Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Proto-oncogene vav (p95vav)

 VAV_MOUSE               Reviewed;         845 AA.
P27870; Q8BTV7;
01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
01-AUG-1992, sequence version 1.
28-MAR-2018, entry version 193.
RecName: Full=Proto-oncogene vav;
AltName: Full=p95vav;
Name=Vav1; Synonyms=Vav;
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], TISSUE SPECIFICITY, AND MUTAGENESIS OF
CYS-529; CYS-532 AND HIS-554.
PubMed=2069873;
Coppola J., Bryant S., Koda T., Conway D., Barbacid M.;
"Mechanism of activation of the vav protooncogene.";
Cell Growth Differ. 2:95-105(1991).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=1565462;
Adams J.M., Houston H., Allen J., Lints T., Harvey R.;
"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.";
Oncogene 7:611-618(1992).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=NOD; TISSUE=Thymus;
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).
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-93.
PubMed=2005887; DOI=10.1128/MCB.11.4.1912;
Katzav S., Cleveland J.L., Heslop H.E., Pulido D.;
"Loss of the amino-terminal helix-loop-helix domain of the vav proto-
oncogene activates its transforming potential.";
Mol. Cell. Biol. 11:1912-1920(1991).
[5]
INTERACTION WITH TEC.
PubMed=8877094;
Miyazato A., Yamashita Y., Hatake K., Miura Y., Ozawa K., Mano H.;
"Tec protein tyrosine kinase is involved in the signaling mechanism of
granulocyte colony-stimulating factor receptor.";
Cell Growth Differ. 7:1135-1139(1996).
[6]
INTERACTION WITH HCK, AND PHOSPHORYLATION.
PubMed=9400828;
English B.K., Orlicek S.L., Mei Z., Meals E.A.;
"Bacterial LPS and IFN-gamma trigger the tyrosine phosphorylation of
vav in macrophages: evidence for involvement of the hck tyrosine
kinase.";
J. Leukoc. Biol. 62:859-864(1997).
[7]
INTERACTION WITH SLA.
PubMed=10662792; DOI=10.1084/jem.191.3.463;
Sosinowski T., Pandey A., Dixit V.M., Weiss A.;
"Src-like adaptor protein (SLAP) is a negative regulator of T cell
receptor signaling.";
J. Exp. Med. 191:463-474(2000).
[8]
PHOSPHORYLATION, AND INTERACTION WITH CBLB.
PubMed=10646609; DOI=10.1038/35003235;
Chiang Y.J., Kole H.K., Brown K., Naramura M., Fukuhara S., Hu R.-J.,
Jang I.K., Gutkind J.S., Shevach E., Gu H.;
"Cbl-b regulates the CD28 dependence of T-cell activation.";
Nature 403:216-220(2000).
[9]
PHOSPHORYLATION, AND INTERACTION WITH CBLB.
PubMed=10646608; DOI=10.1038/35003228;
Bachmaier K., Krawczyk C., Kozieradzki I., Kong Y.-Y., Sasaki T.,
Oliveira-dos-Santos A., Mariathasan S., Bouchard D., Wakeham A.,
Itie A., Le J., Ohashi P.S., Sarosi I., Nishina H., Lipkowitz S.,
Penninger J.M.;
"Negative regulation of lymphocyte activation and autoimmunity by the
molecular adaptor Cbl-b.";
Nature 403:211-216(2000).
[10]
INTERACTION WITH CLNK.
PubMed=11463797; DOI=10.1074/jbc.M106390200;
Goitsuka R., Tatsuno A., Ishiai M., Kurosaki T., Kitamura D.;
"MIST functions through distinct domains in immunoreceptor signaling
in the presence and absence of LAT.";
J. Biol. Chem. 276:36043-36050(2001).
[11]
POSSIBLE INTERACTION WITH CCPG1.
PubMed=17000758; DOI=10.1128/MCB.00670-06;
Kostenko E.V., Olabisi O.O., Sahay S., Rodriguez P.L., Whitehead I.P.;
"Ccpg1, a novel scaffold protein that regulates the activity of the
Rho guanine nucleotide exchange factor Dbs.";
Mol. Cell. Biol. 26:8964-8975(2006).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-844, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Mast cell;
PubMed=17947660; DOI=10.4049/jimmunol.179.9.5864;
Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,
Kawakami T., Salomon A.R.;
"Quantitative time-resolved phosphoproteomic analysis of mast cell
signaling.";
J. Immunol. 179:5864-5876(2007).
[13]
INTERACTION WITH ANKRD54.
