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P27870

- VAV_MOUSE

UniProt

P27870 - VAV_MOUSE

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Protein

Proto-oncogene vav

Gene

Vav1

Organism
Mus musculus (Mouse)
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. metal ion binding Source: UniProtKB-KW
  2. Rac guanyl-nucleotide exchange factor activity Source: MGI
  3. Rho guanyl-nucleotide exchange factor activity Source: MGI

GO - Biological processi

  1. G-protein coupled receptor signaling pathway Source: MGI
  2. immune response Source: MGI
  3. integrin-mediated signaling pathway Source: MGI
  4. intracellular signal transduction Source: MGI
  5. neutrophil chemotaxis Source: MGI
  6. phagocytosis Source: MGI
  7. positive regulation of cell adhesion Source: MGI
  8. positive regulation of Rac GTPase activity Source: MGI
  9. reactive oxygen species metabolic process Source: MGI
  10. regulation of GTPase activity Source: MGI
  11. small GTPase mediated signal transduction Source: InterPro
  12. T cell activation Source: MGI
  13. T cell differentiation Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Guanine-nucleotide releasing factor

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_188194. Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
REACT_188202. FCERI mediated Ca+2 mobilization.
REACT_188530. FCERI mediated MAPK activation.
REACT_188578. Signaling by SCF-KIT.
REACT_196588. Constitutive PI3K/AKT Signaling in Cancer.
REACT_198374. Regulation of actin dynamics for phagocytic cup formation.
REACT_198634. Regulation of signaling by CBL.
REACT_204733. G alpha (12/13) signalling events.
REACT_209641. NRAGE signals death through JNK.
REACT_210090. Rho GTPase cycle.
REACT_220092. GPVI-mediated activation cascade.
REACT_225836. Interleukin-3, 5 and GM-CSF signaling.
REACT_226341. PIP3 activates AKT signaling.

Names & Taxonomyi

Protein namesi
Recommended name:
Proto-oncogene vav
Alternative name(s):
p95vav
Gene namesi
Name:Vav1
Synonyms:Vav
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 17

Organism-specific databases

MGIiMGI:98923. Vav1.

Subcellular locationi

GO - Cellular componenti

  1. cell-cell junction Source: MGI
  2. cytosol Source: Reactome
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi529 – 5291C → S: Abolishes transforming activity. 1 Publication
Mutagenesisi532 – 5321C → S: Abolishes transforming activity. 1 Publication
Mutagenesisi554 – 5541H → D: Abolishes transforming activity. 1 Publication

Keywords - Diseasei

Proto-oncogene

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 845845Proto-oncogene vavPRO_0000080981Add
BLAST

Amino acid modifications

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

Post-translational modificationi

Phosphorylated by FYN (By similarity). Phosphorylated on tyrosine residues by HCK in response to IFNG and bacterial lipopolysaccharide (LPS).By similarity4 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP27870.
PaxDbiP27870.
PRIDEiP27870.

PTM databases

PhosphoSiteiP27870.

Expressioni

Tissue specificityi

Widely expressed in hematopoietic cells but not in other cell types. Found in the spleen and lung.1 Publication

Gene expression databases

BgeeiP27870.
CleanExiMM_VAV1.
ExpressionAtlasiP27870. baseline and differential.
GenevestigatoriP27870.

Interactioni

Subunit structurei

Interacts with SHB (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. May interact with CCPG1. Interacts with CLNK. Interacts with THEMIS2. Interacts with NEK3 and this interaction is prolactin-dependent. Interacts with ITK. Interacts with PTK2B/PYK2 (By similarity). Interacts with HCK. Interacts with PTK2B/PYK2. Interacts (via SH2 domain) with SYK (By similarity). Interacts with ANKRD54.By similarity8 Publications

Protein-protein interaction databases

BioGridi204500. 8 interactions.
DIPiDIP-31010N.
IntActiP27870. 7 interactions.
MINTiMINT-85069.

