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Tyrosine-protein kinase Lck (EC 2.7.10.2) (Leukocyte C-terminal Src kinase) (LSK) (Lymphocyte cell-specific protein-tyrosine kinase) (Protein YT16) (Proto-oncogene Lck) (T cell-specific protein-tyrosine kinase) (p56-LCK)

 LCK_HUMAN               Reviewed;         509 AA.
P06239; D3DPP8; P07100; Q12850; Q13152; Q5TDH8; Q5TDH9; Q7RTZ3;
Q96DW4; Q9NYT8;
01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 6.
30-AUG-2017, entry version 233.
RecName: Full=Tyrosine-protein kinase Lck;
EC=2.7.10.2;
AltName: Full=Leukocyte C-terminal Src kinase;
Short=LSK;
AltName: Full=Lymphocyte cell-specific protein-tyrosine kinase;
AltName: Full=Protein YT16;
AltName: Full=Proto-oncogene Lck;
AltName: Full=T cell-specific protein-tyrosine kinase;
AltName: Full=p56-LCK;
Name=LCK;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=3493153; DOI=10.1002/eji.1830161229;
Koga Y., Caccia N., Toyonaga B., Spolski R., Yanagi Y., Yoshikai Y.,
Mak T.W.;
"A human T cell-specific cDNA clone (YT16) encodes a protein with
extensive homology to a family of protein-tyrosine kinases.";
Eur. J. Immunol. 16:1643-1646(1986).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=3265417; DOI=10.1002/jcb.240380206;
Perlmutter R.M., Marth J.D., Lewis D.B., Peet R., Ziegler S.F.,
Wilson C.B.;
"Structure and expression of lck transcripts in human lymphoid
cells.";
J. Cell. Biochem. 38:117-126(1988).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2558056; DOI=10.1016/0378-1119(89)90144-3;
Rouer E., van Huynh T., de Souza S.L., Lang M.C., Fischer S.,
Benarous R.;
"Structure of the human lck gene: differences in genomic organisation
within src-related genes affect only N-terminal exons.";
Gene 84:105-113(1989).
[4]
NUCLEOTIDE SEQUENCE [MRNA], VARIANTS LEU-28; GLN-LYS-PRO-232 INS;
VAL-353 AND LEU-447, AND PHOSPHORYLATION AT TYR-394 AND TYR-505.
TISSUE=Leukemia;
PubMed=8139546; DOI=10.1128/MCB.14.4.2429;
Wright D.D., Sefton B.M., Kamps M.P.;
"Oncogenic activation of the Lck protein accompanies translocation of
the LCK gene in the human HSB2 T-cell leukemia.";
Mol. Cell. Biol. 14:2429-2437(1994).
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT), AND ALTERNATIVE SPLICING.
TISSUE=Leukemic T-cell;
PubMed=7495859; DOI=10.1016/0167-4781(95)00162-A;
Vogel L.B., Arthur R., Fujita D.J.;
"An aberrant lck mRNA in two human T-cell lines.";
Biochim. Biophys. Acta 1264:168-172(1995).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=12401726; DOI=10.2337/diabetes.51.11.3326;
Nervi S., Nicodeme S., Gartioux C., Atlan C., Lathrop M., Reviron D.,
Naquet P., Matsuda F., Imbert J., Vialettes B.;
"No association between lck gene polymorphisms and protein level in
type 1 diabetes.";
Diabetes 51:3326-3330(2002).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
TISSUE=Lymph;
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).
[10]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-35.
PubMed=2850479; DOI=10.1128/MCB.8.8.3058;
Garvin A.M., Pawar S., Marth J.D., Perlmutter R.M.;
"Structure of the murine lck gene and its rearrangement in a murine
lymphoma cell line.";
Mol. Cell. Biol. 8:3058-3064(1988).
[11]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-35.
PubMed=2787474; DOI=10.1128/MCB.9.5.2173;
Takadera T., Leung S., Gernone A., Koga Y., Takihara Y.,
Miyamoto N.G., Mak T.W.;
"Structure of the two promoters of the human lck gene: differential
accumulation of two classes of lck transcripts in T cells.";
Mol. Cell. Biol. 9:2173-2180(1989).
[12]
NUCLEOTIDE SEQUENCE [MRNA] OF 14-509.
TISSUE=Peripheral blood lymphocyte;
PubMed=11009097;
DOI=10.1002/1521-4141(200009)30:9<2632::AID-IMMU2632>3.0.CO;2-C;
Boncristiano M., Majolini M.B., D'Elios M.M., Pacini S., Valensin S.,
Ulivieri C., Amedei A., Falini B., Del Prete G., Telford J.L.,
Baldari C.T.;
"Defective recruitment and activation of ZAP-70 in common variable
immunodeficiency patients with T cell defects.";
Eur. J. Immunol. 30:2632-2638(2000).
