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Guanine nucleotide exchange factor VAV3 (VAV-3)

 VAV3_MOUSE              Reviewed;         847 AA.
Q9R0C8; A2CFD7; Q7TS85; Q8BRV2; Q8CCF5; Q8R076; Q9JLS6;
24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
16-AUG-2004, sequence version 2.
05-DEC-2018, entry version 166.
RecName: Full=Guanine nucleotide exchange factor VAV3;
Short=VAV-3;
Name=Vav3;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND NUCLEOTIDE SEQUENCE [MRNA]
OF 1-789 (ISOFORM 3).
TISSUE=Skin;
PubMed=10713454; DOI=10.1016/S0378-1119(00)00026-3;
Trenkle T., McClelland M., Adlkofer K., Welsh J.;
"Major transcript variants of VAV3, a new member of the VAV family of
guanine nucleotide exchange factors.";
Gene 245:139-149(2000).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4), AND
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-731 (ISOFORM 1).
STRAIN=C57BL/6J; TISSUE=Embryonic stomach, and Embryonic testis;
PubMed=16141072; DOI=10.1126/science.1112014;
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.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Brain, and Mammary tumor;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
PROTEIN SEQUENCE OF 143-152, AND IDENTIFICATION BY MASS SPECTROMETRY.
STRAIN=OF1; TISSUE=Hippocampus;
Lubec G., Sunyer B., Chen W.-Q.;
Submitted (JAN-2009) to UniProtKB.
[6]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=15711558; DOI=10.1038/nm1194;
Faccio R., Teitelbaum S.L., Fujikawa K., Chappel J., Zallone A.,
Tybulewicz V.L., Ross F.P., Swat W.;
"Vav3 regulates osteoclast function and bone mass.";
Nat. Med. 11:284-290(2005).
[7]
FUNCTION, AND INTERACTION WITH EPHA2.
PubMed=16782872; DOI=10.1128/MCB.02215-05;
Hunter S.G., Zhuang G., Brantley-Sieders D.M., Swat W., Cowan C.W.,
Chen J.;
"Essential role of Vav family guanine nucleotide exchange factors in
EphA receptor-mediated angiogenesis.";
Mol. Cell. Biol. 26:4830-4842(2006).
[8]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=19147786; DOI=10.1182/blood-2008-07-166702;
Sindrilaru A., Peters T., Schymeinsky J., Oreshkova T., Wang H.,
Gompf A., Mannella F., Wlaschek M., Sunderkotter C., Rudolph K.L.,
Walzog B., Bustelo X.R., Fischer K.D., Scharffetter-Kochanek K.;
"Wound healing defect of Vav3-/- mice due to impaired {beta}2-
integrin-dependent macrophage phagocytosis of apoptotic neutrophils.";
Blood 113:5266-5276(2009).
[9]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Lung, and Spleen;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- 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 (By similarity). 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. 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-mediated macrophage adhesion and,
to a lesser extent, contributes to beta-3-mediated adhesion. Does
not affect integrin beta-1-mediated adhesion. {ECO:0000250,
ECO:0000269|PubMed:15711558, ECO:0000269|PubMed:16782872,
ECO:0000269|PubMed:19147786}.
-!- SUBUNIT: Interacts with the PH domain of APS. Interacts with ROS1;
constitutive interaction that mediates VAV3 phosphorylation (By
similarity). Interacts (via SH2 domains) with the phosphorylated
form of EPHA2. {ECO:0000250, ECO:0000269|PubMed:16782872}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative promoter usage, Alternative splicing; Named isoforms=4;
Name=1; Synonyms=Alpha;
IsoId=Q9R0C8-1; Sequence=Displayed;
Name=2; Synonyms=Beta;
IsoId=Q9R0C8-2; Sequence=Not described;
Name=3; Synonyms=VAV3.1;
IsoId=Q9R0C8-3; Sequence=VSP_042360, VSP_042361;
Note=Produced by alternative promoter usage.;
Name=4;
IsoId=Q9R0C8-4; Sequence=VSP_042362, VSP_042363;
Note=Produced by alternative splicing. No experimental
confirmation available.;
-!- TISSUE SPECIFICITY: Abundantly expressed in osteoclasts and mature
osteoblasts. Also expressed in bone marrow macrophages (at protein
level):.
-!- PTM: Phosphorylated. Phosphorylation can be mediated by ROS1 (By
similarity). In osteoclasts, undergoes tyrosine phosphorylation in
response to CSF1. {ECO:0000250}.