Structurei

Secondary structure

1
845
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi170 – 1778
Turni178 – 1803
Helixi191 – 21929
Helixi221 – 2244
Turni225 – 2273
Helixi230 – 2378
Helixi240 – 25920
Helixi261 – 2633
Helixi266 – 2738
Helixi276 – 2783
Helixi279 – 30022
Helixi302 – 31615
Helixi322 – 3254
Helixi328 – 3336
Helixi336 – 34611
Helixi350 – 38940
Beta strandi390 – 3923
Helixi397 – 4004
Beta strandi402 – 41211
Beta strandi420 – 43718
Beta strandi440 – 4489
Turni449 – 4513
Beta strandi452 – 4554
Beta strandi469 – 4757
Beta strandi481 – 4888
Helixi489 – 50618
Turni509 – 5124
Helixi513 – 5153
Beta strandi518 – 5214
Turni530 – 5323
Beta strandi538 – 5414
Beta strandi543 – 5464
Turni547 – 5493
Helixi555 – 5606
Turni585 – 5873
Beta strandi596 – 5994
Beta strandi603 – 6075
Helixi610 – 6123
Beta strandi624 – 6296
Beta strandi635 – 6417
Turni642 – 6443
Beta strandi647 – 6515
Helixi652 – 6543
Beta strandi655 – 6573
Beta strandi786 – 7916
Beta strandi796 – 8005
Beta strandi808 – 8136
Beta strandi817 – 8259
Beta strandi828 – 8336
Beta strandi836 – 8416

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1F5XNMR-A170-375[»]
1GCPX-ray2.10A/B/C/D595-660[»]
1GCQX-ray1.68C595-660[»]
1K1ZNMR-A583-660[»]
2KBTNMR-A784-844[»]
2VRWX-ray1.85B170-575[»]
ProteinModelPortaliP27870.
SMRiP27870. Positions 2-565, 596-779, 784-844.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP27870.

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.

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.
HOGENOMiHOG000234364.
HOVERGENiHBG018066.
InParanoidiP27870.
KOiK05730.
OMAiSHRVTWD.
PhylomeDBiP27870.
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.
InterProiIPR022613. CAMSAP_CH.
IPR001715. 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:SF112. PTHR22826:SF112. 1 hit.
PfamiPF00130. C1_1. 1 hit.
PF11971. CAMSAP_CH. 1 hit.
PF00169. PH. 1 hit.
PF00621. RhoGEF. 1 hit.
PF00017. SH2. 1 hit.
PF00018. SH3_1. 1 hit.
PF07653. SH3_2. 1 hit.
[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]

Sequencei

Sequence statusi: Complete.