[13]
NUCLEOTIDE SEQUENCE [MRNA] OF 368-509.
PubMed=2835736;
Veillette A., Foss F.M., Sausville E.A., Bolen J.B., Rosen N.;
"Expression of the lck tyrosine kinase gene in human colon carcinoma
and other non-lymphoid human tumor cell lines.";
Oncogene Res. 1:357-374(1987).
[14]
NUCLEOTIDE SEQUENCE [MRNA] OF 375-509.
PubMed=3489486; DOI=10.1016/0167-4889(86)90228-4;
Trevillyan J.M., Lin Y., Chen S.J., Phillips C.A., Canna C.,
Linna T.J.;
"Human T lymphocytes express a protein-tyrosine kinase homologous to
p56LSTRA.";
Biochim. Biophys. Acta 888:286-295(1986).
[15]
PHOSPHORYLATION AT TYR-505.
PubMed=1639064;
Bergman M., Mustelin T., Oetken C., Partanen J., Flint N.A.,
Amrein K.E., Autero M., Burn P., Alitalo K.;
"The human p50csk tyrosine kinase phosphorylates p56lck at Tyr-505 and
down regulates its catalytic activity.";
EMBO J. 11:2919-2924(1992).
[16]
INTERACTION WITH PI3K.
PubMed=7504174; DOI=10.1128/MCB.13.12.7408;
Vogel L.B., Fujita D.J.;
"The SH3 domain of p56lck is involved in binding to
phosphatidylinositol 3'-kinase from T lymphocytes.";
Mol. Cell. Biol. 13:7408-7417(1993).
[17]
INTERACTION WITH KHDRBS1.
PubMed=7852312; DOI=10.1074/jbc.270.6.2506;
Vogel L.B., Fujita D.J.;
"p70 phosphorylation and binding to p56lck is an early event in
interleukin-2-induced onset of cell cycle progression in T-
lymphocytes.";
J. Biol. Chem. 270:2506-2511(1995).
[18]
INTERACTION WITH SQSTM1, AND MUTAGENESIS OF SER-59 AND ARG-154.
PubMed=8618896; DOI=10.1073/pnas.92.26.12338;
Park I., Chung J., Walsh C.T., Yun Y., Strominger J.L., Shin J.;
"Phosphotyrosine-independent binding of a 62-kDa protein to the src
homology 2 (SH2) domain of p56lck and its regulation by
phosphorylation of Ser-59 in the lck unique N-terminal region.";
Proc. Natl. Acad. Sci. U.S.A. 92:12338-12342(1995).
[19]
PHOSPHORYLATION AT TYR-505 BY CSK, AND AUTOPHOSPHORYLATION.
PubMed=8631775; DOI=10.1074/jbc.271.13.7465;
Bougeret C., Delaunay T., Romero F., Jullien P., Sabe H., Hanafusa H.,
Benarous R., Fischer S.;
"Detection of a physical and functional interaction between Csk and
Lck which involves the SH2 domain of Csk and is mediated by
autophosphorylation of Lck on tyrosine 394.";
J. Biol. Chem. 271:7465-7472(1996).
[20]
INTERACTION WITH HIV-1 NEF.
PubMed=8794306;
Greenway A.L., Azad A., Mills J., McPhee D.A.;
"Human immunodeficiency virus type 1 Nef binds directly to LCK and
mitogen-activated protein kinase, inhibiting kinase activity.";
J. Virol. 70:6701-6708(1996).
[21]
INTERACTION WITH AXL.
PubMed=9178760; DOI=10.1038/sj.onc.1201123;
Braunger J., Schleithoff L., Schulz A.S., Kessler H., Lammers R.,
Ullrich A., Bartram C.R., Janssen J.W.;
"Intracellular signaling of the Ufo/Axl receptor tyrosine kinase is
mediated mainly by a multi-substrate docking-site.";
Oncogene 14:2619-2631(1997).
[22]
REVIEW.
PubMed=10848956; DOI=10.1046/j.1432-1327.2000.01412.x;
Isakov N., Biesinger B.;
"Lck protein tyrosine kinase is a key regulator of T-cell activation
and a target for signal intervention by Herpesvirus saimiri and other
viral gene products.";
Eur. J. Biochem. 267:3413-3421(2000).
[23]
SUBCELLULAR LOCATION.
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).
[24]
MASS SPECTROMETRY.
TISSUE=Mammary cancer;
PubMed=11840567;
DOI=10.1002/1615-9861(200202)2:2<212::AID-PROT212>3.0.CO;2-H;
Harris R.A., Yang A., Stein R.C., Lucy K., Brusten L., Herath A.,
Parekh R., Waterfield M.D., O'Hare M.J., Neville M.A., Page M.J.,
Zvelebil M.J.;
"Cluster analysis of an extensive human breast cancer cell line
protein expression map database.";
Proteomics 2:212-223(2002).
[25]
INTERACTION WITH LIME1.