-!- DISRUPTION PHENOTYPE: Mutant mice exhibit increased bone density,
due to diminished bone resorption, including following parathyroid
hormone treatment. This phenotype is due to defective terminal
osteoclast differentiation. They also show a delayed wound repair
program, characterized by a deficit in macrophage emigration to
the wound, a reduced myofibroblast-dependent wound contraction and
a diminished neovascularization in the restoration tissue.
{ECO:0000269|PubMed:15711558, ECO:0000269|PubMed:19147786}.
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EMBL; AF067816; AAF09171.1; -; mRNA.
EMBL; AF140280; AAF20330.2; -; mRNA.
EMBL; AK033253; BAC28212.1; -; mRNA.
EMBL; AK041249; BAC30879.2; -; mRNA.
EMBL; AK147053; BAE27637.1; -; mRNA.
EMBL; AL731716; CAM14541.1; -; Genomic_DNA.
EMBL; AL671857; CAM14541.1; JOINED; Genomic_DNA.
EMBL; AL671987; CAM14541.1; JOINED; Genomic_DNA.
EMBL; AL671857; CAM16459.1; -; Genomic_DNA.
EMBL; AL671987; CAM16459.1; JOINED; Genomic_DNA.
EMBL; AL731716; CAM16459.1; JOINED; Genomic_DNA.
EMBL; AL671987; CAM18527.1; -; Genomic_DNA.
EMBL; AL731716; CAM18527.1; JOINED; Genomic_DNA.
EMBL; AL671857; CAM18527.1; JOINED; Genomic_DNA.
EMBL; CR936838; CAM28077.1; -; Genomic_DNA.
EMBL; CR936848; CAM28077.1; JOINED; Genomic_DNA.
EMBL; CR936849; CAM28077.1; JOINED; Genomic_DNA.
EMBL; CR938729; CAM28077.1; JOINED; Genomic_DNA.
EMBL; CR938729; CAM28109.1; -; Genomic_DNA.
EMBL; CR936848; CAM28109.1; JOINED; Genomic_DNA.
EMBL; CR938729; CAM28111.1; -; Genomic_DNA.
EMBL; CR936838; CAM28111.1; JOINED; Genomic_DNA.
EMBL; CR936848; CAM28111.1; JOINED; Genomic_DNA.
EMBL; CR936849; CAM28111.1; JOINED; Genomic_DNA.
EMBL; CR936849; CAM28160.1; -; Genomic_DNA.
EMBL; CR936838; CAM28160.1; JOINED; Genomic_DNA.
EMBL; CR936848; CAM28160.1; JOINED; Genomic_DNA.
EMBL; CR938729; CAM28160.1; JOINED; Genomic_DNA.
EMBL; CR936848; CAM28169.1; -; Genomic_DNA.
EMBL; CR938729; CAM28169.1; JOINED; Genomic_DNA.
EMBL; CR936848; CAM28172.1; -; Genomic_DNA.
EMBL; CR936838; CAM28172.1; JOINED; Genomic_DNA.
EMBL; CR936849; CAM28172.1; JOINED; Genomic_DNA.
EMBL; CR938729; CAM28172.1; JOINED; Genomic_DNA.
EMBL; BC027242; AAH27242.1; -; mRNA.
EMBL; BC052739; AAH52739.1; -; mRNA.
CCDS; CCDS17773.1; -. [Q9R0C8-1]
CCDS; CCDS59650.1; -. [Q9R0C8-3]
RefSeq; NP_065251.2; NM_020505.2. [Q9R0C8-1]
RefSeq; NP_666251.1; NM_146139.2. [Q9R0C8-3]
UniGene; Mm.282257; -.
ProteinModelPortal; Q9R0C8; -.
SMR; Q9R0C8; -.
BioGrid; 208227; 1.
STRING; 10090.ENSMUSP00000036270; -.
iPTMnet; Q9R0C8; -.
PhosphoSitePlus; Q9R0C8; -.
EPD; Q9R0C8; -.
PaxDb; Q9R0C8; -.
PeptideAtlas; Q9R0C8; -.
PRIDE; Q9R0C8; -.
Ensembl; ENSMUST00000046864; ENSMUSP00000036270; ENSMUSG00000033721. [Q9R0C8-1]
Ensembl; ENSMUST00000106576; ENSMUSP00000102186; ENSMUSG00000033721. [Q9R0C8-3]
GeneID; 57257; -.
KEGG; mmu:57257; -.
UCSC; uc008raf.1; mouse. [Q9R0C8-4]
UCSC; uc008rag.1; mouse. [Q9R0C8-1]
UCSC; uc008rah.1; mouse. [Q9R0C8-3]
CTD; 10451; -.