P27870-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MELWRQCTHW LIQCRVLPPS HRVTWEGAQV CELAQALRDG VLLCQLLNNL
60 70 80 90 100
LPQAINLREV NLRPQMSQFL CLKNIRTFLS TCCEKFGLKR SELFEAFDLF
110 120 130 140 150
DVQDFGKVIY TLSALSWTPI AQNKGIMPFP TEDSALNDED IYSGLSDQID
160 170 180 190 200
DTAEEDEDLY DCVENEEAEG DEIYEDLMRL ESVPTPPKMT EYDKRCCCLR
210 220 230 240 250
EIQQTEEKYT DTLGSIQQHF MKPLQRFLKP QDMETIFVNI EELFSVHTHF
260 270 280 290 300
LKELKDALAG PGATTLYQVF IKYKERFLVY GRYCSQVESA SKHLDQVATA
310 320 330 340 350
REDVQMKLEE CSQRANNGRF TLRDLLMVPM QRVLKYHLLL QELVKHTQDA
360 370 380 390 400
TEKENLRLAL DAMRDLAQCV NEVKRDNETL RQITNFQLSI ENLDQSLANY
410 420 430 440 450
GRPKIDGELK ITSVERRSKT DRYAFLLDKA LLICKRRGDS YDLKASVNLH
460 470 480 490 500
SFQVRDDSSG ERDNKKWSHM FLLIEDQGAQ GYELFFKTRE LKKKWMEQFE
510 520 530 540 550
MAISNIYPEN ATANGHDFQM FSFEETTSCK ACQMLLRGTF YQGYRCYRCR
560 570 580 590 600
APAHKECLGR VPPCGRHGQD FAGTMKKDKL HRRAQDKKRN ELGLPKMEVF
610 620 630 640 650
QEYYGIPPPP GAFGPFLRLN PGDIVELTKA EAEHNWWEGR NTATNEVGWF
660 670 680 690 700
PCNRVHPYVH GPPQDLSVHL WYAGPMERAG AEGILTNRSD GTYLVRQRVK
710 720 730 740 750
DTAEFAISIK YNVEVKHIKI MTSEGLYRIT EKKAFRGLLE LVEFYQQNSL
760 770 780 790 800
KDCFKSLDTT LQFPYKEPER RAISKPPAGS TKYFGTAKAR YDFCARDRSE
810 820 830 840
LSLKEGDIIK ILNKKGQQGW WRGEIYGRIG WFPSNYVEED YSEYC
Length:845
Mass (Da):98,137
Last modified:August 1, 1992 - v1
Checksum:i3666DCCD1C5229DA
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti29 – 291Q → E in AAA63402. (PubMed:2005887)Curated
Sequence conflicti226 – 2261R → L in BAC40436. (PubMed:16141072)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X64361 mRNA. Translation: CAA45713.1.
AK088586 mRNA. Translation: BAC40436.1.
M59833 mRNA. Translation: AAA63402.1.
CCDSiCCDS28931.1.
PIRiA61187. TVMSVV.
RefSeqiNP_035821.3. NM_011691.4.
UniGeneiMm.248172.

Genome annotation databases

EnsembliENSMUST00000005889; ENSMUSP00000005889; ENSMUSG00000034116.
GeneIDi22324.
KEGGimmu:22324.
UCSCiuc008dep.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X64361 mRNA. Translation: CAA45713.1 .
AK088586 mRNA. Translation: BAC40436.1 .
M59833 mRNA. Translation: AAA63402.1 .
CCDSi CCDS28931.1.
PIRi A61187. TVMSVV.
RefSeqi NP_035821.3. NM_011691.4.
UniGenei Mm.248172.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1F5X NMR - A 170-375 [» ]
1GCP X-ray 2.10 A/B/C/D 595-660 [» ]
1GCQ X-ray 1.68 C 595-660 [» ]
1K1Z NMR - A 583-660 [» ]
2KBT NMR - A 784-844 [» ]
2VRW X-ray 1.85 B 170-575 [» ]
ProteinModelPortali P27870.
SMRi P27870. Positions 2-565, 596-779, 784-844.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 204500. 8 interactions.
DIPi DIP-31010N.
IntActi P27870. 7 interactions.
MINTi MINT-85069.

PTM databases

PhosphoSitei P27870.

Proteomic databases

MaxQBi P27870.
PaxDbi P27870.
PRIDEi P27870.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000005889 ; ENSMUSP00000005889 ; ENSMUSG00000034116 .
GeneIDi 22324.
KEGGi mmu:22324.
UCSCi uc008dep.2. mouse.

Organism-specific databases

CTDi 7409.
MGIi MGI:98923. Vav1.

Phylogenomic databases

eggNOGi NOG326494.
HOGENOMi HOG000234364.
HOVERGENi HBG018066.
InParanoidi P27870.
KOi K05730.
OMAi SHRVTWD.
PhylomeDBi P27870.
TreeFami TF316171.

Enzyme and pathway databases

Reactomei REACT_188194. Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
REACT_188202. FCERI mediated Ca+2 mobilization.
REACT_188530. FCERI mediated MAPK activation.
REACT_188578. Signaling by SCF-KIT.
REACT_196588. Constitutive PI3K/AKT Signaling in Cancer.
REACT_198374. Regulation of actin dynamics for phagocytic cup formation.
REACT_198634. Regulation of signaling by CBL.
REACT_204733. G alpha (12/13) signalling events.
REACT_209641. NRAGE signals death through JNK.
REACT_210090. Rho GTPase cycle.
REACT_220092. GPVI-mediated activation cascade.
REACT_225836. Interleukin-3, 5 and GM-CSF signaling.
REACT_226341. PIP3 activates AKT signaling.