PubMed=14610046; DOI=10.1084/jem.20031484;
Brdickova N., Brdicka T., Angelisova P., Horvath O., Spicka J.,
Hilgert I., Paces J., Simeoni L., Kliche S., Merten C., Schraven B.,
Horejsi V.;
"LIME: a new membrane raft-associated adaptor protein involved in CD4
and CD8 coreceptor signaling.";
J. Exp. Med. 198:1453-1462(2003).
[26]
INTERACTION WITH LIME1.
PubMed=14610044; DOI=10.1084/jem.20030232;
Hur E.M., Son M., Lee O.-H., Choi Y.B., Park C., Lee H., Yun Y.;
"LIME, a novel transmembrane adaptor protein, associates with p56lck
and mediates T cell activation.";
J. Exp. Med. 198:1463-1473(2003).
[27]
INTERACTION WITH PTPRH.
PubMed=12837766; DOI=10.1074/jbc.M300648200;
Ito T., Okazawa H., Maruyama K., Tomizawa K., Motegi S., Ohnishi H.,
Kuwano H., Kosugi A., Matozaki T.;
"Interaction of SAP-1, a transmembrane-type protein-tyrosine
phosphatase, with the tyrosine kinase Lck. Roles in regulation of T
cell function.";
J. Biol. Chem. 278:34854-34863(2003).
[28]
INTERACTION WITH UNC119.
PubMed=14757743; DOI=10.1084/jem.20030589;
Gorska M.M., Stafford S.J., Cen O., Sur S., Alam R.;
"Unc119, a novel activator of Lck/Fyn, is essential for T cell
activation.";
J. Exp. Med. 199:369-379(2004).
[29]
FUNCTION IN PHOSPHORYLATION OF ZAP70.
PubMed=16339550; DOI=10.4049/jimmunol.175.12.8123;
Gelkop S., Gish G.D., Babichev Y., Pawson T., Isakov N.;
"T cell activation-induced CrkII binding to the Zap70 protein tyrosine
kinase is mediated by Lck-dependent phosphorylation of Zap70 tyrosine
315.";
J. Immunol. 175:8123-8132(2005).
[30]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-505, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=15592455; DOI=10.1038/nbt1046;
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
Zha X.-M., Polakiewicz R.D., Comb M.J.;
"Immunoaffinity profiling of tyrosine phosphorylation in cancer
cells.";
Nat. Biotechnol. 23:94-101(2005).
[31]
DEPHOSPHORYLATION BY PTN22.
PubMed=16461343; DOI=10.1074/jbc.M600498200;
Wu J., Katrekar A., Honigberg L.A., Smith A.M., Conn M.T., Tang J.,
Jeffery D., Mortara K., Sampang J., Williams S.R., Buggy J.,
Clark J.M.;
"Identification of substrates of human protein-tyrosine phosphatase
PTPN22.";
J. Biol. Chem. 281:11002-11010(2006).
[32]
FUNCTION IN PHOSPHORYLATION OF TYROBP.
PubMed=16709819; DOI=10.4049/jimmunol.176.11.6615;
Mason L.H., Willette-Brown J., Taylor L.S., McVicar D.W.;
"Regulation of Ly49D/DAP12 signal transduction by Src-family kinases
and CD45.";
J. Immunol. 176:6615-6623(2006).
[33]
INTERACTION WITH EPHA1; PTK2B AND PI3-KINASE.
PubMed=17634955; DOI=10.1002/eji.200737111;
Hjorthaug H.S., Aasheim H.C.;
"Ephrin-A1 stimulates migration of CD8+CCR7+ T lymphocytes.";
Eur. J. Immunol. 37:2326-2336(2007).
[34]
INTERACTION WITH CEACAM1.
PubMed=18424730; DOI=10.4049/jimmunol.180.9.6085;
Chen Z., Chen L., Qiao S.W., Nagaishi T., Blumberg R.S.;
"Carcinoembryonic antigen-related cell adhesion molecule 1 inhibits
proximal TCR signaling by targeting ZAP-70.";
J. Immunol. 180:6085-6093(2008).
[35]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-505, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[36]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-505, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
Mann M., Daub H.;
"Large-scale proteomics analysis of the human kinome.";
Mol. Cell. Proteomics 8:1751-1764(2009).
[37]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-102; THR-159; SER-162;
SER-194 AND TYR-505, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[38]
FUNCTION IN PHOSPHORYLATION OF RUNX3.
PubMed=20100835; DOI=10.1074/jbc.M109.071381;
Goh Y.M., Cinghu S., Hong E.T., Lee Y.S., Kim J.H., Jang J.W.,
Li Y.H., Chi X.Z., Lee K.S., Wee H., Ito Y., Oh B.C., Bae S.C.;
"Src kinase phosphorylates RUNX3 at tyrosine residues and localizes
the protein in the cytoplasm.";
J. Biol. Chem. 285:10122-10129(2010).
[39]
FUNCTION IN PTK2B/PYK2 PHOSPHORYLATION.