MGI; MGI:1888518; Vav3.
eggNOG; KOG2996; Eukaryota.
eggNOG; ENOG410XPH6; LUCA.
GeneTree; ENSGT00940000155252; -.
HOGENOM; HOG000234364; -.
HOVERGEN; HBG018066; -.
InParanoid; Q9R0C8; -.
KO; K05730; -.
OMA; AKQDRHI; -.
OrthoDB; EOG091G01O3; -.
PhylomeDB; Q9R0C8; -.
TreeFam; TF316171; -.
Reactome; R-MMU-114604; GPVI-mediated activation cascade.
Reactome; R-MMU-193648; NRAGE signals death through JNK.
Reactome; R-MMU-194840; Rho GTPase cycle.
Reactome; R-MMU-2029482; Regulation of actin dynamics for phagocytic cup formation.
Reactome; R-MMU-2424491; DAP12 signaling.
Reactome; R-MMU-2871796; FCERI mediated MAPK activation.
Reactome; R-MMU-2871809; FCERI mediated Ca+2 mobilization.
Reactome; R-MMU-3928665; EPH-ephrin mediated repulsion of cells.
Reactome; R-MMU-416482; G alpha (12/13) signalling events.
Reactome; R-MMU-4420097; VEGFA-VEGFR2 Pathway.
Reactome; R-MMU-5218920; VEGFR2 mediated vascular permeability.
ChiTaRS; Vav3; mouse.
PRO; PR:Q9R0C8; -.
Proteomes; UP000000589; Chromosome 3.
Bgee; ENSMUSG00000033721; Expressed in 267 organ(s), highest expression level in habenula.
CleanEx; MM_VAV3; -.
Genevisible; Q9R0C8; MM.
GO; GO:0005737; C:cytoplasm; IDA:MGI.
GO; GO:0005886; C:plasma membrane; IDA:MGI.
GO; GO:0005154; F:epidermal growth factor receptor binding; IPI:MGI.
GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IMP:MGI.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0030676; F:Rac guanyl-nucleotide exchange factor activity; IGI:MGI.
GO; GO:0005089; F:Rho guanyl-nucleotide exchange factor activity; IGI:MGI.
GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
GO; GO:0050853; P:B cell receptor signaling pathway; ISO:MGI.
GO; GO:0016477; P:cell migration; IGI:MGI.
GO; GO:0030031; P:cell projection assembly; IGI:MGI.
GO; GO:0006974; P:cellular response to DNA damage stimulus; ISO:MGI.
GO; GO:0007229; P:integrin-mediated signaling pathway; IGI:MGI.
GO; GO:0030032; P:lamellipodium assembly; IGI:MGI.
GO; GO:0030593; P:neutrophil chemotaxis; IGI:MGI.
GO; GO:0030890; P:positive regulation of B cell proliferation; ISO:MGI.
GO; GO:0045785; P:positive regulation of cell adhesion; IGI:MGI.
GO; GO:0043552; P:positive regulation of phosphatidylinositol 3-kinase activity; IGI:MGI.
GO; GO:0008361; P:regulation of cell size; IEA:Ensembl.
GO; GO:0043087; P:regulation of GTPase activity; IGI:MGI.
GO; GO:0035023; P:regulation of Rho protein signal transduction; IEA:InterPro.
GO; GO:0042493; P:response to drug; ISO:MGI.
GO; GO:0007264; P:small GTPase mediated signal transduction; IMP:MGI.
GO; GO:0006906; P:vesicle fusion; IGI:MGI.
CDD; cd00029; C1; 1.
CDD; cd00014; CH; 1.
CDD; cd01223; PH_Vav; 1.
CDD; cd00160; RhoGEF; 1.
CDD; cd10407; SH2_Vav3; 1.
CDD; cd11978; SH3_VAV3_2; 1.
Gene3D; 1.10.418.10; -; 1.
Gene3D; 1.20.900.10; -; 1.
Gene3D; 2.30.29.30; -; 1.
Gene3D; 3.30.505.10; -; 1.
InterPro; IPR022613; CAMSAP_CH.
InterPro; IPR001715; CH-domain.
InterPro; IPR036872; CH_dom_sf.
InterPro; IPR035899; DBL_dom_sf.
InterPro; IPR000219; DH-domain.
InterPro; IPR001331; GDS_CDC24_CS.
InterPro; IPR002219; PE/DAG-bd.
InterPro; IPR011993; PH-like_dom_sf.
InterPro; IPR001849; PH_domain.
InterPro; IPR037832; PH_Vav.
InterPro; IPR000980; SH2.
InterPro; IPR036860; SH2_dom_sf.
