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Q9UKW4 (VAV3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 144. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Guanine nucleotide exchange factor VAV3

Short name=VAV-3
Gene names
Name:VAV3
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length847 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Subunit structure

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. Ref.7 Ref.8 Ref.9

Tissue specificity

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. Ref.1 Ref.7

Induction

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

Post-translational modification

Phosphorylated. Phosphorylation can be mediated by ROS1. In osteoclasts, undergoes tyrosine phosphorylation in response to CSF1 By similarity. Ref.7

Sequence similarities

Contains 1 CH (calponin-homology) domain.

Contains 1 DH (DBL-homology) domain.

Contains 1 PH domain.

Contains 1 phorbol-ester/DAG-type zinc finger.

Contains 1 SH2 domain.

Contains 2 SH3 domains.

Sequence caution

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

Ontologies

Keywords
   Biological processAngiogenesis
   Coding sequence diversityAlternative promoter usage
Alternative splicing
Polymorphism
   DomainRepeat
SH2 domain
SH3 domain
Zinc-finger
   LigandMetal-binding
Zinc
   Molecular functionGuanine-nucleotide releasing factor
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processB cell receptor signaling pathway

Inferred from mutant phenotype PubMed 17875758. Source: UniProtKB

Fc-epsilon receptor signaling pathway

Traceable author statement. Source: Reactome

Fc-gamma receptor signaling pathway involved in phagocytosis

Traceable author statement. Source: Reactome

angiogenesis

Inferred from electronic annotation. Source: UniProtKB-KW

apoptotic signaling pathway

Traceable author statement. Source: Reactome

blood coagulation

Traceable author statement. Source: Reactome

cell migration

Inferred from electronic annotation. Source: Ensembl

cellular response to DNA damage stimulus

Inferred from mutant phenotype PubMed 17875758. Source: UniProtKB

innate immune response

Traceable author statement. Source: Reactome

integrin-mediated signaling pathway

Inferred from electronic annotation. Source: Ensembl

lamellipodium assembly

Inferred from electronic annotation. Source: Ensembl

neurotrophin TRK receptor signaling pathway

Traceable author statement. Source: Reactome

platelet activation

Traceable author statement. Source: Reactome

positive regulation of B cell proliferation

Inferred from mutant phenotype PubMed 17875758. Source: UniProtKB

positive regulation of GTPase activity

Traceable author statement Ref.2. Source: GOC

positive regulation of apoptotic process

Traceable author statement. Source: Reactome

positive regulation of cell adhesion

Inferred from electronic annotation. Source: Ensembl

positive regulation of phosphatidylinositol 3-kinase activity

Inferred from electronic annotation. Source: Ensembl

positive regulation of signal transduction

Traceable author statement Ref.2. Source: GOC

regulation of small GTPase mediated signal transduction

Traceable author statement. Source: Reactome

response to drug

Inferred from mutant phenotype PubMed 17875758. Source: UniProtKB

small GTPase mediated signal transduction

Traceable author statement. Source: Reactome

vesicle fusion

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcytosol

Traceable author statement. Source: Reactome

plasma membrane

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionGTPase activator activity

Traceable author statement Ref.2. Source: ProtInc

Rac guanyl-nucleotide exchange factor activity

Inferred from electronic annotation. Source: Ensembl

SH3/SH2 adaptor activity

Traceable author statement Ref.2. Source: ProtInc

guanyl-nucleotide exchange factor activity

Inferred from experiment. Source: Reactome

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

GRB2P629935EBI-297568,EBI-401755
PIK3R1P279862EBI-297568,EBI-79464

Alternative products

This entry describes 4 isoforms produced by alternative promoter usage and alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9UKW4-1)

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.
Isoform 2 (identifier: Q9UKW4-2)

Also known as: Beta;

The sequence of this isoform differs from the canonical sequence as follows:
     1-107: MEPWKQCAQW...DLFDVRDFGK → MQLPDCPCRAHLP
Isoform 3 (identifier: Q9UKW4-3)

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.
Isoform 4 (identifier: Q9UKW4-4)

The sequence of this isoform differs from the canonical sequence as follows:
     783-784: SL → SSPSLFCGFSFVTPPDYSFVPPSSTPFWSV
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 847847Guanine nucleotide exchange factor VAV3
PRO_0000080986

Regions

Domain1 – 119119CH
Domain192 – 371180DH
Domain400 – 502103PH
Domain592 – 66069SH3 1
Domain672 – 76695SH2
Domain788 – 84760SH3 2
Zinc finger513 – 56250Phorbol-ester/DAG-type
Region560 – 847288Sufficient for interaction with ROS1