PubMed=20028775; DOI=10.1189/jlb.0409227;
Collins M., Tremblay M., Chapman N., Curtiss M., Rothman P.B.,
Houtman J.C.;
"The T cell receptor-mediated phosphorylation of Pyk2 tyrosines 402
and 580 occurs via a distinct mechanism than other receptor systems.";
J. Leukoc. Biol. 87:691-701(2010).
[40]
FUNCTION IN PHOSPHORYLATION OF RHOH.
PubMed=20851766; DOI=10.1016/j.cellsig.2010.09.009;
Wang H., Zeng X., Fan Z., Lim B.;
"RhoH modulates pre-TCR and TCR signalling by regulating LCK.";
Cell. Signal. 23:249-258(2011).
[41]
FUNCTION IN TCR SIGNALING, PHOSPHORYLATION, AND DEPHOSPHORYLATION AT
TYR-394 BY PTPN2.
PubMed=22080863; DOI=10.1172/JCI59492;
Wiede F., Shields B.J., Chew S.H., Kyparissoudis K., van Vliet C.,
Galic S., Tremblay M.L., Russell S.M., Godfrey D.I., Tiganis T.;
"T cell protein tyrosine phosphatase attenuates T cell signaling to
maintain tolerance in mice.";
J. Clin. Invest. 121:4758-4774(2011).
[42]
FUNCTION IN PHOSPHORYLATION OF MAPT.
PubMed=21269457; DOI=10.1186/1750-1326-6-12;
Scales T.M., Derkinderen P., Leung K.Y., Byers H.L., Ward M.A.,
Price C., Bird I.N., Perera T., Kellie S., Williamson R.,
Anderton B.H., Reynolds C.H.;
"Tyrosine phosphorylation of tau by the SRC family kinases lck and
fyn.";
Mol. Neurodegener. 6:12-12(2011).
[43]
ENZYME REGULATION.
PubMed=21917715; DOI=10.1126/scisignal.2001893;
Schoenborn J.R., Tan Y.X., Zhang C., Shokat K.M., Weiss A.;
"Feedback circuits monitor and adjust Basal lck-dependent events in T
cell receptor signaling.";
Sci. Signal. 4:RA59-RA59(2011).
[44]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-505, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[45]
INTERACTION WITH HERPES SIMPLEX VIRUS 1 UL46.
PubMed=23946459; DOI=10.1128/JVI.01702-13;
Strunk U., Saffran H.A., Wu F.W., Smiley J.R.;
"Role of herpes simplex virus VP11/12 tyrosine-based motifs in binding
and activation of the Src family kinase Lck and recruitment of p85,
Grb2, and Shc.";
J. Virol. 87:11276-11286(2013).
[46]
INTERACTION WITH ARAP AND FYB.
PubMed=27335501; DOI=10.4049/jimmunol.1501913;
Jung S.H., Yoo E.H., Yu M.J., Song H.M., Kang H.Y., Cho J.Y.,
Lee J.R.;
"ARAP, a novel adaptor protein, is required for TCR signaling and
integrin-mediated adhesion.";
J. Immunol. 197:942-952(2016).
[47]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 53-226.
PubMed=7512222; DOI=10.1038/368764a0;
Eck M.J., Atweell S.K., Shoelson S.E., Harrison S.C.;
"Structure of the regulatory domains of the Src-family tyrosine kinase
Lck.";
Nature 368:764-769(1994).
[48]
X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 127-221.
PubMed=7532720; DOI=10.1006/jmbi.1994.0089;
Mikol V., Baumann G., Keller T.H., Manning U.M., Zurini M.G.M.;
"The crystal structures of the SH2 domain of p56lck complexed with two
phosphonopeptides suggest a gated peptide binding site.";
J. Mol. Biol. 246:344-355(1995).
[49]
X-RAY CRYSTALLOGRAPHY (1.0 ANGSTROMS) OF 122-226.
PubMed=8604142; DOI=10.1006/jmbi.1996.0112;
Tong L., Warren T.C., King J., Betageri R., Rose J., Jakes S.;
"Crystal structures of the human p56lck SH2 domain in complex with two
short phosphotyrosyl peptides at 1.0-A and 1.8-A resolution.";
J. Mol. Biol. 256:601-610(1996).
[50]
X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 231-501.
PubMed=8945479; DOI=10.1038/384484a0;
Yamaguchi H., Hendrickson W.A.;
"Structural basis for activation of human lymphocyte kinase Lck upon
tyrosine phosphorylation.";
Nature 384:484-489(1996).
[51]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 119-226.
PubMed=9685372; DOI=10.1074/jbc.273.32.20238;
Tong L., Warren T.C., Lukas S., Schembri-King J., Betageri R.,
Proudfoot J.R., Jakes S.;
"Carboxymethyl-phenylalanine as a replacement for phosphotyrosine in
SH2 domain binding.";
J. Biol. Chem. 273:20238-20242(1998).
[52]
VARIANT IMD22 PRO-341.