InterPro; IPR036028; SH3-like_dom_sf.
InterPro; IPR001452; SH3_domain.
InterPro; IPR003096; SM22_calponin.
InterPro; IPR035881; VAV3_SH2.
InterPro; IPR035734; VAV3_SH3_2.
Pfam; PF00130; C1_1; 1.
Pfam; PF11971; CAMSAP_CH; 1.
Pfam; PF00169; PH; 1.
Pfam; PF00621; RhoGEF; 1.
Pfam; PF00017; SH2; 1.
Pfam; PF00018; SH3_1; 1.
Pfam; PF07653; SH3_2; 1.
PRINTS; PR00401; SH2DOMAIN.
PRINTS; PR00452; SH3DOMAIN.
PRINTS; PR00888; SM22CALPONIN.
SMART; SM00109; C1; 1.
SMART; SM00033; CH; 1.
SMART; SM00233; PH; 1.
SMART; SM00325; RhoGEF; 1.
SMART; SM00252; SH2; 1.
SMART; SM00326; SH3; 2.
SUPFAM; SSF47576; SSF47576; 1.
SUPFAM; SSF48065; SSF48065; 1.
SUPFAM; SSF50044; SSF50044; 2.
SUPFAM; SSF55550; SSF55550; 1.
PROSITE; PS50021; CH; 1.
PROSITE; PS00741; DH_1; 1.
PROSITE; PS50010; DH_2; 1.
PROSITE; PS50003; PH_DOMAIN; 1.
PROSITE; PS50001; SH2; 1.
PROSITE; PS50002; SH3; 2.
PROSITE; PS00479; ZF_DAG_PE_1; 1.
PROSITE; PS50081; ZF_DAG_PE_2; 1.
1: Evidence at protein level;
Alternative promoter usage; Alternative splicing; Angiogenesis;
Complete proteome; Direct protein sequencing;
Guanine-nucleotide releasing factor; Metal-binding; Phosphoprotein;
Reference proteome; Repeat; SH2 domain; SH3 domain; Zinc; Zinc-finger.
CHAIN 1 847 Guanine nucleotide exchange factor VAV3.
/FTId=PRO_0000080987.
DOMAIN 1 119 Calponin-homology (CH).
{ECO:0000255|PROSITE-ProRule:PRU00044}.
DOMAIN 192 371 DH. {ECO:0000255|PROSITE-
ProRule:PRU00062}.
DOMAIN 400 502 PH. {ECO:0000255|PROSITE-
ProRule:PRU00145}.
DOMAIN 592 660 SH3 1. {ECO:0000255|PROSITE-
ProRule:PRU00192}.
DOMAIN 672 766 SH2. {ECO:0000255|PROSITE-
ProRule:PRU00191}.
DOMAIN 788 847 SH3 2. {ECO:0000255|PROSITE-
ProRule:PRU00192}.
ZN_FING 513 562 Phorbol-ester/DAG-type.
{ECO:0000255|PROSITE-ProRule:PRU00226}.
REGION 560 847 Sufficient for interaction with ROS1.
{ECO:0000250}.
MOD_RES 141 141 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q9UKW4}.
VAR_SEQ 1 560 Missing (in isoform 3).
{ECO:0000303|PubMed:10713454,
ECO:0000303|PubMed:16141072}.
/FTId=VSP_042360.
VAR_SEQ 561 568 NCGRVNSV -> MPIFTFVS (in isoform 3).
{ECO:0000303|PubMed:10713454,
ECO:0000303|PubMed:16141072}.
/FTId=VSP_042361.
VAR_SEQ 569 574 EQGPFK -> GKSCLL (in isoform 4).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_042362.
VAR_SEQ 575 847 Missing (in isoform 4).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_042363.
CONFLICT 355 355 K -> R (in Ref. 2; BAC30879).
{ECO:0000305}.
CONFLICT 452 452 I -> T (in Ref. 2; BAC28212).
{ECO:0000305}.
