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Tyrosine-protein kinase CSK (EC 2.7.10.2) (C-Src kinase) (Protein-tyrosine kinase MPK-2) (p50CSK)

 CSK_MOUSE               Reviewed;         450 AA.
P41241; Q03143; Q80WU4; Q8VCW1;
01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
27-JUL-2011, sequence version 2.
22-NOV-2017, entry version 180.
RecName: Full=Tyrosine-protein kinase CSK;
EC=2.7.10.2 {ECO:0000250|UniProtKB:P41240};
AltName: Full=C-Src kinase;
AltName: Full=Protein-tyrosine kinase MPK-2;
AltName: Full=p50CSK;
Name=Csk;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Brain;
PubMed=7511815; DOI=10.1073/pnas.91.7.2597;
Klages S., Adam D., Class K., Fargnoli J., Bolen J.B., Penhallow R.C.;
"Ctk: a protein-tyrosine kinase related to Csk that defines an enzyme
family.";
Proc. Natl. Acad. Sci. U.S.A. 91:2597-2601(1994).
[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 MRNA].
STRAIN=NOD; TISSUE=Spleen;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J, and FVB/N; TISSUE=Brain, and Colon;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 316-367.
STRAIN=C57BL/6J; TISSUE=Embryonic brain;
PubMed=1281307;
Gilardi-Hebenstreit P., Nieto M.A., Frain M., Mattei M.-G.,
Chestier A., Wilkinson D.G., Charnay P.;
"An Eph-related receptor protein tyrosine kinase gene segmentally
expressed in the developing mouse hindbrain.";
Oncogene 7:2499-2506(1992).
[6]
PROTEIN SEQUENCE OF 338-347, AND IDENTIFICATION BY MASS SPECTROMETRY.
STRAIN=OF1; TISSUE=Hippocampus;
Lubec G., Sunyer B., Chen W.-Q.;
Submitted (JAN-2009) to UniProtKB.
[7]
DISRUPTION PHENOTYPE.
PubMed=7685657; DOI=10.1016/0092-8674(93)90641-3;
Imamoto A., Soriano P.;
"Disruption of the csk gene, encoding a negative regulator of Src
family tyrosine kinases, leads to neural tube defects and embryonic
lethality in mice.";
Cell 73:1117-1124(1993).
[8]
INTERACTION WITH PTPN22.
PubMed=8890164;
Cloutier J.-F., Veillette A.;
"Association of inhibitory tyrosine protein kinase p50csk with protein
tyrosine phosphatase PEP in T cells and other hemopoietic cells.";
EMBO J. 15:4909-4918(1996).
[9]
INTERACTION WITH TGFB1I1.
PubMed=9858471;
Thomas S.M., Hagel M., Turner C.E.;
"Characterization of a focal adhesion protein, Hic-5, that shares
extensive homology with paxillin.";
J. Cell Sci. 112:181-190(1999).
[10]
INTERACTION WITH PAG1.
PubMed=12218089; DOI=10.4049/jimmunol.169.6.2813;
Yasuda K., Nagafuku M., Shima T., Okada M., Yagi T., Yamada T.,
Minaki Y., Kato A., Tani-Ichi S., Hamaoka T., Kosugi A.;
"Fyn is essential for tyrosine phosphorylation of Csk-binding
protein/phosphoprotein associated with glycolipid-enriched
microdomains in lipid rafts in resting T cells.";
J. Immunol. 169:2813-2817(2002).
[11]
INTERACTION WITH PAG1.
PubMed=12612075; DOI=10.1128/MCB.23.6.2017-2028.2003;
Davidson D., Bakinowski M., Thomas M.L., Horejsi V., Veillette A.;
"Phosphorylation-dependent regulation of T-cell activation by PAG/Cbp,
a lipid raft-associated transmembrane adaptor.";
Mol. Cell. Biol. 23:2017-2028(2003).
[12]
INTERACTION WITH PAG1, AND SUBCELLULAR LOCATION.
PubMed=16166631; DOI=10.1128/MCB.25.19.8486-8495.2005;
Xu S., Huo J., Tan J.E.-L., Lam K.-P.;
"Cbp deficiency alters Csk localization in lipid rafts but does not
affect T-cell development.";
Mol. Cell. Biol. 25:8486-8495(2005).
[13]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=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).
[14]
STRUCTURE BY NMR OF 1-83.
PubMed=11685249; DOI=10.1038/nsb1101-998;
Ghose R., Shekhtman A., Goger M.J., Ji H., Cowburn D.;
"A novel, specific interaction involving the Csk SH3 domain and its
natural ligand.";
Nat. Struct. Biol. 8:998-1004(2001).