PubMed=22985903; DOI=10.1016/j.jaci.2012.07.029;
Hauck F., Randriamampita C., Martin E., Gerart S., Lambert N., Lim A.,
Soulier J., Maciorowski Z., Touzot F., Moshous D., Quartier P.,
Heritier S., Blanche S., Rieux-Laucat F., Brousse N., Callebaut I.,
Veillette A., Hivroz C., Fischer A., Latour S., Picard C.;
"Primary T-cell immunodeficiency with immunodysregulation caused by
autosomal recessive LCK deficiency.";
J. Allergy Clin. Immunol. 130:1144-1152(2012).
-!- FUNCTION: Non-receptor tyrosine-protein kinase that plays an
essential role in the selection and maturation of developing T-
cells in the thymus and in the function of mature T-cells. Plays a
key role in T-cell antigen receptor (TCR)-linked signal
transduction pathways. Constitutively associated with the
cytoplasmic portions of the CD4 and CD8 surface receptors.
Association of the TCR with a peptide antigen-bound MHC complex
facilitates the interaction of CD4 and CD8 with MHC class II and
class I molecules, respectively, thereby recruiting the associated
LCK protein to the vicinity of the TCR/CD3 complex. LCK then
phosphorylates tyrosine residues within the immunoreceptor
tyrosine-based activation motifs (ITAM) of the cytoplasmic tails
of the TCR-gamma chains and CD3 subunits, initiating the TCR/CD3
signaling pathway. Once stimulated, the TCR recruits the tyrosine
kinase ZAP70, that becomes phosphorylated and activated by LCK.
Following this, a large number of signaling molecules are
recruited, ultimately leading to lymphokine production. LCK also
contributes to signaling by other receptor molecules. Associates
directly with the cytoplasmic tail of CD2, which leads to
hyperphosphorylation and activation of LCK. Also plays a role in
the IL2 receptor-linked signaling pathway that controls the T-cell
proliferative response. Binding of IL2 to its receptor results in
increased activity of LCK. Is expressed at all stages of thymocyte
development and is required for the regulation of maturation
events that are governed by both pre-TCR and mature alpha beta
TCR. Phosphorylates other substrates including RUNX3, PTK2B/PYK2,
the microtubule-associated protein MAPT, RHOH or TYROBP. Interacts
with ARAP (PubMed:27335501). {ECO:0000269|PubMed:16339550,
ECO:0000269|PubMed:16709819, ECO:0000269|PubMed:20028775,
ECO:0000269|PubMed:20100835, ECO:0000269|PubMed:20851766,
ECO:0000269|PubMed:21269457, ECO:0000269|PubMed:22080863,
ECO:0000269|PubMed:27335501}.
-!- CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a
[protein]-L-tyrosine phosphate. {ECO:0000255|PROSITE-
ProRule:PRU10028}.
-!- ENZYME REGULATION: The relative activities of the inhibitory
tyrosine-protein kinase CSK and the activating tyrosine-protein
phosphatase PTPRC/CD45 determine the level of LCK activity. These
interactions allow rapid and efficient activation of LCK in
response to TCR stimulation. {ECO:0000269|PubMed:21917715}.
-!- SUBUNIT: Binds to the cytoplasmic domain of cell surface
receptors, such as AXL, CD2, CD4, CD5, CD8, CD44, CD45 and CD122.
Also binds to effector molecules, such as PI4K, VAV1, RASA1, FYB
and to other protein kinases including CDK1, RAF1, ZAP70 and SYK.
Binds to phosphatidylinositol 3'-kinase (PI3K) from T-lymphocytes
through its SH3 domain and to the tyrosine phosphorylated form of
KHDRBS1/p70 through its SH2 domain. Binds to HIV-1 Nef through its
SH3 domain. This interaction inhibits its tyrosine-kinase
activity. Interacts with herpes simplex virus 1 UL46; this
interaction activates LCK. Interacts with SQSTM1. Interacts with
phosphorylated LIME1. Interacts with CBLB and PTPRH. Interacts
with RUNX3. Forms a signaling complex with EPHA1, PTK2B AND PI3-
KINASE; upon activation by EFNA1 which may regulate T-lymphocyte
migration. Associates with ZAP70 and RHOH; these interactions
allow LCK-mediated RHOH and CD3 subunit phosphorylation in the
presence of functional ZAP70. Interacts with UNC119; this
interaction plays a crucial role in activation of LCK. Interacts
with CEACAM1 (via cytoplasmic domain); mediates CEACAM1
phosphorylation resulting in PTPN6 recruitment that
dephosphorylates TCR stimulation-induced CD247 and ZAP70
(PubMed:18424730). {ECO:0000269|PubMed:12837766,
ECO:0000269|PubMed:14610044, ECO:0000269|PubMed:14610046,
ECO:0000269|PubMed:14757743, ECO:0000269|PubMed:17634955,
ECO:0000269|PubMed:18424730, ECO:0000269|PubMed:23946459,
ECO:0000269|PubMed:7504174, ECO:0000269|PubMed:7852312,
ECO:0000269|PubMed:8618896, ECO:0000269|PubMed:8794306,
ECO:0000269|PubMed:9178760}.