SEQUENCE 847 AA; 97968 MW; 727C9BF50DF8CF19 CRC64;
MEPWKQCAQW LIHSKVLPPN HRVTWDSAQV FDLAQTLRDG VLLCQLLNNL RPHSINLKEI
NLRPQMSQFL CLKNIRTFLA ACCDTFGMRK SELFEAFDLF DVRDFGKVIE TLSRLSRTPI
ALATGIRPFP TEESINDEDI YKGLPDLIDE TRVEDEEDLY DCVYGEDEGG EVYEDLMKAE
EAQQPKSQEN DIRSCCLAEI RQTEEKYTET LESIEKYFMA PLKRFLTAAE FDSVFINIPD
LVKVHRSLMQ EIHDSIVNKD DQNLYQVFIN YKERLVIYGQ YCSGVESAIS NLDYISKTKE
DVKLKLEECS KRANNGKFTL RDLLVVPMQR VLKYHLLLQE LVKHTHDPME KANLKLALDA
MKDLAQYVNE VKRDNETLRE IKQFQLSIEN LNQPVLLFGR PQGDGEIRIT TLDKHTKQER
HIFLFDLAVI VCKRKGDNYE MKEIIDLQQY KIANNPTTDK ENKKWSYGFY LIHTQGQNGL
EFYCKTKDLK KKWLEQFEMA LSNIRPDYAD SNFHDFKMHT FTRVTSCRVC QMLLRGTFYQ
GYLCFKCGAK AHKECLGRVD NCGRVNSVEQ GPFKPPEKRT NGLRRASRQV DPGLPKMQVI
RNYTGTPAPG LHEGPPLHIQ AGDTVELLRG DAHSVFWQGR NLASGEVGFF PSDAVKPSPC
VPKPVDYSCQ PWYAGPMERL QAETELINRV NSTYLVRHRT KESGEYAISI KYNNEAKHIK
ILTRDGFFHI AENRKFKSLM ELVEYYKHHS LKEGFRTLDT TLQFPYKEPE QPAGQRGNRT
GNSLLSPKVL GIAIARYDFC ARDMRELSLL KGDMVKIYTK MSANGWWRGE VNGRVGWFPS
TYVEEDE


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YHB0679Mo Mouse Guanine nucleotide exchange factor VAV3,VAV3 ELISA Kit 48T
CSB-EL025805MO Mouse Guanine nucleotide exchange factor VAV3(VAV3) ELISA kit 96T
E0645Hu Human Guanine nucleotide exchange factor VAV3,VAV3 ELISA Kit 48T
E0960Mo Mouse Guanine nucleotide exchange factor VAV3,VAV3 ELISA Kit 48T
CSB-EL025805HU Human Guanine nucleotide exchange factor VAV3(VAV3) ELISA kit 96T
E0959Mo Mouse Guanine nucleotide exchange factor VAV3,VAV3 ELISA Kit 48T
YHB1456Hu Human Guanine nucleotide exchange factor VAV3,VAV3 ELISA Kit 96T
YHB0679Mo Mouse Guanine nucleotide exchange factor VAV3,VAV3 ELISA Kit 96T
CSB-EL025805HU Human Guanine nucleotide exchange factor VAV3(VAV3) ELISA kit SpeciesHuman 96T
CSB-EL025805MO Mouse Guanine nucleotide exchange factor VAV3(VAV3) ELISA kit SpeciesMouse 96T
EIAAB45708 Guanine nucleotide exchange factor VAV3,Homo sapiens,Human,VAV3,VAV-3
E0219m ELISA Kit FOR Guanine nucleotide exchange factor VAV3; organism: Mouse; gene name: Vav3 96T
VAV3 VAV3 Gene vav 3 guanine nucleotide exchange factor
EIAAB35856 Homo sapiens,Human,KIAA0313,Neural RAP guanine nucleotide exchange protein,nRap GEP,NRAPGEP,PDZ domain-containing guanine nucleotide exchange factor 1,PDZGEF1,PDZ-GEF1,RA-GEF,Rap guanine nucleotide ex
EIAAB39882 Deafness locus-associated putative guanine nucleotide exchange factor,DelGEF,DELGEF,GNEFR,Guanine nucleotide exchange factor-related protein,Homo sapiens,Human,Secretion-regulating guanine nucleotide
EIAAB39884 Deafness locus-associated putative guanine nucleotide exchange factor,DelGEF,Delgef,Gnefr,Guanine nucleotide exchange factor-related protein,Mouse,Mus musculus,Secretion-regulating guanine nucleotide
EM354 Guanine nucleotide exchange factor VAV3 Elisa Kit 96T
EH778 Guanine nucleotide exchange factor VAV3 Elisa Kit 96T
EIAAB35861 cAMP-dependent Rap1 guanine-nucleotide exchange factor,cAMP-GEFII,cAMP-regulated guanine nucleotide exchange factor II,Cgef2,EPAC 2,Epac2,Exchange factor directly activated by cAMP 2,Exchange protein
EIAAB34493 190 kDa guanine nucleotide exchange factor,Kiaa1998,Mouse,Mus musculus,p190RhoGEF,p190-RhoGEF,Rgnef,Rho-guanine nucleotide exchange factor,Rho-interacting protein 2,Rhoip2,Rip2


 

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