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

 SRC_MOUSE               Reviewed;         541 AA.
P05480; Q2M4I4;
01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
27-JUL-2011, sequence version 4.
27-SEP-2017, entry version 195.
RecName: Full=Neuronal proto-oncogene tyrosine-protein kinase Src;
EC=2.7.10.2;
AltName: Full=Proto-oncogene c-Src;
AltName: Full=pp60c-src;
Short=p60-Src;
Name=Src;
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].
STRAIN=BALB/cJ;
PubMed=2440106; DOI=10.1126/science.2440106;
Martinez R., Mathey-Prevot B., Bernards A., Baltimore D.;
"Neuronal pp60c-src contains a six-amino acid insertion relative to
its non-neuronal counterpart.";
Science 237:411-415(1987).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=CAST/EiJ; TISSUE=Brain;
Farber C.R., Corva P.M., Medrano J.F.;
"Characterization of quantitative trait loci influencing growth and
adiposity using congenic mouse strains.";
Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases.
[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 GENOMIC DNA].
Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[5]
INTERACTION WITH CSF1R.
PubMed=7681396;
Courtneidge S.A., Dhand R., Pilat D., Twamley G.M., Waterfield M.D.,
Roussel M.F.;
"Activation of Src family kinases by colony stimulating factor-1, and
their association with its receptor.";
EMBO J. 12:943-950(1993).
[6]
INTERACTION WITH ERBB2.
PubMed=7542762;
Muthuswamy S.K., Muller W.J.;
"Direct and specific interaction of c-Src with Neu is involved in
signaling by the epidermal growth factor receptor.";
Oncogene 11:271-279(1995).
[7]
FUNCTION IN IL11-SIGNALING.
PubMed=8641341;
Fuhrer D.K., Yang Y.C.;
"Activation of Src-family protein tyrosine kinases and
phosphatidylinositol 3-kinase in 3T3-L1 mouse preadipocytes by
interleukin-11.";
Exp. Hematol. 24:195-203(1996).
[8]
ENZYME REGULATION.
PubMed=8910389; DOI=10.1074/jbc.271.44.27895;
Rodriguez-Fernandez J.L., Rozengurt E.;
"Bombesin, bradykinin, vasopressin, and phorbol esters rapidly and
transiently activate Src family tyrosine kinases in Swiss 3T3 cells.
Dissociation from tyrosine phosphorylation of p125 focal adhesion
kinase.";
J. Biol. Chem. 271:27895-27901(1996).
[9]
FUNCTION, AND INTERACTION WITH STAT1.
PubMed=9344858; DOI=10.1006/bbrc.1997.7493;
Cirri P., Chiarugi P., Marra F., Raugei G., Camici G., Manao G.,
Ramponi G.;
"c-Src activates both STAT1 and STAT3 in PDGF-stimulated NIH3T3
cells.";
Biochem. Biophys. Res. Commun. 239:493-497(1997).
[10]
INTERACTION WITH DDEF1/ASAP1.
PubMed=9819391; DOI=10.1128/MCB.18.12.7038;
Brown M.T., Andrade J., Radhakrishna H., Donaldson J.G., Cooper J.A.,
Randazzo P.A.;
"ASAP1, a phospholipid-dependent arf GTPase-activating protein that
associates with and is phosphorylated by Src.";
Mol. Cell. Biol. 18:7038-7051(1998).
[11]
IDENTIFICATION IN A COMPLEX WITH NCAM1; CDH2; PLCG1; FRS2; FGFR4;
SHC1; GAP43 AND CTTN.
PubMed=11433297; DOI=10.1038/35083041;
Cavallaro U., Niedermeyer J., Fuxa M., Christofori G.;
"N-CAM modulates tumour-cell adhesion to matrix by inducing FGF-
receptor signalling.";
Nat. Cell Biol. 3:650-657(2001).
[12]
INTERACTION WITH PDGFRA.
PubMed=14644164; DOI=10.1016/j.yexcr.2003.08.001;
Avrov K., Kazlauskas A.;
"The role of c-Src in platelet-derived growth factor alpha receptor
internalization.";
Exp. Cell Res. 291:426-434(2003).
[13]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=12615910; DOI=10.1083/jcb.200209098;
Miyazaki T., Neff L., Tanaka S., Horne W.C., Baron R.;
"Regulation of cytochrome c oxidase activity by c-Src in
osteoclasts.";
J. Cell Biol. 160:709-718(2003).
[14]
INTERACTION WITH EPHB1.