-!- INTERACTION:
Self; NbExp=3; IntAct=EBI-1348, EBI-1348;
P22575:- (xeno); NbExp=7; IntAct=EBI-1348, EBI-866709;
Q9YJQ8:- (xeno); NbExp=2; IntAct=EBI-1348, EBI-7709835;
Q13444:ADAM15; NbExp=3; IntAct=EBI-1348, EBI-77818;
P10275:AR; NbExp=7; IntAct=EBI-1348, EBI-608057;
P20749:BCL3; NbExp=3; IntAct=EBI-1348, EBI-958997;
P01730:CD4; NbExp=2; IntAct=EBI-1348, EBI-353826;
Q5VV42:CDKAL1; NbExp=3; IntAct=EBI-1348, EBI-10194801;
Q13480:GAB1; NbExp=10; IntAct=EBI-1348, EBI-517684;
P08238:HSP90AB1; NbExp=2; IntAct=EBI-1348, EBI-352572;
Q07666:KHDRBS1; NbExp=5; IntAct=EBI-1348, EBI-1364;
P10721:KIT; NbExp=8; IntAct=EBI-1348, EBI-1379503;
O43561:LAT; NbExp=2; IntAct=EBI-1348, EBI-1222766;
Q9BRK4:LZTS2; NbExp=3; IntAct=EBI-1348, EBI-741037;
Q9H204:MED28; NbExp=4; IntAct=EBI-1348, EBI-514199;
P08581:MET; NbExp=3; IntAct=EBI-1348, EBI-1039152;
P04150:NR3C1; NbExp=3; IntAct=EBI-1348, EBI-493507;
Q04759:PRKCQ; NbExp=2; IntAct=EBI-1348, EBI-374762;
Q9Y2R2:PTPN22; NbExp=6; IntAct=EBI-1348, EBI-1211241;
P29350:PTPN6; NbExp=5; IntAct=EBI-1348, EBI-78260;
P08575:PTPRC; NbExp=7; IntAct=EBI-1348, EBI-1341;
Q9NP31:SH2D2A; NbExp=12; IntAct=EBI-1348, EBI-490630;
P43405:SYK; NbExp=7; IntAct=EBI-1348, EBI-78302;
P0CG48:UBC; NbExp=2; IntAct=EBI-1348, EBI-3390054;
P43403:ZAP70; NbExp=2; IntAct=EBI-1348, EBI-1211276;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12218089}.
Cell membrane {ECO:0000269|PubMed:12218089}; Lipid-anchor
{ECO:0000269|PubMed:12218089}; Cytoplasmic side
{ECO:0000269|PubMed:12218089}. Note=Present in lipid rafts in an
inactive form.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=Long;
IsoId=P06239-1; Sequence=Displayed;
Name=Short;
IsoId=P06239-2; Sequence=VSP_005000, VSP_005001;
Note=No experimental confirmation available.;
Name=3;
IsoId=P06239-3; Sequence=VSP_016049;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Expressed specifically in lymphoid cells.
-!- DOMAIN: The SH2 domain mediates interaction with SQSTM1.
Interaction is regulated by Ser-59 phosphorylation.
-!- PTM: Autophosphorylated on Tyr-394, increasing enzymatic activity,
this site is dephosphorylated by PTN22. Phosphorylated on Tyr-505
by CSK, decreasing activity. Dephosphorylated by PTPRC/CD45.
Dephosphorylation at Tyr-394 by PTPN2 negatively regulates T-cell
receptor signaling. {ECO:0000269|PubMed:1639064,
ECO:0000269|PubMed:22080863, ECO:0000269|PubMed:8139546,
ECO:0000269|PubMed:8631775}.
-!- PTM: Myristoylation is required prior to palmitoylation.
{ECO:0000250}.
-!- PTM: Palmitoylation regulates subcellular location. {ECO:0000250}.
-!- MASS SPECTROMETRY: Mass=57869.42; Method=MALDI; Range=2-509;
Evidence={ECO:0000269|PubMed:11840567};
-!- DISEASE: Note=A chromosomal aberration involving LCK is found in
leukemias. Translocation t(1;7)(p34;q34) with TCRB.
-!- DISEASE: Immunodeficiency 22 (IMD22) [MIM:615758]: A primary
immunodeficiency characterized by T-cell dysfunction. Affected
individuals present with lymphopenia, recurrent infections, severe
diarrhea, and failure to thrive. {ECO:0000269|PubMed:22985903}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
kinase family. SRC subfamily. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
-!- SEQUENCE CAUTION:
Sequence=CAI22320.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=CAI22321.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/LCKID14ch1p34.html";
-!- WEB RESOURCE: Name=Wikipedia; Note=Lck entry;
URL="https://en.wikipedia.org/wiki/Lck";
-----------------------------------------------------------------------
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EMBL; X05027; CAA28691.1; -; mRNA.
EMBL; X13529; CAA31884.1; -; mRNA.
EMBL; M36881; AAA59502.1; -; mRNA.
EMBL; X14055; CAA32211.1; -; Genomic_DNA.
EMBL; X14053; CAA32211.1; JOINED; Genomic_DNA.
EMBL; X14054; CAA32211.1; JOINED; Genomic_DNA.
EMBL; U07236; AAA18225.1; -; mRNA.
EMBL; U23852; AAC50287.1; -; mRNA.
EMBL; BN000073; CAD55807.1; -; Genomic_DNA.
EMBL; AL121991; CAI22320.1; ALT_INIT; Genomic_DNA.
EMBL; AL121991; CAI22321.1; ALT_INIT; Genomic_DNA.
EMBL; CH471059; EAX07543.1; -; Genomic_DNA.
EMBL; CH471059; EAX07546.1; -; Genomic_DNA.
EMBL; BC013200; AAH13200.1; -; mRNA.
EMBL; M21510; AAA59501.1; ALT_TERM; Genomic_DNA.
EMBL; M26692; AAA59503.1; -; Genomic_DNA.
EMBL; AF228313; AAF34794.1; -; mRNA.
EMBL; X06369; CAA29667.1; -; mRNA.
EMBL; X04476; CAA28165.1; -; mRNA.
CCDS; CCDS359.1; -. [P06239-1]
PIR; JQ0152; OKHULK.
RefSeq; NP_001036236.1; NM_001042771.2. [P06239-1]
RefSeq; NP_005347.3; NM_005356.4. [P06239-1]
UniGene; Hs.470627; -.
PDB; 1BHF; X-ray; 1.80 A; A=119-226.
PDB; 1BHH; X-ray; 1.90 A; A=119-226, B=124-226.
PDB; 1CWD; X-ray; 2.25 A; L=127-222.
PDB; 1CWE; X-ray; 2.30 A; A/C=127-222.
PDB; 1FBZ; X-ray; 2.40 A; A/B=123-226.
PDB; 1H92; NMR; -; A=59-120.
PDB; 1IJR; X-ray; 2.20 A; A=124-226.
PDB; 1KIK; NMR; -; A=64-120.
PDB; 1LCJ; X-ray; 1.80 A; A=119-226.
PDB; 1LCK; X-ray; 2.50 A; A=53-226, B=502-509.
PDB; 1LKK; X-ray; 1.00 A; A=122-226.
PDB; 1LKL; X-ray; 1.80 A; A=123-226.
PDB; 1Q68; NMR; -; B=7-35.
PDB; 1Q69; NMR; -; B=7-35.
PDB; 1QPC; X-ray; 1.60 A; A=231-509.
PDB; 1QPD; X-ray; 2.00 A; A=231-509.
PDB; 1QPE; X-ray; 2.00 A; A=231-509.
PDB; 1QPJ; X-ray; 2.20 A; A=231-509.
PDB; 1X27; X-ray; 2.70 A; A/B/C/D/E/F=64-226.
PDB; 2IIM; X-ray; 1.00 A; A=59-119.
PDB; 2OF2; X-ray; 2.00 A; A=231-501.
PDB; 2OF4; X-ray; 2.70 A; A=231-501.
PDB; 2OFU; X-ray; 2.00 A; A=229-501.
PDB; 2OFV; X-ray; 2.00 A; A/B=232-498.
PDB; 2OG8; X-ray; 2.30 A; A/B=237-499.
PDB; 2PL0; X-ray; 2.80 A; A=225-509.
PDB; 2ZM1; X-ray; 2.10 A; A=225-509.
PDB; 2ZM4; X-ray; 2.70 A; A=225-509.
PDB; 2ZYB; X-ray; 2.55 A; A=225-509.
PDB; 3AC1; X-ray; 1.99 A; A=225-509.
PDB; 3AC2; X-ray; 2.10 A; A=225-509.
PDB; 3AC3; X-ray; 2.55 A; A=225-509.
PDB; 3AC4; X-ray; 2.70 A; A=225-509.
PDB; 3AC5; X-ray; 2.50 A; A=225-509.
PDB; 3AC8; X-ray; 2.30 A; A=225-509.
PDB; 3ACJ; X-ray; 2.20 A; A=225-509.
PDB; 3ACK; X-ray; 2.60 A; A=225-509.
PDB; 3AD4; X-ray; 2.20 A; A=225-509.