PubMed=19064729; DOI=10.1182/blood-2008-04-153452;
Samuels A.L., Klinken S.P., Ingley E.;
"Liar, a novel Lyn-binding nuclear/cytoplasmic shuttling protein that
influences erythropoietin-induced differentiation.";
Blood 113:3845-3856(2009).
[14]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=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).
[15]
INTERACTION WITH THEMIS2.
PubMed=20644716; DOI=10.1371/journal.pone.0011465;
Peirce M.J., Brook M., Morrice N., Snelgrove R., Begum S.,
Lanfrancotti A., Notley C., Hussell T., Cope A.P., Wait R.;
"Themis2/ICB1 is a signaling scaffold that selectively regulates
macrophage Toll-like receptor signaling and cytokine production.";
PLoS ONE 5:E11465-E11465(2010).
[16]
INTERACTION WITH CD6.
PubMed=24584089; DOI=10.1038/ni.2843;
Roncagalli R., Hauri S., Fiore F., Liang Y., Chen Z., Sansoni A.,
Kanduri K., Joly R., Malzac A., Laehdesmaeki H., Lahesmaa R.,
Yamasaki S., Saito T., Malissen M., Aebersold R., Gstaiger M.,
Malissen B.;
"Quantitative proteomics analysis of signalosome dynamics in primary T
cells identifies the surface receptor CD6 as a Lat adaptor-independent
TCR signaling hub.";
Nat. Immunol. 15:384-392(2014).
-!- FUNCTION: Couples tyrosine kinase signals with the activation of
the Rho/Rac GTPases, thus leading to cell differentiation and/or
proliferation.
-!- SUBUNIT: 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 (PubMed:10646609,
PubMed:10646608). May interact with CCPG1 (PubMed:17000758).
Interacts with CLNK (PubMed:11463797). Interacts with THEMIS2
(PubMed:20644716). 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 (PubMed:19064729). Interacts with CD6
(PubMed:24584089). {ECO:0000250|UniProtKB:P15498,
ECO:0000269|PubMed:10646608, ECO:0000269|PubMed:10646609,
ECO:0000269|PubMed:10662792, ECO:0000269|PubMed:11463797,
ECO:0000269|PubMed:19064729, ECO:0000269|PubMed:20644716,
ECO:0000269|PubMed:24584089, ECO:0000269|PubMed:8877094,
ECO:0000269|PubMed:9400828}.
-!- INTERACTION:
P61979:Hnrnpk; NbExp=3; IntAct=EBI-1697, EBI-299907;
P19878:NCF2 (xeno); NbExp=4; IntAct=EBI-1697, EBI-489611;
-!- TISSUE SPECIFICITY: Widely expressed in hematopoietic cells but
not in other cell types. Found in the spleen and lung.
{ECO:0000269|PubMed:2069873}.
-!- DOMAIN: The DH domain is involved in interaction with CCPG1.
-!- PTM: Phosphorylated by FYN (By similarity). Phosphorylated on
tyrosine residues by HCK in response to IFNG and bacterial
lipopolysaccharide (LPS). {ECO:0000250,
ECO:0000269|PubMed:10646608, ECO:0000269|PubMed:10646609,
ECO:0000269|PubMed:9400828}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; X64361; CAA45713.1; -; mRNA.
EMBL; AK088586; BAC40436.1; -; mRNA.
EMBL; M59833; AAA63402.1; -; mRNA.
CCDS; CCDS28931.1; -.
PIR; A61187; TVMSVV.
RefSeq; NP_035821.3; NM_011691.4.
UniGene; Mm.248172; -.
PDB; 1F5X; NMR; -; A=170-375.
PDB; 1GCP; X-ray; 2.10 A; A/B/C/D=595-660.
PDB; 1GCQ; X-ray; 1.68 A; C=595-660.
PDB; 1K1Z; NMR; -; A=583-660.