-!- FUNCTION: Non-receptor tyrosine-protein kinase that plays an
important role in the regulation of cell growth, differentiation,
migration and immune response. Phosphorylates tyrosine residues
located in the C-terminal tails of Src-family kinases (SFKs)
including LCK, SRC, HCK, FYN, LYN or YES1. Upon tail
phosphorylation, Src-family members engage in intramolecular
interactions between the phosphotyrosine tail and the SH2 domain
that result in an inactive conformation. To inhibit SFKs, CSK is
recruited to the plasma membrane via binding to transmembrane
proteins or adapter proteins located near the plasma membrane.
Suppresses signaling by various surface receptors, including T-
cell receptor (TCR) and B-cell receptor (BCR) by phosphorylating
and maintaining inactive several positive effectors such as FYN or
LCK (By similarity). {ECO:0000250}.
-!- CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a
[protein]-L-tyrosine phosphate. {ECO:0000250|UniProtKB:P41240,
ECO:0000255|PROSITE-ProRule:PRU10028}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000250|UniProtKB:P41240};
Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
Evidence={ECO:0000250|UniProtKB:P41240};
-!- SUBUNIT: Homodimer (via SH3-domain) (By similarity). Interacts
with PTPN22 (PubMed:8890164). Interacts with phosphorylated SIT1,
PAG1, LIME1 and TGFB1I1; these interactions serve to recruit CSK
to the membrane where it can phosphorylate and inhibit Src-family
kinases (PubMed:9858471, PubMed:12218089, PubMed:12612075,
PubMed:16166631). Interacts with SRCIN1 (By similarity). Interacts
with RHOH (By similarity). Interacts (via SH2 domain) with SCIMP
(By similarity). {ECO:0000250|UniProtKB:P41240,
ECO:0000269|PubMed:12218089, ECO:0000269|PubMed:12612075,
ECO:0000269|PubMed:16166631, ECO:0000269|PubMed:8890164,
ECO:0000269|PubMed:9858471}.
-!- INTERACTION:
Q3U1F9:Pag1; NbExp=9; IntAct=EBI-2553183, EBI-8468834;
P42337:Pik3ca; NbExp=2; IntAct=EBI-2553183, EBI-641748;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16166631}.
Cell membrane {ECO:0000269|PubMed:16166631}. Note=Mainly
cytoplasmic, also present in lipid rafts.
-!- TISSUE SPECIFICITY: Ubiquitous, but most abundant in thymus and
spleen, as well as in neonatal brain.
-!- DOMAIN: The architecture of this protein is similar to that of
Src-family kinases (SFKs) with one N-terminal SH3 domain, one SH2
domain, and a C-terminal kinase domain. {ECO:0000250}.
-!- PTM: Phosphorylated at Ser-364 by PKA, leading to increased
activity. Autophosphorylated (By similarity). {ECO:0000250}.
-!- DISRUPTION PHENOTYPE: Mice die between day 9 and day 10 of
gestation with several defects including a non-functional neural
tube. SRC and FYN kinases show increased activity when CSK is
missing. {ECO:0000269|PubMed:7685657}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
kinase family. CSK subfamily. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
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EMBL; U05247; AAA18766.1; -; mRNA.
EMBL; AY902339; AAX90624.1; -; Genomic_DNA.
EMBL; AK156058; BAE33565.1; -; mRNA.
EMBL; AK170815; BAE42047.1; -; mRNA.
EMBL; BC018394; AAH18394.1; -; mRNA.
EMBL; BC052006; AAH52006.2; -; mRNA.
EMBL; X57242; CAA40518.1; -; mRNA.
CCDS; CCDS23228.1; -.
PIR; I48929; I48929.
RefSeq; NP_001291690.1; NM_001304761.1.
RefSeq; NP_031809.2; NM_007783.3.
RefSeq; XP_006510864.1; XM_006510801.3.
RefSeq; XP_006510865.1; XM_006510802.3.
UniGene; Mm.21974; -.
PDB; 1JEG; NMR; -; A=1-83.
PDBsum; 1JEG; -.
ProteinModelPortal; P41241; -.
SMR; P41241; -.
BioGrid; 198936; 33.
CORUM; P41241; -.
IntAct; P41241; 35.
MINT; MINT-1345201; -.
STRING; 10090.ENSMUSP00000034863; -.
iPTMnet; P41241; -.
