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P15498

- VAV_HUMAN

UniProt

P15498 - VAV_HUMAN

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Protein

Proto-oncogene vav

Gene

VAV1

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

Functioni

Couples tyrosine kinase signals with the activation of the Rho/Rac GTPases, thus leading to cell differentiation and/or proliferation.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri515 – 56450Phorbol-ester/DAG-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. guanyl-nucleotide exchange factor activity Source: Reactome
  2. metal ion binding Source: UniProtKB-KW
  3. Rac guanyl-nucleotide exchange factor activity Source: Ensembl
  4. sequence-specific DNA binding transcription factor activity Source: ProtInc

GO - Biological processi

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

Keywords - Molecular functioni

Guanine-nucleotide releasing factor

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

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

Names & Taxonomyi

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

Organism-specific databases

HGNCiHGNC:12657. VAV1.

Subcellular locationi

GO - Cellular componenti

  1. cell-cell junction Source: Ensembl
  2. cytosol Source: Reactome
  3. plasma membrane Source: Reactome
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

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

Keywords - Diseasei

Proto-oncogene

Organism-specific databases

PharmGKBiPA37280.

PTM / Processingi

Molecule processing

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

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei826 – 8261Phosphotyrosine1 Publication
Modified residuei844 – 8441PhosphotyrosineBy similarity

Post-translational modificationi

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

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP15498.
PaxDbiP15498.
PeptideAtlasiP15498.
PRIDEiP15498.

PTM databases

PhosphoSiteiP15498.

Miscellaneous databases

PMAP-CutDBP15498.

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiP15498.
CleanExiHS_VAV1.
ExpressionAtlasiP15498. baseline and differential.
GenevestigatoriP15498.

Organism-specific databases

HPAiHPA001864.

Interactioni

Subunit structurei

May interact with CCPG1 (By similarity). Interacts with APS, DOCK2, GRB2, GRB3, DOCK2, SLA, TEC and ZNF655/VIK. Interacts with SIAH2; without leading to its degradation. Associates with BLNK, PLCG1, GRB2 and NCK1 in a B-cell antigen receptor-dependent fashion. Interacts with CBLB; which inhibits tyrosine phosphorylation and down-regulates activity. Interacts with SHB and CLNK (By similarity). Interacts with THEMIS2. Interacts with HCK (By similarity). Interacts with NEK3 and this interaction is prolactin-dependent. Interacts with ITK. Interacts with PTK2B/PYK2. Interacts (via SH2 domain) with SYK. Interacts with ANKRD54 (By similarity).By similarity

Binary interactionsi

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

Protein-protein interaction databases

BioGridi113252. 68 interactions.
DIPiDIP-1061N.
IntActiP15498. 27 interactions.
MINTiMINT-1211643.
STRINGi9606.ENSP00000302269.

Structurei

Secondary structure

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

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP15498.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 119119CHPROSITE-ProRule annotationAdd
BLAST
Domaini194 – 373180DHPROSITE-ProRule annotationAdd
BLAST
Domaini402 – 504103PHPROSITE-ProRule annotationAdd
BLAST
Domaini617 – 66044SH3 1PROSITE-ProRule annotationAdd
BLAST
Domaini671 – 76595SH2PROSITE-ProRule annotationAdd
BLAST
Domaini782 – 84261SH3 2PROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi33 – 9967Leu-richAdd
BLAST

Domaini

The DH domain is involved in interaction with CCPG1.By similarity

Sequence similaritiesi

Contains 1 CH (calponin-homology) domain.PROSITE-ProRule annotation
Contains 1 DH (DBL-homology) domain.PROSITE-ProRule annotation
Contains 1 PH domain.PROSITE-ProRule annotation
Contains 1 phorbol-ester/DAG-type zinc finger.PROSITE-ProRule annotation
Contains 1 SH2 domain.PROSITE-ProRule annotation
Contains 2 SH3 domains.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri515 – 56450Phorbol-ester/DAG-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Repeat, SH2 domain, SH3 domain, Zinc-finger

Phylogenomic databases

eggNOGiNOG326494.
GeneTreeiENSGT00740000115307.
HOGENOMiHOG000234364.
HOVERGENiHBG018066.
InParanoidiP15498.
KOiK05730.
OMAiSHRVTWD.
OrthoDBiEOG73FQKZ.
PhylomeDBiP15498.
TreeFamiTF316171.