PubMed=12925710; DOI=10.1083/jcb.200302073;
Vindis C., Cerretti D.P., Daniel T.O., Huynh-Do U.;
"EphB1 recruits c-Src and p52Shc to activate MAPK/ERK and promote
chemotaxis.";
J. Cell Biol. 162:661-671(2003).
[15]
FUNCTION, AND INTERACTION WITH PTK2B/PYK2.
PubMed=14739300; DOI=10.1074/jbc.M311032200;
Miyazaki T., Sanjay A., Neff L., Tanaka S., Horne W.C., Baron R.;
"Src kinase activity is essential for osteoclast function.";
J. Biol. Chem. 279:17660-17666(2004).
[16]
INTERACTION WITH FLT3.
PubMed=16684964; DOI=10.1182/blood-2005-07-008896;
Heiss E., Masson K., Sundberg C., Pedersen M., Sun J., Bengtsson S.,
Ronnstrand L.;
"Identification of Y589 and Y599 in the juxtamembrane domain of Flt3
as ligand-induced autophosphorylation sites involved in binding of Src
family kinases and the protein tyrosine phosphatase SHP2.";
Blood 108:1542-1550(2006).
[17]
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).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-192, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain;
PubMed=18034455; DOI=10.1021/pr0701254;
Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
"Large-scale identification and evolution indexing of tyrosine
phosphorylation sites from murine brain.";
J. Proteome Res. 7:311-318(2008).
[19]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
Thibault P.;
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Immunity 30:143-154(2009).
[20]
INTERACTION WITH ARRB2.
PubMed=19122674; DOI=10.1038/nature07617;
Luan B., Zhao J., Wu H., Duan B., Shu G., Wang X., Li D., Jia W.,
Kang J., Pei G.;
"Deficiency of a beta-arrestin-2 signal complex contributes to insulin
resistance.";
Nature 457:1146-1149(2009).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17; SER-21 AND SER-74,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Heart, Kidney, Lung, Spleen, and Testis;
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).
[22]
INTERACTION WITH DDR1.
PubMed=20093046; DOI=10.1016/j.carpath.2009.12.006;
Lu K.K., Trcka D., Bendeck M.P.;
"Collagen stimulates discoidin domain receptor 1-mediated migration of
smooth muscle cells through Src.";
Cardiovasc. Pathol. 20:71-76(2011).
[23]
FUNCTION, INTERACTION WITH ARHGEF5, AND SUBCELLULAR LOCATION.
PubMed=21525037; DOI=10.1242/jcs.080291;
Kuroiwa M., Oneyama C., Nada S., Okada M.;
"The guanine nucleotide exchange factor Arhgef5 plays crucial roles in
Src-induced podosome formation.";
J. Cell Sci. 124:1726-1738(2011).
[24]
REVIEW ON FUNCTION.
PubMed=8672527; DOI=10.1016/0304-419X(96)00003-0;
Brown M.T., Cooper J.A.;
"Regulation, substrates and functions of src.";
Biochim. Biophys. Acta 1287:121-149(1996).
[25]
REVIEW ON FUNCTION.
PubMed=9442882; DOI=10.1146/annurev.cellbio.13.1.513;
Thomas S.M., Brugge J.S.;
"Cellular functions regulated by Src family kinases.";
Annu. Rev. Cell Dev. Biol. 13:513-609(1997).
[26]
REVIEW ON FUNCTION.
PubMed=11964124; DOI=10.1007/s00018-002-8438-2;
Ma Y.C., Huang X.Y.;
"Novel regulation and function of Src tyrosine kinase.";
Cell. Mol. Life Sci. 59:456-462(2002).
-!- 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).
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). 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. Also
plays a role in PDGF-mediated tyrosine phosphorylation of both
STAT1 and STAT3, leading to increased DNA binding activity of
these transcription factors. Involved in the RAS pathway through
phosphorylation of RASA1 and RASGRF1. Plays a role in EGF-mediated
calcium-activated chloride channel activation. 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. 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. Phosphorylates DDR2 on
tyrosine residues, thereby promoting its subsequent
autophosphorylation. Phosphorylates RUNX3 and COX2 on tyrosine
residues, TNK2 on 'Tyr-284' and CBL on 'Tyr-731'. Enhances
DDX58/RIG-I-elicited antiviral signaling. Phosphorylates PDPK1 at
'Tyr-9', 'Tyr-373' and 'Tyr-376'. Phosphorylates BCAR1 at 'Tyr-
132'. Phosphorylates CBLC at multiple tyrosine residues,
phosphorylation at 'Tyr-341' activates CBLC E3 activity. Required
for podosome formation (PubMed:21525037).