PhosphoSitePlus; P41241; -.
EPD; P41241; -.
MaxQB; P41241; -.
PaxDb; P41241; -.
PeptideAtlas; P41241; -.
PRIDE; P41241; -.
Ensembl; ENSMUST00000034863; ENSMUSP00000034863; ENSMUSG00000032312.
Ensembl; ENSMUST00000215396; ENSMUSP00000150590; ENSMUSG00000032312.
Ensembl; ENSMUST00000217314; ENSMUSP00000150984; ENSMUSG00000032312.
GeneID; 12988; -.
KEGG; mmu:12988; -.
UCSC; uc009pvk.2; mouse.
CTD; 1445; -.
MGI; MGI:88537; Csk.
eggNOG; KOG0197; Eukaryota.
eggNOG; COG0515; LUCA.
GeneTree; ENSGT00760000119011; -.
HOGENOM; HOG000233858; -.
HOVERGEN; HBG008761; -.
InParanoid; P41241; -.
KO; K05728; -.
OMA; WALNMKD; -.
OrthoDB; EOG091G05PB; -.
TreeFam; TF351634; -.
BRENDA; 2.7.10.2; 3474.
Reactome; R-MMU-180292; GAB1 signalosome.
Reactome; R-MMU-202427; Phosphorylation of CD3 and TCR zeta chains.
Reactome; R-MMU-354192; Integrin alphaIIb beta3 signaling.
Reactome; R-MMU-389948; PD-1 signaling.
EvolutionaryTrace; P41241; -.
PRO; PR:P41241; -.
Proteomes; UP000000589; Chromosome 9.
Bgee; ENSMUSG00000032312; -.
CleanEx; MM_CSK; -.
ExpressionAtlas; P41241; baseline and differential.
Genevisible; P41241; MM.
GO; GO:0005911; C:cell-cell junction; IDA:MGI.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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:0045121; C:membrane raft; IEA:Ensembl.
GO; GO:0005886; C:plasma membrane; ISO:MGI.
GO; GO:0005524; F:ATP binding; TAS:HGNC.
GO; GO:0042802; F:identical protein binding; ISO:MGI.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IBA:GO_Central.
GO; GO:0070064; F:proline-rich region binding; IEA:Ensembl.
GO; GO:0034236; F:protein kinase A catalytic subunit binding; ISO:MGI.
GO; GO:0019903; F:protein phosphatase binding; IEA:Ensembl.
GO; GO:0004713; F:protein tyrosine kinase activity; ISS:UniProtKB.
GO; GO:0005102; F:receptor binding; IBA:GO_Central.
GO; GO:0016740; F:transferase activity; TAS:HGNC.
GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
GO; GO:0034332; P:adherens junction organization; IBA:GO_Central.
GO; GO:0007420; P:brain development; IEA:Ensembl.
GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
GO; GO:0071375; P:cellular response to peptide hormone stimulus; IEA:Ensembl.
GO; GO:0007417; P:central nervous system development; IBA:GO_Central.
GO; GO:0045087; P:innate immune response; IBA:GO_Central.
GO; GO:0035556; P:intracellular signal transduction; TAS:HGNC.
GO; GO:0045779; P:negative regulation of bone resorption; IEA:Ensembl.
GO; GO:0008285; P:negative regulation of cell proliferation; IMP:MGI.
GO; GO:0070373; P:negative regulation of ERK1 and ERK2 cascade; IEA:Ensembl.
GO; GO:0042997; P:negative regulation of Golgi to plasma membrane protein transport; ISO:MGI.
GO; GO:0032715; P:negative regulation of interleukin-6 production; IEA:Ensembl.
GO; GO:0033673; P:negative regulation of kinase activity; IEA:Ensembl.
GO; GO:0010989; P:negative regulation of low-density lipoprotein particle clearance; IEA:Ensembl.
GO; GO:0050765; P:negative regulation of phagocytosis; IEA:Ensembl.
GO; GO:0048709; P:oligodendrocyte differentiation; IEA:Ensembl.
GO; GO:0038083; P:peptidyl-tyrosine autophosphorylation; IBA:GO_Central.
GO; GO:0043406; P:positive regulation of MAP kinase activity; IEA:Ensembl.
GO; GO:0006468; P:protein phosphorylation; TAS:HGNC.
GO; GO:0001817; P:regulation of cytokine production; IBA:GO_Central.
GO; GO:0060368; P:regulation of Fc receptor mediated stimulatory signaling pathway; IBA:GO_Central.