Family and domain databases

Gene3Di1.10.418.10. 1 hit.
1.20.900.10. 1 hit.
2.30.29.30. 1 hit.
3.30.505.10. 1 hit.
InterProiIPR001715. CH-domain.
IPR000219. DH-domain.
IPR001331. GDS_CDC24_CS.
IPR002219. PE/DAG-bd.
IPR001849. PH_domain.
IPR011993. PH_like_dom.
IPR000980. SH2.
IPR001452. SH3_domain.
IPR003096. SM22_calponin.
IPR028530. Vav.
[Graphical view]
PANTHERiPTHR22826:SF112. PTHR22826:SF112. 1 hit.
PfamiPF00130. C1_1. 1 hit.
PF00307. CH. 1 hit.
PF00169. PH. 1 hit.
PF00621. RhoGEF. 1 hit.
PF00017. SH2. 1 hit.
PF00018. SH3_1. 2 hits.
[Graphical view]
PRINTSiPR00401. SH2DOMAIN.
PR00452. SH3DOMAIN.
PR00888. SM22CALPONIN.
SMARTiSM00109. C1. 1 hit.
SM00033. CH. 1 hit.
SM00233. PH. 1 hit.
SM00325. RhoGEF. 1 hit.
SM00252. SH2. 1 hit.
SM00326. SH3. 2 hits.
[Graphical view]
SUPFAMiSSF47576. SSF47576. 1 hit.
SSF48065. SSF48065. 1 hit.
SSF50044. SSF50044. 1 hit.
SSF55550. SSF55550. 1 hit.
PROSITEiPS50021. CH. 1 hit.
PS00741. DH_1. 1 hit.
PS50010. DH_2. 1 hit.
PS50003. PH_DOMAIN. 1 hit.
PS50001. SH2. 1 hit.
PS50002. SH3. 2 hits.
PS00479. ZF_DAG_PE_1. 1 hit.
PS50081. ZF_DAG_PE_2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

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

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

« Hide

        10         20         30         40         50
MELWRQCTHW LIQCRVLPPS HRVTWDGAQV CELAQALRDG VLLCQLLNNL
60 70 80 90 100
LPHAINLREV NLRPQMSQFL CLKNIRTFLS TCCEKFGLKR SELFEAFDLF
110 120 130 140 150
DVQDFGKVIY TLSALSWTPI AQNRGIMPFP TEEESVGDED IYSGLSDQID
160 170 180 190 200
DTVEEDEDLY DCVENEEAEG DEIYEDLMRS EPVSMPPKMT EYDKRCCCLR
210 220 230 240 250
EIQQTEEKYT DTLGSIQQHF LKPLQRFLKP QDIEIIFINI EDLLRVHTHF
260 270 280 290 300
LKEMKEALGT PGAANLYQVF IKYKERFLVY GRYCSQVESA SKHLDRVAAA
310 320 330 340 350
REDVQMKLEE CSQRANNGRF TLRDLLMVPM QRVLKYHLLL QELVKHTQEA
360 370 380 390 400
MEKENLRLAL DAMRDLAQCV NEVKRDNETL RQITNFQLSI ENLDQSLAHY
410 420 430 440 450
GRPKIDGELK ITSVERRSKM DRYAFLLDKA LLICKRRGDS YDLKDFVNLH
460 470 480 490 500
SFQVRDDSSG DRDNKKWSHM FLLIEDQGAQ GYELFFKTRE LKKKWMEQFE
510 520 530 540 550
MAISNIYPEN ATANGHDFQM FSFEETTSCK ACQMLLRGTF YQGYRCHRCR
560 570 580 590 600
ASAHKECLGR VPPCGRHGQD FPGTMKKDKL HRRAQDKKRN ELGLPKMEVF
610 620 630 640 650
QEYYGLPPPP GAIGPFLRLN PGDIVELTKA EAEQNWWEGR NTSTNEIGWF
660 670 680 690 700
PCNRVKPYVH GPPQDLSVHL WYAGPMERAG AESILANRSD GTFLVRQRVK
710 720 730 740 750
DAAEFAISIK YNVEVKHIKI MTAEGLYRIT EKKAFRGLTE LVEFYQQNSL
760 770 780 790 800
KDCFKSLDTT LQFPFKEPEK RTISRPAVGS TKYFGTAKAR YDFCARDRSE
810 820 830 840
LSLKEGDIIK ILNKKGQQGW WRGEIYGRVG WFPANYVEED YSEYC
Length:845
Mass (Da):98,314
Last modified:February 21, 2001 - v4
Checksum:iAC3BC9736FD2F138
GO
Isoform 2 (identifier: P15498-2) [UniParc]FASTAAdd to Basket

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

Note: No experimental confirmation available.