{ECO:0000269|PubMed:12615910, ECO:0000269|PubMed:14739300,
ECO:0000269|PubMed:21525037, ECO:0000269|PubMed:8641341,
ECO:0000269|PubMed:9344858}.
-!- CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a
[protein]-L-tyrosine phosphate. {ECO:0000255|PROSITE-
ProRule:PRU10028}.
-!- ENZYME REGULATION: Phosphorylation by CSK at Tyr-535 inhibits
kinase activity. Inhibitory phosphorylation at Tyr-535 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. Phosphorylation at Tyr-424 increases
kinase activity. {ECO:0000269|PubMed:8910389}.
-!- SUBUNIT: Interacts with CDCP1, PELP1, TGFB1I1 and TOM1L2.
Interacts with DDEF1/ASAP1 via its SH3 domain. Interacts with
CCPG1. Interacts with the cytoplasmic domain of MUC1,
phosphorylates it and increases binding of MUC1 with beta-catenin.
Interacts with RALGPS1 via its SH3 domain. Interacts with CAV2
(tyrosine phosphorylated form). Interacts (via the SH3 domain and
the protein kinase domain) with ARRB1; the interaction is
independent of the phosphorylation state of SRC C-terminus.
Interacts with FCAMR and PXN. Interacts with ARRB2. Interacts with
ARRB1. Interacts with SRCIN1. Interacts with SRCIN1. Interacts
with NDFIP2 and more weakly with NDFIP1. Interacts with PIK3CA
and/or PIK3C2B, PTK2/FAK1, ESR1 (dimethylated on arginine) and
FAK. Interacts (via SH2 and SH3 domain) with TNK2. Interacts (via
protein kinase domain) with the tyrosine phosphorylated form of
RUNX3 (via runt domain). Interacts with TRAF3 (via RING-type zinc
finger domain). Interacts with DDX58, MAVS and TBK1. Interacts
(via SH2 domain) with RACK1; the interaction is enhanced by
tyrosine phosphorylation of RACK1 and inhibits SRC activity.
Interacts (via SH2 domain) with the 'Tyr-402' phosphorylated form
of PTK2B/PYK2. Interacts (via SH2 domain) with FLT3 (tyrosine
phosphorylated). Identified in a complex containing FGFR4, NCAM1,
CDH2, PLCG1, FRS2, SRC, SHC1, GAP43 and CTTN. Interacts with
EPHB1; activates the MAPK/ERK cascade to regulate cell migration.
Interacts with ERBB2 and STAT1. Interacts with PDGFRA (tyrosine
phosphorylated). Interacts with CSF1R. Interacts (via SH2 domain)
with the 'Tyr-9' phosphorylated form of PDPK1. Interacts with
DDR2. Interacts with AMOTL2; this interaction regulates the
translocation of phosphorylated SRC to peripheral cell-matrix
adhesion sites. Interacts with DDR1 and DAB2. Interacts with
TRAP1. Interacts with CBLC; the interaction is enhanced when SRC
is phosphorylated at 'Tyr-424'. Interacts with ARHGEF5
(PubMed:21525037). Interacts (via cytoplasmic domain) with CEACAM1
(via SH2 domain); this interaction is regulated by trans-
homophilic cell adhesion (By similarity). Interacts with MPP2 (By
similarity). {ECO:0000250|UniProtKB:P12931,
ECO:0000250|UniProtKB:Q9WUD9, ECO:0000269|PubMed:11433297,
ECO:0000269|PubMed:12925710, ECO:0000269|PubMed:14644164,
ECO:0000269|PubMed:14739300, ECO:0000269|PubMed:16684964,
ECO:0000269|PubMed:17000758, ECO:0000269|PubMed:19122674,
ECO:0000269|PubMed:20093046, ECO:0000269|PubMed:21525037,
ECO:0000269|PubMed:7542762, ECO:0000269|PubMed:7681396,
ECO:0000269|PubMed:9344858, ECO:0000269|PubMed:9819391}.