Miscellaneous databases

EvolutionaryTracei P27870.
NextBioi 302549.
PROi P27870.
SOURCEi Search...

Gene expression databases

Bgeei P27870.
CleanExi MM_VAV1.
ExpressionAtlasi P27870. baseline and differential.
Genevestigatori P27870.

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 IPR022613. CAMSAP_CH.
IPR001715. 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 ]
PANTHERi PTHR22826:SF112. PTHR22826:SF112. 1 hit.
Pfami PF00130. C1_1. 1 hit.
PF11971. CAMSAP_CH. 1 hit.
PF00169. PH. 1 hit.
PF00621. RhoGEF. 1 hit.
PF00017. SH2. 1 hit.
PF00018. SH3_1. 1 hit.
PF07653. SH3_2. 1 hit.
[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], TISSUE SPECIFICITY, MUTAGENESIS OF CYS-529; CYS-532 AND HIS-554.
  2. "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: NUCLEOTIDE SEQUENCE [MRNA].
  3. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: NOD.
    Tissue: Thymus.
  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 [MRNA] OF 1-93.
  5. "Tec protein tyrosine kinase is involved in the signaling mechanism of granulocyte colony-stimulating factor receptor."
    Miyazato A., Yamashita Y., Hatake K., Miura Y., Ozawa K., Mano H.
    Cell Growth Differ. 7:1135-1139(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TEC.
  6. "Bacterial LPS and IFN-gamma trigger the tyrosine phosphorylation of vav in macrophages: evidence for involvement of the hck tyrosine kinase."
    English B.K., Orlicek S.L., Mei Z., Meals E.A.
    J. Leukoc. Biol. 62:859-864(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HCK, PHOSPHORYLATION.
  7. "Src-like adaptor protein (SLAP) is a negative regulator of T cell receptor signaling."
    Sosinowski T., Pandey A., Dixit V.M., Weiss A.
    J. Exp. Med. 191:463-474(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SLA.
  8. Cited for: PHOSPHORYLATION, INTERACTION WITH CBLB.
  9. Cited for: PHOSPHORYLATION, INTERACTION WITH CBLB.
  10. "MIST functions through distinct domains in immunoreceptor signaling in the presence and absence of LAT."
    Goitsuka R., Tatsuno A., Ishiai M., Kurosaki T., Kitamura D.
    J. Biol. Chem. 276:36043-36050(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CLNK.
  11. "Ccpg1, a novel scaffold protein that regulates the activity of the Rho guanine nucleotide exchange factor Dbs."
    Kostenko E.V., Olabisi O.O., Sahay S., Rodriguez P.L., Whitehead I.P.
    Mol. Cell. Biol. 26:8964-8975(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: POSSIBLE INTERACTION WITH CCPG1.
  12. "Quantitative time-resolved phosphoproteomic analysis of mast cell signaling."
    Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y., Kawakami T., Salomon A.R.
    J. Immunol. 179:5864-5876(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-844, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Mast cell.
  13. "Liar, a novel Lyn-binding nuclear/cytoplasmic shuttling protein that influences erythropoietin-induced differentiation."
    Samuels A.L., Klinken S.P., Ingley E.
    Blood 113:3845-3856(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ANKRD54.
  14. "Themis2/ICB1 is a signaling scaffold that selectively regulates macrophage Toll-like receptor signaling and cytokine production."
    Peirce M.J., Brook M., Morrice N., Snelgrove R., Begum S., Lanfrancotti A., Notley C., Hussell T., Cope A.P., Wait R.
    PLoS ONE 5:E11465-E11465(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH THEMIS2.

Entry informationi

Entry nameiVAV_MOUSE
AccessioniPrimary (citable) accession number: P27870
Secondary accession number(s): Q8BTV7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: August 1, 1992
Last modified: October 29, 2014
This is version 158 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3