Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Guanine nucleotide exchange factor VAV3

Gene

VAV3

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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. Rac guanyl-nucleotide exchange factor activity Source: Ensembl
  5. SH3/SH2 adaptor activity Source: ProtInc

GO - Biological processi

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

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_228016. VEGFR2 mediated vascular permeability.
REACT_228166. VEGFA-VEGFR2 Pathway.
REACT_228189. EPH-ephrin mediated repulsion of cells.
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: UniProtKB
  3. plasma membrane Source: Ensembl
Complete GO annotation...

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 – 1411Phosphotyrosine1 Publication

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

BgeeiQ9UKW4.
CleanExiHS_VAV3.
ExpressionAtlasiQ9UKW4. baseline and differential.
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 – 1311Combined sources
Helixi30 – 389Combined sources
Helixi41 – 5010Combined sources
Helixi57 – 593Combined sources
Helixi68 – 8417Combined sources
Turni90 – 923Combined sources
Helixi96 – 1005Combined sources
Helixi106 – 11510Combined sources
Helixi121 – 1244Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00740000115307.
HOGENOMiHOG000049191.
HOVERGENiHBG018066.
InParanoidiQ9UKW4.
KOiK05730.
OMAiGPPLHIQ.
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.
IPR002219. PE/DAG-bd.
IPR001849. PH_domain.
IPR011993. PH_like_dom.
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. AlignAdd to basket

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

        10         20         30         40         50
MEPWKQCAQW LIHCKVLPTN HRVTWDSAQV FDLAQTLRDG VLLCQLLNNL
60 70 80 90 100
RAHSINLKEI NLRPQMSQFL CLKNIRTFLT ACCETFGMRK SELFEAFDLF
110 120 130 140 150
DVRDFGKVIE TLSRLSRTPI ALATGIRPFP TEESINDEDI YKGLPDLIDE
160 170 180 190 200
TLVEDEEDLY DCVYGEDEGG EVYEDLMKAE EAHQPKCPEN DIRSCCLAEI
210 220 230 240 250
KQTEEKYTET LESIEKYFMA PLKRFLTAAE FDSVFINIPE LVKLHRNLMQ
260 270 280 290 300
EIHDSIVNKN DQNLYQVFIN YKERLVIYGQ YCSGVESAIS SLDYISKTKE
310 320 330 340 350
DVKLKLEECS KRANNGKFTL RDLLVVPMQR VLKYHLLLQE LVKHTTDPTE
360 370 380 390 400
KANLKLALDA MKDLAQYVNE VKRDNETLRE IKQFQLSIEN LNQPVLLFGR
410 420 430 440 450
PQGDGEIRIT TLDKHTKQER HIFLFDLAVI VCKRKGDNYE MKEIIDLQQY
460 470 480 490 500
KIANNPTTDK ENKKWSYGFY LIHTQGQNGL EFYCKTKDLK KKWLEQFEMA
510 520 530 540 550
LSNIRPDYAD SNFHDFKMHT FTRVTSCKVC QMLLRGTFYQ GYLCFKCGAR
560 570 580 590 600
AHKECLGRVD NCGRVNSGEQ GTLKLPEKRT NGLRRTPKQV DPGLPKMQVI
610 620 630 640 650
RNYSGTPPPA LHEGPPLQLQ AGDTVELLKG DAHSLFWQGR NLASGEVGFF
660 670 680 690 700
PSDAVKPCPC VPKPVDYSCQ PWYAGAMERL QAETELINRV NSTYLVRHRT
710 720 730 740 750
KESGEYAISI KYNNEAKHIK ILTRDGFFHI AENRKFKSLM ELVEYYKHHS
760 770 780 790 800
LKEGFRTLDT TLQFPYKEPE HSAGQRGNRA GNSLLSPKVL GIAIARYDFC
810 820 830 840
ARDMRELSLL KGDVVKIYTK MSANGWWRGE VNGRVGWFPS TYVEEDE
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.Curated

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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

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

Protein-protein interaction databases

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

PTM databases

PhosphoSiteiQ9UKW4.

Polymorphism databases

DMDMi12643372.

Proteomic databases

MaxQBiQ9UKW4.
PaxDbiQ9UKW4.
PRIDEiQ9UKW4.

Protocols and materials databases

DNASUi10451.
Structural Biology KnowledgebaseSearch...

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]

Organism-specific databases

CTDi10451.
GeneCardsiGC01M108113.
HGNCiHGNC:12659. VAV3.
HPAiCAB002012.
HPA028138.
MIMi605541. gene.
neXtProtiNX_Q9UKW4.
PharmGKBiPA37282.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG326494.
GeneTreeiENSGT00740000115307.
HOGENOMiHOG000049191.
HOVERGENiHBG018066.
InParanoidiQ9UKW4.
KOiK05730.
OMAiGPPLHIQ.
OrthoDBiEOG73FQKZ.
PhylomeDBiQ9UKW4.
TreeFamiTF316171.

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_228016. VEGFR2 mediated vascular permeability.
REACT_228166. VEGFA-VEGFR2 Pathway.
REACT_228189. EPH-ephrin mediated repulsion of cells.
SignaLinkiQ9UKW4.

Miscellaneous databases

ChiTaRSiVAV3. human.
EvolutionaryTraceiQ9UKW4.
GeneWikiiVAV3.
GenomeRNAii10451.
NextBioi39617.
PROiQ9UKW4.
SOURCEiSearch...

Gene expression databases

BgeeiQ9UKW4.
CleanExiHS_VAV3.
ExpressionAtlasiQ9UKW4. baseline and differential.
GenevestigatoriQ9UKW4.

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.
IPR002219. PE/DAG-bd.
IPR001849. PH_domain.
IPR011993. PH_like_dom.
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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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: March 4, 2015
This is version 153 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.