PDB; 2KBT; NMR; -; A=784-844.
PDB; 2VRW; X-ray; 1.85 A; B=170-575.
PDBsum; 1F5X; -.
PDBsum; 1GCP; -.
PDBsum; 1GCQ; -.
PDBsum; 1K1Z; -.
PDBsum; 2KBT; -.
PDBsum; 2VRW; -.
ProteinModelPortal; P27870; -.
SMR; P27870; -.
BioGrid; 204500; 9.
DIP; DIP-31010N; -.
IntAct; P27870; 15.
MINT; P27870; -.
STRING; 10090.ENSMUSP00000005889; -.
iPTMnet; P27870; -.
PhosphoSitePlus; P27870; -.
EPD; P27870; -.
PaxDb; P27870; -.
PeptideAtlas; P27870; -.
PRIDE; P27870; -.
Ensembl; ENSMUST00000005889; ENSMUSP00000005889; ENSMUSG00000034116.
GeneID; 22324; -.
KEGG; mmu:22324; -.
UCSC; uc008dep.2; mouse.
CTD; 7409; -.
MGI; MGI:98923; Vav1.
eggNOG; KOG2996; Eukaryota.
eggNOG; ENOG410XPH6; LUCA.
GeneTree; ENSGT00910000144110; -.
HOGENOM; HOG000234364; -.
HOVERGEN; HBG018066; -.
InParanoid; P27870; -.
KO; K05730; -.
OMA; DKRECCL; -.
OrthoDB; EOG091G01O3; -.
PhylomeDB; P27870; -.
TreeFam; TF316171; -.
Reactome; R-MMU-114604; GPVI-mediated activation cascade.
Reactome; R-MMU-1257604; PIP3 activates AKT signaling.
Reactome; R-MMU-1433557; Signaling by SCF-KIT.
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-2871796; FCERI mediated MAPK activation.
Reactome; R-MMU-2871809; FCERI mediated Ca+2 mobilization.
Reactome; R-MMU-389359; CD28 dependent Vav1 pathway.
Reactome; R-MMU-416482; G alpha (12/13) signalling events.
Reactome; R-MMU-4420097; VEGFA-VEGFR2 Pathway.
Reactome; R-MMU-512988; Interleukin-3, 5 and GM-CSF signaling.
Reactome; R-MMU-5218920; VEGFR2 mediated vascular permeability.
Reactome; R-MMU-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
Reactome; R-MMU-912631; Regulation of signaling by CBL.
Reactome; R-MMU-983695; Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
EvolutionaryTrace; P27870; -.
PRO; PR:P27870; -.
Proteomes; UP000000589; Chromosome 17.
Bgee; ENSMUSG00000034116; -.
CleanEx; MM_VAV1; -.
ExpressionAtlas; P27870; baseline and differential.
Genevisible; P27870; MM.
GO; GO:0005911; C:cell-cell junction; IDA:MGI.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; ISO:MGI.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0001784; F:phosphotyrosine residue binding; ISO:MGI.
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:0007186; P:G-protein coupled receptor signaling pathway; IGI:MGI.
GO; GO:0006955; P:immune response; IMP:MGI.
GO; GO:0007229; P:integrin-mediated signaling pathway; IGI:MGI.
GO; GO:0035556; P:intracellular signal transduction; IMP:MGI.
GO; GO:0030593; P:neutrophil chemotaxis; IGI:MGI.
GO; GO:0006909; P:phagocytosis; IGI:MGI.
GO; GO:0045785; P:positive regulation of cell adhesion; IGI:MGI.
GO; GO:0043547; P:positive regulation of GTPase activity; IGI:MGI.
GO; GO:0045954; P:positive regulation of natural killer cell mediated cytotoxicity; IGI:MGI.
GO; GO:0072593; P:reactive oxygen species metabolic process; 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:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
GO; GO:0042110; P:T cell activation; IMP:MGI.
GO; GO:0030217; P:T cell differentiation; IGI:MGI.
CDD; cd00029; C1; 1.
CDD; cd01223; PH_Vav; 1.
CDD; cd00160; RhoGEF; 1.
CDD; cd10405; SH2_Vav1; 1.
CDD; cd11979; SH3_VAV1_1; 1.