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

Sequence cautioni

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

Experimental Info

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

Natural variant

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

Alternative sequence

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

Sequence databases

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

Genome annotation databases

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

Polymorphism databases

DMDMi13124807.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

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

3D structure databases

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

Protein-protein interaction databases

BioGridi 113252. 68 interactions.
DIPi DIP-1061N.
IntActi P15498. 27 interactions.
MINTi MINT-1211643.
STRINGi 9606.ENSP00000302269.

PTM databases

PhosphoSitei P15498.

Polymorphism databases

DMDMi 13124807.

Proteomic databases

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

Protocols and materials databases

DNASUi 7409.
Structural Biology Knowledgebase Search...

Genome annotation databases

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

Organism-specific databases

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

Phylogenomic databases

eggNOGi NOG326494.
GeneTreei ENSGT00740000115307.
HOGENOMi HOG000234364.
HOVERGENi HBG018066.
InParanoidi P15498.
KOi K05730.
OMAi SHRVTWD.
OrthoDBi EOG73FQKZ.
PhylomeDBi P15498.
TreeFami TF316171.

Enzyme and pathway databases

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

Miscellaneous databases

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

Gene expression databases

Bgeei P15498.
CleanExi HS_VAV1.
ExpressionAtlasi P15498. baseline and differential.
Genevestigatori P15498.