GO; GO:0050863; P:regulation of T cell activation; TAS:HGNC.
GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA:GO_Central.
CDD; cd09937; SH2_csk_like; 1.
Gene3D; 3.30.505.10; -; 1.
InterPro; IPR035026; CSK.
InterPro; IPR035027; Csk-like_SH2.
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.
PANTHER; PTHR24418:SF307; PTHR24418:SF307; 1.
Pfam; PF07714; Pkinase_Tyr; 1.
Pfam; PF00017; SH2; 1.
Pfam; PF00018; SH3_1; 1.
PRINTS; PR00401; SH2DOMAIN.
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; Acetylation; Adaptive immunity; ATP-binding;
Cell membrane; Complete proteome; Cytoplasm;
Direct protein sequencing; Immunity; Kinase; Magnesium; Manganese;
Membrane; Metal-binding; Nucleotide-binding; Phosphoprotein;
Reference proteome; SH2 domain; SH3 domain; Transferase;
Tyrosine-protein kinase.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:P41240}.
CHAIN 2 450 Tyrosine-protein kinase CSK.
/FTId=PRO_0000088071.
DOMAIN 9 70 SH3. {ECO:0000255|PROSITE-
ProRule:PRU00192}.
DOMAIN 82 171 SH2. {ECO:0000255|PROSITE-
ProRule:PRU00191}.
DOMAIN 195 449 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 201 209 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
REGION 9 70 Interaction with PTPN22.
{ECO:0000269|PubMed:8890164}.
ACT_SITE 314 314 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10028}.
BINDING 222 222 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 2 2 N-acetylserine.
{ECO:0000250|UniProtKB:P41240}.
MOD_RES 184 184 Phosphotyrosine.
{ECO:0000250|UniProtKB:P41240}.
MOD_RES 304 304 Phosphotyrosine.
{ECO:0000250|UniProtKB:P41240}.
MOD_RES 364 364 Phosphoserine; by PKA.
{ECO:0000250|UniProtKB:P41240}.
MOD_RES 416 416 Phosphotyrosine; by autocatalysis.
{ECO:0000250|UniProtKB:P41240}.
CONFLICT 299 299 C -> L (in Ref. 1; AAA18766).
{ECO:0000305}.
CONFLICT 417 417 E -> D (in Ref. 1; AAA18766).
{ECO:0000305}.
CONFLICT 423 423 W -> S (in Ref. 1; AAA18766).
{ECO:0000305}.
STRAND 13 18 {ECO:0000244|PDB:1JEG}.
STRAND 35 41 {ECO:0000244|PDB:1JEG}.
STRAND 43 51 {ECO:0000244|PDB:1JEG}.
STRAND 57 61 {ECO:0000244|PDB:1JEG}.
HELIX 62 64 {ECO:0000244|PDB:1JEG}.
STRAND 65 67 {ECO:0000244|PDB:1JEG}.
SEQUENCE 450 AA; 50716 MW; E8D3EC9357B86277 CRC64;
MSAIQAAWPS GTECIAKYNF HGTAEQDLPF CKGDVLTIVA VTKDPNWYKA KNKVGREGII
PANYVQKREG VKAGTKLSLM PWFHGKITRE QAERLLYPPE TGLFLVREST NYPGDYTLCV
SCEGKVEHYR IMYHASKLSI DEEVYFENLM QLVEHYTTDA DGLCTRLIKP KVMEGTVAAQ
DEFYRSGWAL NMKELKLLQT IGKGEFGDVM LGDYRGNKVA VKCIKNDATA QAFLAEASVM
TQLRHSNLVQ LLGVIVEEKG GLYIVTEYMA KGSLVDYLRS RGRSVLGGDC LLKFSLDVCE
AMEYLEGNNF VHRDLAARNV LVSEDNVAKV SDFGLTKEAS STQDTGKLPV KWTAPEALRE
KKFSTKSDVW SFGILLWEIY SFGRVPYPRI PLKDVVPRVE KGYKMDAPDG CPPAVYEVMK
NCWHLDAATR PTFLQLREQL EHIKTHELHL


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U1915h CLIA kit Agammaglobulinaemia tyrosine kinase,AGMX1,ATK,ATK,B-cell progenitor kinase,BPK,BPK,Bruton tyrosine kinase,BTK,Homo sapiens,Human,Tyrosine-protein kinase BTK 96T
E1915h ELISA kit Agammaglobulinaemia tyrosine kinase,AGMX1,ATK,ATK,B-cell progenitor kinase,BPK,BPK,Bruton tyrosine kinase,BTK,Homo sapiens,Human,Tyrosine-protein kinase BTK 96T