-!- INTERACTION:
Q63767:Bcar1 (xeno); NbExp=2; IntAct=EBI-298680, EBI-1176801;
P07141:Csf1; NbExp=2; IntAct=EBI-298680, EBI-777188;
P31016:Dlg4 (xeno); NbExp=9; IntAct=EBI-298680, EBI-375655;
O70469:Dok2; NbExp=4; IntAct=EBI-298680, EBI-2642743;
Q8T4F7:ena (xeno); NbExp=2; IntAct=EBI-298680, EBI-466810;
P54763:Ephb2; NbExp=3; IntAct=EBI-298680, EBI-537711;
Q00959:Grin2a (xeno); NbExp=5; IntAct=EBI-298680, EBI-630970;
P19367:HK1 (xeno); NbExp=8; IntAct=EBI-298680, EBI-713162;
P52789:HK2 (xeno); NbExp=4; IntAct=EBI-298680, EBI-741469;
P05106:ITGB3 (xeno); NbExp=5; IntAct=EBI-298680, EBI-702847;
Q9WU78:Pdcd6ip; NbExp=2; IntAct=EBI-298680, EBI-641897;
Q05397:PTK2 (xeno); NbExp=5; IntAct=EBI-298680, EBI-702142;
P18052:Ptpra; NbExp=2; IntAct=EBI-298680, EBI-6597520;
P49023:PXN (xeno); NbExp=2; IntAct=EBI-298680, EBI-702209;
Q01973:ROR1 (xeno); NbExp=3; IntAct=EBI-298680, EBI-6082337;
P70315:Was; NbExp=2; IntAct=EBI-298680, EBI-644195;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12615910,
ECO:0000269|PubMed:21525037}. Mitochondrion inner membrane
{ECO:0000269|PubMed:12615910}. Nucleus
{ECO:0000269|PubMed:12615910}. Cytoplasm, cytoskeleton
{ECO:0000269|PubMed:12615910}. Note=Localizes to focal adhesion
sites after integrin engagement. Localization to focal adhesion
sites requires myristoylation and the SH3 domain.
-!- PTM: Myristoylated at Gly-2, and this is essential for targeting
to membranes. {ECO:0000250}.
-!- PTM: Dephosphorylated at Tyr-535 by PTPRJ (By similarity).
Phosphorylated on Tyr-535 by c-Src kinase (CSK). The
phosphorylated form is termed pp60c-src. Dephosphorylated by PTPRJ
at Tyr-424. Normally maintained in an inactive conformation with
the SH2 domain engaged with Tyr-535, the SH3 domain engaged with
the SH2-kinase linker, and Tyr-424 dephosphorylated.
Dephosphorylation of Tyr-535 as a result of protein tyrosine
phosphatase (PTP) action disrupts the intramolecular interaction
between the SH2 domain and Tyr-535, Tyr-424 can then become
autophosphorylated, resulting in SRC activation. Phosphorylation
of Tyr-535 by CSK allows this interaction to reform, resulting in
SRC inactivation. CDK5-mediated phosphorylation at Ser-74 targets
SRC to ubiquitin-dependent degradation and thus leads to
cytoskeletal reorganization. Phosphorylated by PTK2/FAK1; this
enhances kinase activity. Phosphorylated by PTK2B/PYK2; this
enhances kinase activity (By similarity). {ECO:0000250}.
-!- 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-424 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; M17031; AAA40135.1; -; mRNA.
EMBL; AY902331; AAX90616.1; -; Genomic_DNA.
EMBL; AL672259; CAM16141.1; -; Genomic_DNA.
EMBL; CH466551; EDL06234.1; -; Genomic_DNA.
CCDS; CCDS38305.1; -.
PIR; A43610; A43610.
RefSeq; NP_001020566.1; NM_001025395.2.
RefSeq; NP_033297.2; NM_009271.3.
UniGene; Mm.22845; -.
ProteinModelPortal; P05480; -.
SMR; P05480; -.
BioGrid; 203491; 42.
CORUM; P05480; -.
DIP; DIP-31071N; -.
IntAct; P05480; 32.
MINT; MINT-85032; -.
STRING; 10090.ENSMUSP00000090237; -.
BindingDB; P05480; -.
ChEMBL; CHEMBL3074; -.
iPTMnet; P05480; -.
PhosphoSitePlus; P05480; -.
MaxQB; P05480; -.
PaxDb; P05480; -.
PeptideAtlas; P05480; -.
PRIDE; P05480; -.
Ensembl; ENSMUST00000092576; ENSMUSP00000090237; ENSMUSG00000027646.
Ensembl; ENSMUST00000109529; ENSMUSP00000105155; ENSMUSG00000027646.
GeneID; 20779; -.
KEGG; mmu:20779; -.
