HUMAN
    AccessioniPrimary (citable) accession number: P52735
    Secondary accession number(s): A2RUM4
    , A8MQ12, B6ZDF5, Q5SYV3, Q5SYV4, Q5SYV5, Q6N012, Q6PIJ9, Q6Q317
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: July 22, 2008
    Last modified: October 1, 2014
    This is version 152 of the entry and version 2 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 9
      Human chromosome 9: 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