CDD; cd11976; SH3_VAV1_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; IPR028530; Vav1.
InterPro; IPR035879; VAV1_SH2.
InterPro; IPR035730; VAV1_SH3_1.
InterPro; IPR035729; VAV1_SH3_2.
PANTHER; PTHR22826:SF112; PTHR22826:SF112; 1.
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; 2.
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; 1.
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;
3D-structure; Complete proteome; Guanine-nucleotide releasing factor;
Metal-binding; Phosphoprotein; Proto-oncogene; Reference proteome;
Repeat; SH2 domain; SH3 domain; Zinc; Zinc-finger.
CHAIN 1 845 Proto-oncogene vav.
/FTId=PRO_0000080981.
DOMAIN 1 119 Calponin-homology (CH).
{ECO:0000255|PROSITE-ProRule:PRU00044}.
DOMAIN 194 373 DH. {ECO:0000255|PROSITE-
ProRule:PRU00062}.
DOMAIN 402 504 PH. {ECO:0000255|PROSITE-
ProRule:PRU00145}.
DOMAIN 592 660 SH3 1. {ECO:0000255|PROSITE-
ProRule:PRU00192}.
DOMAIN 671 765 SH2. {ECO:0000255|PROSITE-
ProRule:PRU00191}.
DOMAIN 782 842 SH3 2. {ECO:0000255|PROSITE-
ProRule:PRU00192}.
ZN_FING 515 564 Phorbol-ester/DAG-type.
{ECO:0000255|PROSITE-ProRule:PRU00226}.
COMPBIAS 33 99 Leu-rich.
MOD_RES 826 826 Phosphotyrosine.
{ECO:0000250|UniProtKB:P15498}.
MOD_RES 844 844 Phosphotyrosine.
{ECO:0000244|PubMed:17947660}.
MUTAGEN 529 529 C->S: Abolishes transforming activity.
{ECO:0000269|PubMed:2069873}.
MUTAGEN 532 532 C->S: Abolishes transforming activity.
{ECO:0000269|PubMed:2069873}.
MUTAGEN 554 554 H->D: Abolishes transforming activity.
{ECO:0000269|PubMed:2069873}.
CONFLICT 29 29 Q -> E (in Ref. 4; AAA63402).
{ECO:0000305}.
CONFLICT 226 226 R -> L (in Ref. 3; BAC40436).
{ECO:0000305}.
HELIX 170 177 {ECO:0000244|PDB:1F5X}.
TURN 178 180 {ECO:0000244|PDB:1F5X}.
HELIX 191 219 {ECO:0000244|PDB:2VRW}.
HELIX 221 224 {ECO:0000244|PDB:2VRW}.
TURN 225 227 {ECO:0000244|PDB:2VRW}.
HELIX 230 237 {ECO:0000244|PDB:2VRW}.
HELIX 240 259 {ECO:0000244|PDB:2VRW}.
HELIX 261 263 {ECO:0000244|PDB:2VRW}.
HELIX 266 273 {ECO:0000244|PDB:2VRW}.
HELIX 276 278 {ECO:0000244|PDB:2VRW}.
HELIX 279 300 {ECO:0000244|PDB:2VRW}.
HELIX 302 316 {ECO:0000244|PDB:2VRW}.
HELIX 322 325 {ECO:0000244|PDB:2VRW}.
HELIX 328 333 {ECO:0000244|PDB:2VRW}.
HELIX 336 346 {ECO:0000244|PDB:2VRW}.
HELIX 350 389 {ECO:0000244|PDB:2VRW}.
STRAND 390 392 {ECO:0000244|PDB:2VRW}.
HELIX 397 400 {ECO:0000244|PDB:2VRW}.
STRAND 402 412 {ECO:0000244|PDB:2VRW}.
STRAND 420 437 {ECO:0000244|PDB:2VRW}.
STRAND 440 448 {ECO:0000244|PDB:2VRW}.
TURN 449 451 {ECO:0000244|PDB:2VRW}.
STRAND 452 455 {ECO:0000244|PDB:2VRW}.
STRAND 469 475 {ECO:0000244|PDB:2VRW}.
STRAND 481 488 {ECO:0000244|PDB:2VRW}.
HELIX 489 506 {ECO:0000244|PDB:2VRW}.
TURN 509 512 {ECO:0000244|PDB:2VRW}.
HELIX 513 515 {ECO:0000244|PDB:2VRW}.
STRAND 518 521 {ECO:0000244|PDB:2VRW}.
TURN 530 532 {ECO:0000244|PDB:2VRW}.
STRAND 538 541 {ECO:0000244|PDB:2VRW}.
STRAND 543 546 {ECO:0000244|PDB:2VRW}.
TURN 547 549 {ECO:0000244|PDB:2VRW}.
HELIX 555 560 {ECO:0000244|PDB:2VRW}.
TURN 585 587 {ECO:0000244|PDB:1K1Z}.
STRAND 596 599 {ECO:0000244|PDB:1GCQ}.
STRAND 603 607 {ECO:0000244|PDB:1GCQ}.
HELIX 610 612 {ECO:0000244|PDB:1GCQ}.
STRAND 624 629 {ECO:0000244|PDB:1GCQ}.
STRAND 635 641 {ECO:0000244|PDB:1GCQ}.
TURN 642 644 {ECO:0000244|PDB:1GCQ}.
STRAND 647 651 {ECO:0000244|PDB:1GCQ}.
HELIX 652 654 {ECO:0000244|PDB:1GCQ}.
STRAND 655 657 {ECO:0000244|PDB:1GCQ}.
STRAND 786 791 {ECO:0000244|PDB:2KBT}.
STRAND 796 800 {ECO:0000244|PDB:2KBT}.
STRAND 808 813 {ECO:0000244|PDB:2KBT}.
STRAND 817 825 {ECO:0000244|PDB:2KBT}.
STRAND 828 833 {ECO:0000244|PDB:2KBT}.
STRAND 836 841 {ECO:0000244|PDB:2KBT}.
SEQUENCE 845 AA; 98137 MW; 3666DCCD1C5229DA CRC64;
MELWRQCTHW LIQCRVLPPS HRVTWEGAQV CELAQALRDG VLLCQLLNNL LPQAINLREV
NLRPQMSQFL CLKNIRTFLS TCCEKFGLKR SELFEAFDLF DVQDFGKVIY TLSALSWTPI
AQNKGIMPFP TEDSALNDED IYSGLSDQID DTAEEDEDLY DCVENEEAEG DEIYEDLMRL
ESVPTPPKMT EYDKRCCCLR EIQQTEEKYT DTLGSIQQHF MKPLQRFLKP QDMETIFVNI
EELFSVHTHF LKELKDALAG PGATTLYQVF IKYKERFLVY GRYCSQVESA SKHLDQVATA
REDVQMKLEE CSQRANNGRF TLRDLLMVPM QRVLKYHLLL QELVKHTQDA TEKENLRLAL
DAMRDLAQCV NEVKRDNETL RQITNFQLSI ENLDQSLANY GRPKIDGELK ITSVERRSKT
DRYAFLLDKA LLICKRRGDS YDLKASVNLH SFQVRDDSSG ERDNKKWSHM FLLIEDQGAQ
GYELFFKTRE LKKKWMEQFE MAISNIYPEN ATANGHDFQM FSFEETTSCK ACQMLLRGTF
YQGYRCYRCR APAHKECLGR VPPCGRHGQD FAGTMKKDKL HRRAQDKKRN ELGLPKMEVF
QEYYGIPPPP GAFGPFLRLN PGDIVELTKA EAEHNWWEGR NTATNEVGWF PCNRVHPYVH
GPPQDLSVHL WYAGPMERAG AEGILTNRSD GTYLVRQRVK DTAEFAISIK YNVEVKHIKI
MTSEGLYRIT EKKAFRGLLE LVEFYQQNSL KDCFKSLDTT LQFPYKEPER RAISKPPAGS
TKYFGTAKAR YDFCARDRSE LSLKEGDIIK ILNKKGQQGW WRGEIYGRIG WFPSNYVEED
YSEYC


Related products :

Catalog number Product name Quantity
EIAAB45702 Mouse,Mus musculus,p95vav,Proto-oncogene vav,Vav,Vav1
EIAAB14724 Feline sarcoma_Fujinami avian sarcoma oncogene homolog,FES,FPS,Homo sapiens,Human,p93c-fes,Proto-oncogene c-Fes,Proto-oncogene c-Fps,Tyrosine-protein kinase Fes_Fps
EIAAB25170 Mos,Oocyte maturation factor mos,Proto-oncogene c-Mos,Proto-oncogene serine_threonine-protein kinase mos,Rat,Rattus norvegicus
EIAAB33701 cRaf,Homo sapiens,Human,Proto-oncogene c-RAF,RAF,RAF proto-oncogene serine_threonine-protein kinase,RAF1,Raf-1