UCSC; uc008npa.1; mouse.
CTD; 6714; -.
MGI; MGI:98397; Src.
eggNOG; KOG0197; Eukaryota.
eggNOG; COG0515; LUCA.
GeneTree; ENSGT00760000118938; -.
HOGENOM; HOG000233858; -.
HOVERGEN; HBG008761; -.
InParanoid; P05480; -.
KO; K05704; -.
OMA; CQCWRKD; -.
OrthoDB; EOG091G0D46; -.
BRENDA; 2.7.10.2; 3474.
Reactome; R-MMU-1227986; Signaling by ERBB2.
Reactome; R-MMU-1295596; Spry regulation of FGF signaling.
Reactome; R-MMU-1433557; Signaling by SCF-KIT.
Reactome; R-MMU-1433559; Regulation of KIT signaling.
Reactome; R-MMU-177929; Signaling by EGFR.
Reactome; R-MMU-180292; GAB1 signalosome.
Reactome; R-MMU-186763; Downstream signal transduction.
Reactome; R-MMU-191647; c-src mediated regulation of Cx43 function and closure of gap junctions.
Reactome; R-MMU-2029481; FCGR activation.
Reactome; R-MMU-354192; Integrin alphaIIb beta3 signaling.
Reactome; R-MMU-354194; GRB2:SOS provides linkage to MAPK signaling for Integrins.
Reactome; R-MMU-372708; p130Cas linkage to MAPK signaling for integrins.
Reactome; R-MMU-375165; NCAM signaling for neurite out-growth.
Reactome; R-MMU-389356; CD28 co-stimulation.
Reactome; R-MMU-389513; CTLA4 inhibitory signaling.
Reactome; R-MMU-3928662; EPHB-mediated forward signaling.
Reactome; R-MMU-3928663; EPHA-mediated growth cone collapse.
Reactome; R-MMU-3928664; Ephrin signaling.
Reactome; R-MMU-3928665; EPH-ephrin mediated repulsion of cells.
Reactome; R-MMU-418592; ADP signalling through P2Y purinoceptor 1.
Reactome; R-MMU-418885; DCC mediated attractive signaling.
Reactome; R-MMU-418886; Netrin mediated repulsion signals.
Reactome; R-MMU-430116; GP1b-IX-V activation signalling.
Reactome; R-MMU-437239; Recycling pathway of L1.
Reactome; R-MMU-4420097; VEGFA-VEGFR2 Pathway.
Reactome; R-MMU-456926; Thrombin signalling through proteinase activated receptors (PARs).
Reactome; R-MMU-5218921; VEGFR2 mediated cell proliferation.
Reactome; R-MMU-5607764; CLEC7A (Dectin-1) signaling.
Reactome; R-MMU-5663220; RHO GTPases Activate Formins.
Reactome; R-MMU-5673000; RAF activation.
Reactome; R-MMU-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
Reactome; R-MMU-69231; Cyclin D associated events in G1.
Reactome; R-MMU-8853659; RET signaling.
Reactome; R-MMU-8874081; MET activates PTK2 signaling.
Reactome; R-MMU-8934593; Regulation of RUNX1 Expression and Activity.
Reactome; R-MMU-8934903; Receptor Mediated Mitophagy.
Reactome; R-MMU-8941858; Regulation of RUNX3 expression and activity.
ChiTaRS; Src; mouse.
PRO; PR:P05480; -.
Proteomes; UP000000589; Chromosome 2.
Bgee; ENSMUSG00000027646; -.
CleanEx; MM_SRC; -.
ExpressionAtlas; P05480; baseline and differential.
Genevisible; P05480; MM.
GO; GO:0005884; C:actin filament; IDA:MGI.
GO; GO:0005901; C:caveola; IDA:BHF-UCL.
GO; GO:0005737; C:cytoplasm; IDA:CAFA.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0070062; C:extracellular exosome; ISO:MGI.
GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; IBA:GO_Central.
GO; GO:0005770; C:late endosome; ISO:MGI.
GO; GO:0005764; C:lysosome; ISO:MGI.
GO; GO:0005743; C:mitochondrial inner membrane; ISO:MGI.
GO; GO:0005739; C:mitochondrion; ISO:MGI.
GO; GO:0043005; C:neuron projection; IEA:Ensembl.
GO; GO:0005634; C:nucleus; IDA:MGI.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:MGI.
GO; GO:0005886; C:plasma membrane; IDA:MGI.
GO; GO:0002102; C:podosome; IDA:MGI.