Amino acid modifications

Modified residue1411Phosphotyrosine Ref.10

Natural variations

Alternative sequence1 – 560560Missing in isoform 3.
VSP_041360
Alternative sequence1 – 107107MEPWK…RDFGK → MQLPDCPCRAHLP in isoform 2.
VSP_001820
Alternative sequence561 – 5688NCGRVNSG → MPIFTFLS in isoform 3.
VSP_041361
Alternative sequence783 – 7842SL → SSPSLFCGFSFVTPPDYSFV PPSSTPFWSV in isoform 4.
VSP_042359
Natural variant1391D → N.
Corresponds to variant rs34318889 [ dbSNP | Ensembl ].
VAR_061800
Natural variant2981T → S. Ref.1 Ref.6
Corresponds to variant rs7528153 [ dbSNP | Ensembl ].
VAR_033522
Natural variant6161P → S.
Corresponds to variant rs12410676 [ dbSNP | Ensembl ].
VAR_051998
Natural variant6181Q → H.
Corresponds to variant rs12403266 [ dbSNP | Ensembl ].
VAR_033523

Experimental info

Sequence conflict1071K → E in AAC79695. Ref.1
Sequence conflict2171Y → H in AAD20348. Ref.2
Sequence conflict4291V → A in AAD20348. Ref.2

Secondary structure

................... 847
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (Alpha) [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: C1E29F0B094CB721

FASTA84797,776
        10         20         30         40         50         60 
MEPWKQCAQW LIHCKVLPTN HRVTWDSAQV FDLAQTLRDG VLLCQLLNNL RAHSINLKEI 

        70         80         90        100        110        120 
NLRPQMSQFL CLKNIRTFLT ACCETFGMRK SELFEAFDLF DVRDFGKVIE TLSRLSRTPI 

       130        140        150        160        170        180 
ALATGIRPFP TEESINDEDI YKGLPDLIDE TLVEDEEDLY DCVYGEDEGG EVYEDLMKAE 

       190        200        210        220        230        240 
EAHQPKCPEN DIRSCCLAEI KQTEEKYTET LESIEKYFMA PLKRFLTAAE FDSVFINIPE 

       250        260        270        280        290        300 
LVKLHRNLMQ EIHDSIVNKN DQNLYQVFIN YKERLVIYGQ YCSGVESAIS SLDYISKTKE 

       310        320        330        340        350        360 
DVKLKLEECS KRANNGKFTL RDLLVVPMQR VLKYHLLLQE LVKHTTDPTE KANLKLALDA 

       370        380        390        400        410        420 
MKDLAQYVNE VKRDNETLRE IKQFQLSIEN LNQPVLLFGR PQGDGEIRIT TLDKHTKQER 

       430        440        450        460        470        480 
HIFLFDLAVI VCKRKGDNYE MKEIIDLQQY KIANNPTTDK ENKKWSYGFY LIHTQGQNGL 

       490        500        510        520        530        540 
EFYCKTKDLK KKWLEQFEMA LSNIRPDYAD SNFHDFKMHT FTRVTSCKVC QMLLRGTFYQ 

       550        560        570        580        590        600 
GYLCFKCGAR AHKECLGRVD NCGRVNSGEQ GTLKLPEKRT NGLRRTPKQV DPGLPKMQVI 

       610        620        630        640        650        660 
RNYSGTPPPA LHEGPPLQLQ AGDTVELLKG DAHSLFWQGR NLASGEVGFF PSDAVKPCPC 

       670        680        690        700        710        720 
VPKPVDYSCQ PWYAGAMERL QAETELINRV NSTYLVRHRT KESGEYAISI KYNNEAKHIK 

       730        740        750        760        770        780 
ILTRDGFFHI AENRKFKSLM ELVEYYKHHS LKEGFRTLDT TLQFPYKEPE HSAGQRGNRA 

       790        800        810        820        830        840 
GNSLLSPKVL GIAIARYDFC ARDMRELSLL KGDVVKIYTK MSANGWWRGE VNGRVGWFPS 


TYVEEDE 

« Hide

Isoform 2 (Beta) [UniParc].

Checksum: A67868CBD2FFD9A7
Show »

FASTA75386,696
Isoform 3 (VAV3.1) [UniParc].

Checksum: D23C21EBEF7F48CF
Show »

FASTA28732,604
Isoform 4 [UniParc].