Family and domain databases

Gene3Di 1.10.418.10. 1 hit.
1.20.900.10. 1 hit.
2.30.29.30. 1 hit.
3.30.505.10. 1 hit.
InterProi IPR001715. CH-domain.
IPR000219. DH-domain.
IPR001331. GDS_CDC24_CS.
IPR002219. PE/DAG-bd.
IPR001849. PH_domain.
IPR011993. PH_like_dom.
IPR000980. SH2.
IPR001452. SH3_domain.
IPR003096. SM22_calponin.
IPR028530. Vav.
[Graphical view ]
PANTHERi PTHR22826:SF112. PTHR22826:SF112. 1 hit.
Pfami PF00130. C1_1. 1 hit.
PF00307. CH. 1 hit.
PF00169. PH. 1 hit.
PF00621. RhoGEF. 1 hit.
PF00017. SH2. 1 hit.
PF00018. SH3_1. 2 hits.
[Graphical view ]
PRINTSi PR00401. SH2DOMAIN.
PR00452. SH3DOMAIN.
PR00888. SM22CALPONIN.
SMARTi SM00109. C1. 1 hit.
SM00033. CH. 1 hit.
SM00233. PH. 1 hit.
SM00325. RhoGEF. 1 hit.
SM00252. SH2. 1 hit.
SM00326. SH3. 2 hits.
[Graphical view ]
SUPFAMi SSF47576. SSF47576. 1 hit.
SSF48065. SSF48065. 1 hit.
SSF50044. SSF50044. 1 hit.
SSF55550. SSF55550. 1 hit.
PROSITEi PS50021. CH. 1 hit.
PS00741. DH_1. 1 hit.
PS50010. DH_2. 1 hit.
PS50003. PH_DOMAIN. 1 hit.
PS50001. SH2. 1 hit.
PS50002. SH3. 2 hits.
PS00479. ZF_DAG_PE_1. 1 hit.
PS50081. ZF_DAG_PE_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Mechanism of activation of the vav protooncogene."
    Coppola J., Bryant S., Koda T., Conway D., Barbacid M.
    Cell Growth Differ. 2:95-105(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), MUTAGENESIS OF CYS-529.
  2. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "The DNA sequence and biology of human chromosome 19."
    Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V.
    , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
    Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "Loss of the amino-terminal helix-loop-helix domain of the vav proto-oncogene activates its transforming potential."
    Katzav S., Cleveland J.L., Heslop H.E., Pulido D.
    Mol. Cell. Biol. 11:1912-1920(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-61.
  5. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 51-813 (ISOFORM 2).
    Tissue: Spleen.
  6. "vav, a novel human oncogene derived from a locus ubiquitously expressed in hematopoietic cells."
    Katzav S., Martin-Zanca D., Barbacid M.
    EMBO J. 8:2283-2290(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 68-845 (ISOFORM 1).
  7. Romero F.
    Submitted (JAN-1995) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 299-837 (ISOFORM 1).
  8. "The proline-rich region of Vav binds to Grb2 and Grb3-3."
    Ramos-Morales F., Romero F., Schweighoffer F., Bismuth G., Camonis J., Tortolero M., Fischer S.
    Oncogene 11:1665-1669(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 299-334 (ISOFORM 1).
  9. "The hematopoietically expressed vav proto-oncogene shares homology with the dbl GDP-GTP exchange factor, the bcr gene and a yeast gene (CDC24) involved in cytoskeletal organization."
    Adams J.M., Houston H., Allen J., Lints T., Harvey R.
    Oncogene 7:611-618(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: SIMILARITY TO CDC24 FAMILY.
  10. "Functional and physical interactions of Syk family kinases with the Vav proto-oncogene product."
    Deckert M., Tartare-Deckert S., Couture C., Mustelin T., Altman A.
    Immunity 5:591-604(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SYK, MUTAGENESIS OF ARG-696.
  11. "Cbl-b, a member of the Sli-1/c-Cbl protein family, inhibits Vav-mediated c-Jun N-terminal kinase activation."
    Bustelo X.R., Crespo P., Lopez-Barahona M., Gutkind J.S., Barbacid M.
    Oncogene 15:2511-2520(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CBLB.
  12. "BLNK: a central linker protein in B cell activation."
    Fu C., Turck C.W., Kurosaki T., Chan A.C.
    Immunity 9:93-103(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH BLNK; PLCG1; GRB2 AND NCK1.
  13. "hSiah2 is a new Vav binding protein which inhibits Vav-mediated signaling pathways."
    Germani A., Romero F., Houlard M., Camonis J., Gisselbrecht S., Fischer S., Varin-Blank N.
    Mol. Cell. Biol. 19:3798-3807(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SIAH2.
  14. "T-cell receptor antagonists induce Vav phosphorylation by selective activation of Fyn kinase."
    Huang J., Tilly D., Altman A., Sugie K., Grey H.M.
    Proc. Natl. Acad. Sci. U.S.A. 97:10923-10929(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION BY FYN.
  15. "DOCK2 associates with CrkL and regulates Rac1 in human leukemia cell lines."
    Nishihara H., Maeda M., Oda A., Tsuda M., Sawa H., Nagashima K., Tanaka S.
    Blood 100:3968-3974(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DOCK2.
  16. "Shb links SLP-76 and Vav with the CD3 complex in Jurkat T cells."
    Lindholm C.K., Henriksson M.L., Hallberg B., Welsh M.
    Eur. J. Biochem. 269:3279-3288(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SHB.
  17. "Adaptor protein APS binds the NH2-terminal autoinhibitory domain of guanine nucleotide exchange factor Vav3 and augments its activity."
    Yabana N., Shibuya M.
    Oncogene 21:7720-7729(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH APS.
  18. "Kinase-independent functions for Itk in TCR-induced regulation of Vav and the actin cytoskeleton."
    Dombroski D., Houghtling R.A., Labno C.M., Precht P., Takesono A., Caplen N.J., Billadeau D.D., Wange R.L., Burkhardt J.K., Schwartzberg P.L.
    J. Immunol. 174:1385-1392(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ITK.
  19. "Novel association of Vav2 and Nek3 modulates signaling through the human prolactin receptor."
    Miller S.L., DeMaria J.E., Freier D.O., Riegel A.M., Clevenger C.V.
    Mol. Endocrinol. 19:939-949(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NEK3.
  20. "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
    Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
    Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-826, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  21. Cited for: INTERACTION WITH ZNF655/VIK.
  22. "A Pyk2-Vav1 complex is recruited to beta3-adhesion sites to initiate Rho activation."
    Gao C., Blystone S.D.
    Biochem. J. 420:49-56(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PTK2B/PYK2.
  23. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  24. "Solution structure of the SH2 domain of human proto-oncogene protein VAV1."
    RIKEN structural genomics initiative (RSGI)
    Submitted (NOV-2005) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 661-775.

Entry informationi

Entry nameiVAV_HUMAN
AccessioniPrimary (citable) accession number: P15498
Secondary accession number(s): B4DVK9, M0QXX6, Q15860
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: February 21, 2001
Last modified: October 29, 2014
This is version 178 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Miscellaneous

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

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

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

External Data

Dasty 3