GO; GO:0014069; C:postsynaptic density of dendrite; IEA:Ensembl.
GO; GO:0032587; C:ruffle membrane; IDA:MGI.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0045296; F:cadherin binding; ISO:MGI.
GO; GO:0071253; F:connexin binding; IPI:CAFA.
GO; GO:0019899; F:enzyme binding; ISO:MGI.
GO; GO:0046875; F:ephrin receptor binding; IPI:UniProtKB.
GO; GO:0030331; F:estrogen receptor binding; IEA:Ensembl.
GO; GO:0070851; F:growth factor receptor binding; ISO:MGI.
GO; GO:0020037; F:heme binding; ISS:UniProtKB.
GO; GO:0051427; F:hormone receptor binding; IBA:GO_Central.
GO; GO:0005158; F:insulin receptor binding; IEA:Ensembl.
GO; GO:0044325; F:ion channel binding; ISO:MGI.
GO; GO:0016301; F:kinase activity; IMP:MGI.
GO; GO:0019900; F:kinase binding; ISO:MGI.
GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IBA:GO_Central.
GO; GO:0051219; F:phosphoprotein binding; ISO:MGI.
GO; GO:0008022; F:protein C-terminus binding; ISO:MGI.
GO; GO:0019904; F:protein domain specific binding; IPI:MGI.
GO; GO:0004672; F:protein kinase activity; IDA:MGI.
GO; GO:0005080; F:protein kinase C binding; IEA:Ensembl.
GO; GO:0004713; F:protein tyrosine kinase activity; IMP:BHF-UCL.
GO; GO:0005102; F:receptor binding; ISO:MGI.
GO; GO:0097110; F:scaffold protein binding; IPI:BHF-UCL.
GO; GO:0042169; F:SH2 domain binding; ISO:MGI.
GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:Ensembl.
GO; GO:0032148; P:activation of protein kinase B activity; IEA:Ensembl.
GO; GO:0034332; P:adherens junction organization; IEA:Ensembl.
GO; GO:0086098; P:angiotensin-activated signaling pathway involved in heart process; IGI:BHF-UCL.
GO; GO:0007411; P:axon guidance; TAS:Reactome.
GO; GO:0045453; P:bone resorption; IMP:UniProtKB.
GO; GO:0060444; P:branching involved in mammary gland duct morphogenesis; IMP:MGI.
GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
GO; GO:0016477; P:cell migration; IMP:MGI.
GO; GO:0008283; P:cell proliferation; IEA:Ensembl.
GO; GO:0071398; P:cellular response to fatty acid; IEA:Ensembl.
GO; GO:0071498; P:cellular response to fluid shear stress; IMP:MGI.
GO; GO:0071456; P:cellular response to hypoxia; IEA:Ensembl.
GO; GO:0032869; P:cellular response to insulin stimulus; IEA:Ensembl.
GO; GO:0071222; P:cellular response to lipopolysaccharide; IEA:Ensembl.
GO; GO:0071375; P:cellular response to peptide hormone stimulus; IGI:BHF-UCL.
GO; GO:0036120; P:cellular response to platelet-derived growth factor stimulus; IDA:MGI.
GO; GO:0071393; P:cellular response to progesterone stimulus; IEA:Ensembl.
GO; GO:0034614; P:cellular response to reactive oxygen species; IDA:MGI.
GO; GO:0071560; P:cellular response to transforming growth factor beta stimulus; IGI:MGI.
GO; GO:0048013; P:ephrin receptor signaling pathway; TAS:Reactome.
GO; GO:0007173; P:epidermal growth factor receptor signaling pathway; IBA:GO_Central.
GO; GO:0030900; P:forebrain development; IGI:MGI.
GO; GO:0045087; P:innate immune response; IBA:GO_Central.
GO; GO:0007229; P:integrin-mediated signaling pathway; ISO:MGI.
GO; GO:0035556; P:intracellular signal transduction; IGI:MGI.
GO; GO:2000811; P:negative regulation of anoikis; ISO:MGI.
GO; GO:0043066; P:negative regulation of apoptotic process; ISO:MGI.
GO; GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; ISO:MGI.
GO; GO:2001237; P:negative regulation of extrinsic apoptotic signaling pathway; ISO:MGI.
GO; GO:0051895; P:negative regulation of focal adhesion assembly; IEA:Ensembl.
GO; GO:2001243; P:negative regulation of intrinsic apoptotic signaling pathway; ISO:MGI.