Checksum: AD6B651338EEE812
Show »

FASTA875100,828

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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 expand/collapse EMBL AC list , AC114491, AL353892, AL513206, AL591042 Genomic DNA. Translation: CAH72458.1.
AL513206 expand/collapse EMBL AC list , AC114491, AL353892, AL391235, AL591042 Genomic DNA. Translation: CAH73195.1.
AL513206, AC114491, AL591042 Genomic DNA. Translation: CAH73196.1.
AL591042 expand/collapse EMBL AC list , AC114491, AL353892, AL391235, AL513206 Genomic DNA. Translation: CAI14457.1.
AL591042, AC114491, AL513206 Genomic DNA. Translation: CAI14458.1.
AL353892 expand/collapse EMBL AC list , AC114491, AL391235, AL513206, AL591042 Genomic DNA. Translation: CAI21786.1.
CH471156 Genomic DNA. Translation: EAW51252.1.
BC143969 mRNA. Translation: AAI43970.1.
RefSeqNP_001073343.1. NM_001079874.1.
NP_006104.4. NM_006113.4.
XP_005270417.1. XM_005270360.1.
UniGeneHs.267659.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2D86NMR-A1-130[»]
ProteinModelPortalQ9UKW4.
SMRQ9UKW4. Positions 1-563, 594-846.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115715. 15 interactions.
IntActQ9UKW4. 8 interactions.
MINTMINT-256977.
STRING9606.ENSP00000359073.

PTM databases

PhosphoSiteQ9UKW4.

Polymorphism databases

DMDM12643372.

Proteomic databases

PaxDbQ9UKW4.
PRIDEQ9UKW4.

Protocols and materials databases

DNASU10451.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000370056; ENSP00000359073; ENSG00000134215. [Q9UKW4-1]
ENST00000415432; ENSP00000394897; ENSG00000134215. [Q9UKW4-3]
ENST00000527011; ENSP00000432540; ENSG00000134215. [Q9UKW4-4]
GeneID10451.
KEGGhsa:10451.
UCSCuc001dvj.1. human. [Q9UKW4-3]
uc001dvk.1. human. [Q9UKW4-1]
uc010ouw.1. human. [Q9UKW4-4]

Organism-specific databases

CTD10451.
GeneCardsGC01M108113.
HGNCHGNC:12659. VAV3.
HPACAB002012.
HPA028138.
MIM605541. gene.
neXtProtNX_Q9UKW4.
PharmGKBPA37282.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG326494.
HOGENOMHOG000049191.
HOVERGENHBG018066.
InParanoidQ9UKW4.
KOK05730.
OMADPGLPKM.
OrthoDBEOG73FQKZ.
PhylomeDBQ9UKW4.
TreeFamTF316171.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_604. Hemostasis.
REACT_6900. Immune System.
SignaLinkQ9UKW4.

Gene expression databases

ArrayExpressQ9UKW4.
BgeeQ9UKW4.
CleanExHS_VAV3.
GenevestigatorQ9UKW4.

Family and domain databases

Gene3D1.10.418.10. 1 hit.
1.20.900.10. 1 hit.
2.30.29.30. 1 hit.
3.30.505.10. 1 hit.
InterProIPR001715. CH-domain.
IPR000219. DH-domain.
IPR001331. GDS_CDC24_CS.
IPR011993. PH_like_dom.
IPR001849. Pleckstrin_homology.
IPR002219. Prot_Kinase_C-like_PE/DAG-bd.
IPR000980. SH2.
IPR011511. SH3_2.
IPR001452. SH3_domain.
IPR003096. SM22_calponin.
IPR028530. Vav.
[Graphical view]
PANTHERPTHR22826:SF53. PTHR22826:SF53. 1 hit.
PfamPF00130. 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]
PRINTSPR00401. SH2DOMAIN.
PR00452. SH3DOMAIN.
PR00888. SM22CALPONIN.
SMARTSM00109. 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]
SUPFAMSSF47576. SSF47576. 1 hit.
SSF48065. SSF48065. 1 hit.
SSF50044. SSF50044. 2 hits.
SSF55550. SSF55550. 2 hits.
PROSITEPS50021. 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.
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Other

ChiTaRSVAV3. human.
EvolutionaryTraceQ9UKW4.
GeneWikiVAV3.
GenomeRNAi10451.
NextBio39617.
PROQ9UKW4.
SOURCESearch...

Entry information

Entry nameVAV3_HUMAN
AccessionPrimary (citable) accession number: Q9UKW4
Secondary accession number(s): B1AMM0 expand/collapse secondary AC list , B1APV5, B4E232, B7ZLR1, E9PQ97, O60498, O95230, Q9Y5X8
Entry history
Integrated into UniProtKB/Swiss-Prot: January 24, 2001
Last sequence update: May 1, 2000
Last modified: April 16, 2014
This is version 144 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM