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Proto-oncogene tyrosine-protein kinase Src (EC 2.7.10.2) (Proto-oncogene c-Src) (pp60c-src) (p60-Src)

 SRC_RAT                 Reviewed;         536 AA.
Q9WUD9; G3V776; Q45QJ2; Q9JJ10;
30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
13-NOV-2013, sequence version 4.
22-NOV-2017, entry version 170.
RecName: Full=Proto-oncogene tyrosine-protein kinase Src;
EC=2.7.10.2 {ECO:0000269|PubMed:8849729};
AltName: Full=Proto-oncogene c-Src;
AltName: Full=pp60c-src;
Short=p60-Src;
Name=Src;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
STRAIN=Sprague-Dawley; TISSUE=Testis;
Stockand J.D., Al-Khalili O., Spier B.J., Eaton D.C.;
"Rattus norvegicus proto-oncogene encoding tyrosine-protein kinase
pp60-c-src.";
Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY, AND
INDUCTION.
STRAIN=Wistar; TISSUE=Temporal cortex;
PubMed=11249956; DOI=10.1016/S0028-3908(00)00185-4;
Linden A., Storvik M., Lakso M., Haapasalo A., Lee D., Witkin J.M.,
Sei Y., Castren E., Wong G.;
"Increased expression of neuronal Src and tyrosine phosphorylation of
NMDA receptors in rat brain after systemic treatment with MK-801.";
Neuropharmacology 40:469-481(2001).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Brown Norway;
PubMed=15057822; DOI=10.1038/nature02426;
Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T.,
Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A.,
Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M.,
Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K.,
Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S.,
Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J.,
Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y.,
Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A.,
Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J.,
D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R.,
Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A.,
Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E.,
Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E.,
Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D.,
Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M.,
Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O.,
Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O.,
Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H.,
Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S.,
Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J.,
Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E.,
Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F.,
Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K.,
Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S.,
Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M.,
Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M.,
Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A.,
Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S.,
Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G.,
Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H.,
Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R.,
Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M.,
Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H.,
Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S.,
Collins F.S.;
"Genome sequence of the Brown Norway rat yields insights into
mammalian evolution.";
Nature 428:493-521(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 7-529 (ISOFORM 1).
STRAIN=SHR, and Wistar Kyoto;
Jackson E.K., Zhu C.;
"Genetic similarity between spontaneously hypertensive rats and
Wistar-Kyoto rats in the coding regions of signal transduction
proteins.";
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[6]
CATALYTIC ACTIVITY, ENZYME REGULATION, INTERACTION WITH PTK2B/PYK2,
AND PHOSPHORYLATION AT TYR-419.
PubMed=8849729; DOI=10.1038/383547a0;
Dikic I., Tokiwa G., Lev S., Courtneidge S.A., Schlessinger J.;
"A role for Pyk2 and Src in linking G-protein-coupled receptors with
MAP kinase activation.";
Nature 383:547-550(1996).
[7]
INTERACTION WITH ARRB1.
PubMed=10995467; DOI=10.1073/pnas.190276697;
DeFea K.A., Vaughn Z.D., O'Bryan E.M., Nishijima D., Dery O.,
Bunnett N.W.;
"The proliferative and antiapoptotic effects of substance P are
facilitated by formation of a beta -arrestin-dependent scaffolding
complex.";
Proc. Natl. Acad. Sci. U.S.A. 97:11086-11091(2000).
[8]
INTERACTION WITH DDR2.
PubMed=11884411; DOI=10.1074/jbc.M201078200;
Ikeda K., Wang L.H., Torres R., Zhao H., Olaso E., Eng F.J.,
Labrador P., Klein R., Lovett D., Yancopoulos G.D., Friedman S.L.,
Lin H.C.;
"Discoidin domain receptor 2 interacts with Src and Shc following its
activation by type I collagen.";
J. Biol. Chem. 277:19206-19212(2002).
[9]
INTERACTION WITH DAB2.
PubMed=12473651; DOI=10.1074/jbc.M210628200;
Zhou J., Scholes J., Hsieh J.T.;
"Characterization of a novel negative regulator (DOC-2/DAB2) of c-Src
in normal prostatic epithelium and cancer.";
J. Biol. Chem. 278:6936-6941(2003).
[10]
FUNCTION, AND INTERACTION WITH DDR2.
PubMed=16186108; DOI=10.1074/jbc.M506921200;
Yang K., Kim J.H., Kim H.J., Park I.S., Kim I.Y., Yang B.S.;
"Tyrosine 740 phosphorylation of discoidin domain receptor 2 by Src
stimulates intramolecular autophosphorylation and Shc signaling
complex formation.";
J. Biol. Chem. 280:39058-39066(2005).
[11]
INTERACTION WITH CEACAM1.
PubMed=19948503; DOI=10.1083/jcb.200904150;
Mueller M.M., Klaile E., Vorontsova O., Singer B.B., Obrink B.;
"Homophilic adhesion and CEACAM1-S regulate dimerization of CEACAM1-L
and recruitment of SHP-2 and c-Src.";
J. Cell Biol. 187:569-581(2009).
[12]
PHOSPHORYLATION AT TYR-530, AND DEPHOSPHORYLATION AT TYR-530 BY PTPRJ.
PubMed=15735685; DOI=10.1038/sj.onc.1208510;
Pera I.L., Iuliano R., Florio T., Susini C., Trapasso F., Santoro M.,
Chiariotti L., Schettini G., Viglietto G., Fusco A.;
"The rat tyrosine phosphatase eta increases cell adhesion by
activating c-Src through dephosphorylation of its inhibitory
phosphotyrosine residue.";
Oncogene 24:3187-3195(2005).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
-!- FUNCTION: Non-receptor protein tyrosine kinase which is activated
following engagement of many different classes of cellular
receptors including immune response receptors, integrins and other
adhesion receptors, receptor protein tyrosine kinases, G protein-
coupled receptors as well as cytokine receptors. Participates in
signaling pathways that control a diverse spectrum of biological
activities including gene transcription, immune response, cell
adhesion, cell cycle progression, apoptosis, migration, and
transformation. Due to functional redundancy between members of
the SRC kinase family, identification of the specific role of each
SRC kinase is very difficult. SRC appears to be one of the primary
kinases activated following engagement of receptors and plays a
role in the activation of other protein tyrosine kinase (PTK)
families. Receptor clustering or dimerization leads to recruitment
of SRC to the receptor complexes where it phosphorylates the
tyrosine residues within the receptor cytoplasmic domains. Plays
an important role in the regulation of cytoskeletal organization
through phosphorylation of specific substrates such as AFAP1.
Phosphorylation of AFAP1 allows the SRC SH2 domain to bind AFAP1
and to localize to actin filaments. Cytoskeletal reorganization is
also controlled through the phosphorylation of cortactin (CTTN)
(Probable). When cells adhere via focal adhesions to the
extracellular matrix, signals are transmitted by integrins into
the cell resulting in tyrosine phosphorylation of a number of
focal adhesion proteins, including PTK2/FAK1 and paxillin (PXN)
(By similarity). In addition to phosphorylating focal adhesion
proteins, SRC is also active at the sites of cell-cell contact
adherens junctions and phosphorylates substrates such as beta-
catenin (CTNNB1), delta-catenin (CTNND1), and plakoglobin (JUP).
Another type of cell-cell junction, the gap junction, is also a
target for SRC, which phosphorylates connexin-43 (GJA1). SRC is
implicated in regulation of pre-mRNA-processing and phosphorylates
RNA-binding proteins such as KHDRBS1 (Probable). Also plays a role
in PDGF-mediated tyrosine phosphorylation of both STAT1 and STAT3,
leading to increased DNA binding activity of these transcription
factors (By similarity). Involved in the RAS pathway through
phosphorylation of RASA1 and RASGRF1. Plays a role in EGF-mediated
calcium-activated chloride channel activation (By similarity).
Required for epidermal growth factor receptor (EGFR)
internalization through phosphorylation of clathrin heavy chain
(CLTC and CLTCL1) at 'Tyr-1477'. Involved in beta-arrestin (ARRB1
and ARRB2) desensitization through phosphorylation and activation
of GRK2, leading to beta-arrestin phosphorylation and
internalization. Has a critical role in the stimulation of the
CDK20/MAPK3 mitogen-activated protein kinase cascade by epidermal
growth factor (Probable). Might be involved not only in mediating
the transduction of mitogenic signals at the level of the plasma
membrane but also in controlling progression through the cell
cycle via interaction with regulatory proteins in the nucleus.
Plays an important role in osteoclastic bone resorption in
conjunction with PTK2B/PYK2. Both the formation of a SRC-
PTK2B/PYK2 complex and SRC kinase activity are necessary for this
function. Recruited to activated integrins by PTK2B/PYK2, thereby
phosphorylating CBL, which in turn induces the activation and
recruitment of phosphatidylinositol 3-kinase to the cell membrane
in a signaling pathway that is critical for osteoclast function.
Promotes energy production in osteoclasts by activating
mitochondrial cytochrome C oxidase (By similarity). Phosphorylates
DDR2 on tyrosine residues, thereby promoting its subsequent
autophosphorylation (PubMed:16186108). Phosphorylates RUNX3 and
COX2 on tyrosine residues, TNK2 on 'Tyr-284' and CBL on 'Tyr-738'.
Enhances DDX58/RIG-I-elicited antiviral signaling. Phosphorylates
PDPK1 at 'Tyr-9', 'Tyr-373' and 'Tyr-376'. Phosphorylates BCAR1 at
'Tyr-226'. Phosphorylates CBLC at multiple tyrosine residues,
phosphorylation at 'Tyr-341' activates CBLC E3 activity. Involved
in anchorage-independent cell growth (By similarity). Required for
podosome formation (By similarity). {ECO:0000250|UniProtKB:P05480,
ECO:0000250|UniProtKB:P12931, ECO:0000269|PubMed:16186108,
ECO:0000305}.
-!- CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a
[protein]-L-tyrosine phosphate. {ECO:0000255|PROSITE-
ProRule:PRU10028, ECO:0000269|PubMed:8849729}.
-!- ENZYME REGULATION: Phosphorylation by CSK at Tyr-530 inhibits
kinase activity. Inhibitory phosphorylation at Tyr-530 is enhanced
by heme. Further phosphorylation by CDK1 partially reactivates
CSK-inactivated SRC and facilitates complete reactivation by
protein tyrosine phosphatase PTPRC. Integrin engagement stimulates
kinase activity. Phosphorylation by PTK2/FAK1 enhances kinase
activity. Butein and pseudosubstrate-based peptide inhibitors like
CIYKYYF act as inhibitors (By similarity). Phosphorylation at Tyr-
419 increases kinase activity. {ECO:0000250,
ECO:0000269|PubMed:8849729}.
-!- SUBUNIT: Interacts with DDEF1/ASAP1; via the SH3 domain (By
similarity). Interacts with CCPG1 (By similarity). Identified in a
complex containing FGFR4, NCAM1, CDH2, PLCG1, FRS2, SRC, SHC1,
GAP43 and CTTN (By similarity). Interacts with ERBB2, STAT1 and
PNN (By similarity). Interacts with CDCP1, PELP1, TGFB1I1 and
TOM1L2 (By similarity). Interacts with the cytoplasmic domain of
MUC1, phosphorylates it and increases binding of MUC1 with beta-
catenin (By similarity). Interacts with RALGPS1; via the SH3
domain (By similarity). Interacts with CAV2 (tyrosine
phosphorylated form) (By similarity). Interacts (via the SH3
domain and the protein kinase domain) with ARRB1; the interaction
is independent of the phosphorylation state of SRC C-terminus
(PubMed:10995467). Interacts with ARRB1 and ARRB2
(PubMed:10995467) (By similarity). Interacts with SRCIN1 (By
similarity). Interacts with NDFIP2 and more weakly with NDFIP1 (By
similarity). Interacts with PIK3CA and/or PIK3C2B, PTK2/FAK1 and
ESR1 (dimethylated on arginine) (PubMed:8849729). Interacts with
FASLG (By similarity). Interacts (via SH2 domain) with the 'Tyr-
402' phosphorylated form of PTK2B/PYK2 (PubMed:8849729). Interacts
(via SH2 domain) with FLT3 (tyrosine phosphorylated) (By
similarity). Interacts (via SH2 and SH3 domain) with TNK2 (By
similarity). Interacts (via protein kinase domain) with the
tyrosine phosphorylated form of RUNX3 (via runt domain) (By
similarity). Interacts with TRAF3 (via RING-type zinc finger
domain) (By similarity). Interacts with DDX58, MAVS and TBK1 (By
similarity). Interacts (via SH2 domain) with RACK1; the
interaction is enhanced by tyrosine phosphorylation of RACK1 and
inhibits SRC activity (By similarity). Interacts with EPHB1;
activates the MAPK/ERK cascade to regulate cell migration (By
similarity). Interacts with FCAMR (By similarity). Interacts with
PDGFRA (tyrosine phosphorylated) (By similarity). Interacts with
CSF1R (By similarity). Interacts with DDR1 (By similarity).
Interacts (via SH2 domain) with the 'Tyr-9' phosphorylated form of
PDPK1 (By similarity). Interacts with AMOTL2; this interaction
promotes the translocation of phosphorylated SRC to peripheral
cell-matrix adhesion sites (By similarity). Interacts with DDR2
and DAB2 (PubMed:11884411, PubMed:12473651, PubMed:16186108).
Interacts with TRAP1 (By similarity). Interacts with CBLC; the
interaction is enhanced when SRC is phosphorylated at Tyr-419 (By
similarity). Interacts with ARHGEF5 (By similarity). Interacts
(via cytoplasmic domain) with CEACAM1 (via SH2 domain); this
interaction is regulated by trans-homophilic cell adhesion
(PubMed:19948503). Interacts with MPP2 (By similarity). Interacts
with PRR7 (By similarity). Interacts (via kinase domain and to a
lesser extent the SH2 domain) directly with PDLIM4; this
interaction results in PTPN13-mediated dephosphorylation of this
protein leading to its inactivation (By similarity).
{ECO:0000250|UniProtKB:P05480, ECO:0000250|UniProtKB:P12931,
ECO:0000269|PubMed:10995467, ECO:0000269|PubMed:11884411,
ECO:0000269|PubMed:12473651, ECO:0000269|PubMed:16186108,
ECO:0000269|PubMed:19948503, ECO:0000269|PubMed:8849729}.
-!- INTERACTION:
P22002:Cacna1c; NbExp=4; IntAct=EBI-7784541, EBI-1185084;
P28648:Cd63; NbExp=2; IntAct=EBI-7784541, EBI-7784314;
O08617:Ptprr; NbExp=2; IntAct=EBI-7784541, EBI-8584374;
-!- SUBCELLULAR LOCATION: Cell membrane
{ECO:0000250|UniProtKB:P05480}. Mitochondrion inner membrane
{ECO:0000250|UniProtKB:P05480}. Nucleus
{ECO:0000250|UniProtKB:P05480}. Cytoplasm, cytoskeleton
{ECO:0000250|UniProtKB:P05480}. Cytoplasm, perinuclear region
{ECO:0000250|UniProtKB:P12931}. Note=Localizes to focal adhesion
sites following integrin engagement. Localization to focal
adhesion sites requires myristoylation and the SH3 domain.
Colocalizes with PDLIM4 at the perinuclear region, but not at
focal adhesions. {ECO:0000250|UniProtKB:P12931}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9WUD9-1; Sequence=Displayed;
Name=2; Synonyms=Neuronal Src;
IsoId=Q9WUD9-2; Sequence=VSP_053395;
-!- TISSUE SPECIFICITY: Isoform 2 is expressed in the brain with
highest expression in the pyramidal layers of the hippocampus and
the granular layer of the dentate gyrus and moderate expression in
cortical regions, with higher levels in the superficial layers
than in the deep layers. Isoform 2 may be neuron-specific. Isoform
1 is expressed at very low levels in the forebrain.
{ECO:0000269|PubMed:11249956}.
-!- INDUCTION: Isoform 2 is up-regulated by MK-801, an uncompetitive
N-methyl-d-aspartate (NMDA) receptor antagonist, mostly in the
superficial layers of the parietal, temporal, occipital and
frontal cortices. {ECO:0000269|PubMed:11249956}.
-!- PTM: Myristoylated at Gly-2, and this is essential for targeting
to membranes. {ECO:0000250}.
-!- PTM: Dephosphorylated at Tyr-530 by PTPRJ. Phosphorylated on Tyr-
530 by c-Src kinase (CSK). The phosphorylated form is termed
pp60c-src (By similarity). Dephosphorylated by PTPRJ at Tyr-419.
Normally maintained in an inactive conformation with the SH2
domain engaged with Tyr-530, the SH3 domain engaged with the SH2-
kinase linker, and Tyr-419 dephosphorylated. Dephosphorylation of
Tyr-530 as a result of protein tyrosine phosphatase (PTP) action
disrupts the intramolecular interaction between the SH2 domain and
Tyr-530, Tyr-419 can then become autophosphorylated, resulting in
SRX activation. Phosphorylation of Tyr-530 by CSK allows this
interaction to reform, resulting in SRC inactivation. CDK5-
mediated phosphorylation at Ser-75 targets SRC to ubiquitin-
dependent degradation and thus leads to cytoskeletal
reorganization. Phosphorylated by PTK2/FAK1; this enhances kinase
activity (By similarity). Phosphorylated by PTK2B/PYK2; this
enhances kinase activity. {ECO:0000250,
ECO:0000269|PubMed:15735685, ECO:0000269|PubMed:8849729}.
-!- PTM: S-nitrosylation is important for activation of its kinase
activity. {ECO:0000250}.
-!- PTM: Ubiquitinated in response to CDK5-mediated phosphorylation.
Ubiquitination mediated by CBLC requires SRC autophosphorylation
at Tyr-419 and may lead to lysosomal degradation (By similarity).
{ECO:0000250}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
kinase family. SRC subfamily. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
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EMBL; AF130457; AAD24180.1; -; mRNA.
EMBL; AF157016; AAF80335.1; -; mRNA.
EMBL; AABR06027223; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH474005; EDL96675.1; -; Genomic_DNA.
EMBL; CH474005; EDL96676.1; -; Genomic_DNA.
EMBL; CH474005; EDL96677.1; -; Genomic_DNA.
EMBL; CH474005; EDL96678.1; -; Genomic_DNA.
EMBL; CH474005; EDL96679.1; -; Genomic_DNA.
EMBL; DQ120509; AAZ23848.1; -; mRNA.
EMBL; DQ120510; AAZ23849.1; -; mRNA.
RefSeq; NP_114183.1; NM_031977.1. [Q9WUD9-2]
RefSeq; XP_008760609.1; XM_008762387.2. [Q9WUD9-2]
RefSeq; XP_008760610.1; XM_008762388.2. [Q9WUD9-2]
RefSeq; XP_017447554.1; XM_017592065.1. [Q9WUD9-2]
RefSeq; XP_017447555.1; XM_017592066.1. [Q9WUD9-2]
RefSeq; XP_017447556.1; XM_017592067.1. [Q9WUD9-2]
RefSeq; XP_017447557.1; XM_017592068.1. [Q9WUD9-2]
RefSeq; XP_017447558.1; XM_017592069.1. [Q9WUD9-2]
RefSeq; XP_017447559.1; XM_017592070.1. [Q9WUD9-2]
RefSeq; XP_017447560.1; XM_017592071.1. [Q9WUD9-2]
RefSeq; XP_017447561.1; XM_017592072.1. [Q9WUD9-1]
UniGene; Rn.112600; -.
SMR; Q9WUD9; -.
BioGrid; 249840; 11.
CORUM; Q9WUD9; -.
DIP; DIP-42731N; -.
ELM; Q9WUD9; -.
IntAct; Q9WUD9; 10.
MINT; MINT-1488989; -.
STRING; 10116.ENSRNOP00000012739; -.
BindingDB; Q9WUD9; -.
ChEMBL; CHEMBL3014; -.
iPTMnet; Q9WUD9; -.
PhosphoSitePlus; Q9WUD9; -.
PaxDb; Q9WUD9; -.
PeptideAtlas; Q9WUD9; -.
PRIDE; Q9WUD9; -.
Ensembl; ENSRNOT00000012739; ENSRNOP00000012739; ENSRNOG00000009495. [Q9WUD9-1]
Ensembl; ENSRNOT00000080516; ENSRNOP00000071837; ENSRNOG00000009495. [Q9WUD9-2]
GeneID; 83805; -.
KEGG; rno:83805; -.
UCSC; RGD:620795; rat. [Q9WUD9-1]
CTD; 6714; -.
RGD; 620795; Src.
eggNOG; KOG0197; Eukaryota.
eggNOG; COG0515; LUCA.
GeneTree; ENSGT00760000118938; -.
HOGENOM; HOG000233858; -.
HOVERGEN; HBG008761; -.
InParanoid; Q9WUD9; -.
KO; K05704; -.
OMA; CQCWRKD; -.
TreeFam; TF351634; -.
BRENDA; 2.7.10.2; 5301.
Reactome; R-RNO-1227986; Signaling by ERBB2.
Reactome; R-RNO-1295596; Spry regulation of FGF signaling.
Reactome; R-RNO-1433557; Signaling by SCF-KIT.
Reactome; R-RNO-1433559; Regulation of KIT signaling.
Reactome; R-RNO-177929; Signaling by EGFR.
Reactome; R-RNO-180292; GAB1 signalosome.
Reactome; R-RNO-186763; Downstream signal transduction.
Reactome; R-RNO-191647; c-src mediated regulation of Cx43 function and closure of gap junctions.
Reactome; R-RNO-2029481; FCGR activation.
Reactome; R-RNO-354192; Integrin alphaIIb beta3 signaling.
Reactome; R-RNO-354194; GRB2:SOS provides linkage to MAPK signaling for Integrins.
Reactome; R-RNO-372708; p130Cas linkage to MAPK signaling for integrins.
Reactome; R-RNO-389356; CD28 co-stimulation.
Reactome; R-RNO-389513; CTLA4 inhibitory signaling.
Reactome; R-RNO-3928662; EPHB-mediated forward signaling.
Reactome; R-RNO-3928663; EPHA-mediated growth cone collapse.
Reactome; R-RNO-3928664; Ephrin signaling.
Reactome; R-RNO-3928665; EPH-ephrin mediated repulsion of cells.
Reactome; R-RNO-418592; ADP signalling through P2Y purinoceptor 1.
Reactome; R-RNO-418885; DCC mediated attractive signaling.
Reactome; R-RNO-430116; GP1b-IX-V activation signalling.
Reactome; R-RNO-437239; Recycling pathway of L1.
Reactome; R-RNO-4420097; VEGFA-VEGFR2 Pathway.
Reactome; R-RNO-456926; Thrombin signalling through proteinase activated receptors (PARs).
Reactome; R-RNO-5218921; VEGFR2 mediated cell proliferation.
Reactome; R-RNO-5607764; CLEC7A (Dectin-1) signaling.
Reactome; R-RNO-5663220; RHO GTPases Activate Formins.
Reactome; R-RNO-5673000; RAF activation.
Reactome; R-RNO-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
Reactome; R-RNO-69231; Cyclin D associated events in G1.
Reactome; R-RNO-8853659; RET signaling.
Reactome; R-RNO-8874081; MET activates PTK2 signaling.
Reactome; R-RNO-8934593; Regulation of RUNX1 Expression and Activity.
Reactome; R-RNO-8934903; Receptor Mediated Mitophagy.
Reactome; R-RNO-8941858; Regulation of RUNX3 expression and activity.
PRO; PR:Q9WUD9; -.
Proteomes; UP000002494; Chromosome 3.
Bgee; ENSRNOG00000009495; -.
Genevisible; Q9WUD9; RN.
GO; GO:0005884; C:actin filament; ISO:RGD.
GO; GO:0005901; C:caveola; IDA:RGD.
GO; GO:0005737; C:cytoplasm; ISO:RGD.
GO; GO:0005829; C:cytosol; ISO:RGD.
GO; GO:0070062; C:extracellular exosome; ISO:RGD.
GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; IBA:GO_Central.
GO; GO:0005770; C:late endosome; ISO:RGD.
GO; GO:0005764; C:lysosome; ISO:RGD.
GO; GO:0016020; C:membrane; IDA:RGD.
GO; GO:0005743; C:mitochondrial inner membrane; ISS:UniProtKB.
GO; GO:0005739; C:mitochondrion; ISO:RGD.
GO; GO:0043005; C:neuron projection; IDA:RGD.
GO; GO:0005634; C:nucleus; ISO:RGD.
GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:RGD.
GO; GO:0005886; C:plasma membrane; IDA:RGD.
GO; GO:0002102; C:podosome; ISO:RGD.
GO; GO:0014069; C:postsynaptic density; IDA:RGD.
GO; GO:0032587; C:ruffle membrane; ISO:RGD.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0045296; F:cadherin binding; ISO:RGD.
GO; GO:0050839; F:cell adhesion molecule binding; IPI:RGD.
GO; GO:0071253; F:connexin binding; ISO:RGD.
GO; GO:0019899; F:enzyme binding; IPI:RGD.
GO; GO:0046875; F:ephrin receptor binding; ISO:RGD.
GO; GO:0030331; F:estrogen receptor binding; IPI:RGD.
GO; GO:0070851; F:growth factor receptor binding; ISO:RGD.
GO; GO:0020037; F:heme binding; ISS:UniProtKB.
GO; GO:0005158; F:insulin receptor binding; IPI:RGD.
GO; GO:0044325; F:ion channel binding; IPI:RGD.
GO; GO:0016301; F:kinase activity; ISO:RGD.
GO; GO:0019900; F:kinase binding; ISO:RGD.
GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IBA:GO_Central.
GO; GO:0051219; F:phosphoprotein binding; ISO:RGD.
GO; GO:0008022; F:protein C-terminus binding; IPI:RGD.
GO; GO:0032403; F:protein complex binding; IPI:RGD.
GO; GO:0019904; F:protein domain specific binding; ISO:RGD.
GO; GO:0004672; F:protein kinase activity; ISO:RGD.
GO; GO:0019901; F:protein kinase binding; IPI:RGD.
GO; GO:0005080; F:protein kinase C binding; IPI:RGD.
GO; GO:0004713; F:protein tyrosine kinase activity; IDA:RGD.
GO; GO:0005102; F:receptor binding; IPI:RGD.
GO; GO:0097110; F:scaffold protein binding; ISO:RGD.
GO; GO:0042169; F:SH2 domain binding; ISO:RGD.
GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:RGD.
GO; GO:0032148; P:activation of protein kinase B activity; IMP:UniProtKB.
GO; GO:0034332; P:adherens junction organization; IDA:RGD.
GO; GO:0086098; P:angiotensin-activated signaling pathway involved in heart process; ISO:RGD.
GO; GO:0045453; P:bone resorption; ISS:UniProtKB.
GO; GO:0060444; P:branching involved in mammary gland duct morphogenesis; ISO:RGD.
GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
GO; GO:0016477; P:cell migration; ISO:RGD.
GO; GO:0008283; P:cell proliferation; IDA:RGD.
GO; GO:0098609; P:cell-cell adhesion; IEP:RGD.
GO; GO:0071398; P:cellular response to fatty acid; IEP:RGD.
GO; GO:0071498; P:cellular response to fluid shear stress; ISO:RGD.
GO; GO:0071456; P:cellular response to hypoxia; IEP:RGD.
GO; GO:0032869; P:cellular response to insulin stimulus; IEP:RGD.
GO; GO:0071222; P:cellular response to lipopolysaccharide; IEP:RGD.
GO; GO:0071375; P:cellular response to peptide hormone stimulus; ISO:RGD.
GO; GO:0036120; P:cellular response to platelet-derived growth factor stimulus; ISO:RGD.
GO; GO:0071393; P:cellular response to progesterone stimulus; IMP:BHF-UCL.
GO; GO:0034614; P:cellular response to reactive oxygen species; ISO:RGD.
GO; GO:0071560; P:cellular response to transforming growth factor beta stimulus; ISO:RGD.
GO; GO:0007417; P:central nervous system development; IBA:GO_Central.
GO; GO:0007173; P:epidermal growth factor receptor signaling pathway; IEP:RGD.
GO; GO:0030900; P:forebrain development; ISO:RGD.
GO; GO:0045087; P:innate immune response; IBA:GO_Central.
GO; GO:0007229; P:integrin-mediated signaling pathway; ISO:RGD.
GO; GO:0030520; P:intracellular estrogen receptor signaling pathway; IBA:GO_Central.
GO; GO:0035556; P:intracellular signal transduction; ISO:RGD.
GO; GO:2000811; P:negative regulation of anoikis; ISO:RGD.
GO; GO:0043066; P:negative regulation of apoptotic process; ISO:RGD.
GO; GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; ISO:RGD.
GO; GO:2001237; P:negative regulation of extrinsic apoptotic signaling pathway; ISO:RGD.
GO; GO:0051895; P:negative regulation of focal adhesion assembly; IMP:BHF-UCL.
GO; GO:2001243; P:negative regulation of intrinsic apoptotic signaling pathway; ISO:RGD.
GO; GO:0051902; P:negative regulation of mitochondrial depolarization; ISO:RGD.
GO; GO:0032463; P:negative regulation of protein homooligomerization; ISO:RGD.
GO; GO:0051974; P:negative regulation of telomerase activity; ISO:RGD.
GO; GO:0032211; P:negative regulation of telomere maintenance via telomerase; ISO:RGD.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IMP:UniProtKB.
GO; GO:0048011; P:neurotrophin TRK receptor signaling pathway; IDA:RGD.
GO; GO:0048477; P:oogenesis; ISO:RGD.
GO; GO:0036035; P:osteoclast development; ISO:RGD.
GO; GO:0018105; P:peptidyl-serine phosphorylation; IMP:UniProtKB.
GO; GO:0038083; P:peptidyl-tyrosine autophosphorylation; IBA:GO_Central.
GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; ISO:RGD.
GO; GO:0016310; P:phosphorylation; ISO:RGD.
GO; GO:0043065; P:positive regulation of apoptotic process; IDA:RGD.
GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; ISO:RGD.
GO; GO:0045785; P:positive regulation of cell adhesion; IDA:RGD.
GO; GO:0045737; P:positive regulation of cyclin-dependent protein serine/threonine kinase activity; IMP:UniProtKB.
GO; GO:0050715; P:positive regulation of cytokine secretion; IMP:RGD.
GO; GO:2000573; P:positive regulation of DNA biosynthetic process; IMP:UniProtKB.
GO; GO:0010634; P:positive regulation of epithelial cell migration; ISO:RGD.
GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IMP:UniProtKB.
GO; GO:0010628; P:positive regulation of gene expression; IMP:RGD.
GO; GO:0010907; P:positive regulation of glucose metabolic process; IMP:RGD.
GO; GO:0046628; P:positive regulation of insulin receptor signaling pathway; IDA:RGD.
GO; GO:1902533; P:positive regulation of intracellular signal transduction; IMP:RGD.
GO; GO:2000394; P:positive regulation of lamellipodium morphogenesis; ISO:RGD.
GO; GO:0043406; P:positive regulation of MAP kinase activity; IMP:UniProtKB.
GO; GO:2000386; P:positive regulation of ovarian follicle development; IMP:RGD.
GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; ISO:RGD.
GO; GO:0043552; P:positive regulation of phosphatidylinositol 3-kinase activity; IMP:UniProtKB.
GO; GO:0010641; P:positive regulation of platelet-derived growth factor receptor signaling pathway; IEP:UniProtKB.
GO; GO:0071803; P:positive regulation of podosome assembly; ISO:RGD.
GO; GO:0031954; P:positive regulation of protein autophosphorylation; IMP:UniProtKB.
GO; GO:0051897; P:positive regulation of protein kinase B signaling; ISO:RGD.
GO; GO:1900182; P:positive regulation of protein localization to nucleus; ISO:RGD.
GO; GO:0010954; P:positive regulation of protein processing; ISO:RGD.
GO; GO:0071902; P:positive regulation of protein serine/threonine kinase activity; ISO:RGD.
GO; GO:0051222; P:positive regulation of protein transport; IMP:RGD.
GO; GO:0051057; P:positive regulation of small GTPase mediated signal transduction; ISO:RGD.
GO; GO:0014911; P:positive regulation of smooth muscle cell migration; IMP:RGD.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:UniProtKB.
GO; GO:0001545; P:primary ovarian follicle growth; IMP:RGD.
GO; GO:0050847; P:progesterone receptor signaling pathway; IMP:BHF-UCL.
GO; GO:0046777; P:protein autophosphorylation; IDA:UniProtKB.
GO; GO:0031648; P:protein destabilization; ISO:RGD.
GO; GO:0006468; P:protein phosphorylation; ISO:RGD.
GO; GO:2001286; P:regulation of caveolin-mediated endocytosis; ISO:RGD.
GO; GO:0060491; P:regulation of cell projection assembly; ISO:RGD.
GO; GO:0042127; P:regulation of cell proliferation; IBA:GO_Central.
GO; GO:0022407; P:regulation of cell-cell adhesion; ISO:RGD.
GO; GO:2000641; P:regulation of early endosome to late endosome transport; ISO:RGD.
GO; GO:0010632; P:regulation of epithelial cell migration; ISO:RGD.
GO; GO:0033146; P:regulation of intracellular estrogen receptor signaling pathway; ISO:RGD.
GO; GO:0071801; P:regulation of podosome assembly; IBA:GO_Central.
GO; GO:0043393; P:regulation of protein binding; ISO:RGD.
GO; GO:0010447; P:response to acidic pH; IEP:RGD.
GO; GO:0042493; P:response to drug; IEP:RGD.
GO; GO:0051602; P:response to electrical stimulus; IEP:RGD.
GO; GO:0070542; P:response to fatty acid; IEP:RGD.
GO; GO:0042542; P:response to hydrogen peroxide; IEP:RGD.
GO; GO:0070555; P:response to interleukin-1; ISO:RGD.
GO; GO:0009612; P:response to mechanical stimulus; IEP:RGD.
GO; GO:0051385; P:response to mineralocorticoid; IEP:RGD.
GO; GO:0031667; P:response to nutrient levels; IEP:RGD.
GO; GO:0009615; P:response to virus; IEP:RGD.
GO; GO:0043149; P:stress fiber assembly; ISO:RGD.
GO; GO:0034446; P:substrate adhesion-dependent cell spreading; ISO:RGD.
GO; GO:0045056; P:transcytosis; IDA:RGD.
GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; ISO:RGD.
GO; GO:0060065; P:uterus development; ISO:RGD.
Gene3D; 3.30.505.10; -; 1.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
InterPro; IPR000980; SH2.
InterPro; IPR036860; SH2_dom_sf.
InterPro; IPR036028; SH3-like_dom_sf.
InterPro; IPR001452; SH3_domain.
InterPro; IPR008266; Tyr_kinase_AS.
InterPro; IPR020635; Tyr_kinase_cat_dom.
Pfam; PF07714; Pkinase_Tyr; 1.
Pfam; PF00017; SH2; 1.
Pfam; PF00018; SH3_1; 1.
PRINTS; PR00401; SH2DOMAIN.
PRINTS; PR00452; SH3DOMAIN.
PRINTS; PR00109; TYRKINASE.
SMART; SM00252; SH2; 1.
SMART; SM00326; SH3; 1.
SMART; SM00219; TyrKc; 1.
SUPFAM; SSF50044; SSF50044; 1.
SUPFAM; SSF55550; SSF55550; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PROSITE; PS50001; SH2; 1.
PROSITE; PS50002; SH3; 1.
1: Evidence at protein level;
Alternative splicing; ATP-binding; Cell adhesion; Cell cycle;
Cell membrane; Complete proteome; Cytoplasm; Cytoskeleton; Immunity;
Kinase; Lipoprotein; Membrane; Mitochondrion;
Mitochondrion inner membrane; Myristate; Nucleotide-binding; Nucleus;
Phosphoprotein; Proto-oncogene; Reference proteome; SH2 domain;
SH3 domain; Transferase; Tyrosine-protein kinase; Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:P12931}.
CHAIN 2 536 Proto-oncogene tyrosine-protein kinase
Src.
/FTId=PRO_0000088143.
DOMAIN 84 145 SH3. {ECO:0000255|PROSITE-
ProRule:PRU00192}.
DOMAIN 151 248 SH2. {ECO:0000255|PROSITE-
ProRule:PRU00191}.
DOMAIN 270 523 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 276 284 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
ACT_SITE 389 389 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10028}.
BINDING 298 298 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 17 17 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 34 34 Phosphoserine.
{ECO:0000250|UniProtKB:P12931}.
MOD_RES 69 69 Phosphoserine.
{ECO:0000250|UniProtKB:P12931}.
MOD_RES 74 74 Phosphothreonine.
{ECO:0000250|UniProtKB:P12931}.
MOD_RES 75 75 Phosphoserine; by CDK5.
{ECO:0000250|UniProtKB:P12931}.
MOD_RES 187 187 Phosphotyrosine.
{ECO:0000250|UniProtKB:P05480}.
MOD_RES 419 419 Phosphotyrosine; by FAK2.
{ECO:0000269|PubMed:8849729}.
MOD_RES 420 420 Phosphothreonine; by autocatalysis.
{ECO:0000250}.
MOD_RES 439 439 Phosphotyrosine.
{ECO:0000250|UniProtKB:P12931}.
MOD_RES 511 511 Phosphothreonine.
{ECO:0000250|UniProtKB:P12931}.
MOD_RES 522 522 Phosphotyrosine.
{ECO:0000250|UniProtKB:P12931}.
MOD_RES 530 530 Phosphotyrosine; by CSK.
{ECO:0000250|UniProtKB:P12931}.
LIPID 2 2 N-myristoyl glycine. {ECO:0000250}.
VAR_SEQ 117 117 T -> TRKVDVR (in isoform 2).
{ECO:0000303|PubMed:11249956}.
/FTId=VSP_053395.
CONFLICT 143 143 S -> F (in Ref. 1; AAD24180 and 5;
AAZ23849/AAZ23848). {ECO:0000305}.
CONFLICT 381 381 E -> D (in Ref. 1; AAD24180 and 5;
AAZ23849/AAZ23848). {ECO:0000305}.
CONFLICT 528 528 P -> R (in Ref. 1; AAD24180 and 5;
AAZ23849/AAZ23848). {ECO:0000305}.
SEQUENCE 536 AA; 59973 MW; 453D1E904EC660A3 CRC64;
MGSNKSKPKD ASQRRRSLEP AENVHGAGGA FPASQTPSKP ASADGHRGPN AAFVPPAAAE
PKLFGGFNSS DTVTSPQRAG PLAGGVTTFV ALYDYESRTE TDLSFKKGER LQIVNNTEGD
WWLAHSLSTG QTGYIPSNYV APSDSIQAEE WYFGKITRRE SERLLLNAEN PRGTFLVRES
ETTKGAYCLS VSDFDNAKGL NVKHYKIRKL DSGGFYITSR TQFNSLQQLV AYYSKHADGL
CHRLTTVCPT SKPQTQGLAK DAWEIPRESL RLEVKLGQGC FGEVWMGTWN GTTRVAIKTL
KPGTMSPEAF LQEAQVMKKL RHEKLVQLYA VVSEEPIYIV TEYMNKGSLL DFLKGETGKY
LRLPQLVDMS AQIASGMAYV ERMNYVHRDL RAANILVGEN LVCKVADFGL ARLIEDNEYT
ARQGAKFPIK WTAPEAALYG RFTIKSDVWS FGILLTELTT KGRVPYPGMV NREVLDQVER
GYRMPCPPEC PESLHDLMCQ CWRKEPEERP TFEYLQAFLE DYFTSTEPQY QPGENL


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