GO; GO:0051902; P:negative regulation of mitochondrial depolarization; ISO:MGI.
GO; GO:0032463; P:negative regulation of protein homooligomerization; ISO:MGI.
GO; GO:0051974; P:negative regulation of telomerase activity; ISO:MGI.
GO; GO:0032211; P:negative regulation of telomere maintenance via telomerase; ISO:MGI.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IEA:Ensembl.
GO; GO:0048011; P:neurotrophin TRK receptor signaling pathway; IEA:Ensembl.
GO; GO:0048477; P:oogenesis; IMP:MGI.
GO; GO:0036035; P:osteoclast development; IGI:MGI.
GO; GO:0018105; P:peptidyl-serine phosphorylation; IEA:Ensembl.
GO; GO:0038083; P:peptidyl-tyrosine autophosphorylation; IBA:GO_Central.
GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; IDA:MGI.
GO; GO:0016310; P:phosphorylation; IMP:BHF-UCL.
GO; GO:0048008; P:platelet-derived growth factor receptor signaling pathway; IBA:GO_Central.
GO; GO:0043065; P:positive regulation of apoptotic process; IEA:Ensembl.
GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; IGI:MGI.
GO; GO:0045785; P:positive regulation of cell adhesion; IEA:Ensembl.
GO; GO:0045737; P:positive regulation of cyclin-dependent protein serine/threonine kinase activity; IEA:Ensembl.
GO; GO:0050715; P:positive regulation of cytokine secretion; IEA:Ensembl.
GO; GO:2000573; P:positive regulation of DNA biosynthetic process; IEA:Ensembl.
GO; GO:0010634; P:positive regulation of epithelial cell migration; ISO:MGI.
GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IMP:BHF-UCL.
GO; GO:0010907; P:positive regulation of glucose metabolic process; IEA:Ensembl.
GO; GO:0046628; P:positive regulation of insulin receptor signaling pathway; IEA:Ensembl.
GO; GO:2000394; P:positive regulation of lamellipodium morphogenesis; ISO:MGI.
GO; GO:0043406; P:positive regulation of MAP kinase activity; IEA:Ensembl.
GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IGI:MGI.
GO; GO:0043552; P:positive regulation of phosphatidylinositol 3-kinase activity; IEA:Ensembl.
GO; GO:0010641; P:positive regulation of platelet-derived growth factor receptor signaling pathway; IEA:Ensembl.
GO; GO:0071803; P:positive regulation of podosome assembly; IDA:MGI.
GO; GO:0031954; P:positive regulation of protein autophosphorylation; IEA:Ensembl.
GO; GO:0051897; P:positive regulation of protein kinase B signaling; ISO:MGI.
GO; GO:1900182; P:positive regulation of protein localization to nucleus; IGI:MGI.
GO; GO:0010954; P:positive regulation of protein processing; IGI:MGI.
GO; GO:0071902; P:positive regulation of protein serine/threonine kinase activity; ISO:MGI.
GO; GO:0051057; P:positive regulation of small GTPase mediated signal transduction; ISO:MGI.
GO; GO:0014911; P:positive regulation of smooth muscle cell migration; IEA:Ensembl.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IEA:Ensembl.
GO; GO:0050847; P:progesterone receptor signaling pathway; IBA:GO_Central.
GO; GO:0046777; P:protein autophosphorylation; ISO:MGI.
GO; GO:0031648; P:protein destabilization; IMP:CACAO.
GO; GO:0006468; P:protein phosphorylation; IDA:MGI.
GO; GO:2001286; P:regulation of caveolin-mediated endocytosis; ISO:MGI.
GO; GO:0051726; P:regulation of cell cycle; IBA:GO_Central.
GO; GO:0060491; P:regulation of cell projection assembly; IGI:MGI.
GO; GO:0042127; P:regulation of cell proliferation; IBA:GO_Central.
GO; GO:0022407; P:regulation of cell-cell adhesion; ISO:MGI.
GO; GO:2000641; P:regulation of early endosome to late endosome transport; ISO:MGI.
GO; GO:0010632; P:regulation of epithelial cell migration; ISO:MGI.
GO; GO:0033146; P:regulation of intracellular estrogen receptor signaling pathway; IMP:MGI.
GO; GO:0043393; P:regulation of protein binding; IDA:MGI.
GO; GO:0010447; P:response to acidic pH; IEA:Ensembl.
GO; GO:0042493; P:response to drug; IEA:Ensembl.