EIAAB39852 Homo sapiens,Human,p60-Src,pp60c-src,Proto-oncogene c-Src,Proto-oncogene tyrosine-protein kinase Src,SRC,SRC1
EIAAB25166 Mos,Mouse,Mus musculus,Oocyte maturation factor mos,Proto-oncogene c-Mos,Proto-oncogene serine_threonine-protein kinase mos
EIAAB25167 Homo sapiens,Human,MOS,Oocyte maturation factor mos,Proto-oncogene c-Mos,Proto-oncogene serine_threonine-protein kinase mos
EIAAB33699 cRaf,Proto-oncogene c-RAF,Raf,RAF proto-oncogene serine_threonine-protein kinase,Raf1,Raf-1,Rat,Rattus norvegicus
EIAAB25168 MOS,Oocyte maturation factor mos,Pig,Proto-oncogene c-Mos,Proto-oncogene serine_threonine-protein kinase mos,Sus scrofa
EIAAB33700 Bos taurus,Bovine,cRaf,Proto-oncogene c-RAF,RAF proto-oncogene serine_threonine-protein kinase,RAF1,Raf-1
EIAAB35721 Homo sapiens,Human,Proto-oncogene c-Ros-1,Proto-oncogene tyrosine-protein kinase ROS,ROS1
EIAAB39851 Mouse,Mus musculus,Neuronal proto-oncogene tyrosine-protein kinase Src,p60-Src,pp60c-src,Proto-oncogene c-Src,Src
E1290m ELISA kit Mouse,Mus musculus,Myc,Myc proto-oncogene protein,Proto-oncogene c-Myc,Transcription factor p64 96T
EIAAB46397 Homo sapiens,Human,INT1,Proto-oncogene Int-1 homolog,Proto-oncogene Wnt-1,WNT1
EIAAB34305 Mouse,Mus musculus,Proto-oncogene c-Ret,Proto-oncogene tyrosine-protein kinase receptor Ret,Ret
E1290b ELISA kit Bos taurus,Bovine,MYC,Myc proto-oncogene protein,Proto-oncogene c-Myc,Transcription factor p64 96T
E1290b ELISA Bos taurus,Bovine,MYC,Myc proto-oncogene protein,Proto-oncogene c-Myc,Transcription factor p64 96T
EIAAB46412 Homo sapiens,Human,INT4,Proto-oncogene Int-4 homolog,Proto-oncogene Wnt-3,WNT3
EIAAB35722 Mouse,Mus musculus,Proto-oncogene c-Ros-1,Proto-oncogene tyrosine-protein kinase ROS,Ros1,Ros-1
E1290m ELISA Mouse,Mus musculus,Myc,Myc proto-oncogene protein,Proto-oncogene c-Myc,Transcription factor p64 96T
U1290m CLIA Mouse,Mus musculus,Myc,Myc proto-oncogene protein,Proto-oncogene c-Myc,Transcription factor p64 96T
E1290r ELISA kit Myc,Myc proto-oncogene protein,Proto-oncogene c-Myc,Rat,Rattus norvegicus,Transcription factor p64 96T
E1290r ELISA Myc,Myc proto-oncogene protein,Proto-oncogene c-Myc,Rat,Rattus norvegicus,Transcription factor p64 96T
U1290r CLIA Myc,Myc proto-oncogene protein,Proto-oncogene c-Myc,Rat,Rattus norvegicus,Transcription factor p64 96T
U1290b CLIA Bos taurus,Bovine,MYC,Myc proto-oncogene protein,Proto-oncogene c-Myc,Transcription factor p64 96T


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur