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

 SRC_CHICK               Reviewed;         533 AA.
P00523; Q90992; Q90993; Q91343; Q91345; Q92013; Q98915;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 4.
22-NOV-2017, entry version 204.
RecName: Full=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;
Gallus gallus (Chicken).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes;
Phasianidae; Phasianinae; Gallus.
NCBI_TaxID=9031;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=6299580; DOI=10.1016/0092-8674(83)90073-9;
Takeya T., Hanafusa H.;
"Structure and sequence of the cellular gene homologous to the RSV src
gene and the mechanism for generating the transforming virus.";
Cell 32:881-890(1983).
[2]
ERRATUM, AND SEQUENCE REVISION TO 526.
Takeya T., Hanafusa H.;
Cell 34:319-319(1983).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
TISSUE=Pectoralis muscle;
PubMed=2115117; DOI=10.1128/MCB.10.8.4068;
Dorai T., Wang L.-H.;
"An alternative non-tyrosine protein kinase product of the c-src gene
in chicken skeletal muscle.";
Mol. Cell. Biol. 10:4068-4079(1990).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PHOSPHORYLATION AT TYR-416 AND
TYR-436.
PubMed=8856081; DOI=10.1111/j.1432-1033.1996.0756h.x;
Weijland A., Neubauer G., Courtneidge S.A., Mann M., Wierenga R.K.,
Superti-Furga G.;
"The purification and characterization of the catalytic domain of Src
expressed in Schizosaccharomyces pombe. Comparison of unphosphorylated
and tyrosine phosphorylated species.";
Eur. J. Biochem. 240:756-764(1996).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-7.
PubMed=6292480;
Takeya T., Hanafusa H.;
"DNA sequence of the viral and cellular src gene of chickens. II.
Comparison of the src genes of two strains of Avian sarcoma virus and
of the cellular homolog.";
J. Virol. 44:12-18(1982).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-19 AND 485-534 (ISOFORM 1).
PubMed=1712905; DOI=10.1128/MCB.11.8.4165;
Dorai T., Levy J.B., Kang L., Brugge J.S., Wang L.-H.;
"Analysis of cDNAs of the proto-oncogene c-src: heterogeneity in 5'
exons and possible mechanism for the genesis of the 3' end of v-src.";
Mol. Cell. Biol. 11:4165-4176(1991).
[7]
ATP-BINDING SITE.
PubMed=6431300; DOI=10.1038/310589a0;
Kamps M.P., Taylor S.S., Sefton B.M.;
"Direct evidence that oncogenic tyrosine kinases and cyclic AMP-
dependent protein kinase have homologous ATP-binding sites.";
Nature 310:589-592(1984).
[8]
PHOSPHORYLATION.
PubMed=2996780; DOI=10.1016/0092-8674(85)90281-8;
Gould K.L., Woodgett J.R., Cooper J.A., Buss J.E., Shalloway D.,
Hunter T.;
"Protein kinase C phosphorylates pp60src at a novel site.";
Cell 42:849-857(1985).
[9]
PHOSPHORYLATION AT TYR-416.
PubMed=6273838; DOI=10.1073/pnas.78.10.6013;
Smart J.E., Oppermann H., Czernilofsky A.P., Purchio A.F.,
Erikson R.L., Bishop J.M.;
"Characterization of sites for tyrosine phosphorylation in the
transforming protein of Rous sarcoma virus (pp60v-src) and its normal
cellular homologue (pp60c-src).";
Proc. Natl. Acad. Sci. U.S.A. 78:6013-6017(1981).
[10]
PHOSPHORYLATION AT TYR-527.
PubMed=2420005; DOI=10.1126/science.2420005;
Cooper J.A., Gould K.L., Cartwright C.A., Hunter T.;
"Tyr527 is phosphorylated in pp60c-src: implications for regulation.";
Science 231:1431-1434(1986).
[11]
PHOSPHORYLATION AT THR-34; THR-46 AND SER-72.
PubMed=2470512; DOI=10.1016/0092-8674(89)90791-5;
Shenoy S., Choi J.K., Bagrodia S., Copeland T.D., Maller J.L.,
Shalloway D.;
"Purified maturation promoting factor phosphorylates pp60c-src at the
sites phosphorylated during fibroblast mitosis.";
Cell 57:763-774(1989).
[12]
FUNCTION IN THE NGF AND FGF SIGNALING PATHWAYS.
PubMed=1717492; DOI=10.1083/jcb.115.3.809;
Kremer N.E., D'Arcangelo G., Thomas S.M., DeMarco M., Brugge J.S.,
Halegoua S.;
"Signal transduction by nerve growth factor and fibroblast growth
factor in PC12 cells requires a sequence of src and ras actions.";
J. Cell Biol. 115:809-819(1991).
[13]
SUBCELLULAR LOCATION.
PubMed=1378446; DOI=10.1083/jcb.118.2.321;
Kaplan K.B., Swedlow J.R., Varmus H.E., Morgan D.O.;
"Association of p60c-src with endosomal membranes in mammalian
fibroblasts.";
J. Cell Biol. 118:321-333(1992).
[14]
SUBCELLULAR LOCATION, AND INTERACTION WITH PXN.
PubMed=8325872;
Weng Z., Taylor J.A., Turner C.E., Brugge J.S., Seidel-Dugan C.;
"Detection of Src homology 3-binding proteins, including paxillin, in
normal and v-Src-transformed Balb/c 3T3 cells.";
J. Biol. Chem. 268:14956-14963(1993).
[15]
FUNCTION IN THE EDN1 SIGNALING PATHWAY, AND SUBCELLULAR LOCATION.
PubMed=8550628; DOI=10.1074/jbc.271.1.77;
Simonson M.S., Wang Y., Herman W.H.;
"Nuclear signaling by endothelin-1 requires Src protein-tyrosine
kinases.";
J. Biol. Chem. 271:77-82(1996).
[16]
INTERACTION WITH AFAP-110.
PubMed=9655255;
DOI=10.1002/(SICI)1098-2744(199806)22:2<110::AID-MC6>3.0.CO;2-Q;
Guappone A.C., Weimer T., Flynn D.C.;
"Formation of a stable src-AFAP-110 complex through either an amino-
terminal or a carboxy-terminal SH2-binding motif.";
Mol. Carcinog. 22:110-119(1998).
[17]
INTERACTION WITH GJA1.
PubMed=15492000; DOI=10.1074/jbc.M409552200;
Sorgen P.L., Duffy H.S., Sahoo P., Coombs W., Delmar M., Spray D.C.;
"Structural changes in the carboxyl terminus of the gap junction
protein connexin43 indicates signaling between binding domains for c-
Src and zonula occludens-1.";
J. Biol. Chem. 279:54695-54701(2004).
[18]
FUNCTION, AND MUTAGENESIS OF TYR-527.
PubMed=19307596; DOI=10.1083/jcb.200810155;
Zhang Y., Tu Y., Zhao J., Chen K., Wu C.;
"Reversion-induced LIM interaction with Src reveals a novel Src
inactivation cycle.";
J. Cell Biol. 184:785-792(2009).
[19]
S-NITROSYLATION AT CYS-498, AND MUTAGENESIS OF CYS-498.
PubMed=19948721; DOI=10.1074/jbc.M109.059782;
Rahman M.A., Senga T., Ito S., Hyodo T., Hasegawa H., Hamaguchi M.;
"S-nitrosylation at cysteine 498 of c-Src tyrosine kinase regulates
nitric oxide-mediated cell invasion.";
J. Biol. Chem. 285:3806-3814(2010).
[20]
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).
[21]
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).
[22]
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).
[23]
X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 83-533.
PubMed=9405157; DOI=10.1006/jmbi.1997.1426;
Williams J.C., Weijland A., Gonfloni S., Thompson A.,
Courtneidge S.A., Superti-Furga G., Wierenga R.K.;
"The 2.35 A crystal structure of the inactivated form of chicken Src:
a dynamic molecule with multiple regulatory interactions.";
J. Mol. Biol. 274:757-775(1997).
[24]
STRUCTURE BY NMR OF 81-140.
PubMed=8504863; DOI=10.1016/0014-5793(93)81538-B;
Yu H., Rosen M.K., Schreiber S.L.;
"1H and 15N assignments and secondary structure of the Src SH3
domain.";
FEBS Lett. 324:87-92(1993).
-!- 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 involved in this
process (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). Also active at the sites of cell-cell contact
adherens junctions and at gap junctions. Implicated in the
regulation of pre-mRNA-processing (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 (PubMed:1717492, PubMed:8550628). Involved in
anchorage-independent cell growth (PubMed:19307596).
{ECO:0000250|UniProtKB:P12931, ECO:0000269|PubMed:1717492,
ECO:0000269|PubMed:19307596, ECO:0000269|PubMed:8550628,
ECO:0000305|PubMed:11964124, ECO:0000305|PubMed:8672527,
ECO:0000305|PubMed:9442882}.
-!- CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a
[protein]-L-tyrosine phosphate. {ECO:0000255|PROSITE-
ProRule:PRU10028}.
-!- ENZYME REGULATION: Becomes activated when its major tyrosine
phosphorylation site is not phosphorylated. It can also be
activated by point mutations as well as by truncations at the C-
terminal end or by other mutations. Heme regulates its activity by
enhancing the phosphorylation on Tyr-527 (By similarity).
{ECO:0000250}.
-!- SUBUNIT: Forms a complex with polyoma virus middle T antigen.
Interacts with AFAP-110. Interacts with GJA1 and PXN.
{ECO:0000269|PubMed:15492000, ECO:0000269|PubMed:8325872,
ECO:0000269|PubMed:9655255}.
-!- INTERACTION:
Q90738:AFAP1; NbExp=3; IntAct=EBI-848039, EBI-8562073;
Q9QWY8-1:Asap1 (xeno); NbExp=3; IntAct=EBI-848039, EBI-698517;
Q9QWY8-2:Asap1 (xeno); NbExp=2; IntAct=EBI-848039, EBI-698524;
Q9NZA1:CLIC5 (xeno); NbExp=2; IntAct=EBI-848039, EBI-5658997;
P41240:CSK (xeno); NbExp=6; IntAct=EBI-848039, EBI-1380630;
Q9Y4D1:DAAM1 (xeno); NbExp=3; IntAct=EBI-848039, EBI-2817289;
P03372:ESR1 (xeno); NbExp=2; IntAct=EBI-848039, EBI-78473;
O88703:Hcn2 (xeno); NbExp=5; IntAct=EBI-848039, EBI-771231;
Q00944:PTK2; NbExp=3; IntAct=EBI-848039, EBI-2896409;
P18433:PTPRA (xeno); NbExp=4; IntAct=EBI-848039, EBI-2609645;
P18052:Ptpra (xeno); NbExp=2; IntAct=EBI-848039, EBI-6597520;
Q9QWI6-2:Srcin1 (xeno); NbExp=2; IntAct=EBI-848039, EBI-775607;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:1378446,
ECO:0000269|PubMed:8325872}. Mitochondrion inner membrane
{ECO:0000250|UniProtKB:P05480}. Endosome membrane
{ECO:0000269|PubMed:1378446}; Peripheral membrane protein
{ECO:0000269|PubMed:1378446}. Nucleus
{ECO:0000269|PubMed:8550628}. Cytoplasm, cytoskeleton
{ECO:0000269|PubMed:8325872}. 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.
{ECO:0000250|UniProtKB:P12931}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P00523-1; Sequence=Displayed;
Name=2;
IsoId=P00523-2; Sequence=VSP_011844, VSP_011845;
Note=Membrane-bound.;
-!- TISSUE SPECIFICITY: Expressed to high levels, and with a high
degree of kinase activity, in certain fully differentiated cells
such as neurons, platelets and macrophages. Isoform 1 is widely
expressed. Isoform 2 is expressed only in the muscle.
-!- PTM: Myristoylated at Gly-2, and this is essential for targeting
to membranes. {ECO:0000250}.
-!- PTM: Dephosphorylated at Tyr-527 by PTPRJ. Phosphorylated on Tyr-
527 by c-Src kinase (CSK). The phosphorylated form is termed
pp60c-src. Dephosphorylated by PTPRJ at Tyr-416. Normally
maintained in an inactive conformation with the SH2 domain engaged
with Tyr-527, the SH3 domain engaged with the SH2-kinase linker,
and Tyr-416 dephosphorylated. Dephosphorylation of Tyr-527 as a
result of protein tyrosine phosphatase (PTP) action disrupts the
intramolecular interaction between the SH2 domain and Tyr-527,
Tyr-416 can then become autophosphorylated, resulting in SRC
activation. Phosphorylation of Tyr-527 by CSK allows this
interaction to reform, resulting in SRC inactivation (By
similarity). {ECO:0000250}.
-!- PTM: S-nitrosylation is important for activation of its kinase
activity. {ECO:0000269|PubMed:19948721}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
kinase family. SRC subfamily. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
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EMBL; V00402; CAA23696.1; -; Genomic_DNA.
EMBL; J00908; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; M57290; AAA49078.1; -; mRNA.
EMBL; S43604; AAD13831.1; -; mRNA.
EMBL; S43616; AAD13835.1; -; mRNA.
EMBL; S43587; AAD13830.1; -; mRNA.
EMBL; S43609; AAD13832.1; -; mRNA.
EMBL; S43614; AAD13834.1; -; mRNA.
EMBL; S43579; AAB19353.2; -; mRNA.
PIR; A00630; TVCHS.
RefSeq; NP_990788.2; NM_205457.2. [P00523-1]
UniGene; Gga.46254; -.
UniGene; Gga.9406; -.
PDB; 1F1W; X-ray; 2.10 A; A=145-247.
PDB; 1F2F; X-ray; 1.70 A; A=145-247.
PDB; 1NLO; NMR; -; C=81-140.
PDB; 1NLP; NMR; -; C=81-140.
PDB; 1P13; X-ray; 1.63 A; A/B=145-246.
PDB; 1PRL; NMR; -; C=77-140.
PDB; 1PRM; NMR; -; C=77-140.
PDB; 1RLP; NMR; -; C=77-140.
PDB; 1RLQ; NMR; -; C=77-140.
PDB; 1SRL; NMR; -; A=77-140.
PDB; 1SRM; NMR; -; A=77-140.
PDB; 2HWO; X-ray; 2.50 A; A/B=251-533.
PDB; 2HWP; X-ray; 2.48 A; A/B=251-533.
PDB; 2OIQ; X-ray; 2.07 A; A/B=251-533.
PDB; 2PTK; X-ray; 2.35 A; A=81-533.
PDB; 2QI8; X-ray; 2.32 A; A/B=251-533.
PDB; 2QLQ; X-ray; 2.33 A; A/B=251-533.
PDB; 2QQ7; X-ray; 2.38 A; A/B=251-533.
PDB; 3D7T; X-ray; 2.90 A; B=251-533.
PDB; 3D7U; X-ray; 4.11 A; B/D=260-523.
PDB; 3DQW; X-ray; 2.02 A; A/B/C/D=251-533.
PDB; 3DQX; X-ray; 2.30 A; A/B=251-533.
PDB; 3EL7; X-ray; 2.80 A; A=251-533.
PDB; 3EL8; X-ray; 2.30 A; A/B=251-533.
PDB; 3EN4; X-ray; 2.55 A; A/B=251-533.
PDB; 3EN5; X-ray; 2.66 A; A/B=251-533.
PDB; 3EN6; X-ray; 2.39 A; A/B=251-533.
PDB; 3EN7; X-ray; 2.81 A; A/B=251-533.
PDB; 3F3T; X-ray; 2.50 A; A/B=251-533.
PDB; 3F3U; X-ray; 2.50 A; A/B=251-533.
PDB; 3F3V; X-ray; 2.60 A; A/B=251-533.
PDB; 3F3W; X-ray; 2.60 A; A/B=251-533.
PDB; 3F6X; X-ray; 2.35 A; A/B/C/D=251-533.
PDB; 3FJ5; X-ray; 1.65 A; A/B=85-140.
PDB; 3G5D; X-ray; 2.20 A; A/B=251-533.
PDB; 3G6G; X-ray; 2.31 A; A/B=251-533.
PDB; 3G6H; X-ray; 2.35 A; A/B=251-533.
PDB; 3GEQ; X-ray; 2.20 A; A/B=251-533.
PDB; 3LOK; X-ray; 2.48 A; A/B=251-533.
PDB; 3OEZ; X-ray; 2.40 A; A/B=251-533.
PDB; 3OF0; X-ray; 2.70 A; A/B=251-533.
PDB; 3QLF; X-ray; 2.75 A; A/B=251-533.
PDB; 3QLG; X-ray; 2.75 A; A/B=251-533.
PDB; 3SVV; X-ray; 2.20 A; A/B=251-533.
PDB; 3TZ7; X-ray; 3.30 A; A/B=251-533.
PDB; 3TZ8; X-ray; 2.70 A; A/B=251-533.
PDB; 3TZ9; X-ray; 3.10 A; A/B=251-533.
PDB; 3U4W; X-ray; 1.90 A; A=259-533.
PDB; 3U51; X-ray; 2.24 A; A/B=259-533.
PDB; 3UQF; X-ray; 2.27 A; A/B=251-533.
PDB; 3UQG; X-ray; 2.20 A; A/B=251-533.
PDB; 4AGW; X-ray; 2.60 A; A/B=251-533.
PDB; 4DGG; X-ray; 2.65 A; A/B=251-533.
PDB; 4FIC; X-ray; 2.50 A; A/B=251-533.
PDB; 4HVU; X-ray; 0.98 A; A=85-141.
PDB; 4HVV; X-ray; 1.10 A; A=85-140.
PDB; 4HVW; X-ray; 0.98 A; A=85-141.
PDB; 4JZ3; X-ray; 1.85 A; A=85-141.
PDB; 4JZ4; X-ray; 1.56 A; A/B=85-141.
PDB; 4LE9; X-ray; 1.34 A; A=85-141.
PDB; 4LGG; X-ray; 2.41 A; A/B=264-533.
PDB; 4LGH; X-ray; 2.84 A; A/B=257-533.
PDB; 4MCV; X-ray; 2.73 A; A/B=256-533.
PDB; 4O2P; X-ray; 2.10 A; A/B=251-533.
PDB; 4OML; X-ray; 1.60 A; A=85-141.
PDB; 4OMM; X-ray; 1.90 A; A=85-140.
PDB; 4OMN; X-ray; 1.50 A; A=85-140.
PDB; 4OMO; X-ray; 1.04 A; A/B=85-141.
PDB; 4OMP; X-ray; 2.00 A; A=85-139.
PDB; 4OMQ; X-ray; 2.00 A; A=85-140.
PDB; 4QT7; X-ray; 1.55 A; A=85-141.
PDB; 4RTU; X-ray; 2.45 A; A=85-141.
PDB; 4RTV; X-ray; 1.37 A; A=85-141.
PDB; 4RTW; X-ray; 1.24 A; A/C=85-141.
PDB; 4RTX; X-ray; 1.32 A; A/B/C/D=85-141.
PDB; 4RTY; X-ray; 1.28 A; A=85-141.
PDB; 4RTZ; X-ray; 0.98 A; A=85-141.
PDB; 4U5J; X-ray; 2.26 A; A/B=251-533.
PDB; 4YBJ; X-ray; 2.61 A; A/B=251-533.
PDB; 4YBK; X-ray; 2.50 A; A=251-533.
PDB; 5BMM; X-ray; 2.50 A; A/B=251-533.
PDB; 5D10; X-ray; 2.70 A; A/B=251-533.
PDB; 5D11; X-ray; 2.30 A; A/B=251-533.
PDB; 5D12; X-ray; 3.00 A; A/B=251-533.
PDB; 5EC7; X-ray; 1.65 A; A/B/C=85-140.
PDB; 5ECA; X-ray; 1.16 A; A=85-141.
PDB; 5I11; X-ray; 1.95 A; A=85-141.
PDB; 5J5S; X-ray; 2.15 A; A/B=251-533.
PDB; 5K9I; X-ray; 2.50 A; A/B=251-533.
PDB; 5OAV; X-ray; 0.95 A; A/C=85-141.
PDB; 5OB0; X-ray; 1.17 A; A=85-141.
PDB; 5OB1; X-ray; 1.17 A; A=85-141.
PDB; 5OB2; X-ray; 1.80 A; A/C=85-141.
PDB; 5SWH; X-ray; 2.50 A; A/B=252-533.
PDB; 5SYS; X-ray; 2.80 A; A/B=251-533.
PDB; 5T0P; X-ray; 2.50 A; A/B=251-533.
PDB; 5TEH; X-ray; 2.99 A; A/B=251-533.
PDB; 5XP7; X-ray; 2.01 A; A/B=251-533.
PDBsum; 1F1W; -.
PDBsum; 1F2F; -.
PDBsum; 1NLO; -.
PDBsum; 1NLP; -.
PDBsum; 1P13; -.
PDBsum; 1PRL; -.
PDBsum; 1PRM; -.
PDBsum; 1RLP; -.
PDBsum; 1RLQ; -.
PDBsum; 1SRL; -.
PDBsum; 1SRM; -.
PDBsum; 2HWO; -.
PDBsum; 2HWP; -.
PDBsum; 2OIQ; -.
PDBsum; 2PTK; -.
PDBsum; 2QI8; -.
PDBsum; 2QLQ; -.
PDBsum; 2QQ7; -.
PDBsum; 3D7T; -.
PDBsum; 3D7U; -.
PDBsum; 3DQW; -.
PDBsum; 3DQX; -.
PDBsum; 3EL7; -.
PDBsum; 3EL8; -.
PDBsum; 3EN4; -.
PDBsum; 3EN5; -.
PDBsum; 3EN6; -.
PDBsum; 3EN7; -.
PDBsum; 3F3T; -.
PDBsum; 3F3U; -.
PDBsum; 3F3V; -.
PDBsum; 3F3W; -.
PDBsum; 3F6X; -.
PDBsum; 3FJ5; -.
PDBsum; 3G5D; -.
PDBsum; 3G6G; -.
PDBsum; 3G6H; -.
PDBsum; 3GEQ; -.
PDBsum; 3LOK; -.
PDBsum; 3OEZ; -.
PDBsum; 3OF0; -.
PDBsum; 3QLF; -.
PDBsum; 3QLG; -.
PDBsum; 3SVV; -.
PDBsum; 3TZ7; -.
PDBsum; 3TZ8; -.
PDBsum; 3TZ9; -.
PDBsum; 3U4W; -.
PDBsum; 3U51; -.
PDBsum; 3UQF; -.
PDBsum; 3UQG; -.
PDBsum; 4AGW; -.
PDBsum; 4DGG; -.
PDBsum; 4FIC; -.
PDBsum; 4HVU; -.
PDBsum; 4HVV; -.
PDBsum; 4HVW; -.
PDBsum; 4JZ3; -.
PDBsum; 4JZ4; -.
PDBsum; 4LE9; -.
PDBsum; 4LGG; -.
PDBsum; 4LGH; -.
PDBsum; 4MCV; -.
PDBsum; 4O2P; -.
PDBsum; 4OML; -.
PDBsum; 4OMM; -.
PDBsum; 4OMN; -.
PDBsum; 4OMO; -.
PDBsum; 4OMP; -.
PDBsum; 4OMQ; -.
PDBsum; 4QT7; -.
PDBsum; 4RTU; -.
PDBsum; 4RTV; -.
PDBsum; 4RTW; -.
PDBsum; 4RTX; -.
PDBsum; 4RTY; -.
PDBsum; 4RTZ; -.
PDBsum; 4U5J; -.
PDBsum; 4YBJ; -.
PDBsum; 4YBK; -.
PDBsum; 5BMM; -.
PDBsum; 5D10; -.
PDBsum; 5D11; -.
PDBsum; 5D12; -.
PDBsum; 5EC7; -.
PDBsum; 5ECA; -.
PDBsum; 5I11; -.
PDBsum; 5J5S; -.
PDBsum; 5K9I; -.
PDBsum; 5OAV; -.
PDBsum; 5OB0; -.
PDBsum; 5OB1; -.
PDBsum; 5OB2; -.
PDBsum; 5SWH; -.
PDBsum; 5SYS; -.
PDBsum; 5T0P; -.
PDBsum; 5TEH; -.
PDBsum; 5XP7; -.
ProteinModelPortal; P00523; -.
SMR; P00523; -.
BioGrid; 676691; 1.
DIP; DIP-449N; -.
ELM; P00523; -.
IntAct; P00523; 19.
MINT; MINT-139173; -.
STRING; 9031.ENSGALP00000006117; -.
BindingDB; P00523; -.
ChEMBL; CHEMBL3655; -.
iPTMnet; P00523; -.
PaxDb; P00523; -.
Ensembl; ENSGALT00000084821; ENSGALP00000063464; ENSGALG00000003855. [P00523-2]
GeneID; 396442; -.
KEGG; gga:396442; -.
CTD; 6714; -.
eggNOG; KOG0197; Eukaryota.
eggNOG; COG0515; LUCA.
GeneTree; ENSGT00760000118938; -.
HOVERGEN; HBG008761; -.
InParanoid; P00523; -.
KO; K05704; -.
OMA; CQCWRKD; -.
OrthoDB; EOG091G0D46; -.
PhylomeDB; P00523; -.
TreeFam; TF351634; -.
BRENDA; 2.7.10.2; 1306.
Reactome; R-GGA-1227986; Signaling by ERBB2.
Reactome; R-GGA-1295596; Spry regulation of FGF signaling.
Reactome; R-GGA-1433557; Signaling by SCF-KIT.
Reactome; R-GGA-1433559; Regulation of KIT signaling.
Reactome; R-GGA-177929; Signaling by EGFR.
Reactome; R-GGA-180292; GAB1 signalosome.
Reactome; R-GGA-186763; Downstream signal transduction.
Reactome; R-GGA-191647; c-src mediated regulation of Cx43 function and closure of gap junctions.
Reactome; R-GGA-354192; Integrin alphaIIb beta3 signaling.
Reactome; R-GGA-354194; GRB2:SOS provides linkage to MAPK signaling for Integrins.
Reactome; R-GGA-372708; p130Cas linkage to MAPK signaling for integrins.
Reactome; R-GGA-389356; CD28 co-stimulation.
Reactome; R-GGA-389513; CTLA4 inhibitory signaling.
Reactome; R-GGA-3928662; EPHB-mediated forward signaling.
Reactome; R-GGA-3928664; Ephrin signaling.
Reactome; R-GGA-3928665; EPH-ephrin mediated repulsion of cells.
Reactome; R-GGA-418592; ADP signalling through P2Y purinoceptor 1.
Reactome; R-GGA-418885; DCC mediated attractive signaling.
Reactome; R-GGA-430116; GP1b-IX-V activation signalling.
Reactome; R-GGA-4420097; VEGFA-VEGFR2 Pathway.
Reactome; R-GGA-456926; Thrombin signalling through proteinase activated receptors (PARs).
Reactome; R-GGA-5218921; VEGFR2 mediated cell proliferation.
Reactome; R-GGA-5663220; RHO GTPases Activate Formins.
Reactome; R-GGA-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
Reactome; R-GGA-8853659; RET signaling.
Reactome; R-GGA-8874081; MET activates PTK2 signaling.
Reactome; R-GGA-8934593; Regulation of RUNX1 Expression and Activity.
Reactome; R-GGA-8934903; Receptor Mediated Mitophagy.
Reactome; R-GGA-8941858; Regulation of RUNX3 expression and activity.
EvolutionaryTrace; P00523; -.
PRO; PR:P00523; -.
Proteomes; UP000000539; Chromosome 20.
Bgee; ENSGALG00000003855; -.
GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; IBA:GO_Central.
GO; GO:0005743; C:mitochondrial inner membrane; ISS:UniProtKB.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0043234; C:protein complex; IMP:CAFA.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0071253; F:connexin binding; IPI:CAFA.
GO; GO:0070851; F:growth factor receptor binding; IBA:GO_Central.
GO; GO:0020037; F:heme binding; ISS:UniProtKB.
GO; GO:0051427; F:hormone receptor binding; IBA:GO_Central.
GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IBA:GO_Central.
GO; GO:0019903; F:protein phosphatase binding; IPI:UniProtKB.
GO; GO:0004713; F:protein tyrosine kinase activity; EXP:Reactome.
GO; GO:0045453; P:bone resorption; IBA:GO_Central.
GO; GO:0007155; P:cell adhesion; IBA:GO_Central.
GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
GO; GO:0016477; P:cell migration; IBA:GO_Central.
GO; GO:0007417; P:central nervous system development; IBA:GO_Central.
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:0045087; P:innate immune response; IBA:GO_Central.
GO; GO:0030520; P:intracellular estrogen receptor signaling pathway; IBA:GO_Central.
GO; GO:2001237; P:negative regulation of extrinsic apoptotic signaling pathway; IBA:GO_Central.
GO; GO:2001243; P:negative regulation of intrinsic apoptotic signaling pathway; IBA:GO_Central.
GO; GO:0036035; P:osteoclast development; IBA:GO_Central.
GO; GO:0038083; P:peptidyl-tyrosine autophosphorylation; IBA:GO_Central.
GO; GO:0048008; P:platelet-derived growth factor receptor signaling pathway; IBA:GO_Central.
GO; GO:0050847; P:progesterone receptor signaling pathway; IBA:GO_Central.
GO; GO:0051726; P:regulation of cell cycle; IBA:GO_Central.
GO; GO:0042127; P:regulation of cell proliferation; IBA:GO_Central.
GO; GO:0071801; P:regulation of podosome assembly; IBA:GO_Central.
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;
3D-structure; Alternative splicing; ATP-binding; Cell adhesion;
Cell cycle; Cell membrane; Complete proteome; Cytoplasm; Cytoskeleton;
Endosome; Immunity; Kinase; Lipoprotein; Membrane; Mitochondrion;
Mitochondrion inner membrane; Myristate; Nucleotide-binding; Nucleus;
Phosphoprotein; Proto-oncogene; Reference proteome; S-nitrosylation;
SH2 domain; SH3 domain; Transferase; Tyrosine-protein kinase.
INIT_MET 1 1 Removed. {ECO:0000250}.
CHAIN 2 533 Proto-oncogene tyrosine-protein kinase
Src.
/FTId=PRO_0000088144.
DOMAIN 81 142 SH3. {ECO:0000255|PROSITE-
ProRule:PRU00192}.
DOMAIN 148 245 SH2. {ECO:0000255|PROSITE-
ProRule:PRU00191}.
DOMAIN 267 520 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 273 281 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
ACT_SITE 386 386 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10028}.
BINDING 295 295 ATP.
MOD_RES 12 12 Phosphoserine; by PKC.
{ECO:0000269|PubMed:2996780}.
MOD_RES 34 34 Phosphothreonine.
{ECO:0000269|PubMed:2470512}.
MOD_RES 46 46 Phosphothreonine.
{ECO:0000269|PubMed:2470512}.
MOD_RES 72 72 Phosphoserine.
{ECO:0000269|PubMed:2470512}.
MOD_RES 416 416 Phosphotyrosine; by autocatalysis.
{ECO:0000269|PubMed:6273838,
ECO:0000269|PubMed:8856081}.
MOD_RES 436 436 Phosphotyrosine; by autocatalysis.
{ECO:0000269|PubMed:8856081}.
MOD_RES 498 498 S-nitrosocysteine.
{ECO:0000269|PubMed:19948721}.
MOD_RES 527 527 Phosphotyrosine; by CSK.
{ECO:0000269|PubMed:2420005}.
LIPID 2 2 N-myristoyl glycine. {ECO:0000250}.
VAR_SEQ 183 193 AYCLSVSDFDN -> DPCIPLPSCLC (in isoform
2). {ECO:0000303|PubMed:2115117}.
/FTId=VSP_011844.
VAR_SEQ 194 533 Missing (in isoform 2).
{ECO:0000303|PubMed:2115117}.
/FTId=VSP_011845.
MUTAGEN 498 498 C->A: Significant reduction in S-
nitrosylation.
{ECO:0000269|PubMed:19948721}.
MUTAGEN 527 527 Y->F: Constitutively active.
{ECO:0000269|PubMed:19307596}.
CONFLICT 301 301 T -> N (in Ref. 1). {ECO:0000305}.
CONFLICT 501 501 K -> R (in Ref. 1). {ECO:0000305}.
STRAND 86 90 {ECO:0000244|PDB:5OAV}.
STRAND 95 99 {ECO:0000244|PDB:5ECA}.
STRAND 107 112 {ECO:0000244|PDB:5OAV}.
STRAND 115 123 {ECO:0000244|PDB:5OAV}.
TURN 124 126 {ECO:0000244|PDB:5OAV}.
STRAND 129 133 {ECO:0000244|PDB:5OAV}.
HELIX 134 136 {ECO:0000244|PDB:5OAV}.
STRAND 137 139 {ECO:0000244|PDB:5OAV}.
HELIX 143 145 {ECO:0000244|PDB:2PTK}.
STRAND 149 152 {ECO:0000244|PDB:1F1W}.
HELIX 155 162 {ECO:0000244|PDB:1P13}.
STRAND 165 167 {ECO:0000244|PDB:2PTK}.
STRAND 172 176 {ECO:0000244|PDB:1P13}.
STRAND 178 180 {ECO:0000244|PDB:1P13}.
STRAND 184 192 {ECO:0000244|PDB:1P13}.
TURN 193 195 {ECO:0000244|PDB:1P13}.
STRAND 196 206 {ECO:0000244|PDB:1P13}.
STRAND 212 215 {ECO:0000244|PDB:1P13}.
STRAND 218 222 {ECO:0000244|PDB:1P13}.
HELIX 223 232 {ECO:0000244|PDB:1P13}.
STRAND 237 239 {ECO:0000244|PDB:1P13}.
STRAND 253 258 {ECO:0000244|PDB:2PTK}.
STRAND 259 261 {ECO:0000244|PDB:3GEQ}.
HELIX 264 266 {ECO:0000244|PDB:3U4W}.
STRAND 267 275 {ECO:0000244|PDB:3U4W}.
STRAND 277 286 {ECO:0000244|PDB:3U4W}.
TURN 287 289 {ECO:0000244|PDB:3U4W}.
STRAND 290 297 {ECO:0000244|PDB:3U4W}.
TURN 299 301 {ECO:0000244|PDB:5XP7}.
HELIX 304 314 {ECO:0000244|PDB:3U4W}.
STRAND 325 329 {ECO:0000244|PDB:3U4W}.
STRAND 331 333 {ECO:0000244|PDB:3U4W}.
STRAND 335 338 {ECO:0000244|PDB:3U4W}.
HELIX 346 351 {ECO:0000244|PDB:3U4W}.
HELIX 353 357 {ECO:0000244|PDB:3U4W}.
HELIX 360 379 {ECO:0000244|PDB:3U4W}.
HELIX 389 391 {ECO:0000244|PDB:3U4W}.
STRAND 392 394 {ECO:0000244|PDB:3U4W}.
HELIX 396 398 {ECO:0000244|PDB:3U4W}.
STRAND 400 402 {ECO:0000244|PDB:3U4W}.
HELIX 405 407 {ECO:0000244|PDB:2QI8}.
HELIX 408 410 {ECO:0000244|PDB:3U4W}.
HELIX 414 417 {ECO:0000244|PDB:3U4W}.
STRAND 421 424 {ECO:0000244|PDB:5BMM}.
HELIX 426 428 {ECO:0000244|PDB:3U4W}.
HELIX 431 436 {ECO:0000244|PDB:3U4W}.
HELIX 441 456 {ECO:0000244|PDB:3U4W}.
TURN 457 459 {ECO:0000244|PDB:3U4W}.
HELIX 468 476 {ECO:0000244|PDB:3U4W}.
HELIX 489 498 {ECO:0000244|PDB:3U4W}.
HELIX 503 505 {ECO:0000244|PDB:3U4W}.
HELIX 509 517 {ECO:0000244|PDB:3U4W}.
HELIX 519 522 {ECO:0000244|PDB:3U4W}.
SEQUENCE 533 AA; 60010 MW; ABDB036F7D63C30A CRC64;
MGSSKSKPKD PSQRRRSLEP PDSTHHGGFP ASQTPNKTAA PDTHRTPSRS FGTVATEPKL
FGGFNTSDTV TSPQRAGALA GGVTTFVALY DYESRTETDL SFKKGERLQI VNNTEGDWWL
AHSLTTGQTG YIPSNYVAPS DSIQAEEWYF GKITRRESER LLLNPENPRG TFLVRESETT
KGAYCLSVSD FDNAKGLNVK HYKIRKLDSG GFYITSRTQF SSLQQLVAYY SKHADGLCHR
LTNVCPTSKP QTQGLAKDAW EIPRESLRLE VKLGQGCFGE VWMGTWNGTT RVAIKTLKPG
TMSPEAFLQE AQVMKKLRHE KLVQLYAVVS EEPIYIVTEY MSKGSLLDFL KGEMGKYLRL
PQLVDMAAQI ASGMAYVERM NYVHRDLRAA NILVGENLVC KVADFGLARL IEDNEYTARQ
GAKFPIKWTA PEAALYGRFT IKSDVWSFGI LLTELTTKGR VPYPGMVNRE VLDQVERGYR
MPCPPECPES LHDLMCQCWR KDPEERPTFE YLQAFLEDYF TSTEPQYQPG ENL


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