GO; GO:0051602; P:response to electrical stimulus; IEA:Ensembl.
GO; GO:0042542; P:response to hydrogen peroxide; IEA:Ensembl.
GO; GO:0070555; P:response to interleukin-1; ISO:MGI.
GO; GO:0009612; P:response to mechanical stimulus; IEA:Ensembl.
GO; GO:0051385; P:response to mineralocorticoid; IEA:Ensembl.
GO; GO:0031667; P:response to nutrient levels; IEA:Ensembl.
GO; GO:0009615; P:response to virus; IEA:Ensembl.
GO; GO:0016337; P:single organismal cell-cell adhesion; IEA:Ensembl.
GO; GO:0043149; P:stress fiber assembly; ISO:MGI.
GO; GO:0034446; P:substrate adhesion-dependent cell spreading; IDA:MGI.
GO; GO:0045056; P:transcytosis; IEA:Ensembl.
GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; ISO:MGI.
GO; GO:0060065; P:uterus development; IMP:MGI.
GO; GO:0048010; P:vascular endothelial growth factor receptor signaling pathway; TAS:Reactome.
Gene3D; 3.30.505.10; -; 1.
InterPro; IPR011009; Kinase-like_dom.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
InterPro; IPR000980; SH2.
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;
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 2 541 Neuronal proto-oncogene tyrosine-protein
kinase Src.
/FTId=PRO_0000088142.
DOMAIN 83 150 SH3. {ECO:0000255|PROSITE-
ProRule:PRU00192}.
DOMAIN 156 253 SH2. {ECO:0000255|PROSITE-
ProRule:PRU00191}.
DOMAIN 275 528 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 281 289 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
ACT_SITE 394 394 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10028}.
BINDING 303 303 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 17 17 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 21 21 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 34 34 Phosphoserine.
{ECO:0000250|UniProtKB:P12931}.
MOD_RES 68 68 Phosphoserine.
{ECO:0000250|UniProtKB:P12931}.
MOD_RES 73 73 Phosphothreonine.
{ECO:0000250|UniProtKB:P12931}.
MOD_RES 74 74 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 192 192 Phosphotyrosine.
{ECO:0000244|PubMed:18034455}.
MOD_RES 424 424 Phosphotyrosine; by autocatalysis.
{ECO:0000250|UniProtKB:P12931}.
MOD_RES 424 424 Phosphotyrosine; by FAK2. {ECO:0000250}.
MOD_RES 444 444 Phosphotyrosine.
{ECO:0000250|UniProtKB:P12931}.
MOD_RES 516 516 Phosphothreonine.
{ECO:0000250|UniProtKB:P12931}.
MOD_RES 527 527 Phosphotyrosine.
{ECO:0000250|UniProtKB:P12931}.
MOD_RES 535 535 Phosphotyrosine; by CSK.
{ECO:0000250|UniProtKB:P12931}.
LIPID 2 2 N-myristoyl glycine. {ECO:0000250}.
CONFLICT 80 80 P -> A (in Ref. 1; AAA40135).
{ECO:0000305}.
SEQUENCE 541 AA; 60645 MW; 0534AF027783BCCF CRC64;
MGSNKSKPKD ASQRRRSLEP SENVHGAGGA FPASQTPSKP ASADGHRGPS AAFVPPAAEP
KLFGGFNSSD TVTSPQRAGP LAGGVTTFVA LYDYESRTET DLSFKKGERL QIVNNTRKVD
VREGDWWLAH SLSTGQTGYI PSNYVAPSDS IQAEEWYFGK ITRRESERLL LNAENPRGTF
LVRESETTKG AYCLSVSDFD NAKGLNVKHY KIRKLDSGGF YITSRTQFNS LQQLVAYYSK
HADGLCHRLT TVCPTSKPQT QGLAKDAWEI PRESLRLEVK LGQGCFGEVW MGTWNGTTRV
AIKTLKPGTM SPEAFLQEAQ VMKKLRHEKL VQLYAVVSEE PIYIVTEYMN KGSLLDFLKG
ETGKYLRLPQ LVDMSAQIAS GMAYVERMNY VHRDLRAANI LVGENLVCKV ADFGLARLIE
DNEYTARQGA KFPIKWTAPE AALYGRFTIK SDVWSFGILL TELTTKGRVP YPGMVNREVL
DQVERGYRMP CPPECPESLH DLMCQCWRKE PEERPTFEYL QAFLEDYFTS TEPQYQPGEN
L


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