E1915h ELISA Agammaglobulinaemia tyrosine kinase,AGMX1,ATK,ATK,B-cell progenitor kinase,BPK,BPK,Bruton tyrosine kinase,BTK,Homo sapiens,Human,Tyrosine-protein kinase BTK 96T
U1915h CLIA Agammaglobulinaemia tyrosine kinase,AGMX1,ATK,ATK,B-cell progenitor kinase,BPK,BPK,Bruton tyrosine kinase,BTK,Homo sapiens,Human,Tyrosine-protein kinase BTK 96T
EIAAB33009 Chicken,Gallus gallus,Inactive tyrosine-protein kinase 7,Kinase-like protein,KLG,Protein-tyrosine kinase 7,Pseudo tyrosine kinase receptor 7,PTK7,Tyrosine-protein kinase-like 7
EIAAB44680 BYK,DTK,Homo sapiens,Human,RSE,SKY,TYRO3,Tyrosine-protein kinase byk,Tyrosine-protein kinase DTK,Tyrosine-protein kinase receptor TYRO3,Tyrosine-protein kinase RSE,Tyrosine-protein kinase SKY
18-661-15209 Tyrosine-protein kinase BTK - EC 2.7.10.2; Bruton tyrosine kinase; Agammaglobulinaemia tyrosine kinase; ATK; B cell progenitor kinase; BPK Polyclonal 0.1 mg
U2227h CLIA BMX,Bone marrow tyrosine kinase gene in chromosome X protein,Cytoplasmic tyrosine-protein kinase BMX,Epithelial and endothelial tyrosine kinase,ETK,Homo sapiens,Human,NTK38 96T
E2227h ELISA BMX,Bone marrow tyrosine kinase gene in chromosome X protein,Cytoplasmic tyrosine-protein kinase BMX,Epithelial and endothelial tyrosine kinase,ETK,Homo sapiens,Human,NTK38 96T
U2227h CLIA kit BMX,Bone marrow tyrosine kinase gene in chromosome X protein,Cytoplasmic tyrosine-protein kinase BMX,Epithelial and endothelial tyrosine kinase,ETK,Homo sapiens,Human,NTK38 96T
E2227h ELISA kit BMX,Bone marrow tyrosine kinase gene in chromosome X protein,Cytoplasmic tyrosine-protein kinase BMX,Epithelial and endothelial tyrosine kinase,ETK,Homo sapiens,Human,NTK38 96T
E2227h BMX,Bone marrow tyrosine kinase gene in chromosome X protein,Cytoplasmic tyrosine-protein kinase BMX,Epithelial and endothelial tyrosine kinase,ETK,Homo sapiens,Human,NTK38
EIAAB13100 EK6,ELK,ELK,EPH tyrosine kinase 2,EPHB1,EPH-like kinase 6,Ephrin type-B receptor 1,EPHT2,hEK6,HEK6,Homo sapiens,Human,NET,NET,Neuronally-expressed EPH-related tyrosine kinase,Tyrosine-protein kinase r
10-782-55014 Cytoplasmic tyrosine-protein kinase BMX - EC 2.7.10.2; Bone marrow tyrosine kinase gene in chromosome X protein; Epithelial and endothelial tyrosine kinase; ETK; NTK38 N_A 0.01 mg
10-782-55014 Cytoplasmic tyrosine-protein kinase BMX - EC 2.7.10.2; Bone marrow tyrosine kinase gene in chromosome X protein; Epithelial and endothelial tyrosine kinase; ETK; NTK38 N_A 0.005 mg
10-782-55014 Cytoplasmic tyrosine-protein kinase BMX - EC 2.7.10.2; Bone marrow tyrosine kinase gene in chromosome X protein; Epithelial and endothelial tyrosine kinase; ETK; NTK38 N_A 0.001 mg
10-782-55014 Cytoplasmic tyrosine-protein kinase BMX - EC 2.7.10.2; Bone marrow tyrosine kinase gene in chromosome X protein; Epithelial and endothelial tyrosine kinase; ETK; NTK38 N_A 0.02 mg
EIAAB14369 CADTK,CAK-beta,Calcium-dependent tyrosine kinase,Cell adhesion kinase beta,FADK 2,Fak2,Focal adhesion kinase 2,Proline-rich tyrosine kinase 2,Protein-tyrosine kinase 2-beta,Ptk2b,Pyk2,Rat,Rattus norve


 

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