PDB; 3AD5; X-ray; 2.00 A; A=225-509.
PDB; 3AD6; X-ray; 2.15 A; A=225-509.
PDB; 3B2W; X-ray; 2.30 A; A=226-502.
PDB; 3BRH; X-ray; 2.20 A; C/D=391-397.
PDB; 3BYM; X-ray; 2.00 A; A=230-501.
PDB; 3BYO; X-ray; 2.00 A; A=231-501.
PDB; 3BYS; X-ray; 2.20 A; A=225-501.
PDB; 3BYU; X-ray; 2.30 A; A=225-501.
PDB; 3KMM; X-ray; 2.80 A; A=229-509.
PDB; 3KXZ; X-ray; 2.37 A; A=225-509.
PDB; 3LCK; X-ray; 1.70 A; A=231-501.
PDB; 3MPM; X-ray; 1.95 A; A=237-501.
PDB; 4C3F; X-ray; 1.72 A; A=237-501.
PDB; 4D8K; X-ray; 2.36 A; A=53-226.
PDB; 5MTM; X-ray; 2.40 A; A=118-231.
PDB; 5MTN; X-ray; 2.85 A; A=118-231.
PDBsum; 1BHF; -.
PDBsum; 1BHH; -.
PDBsum; 1CWD; -.
PDBsum; 1CWE; -.
PDBsum; 1FBZ; -.
PDBsum; 1H92; -.
PDBsum; 1IJR; -.
PDBsum; 1KIK; -.
PDBsum; 1LCJ; -.
PDBsum; 1LCK; -.
PDBsum; 1LKK; -.
PDBsum; 1LKL; -.
PDBsum; 1Q68; -.
PDBsum; 1Q69; -.
PDBsum; 1QPC; -.
PDBsum; 1QPD; -.
PDBsum; 1QPE; -.
PDBsum; 1QPJ; -.
PDBsum; 1X27; -.
PDBsum; 2IIM; -.
PDBsum; 2OF2; -.
PDBsum; 2OF4; -.
PDBsum; 2OFU; -.
PDBsum; 2OFV; -.
PDBsum; 2OG8; -.
PDBsum; 2PL0; -.
PDBsum; 2ZM1; -.
PDBsum; 2ZM4; -.
PDBsum; 2ZYB; -.
PDBsum; 3AC1; -.
PDBsum; 3AC2; -.
PDBsum; 3AC3; -.
PDBsum; 3AC4; -.
PDBsum; 3AC5; -.
PDBsum; 3AC8; -.
PDBsum; 3ACJ; -.
PDBsum; 3ACK; -.
PDBsum; 3AD4; -.
PDBsum; 3AD5; -.
PDBsum; 3AD6; -.
PDBsum; 3B2W; -.
PDBsum; 3BRH; -.
PDBsum; 3BYM; -.
PDBsum; 3BYO; -.
PDBsum; 3BYS; -.
PDBsum; 3BYU; -.
PDBsum; 3KMM; -.
PDBsum; 3KXZ; -.
PDBsum; 3LCK; -.
PDBsum; 3MPM; -.
PDBsum; 4C3F; -.
PDBsum; 4D8K; -.
PDBsum; 5MTM; -.
PDBsum; 5MTN; -.
ProteinModelPortal; P06239; -.
SMR; P06239; -.
BioGrid; 110124; 89.
DIP; DIP-553N; -.
ELM; P06239; -.
IntAct; P06239; 73.
MINT; MINT-110378; -.
STRING; 9606.ENSP00000337825; -.
BindingDB; P06239; -.
ChEMBL; CHEMBL258; -.
DrugBank; DB06925; 3-(2-AMINOQUINAZOLIN-6-YL)-4-METHYL-N-[3-(TRIFLUOROMETHYL)PHENYL]BENZAMIDE.
DrugBank; DB01254; Dasatinib.
DrugBank; DB09079; Nintedanib.
DrugBank; DB04395; Phosphoaminophosphonic Acid-Adenylate Ester.
DrugBank; DB08901; Ponatinib.
DrugBank; DB02010; Staurosporine.
GuidetoPHARMACOLOGY; 2053; -.
iPTMnet; P06239; -.
PhosphoSitePlus; P06239; -.
SwissPalm; P06239; -.
BioMuta; LCK; -.
DMDM; 125474; -.
EPD; P06239; -.
MaxQB; P06239; -.
PaxDb; P06239; -.
PeptideAtlas; P06239; -.
PRIDE; P06239; -.
DNASU; 3932; -.
Ensembl; ENST00000333070; ENSP00000328213; ENSG00000182866. [P06239-3]
Ensembl; ENST00000336890; ENSP00000337825; ENSG00000182866. [P06239-1]
Ensembl; ENST00000619559; ENSP00000477713; ENSG00000182866. [P06239-1]
GeneID; 3932; -.
KEGG; hsa:3932; -.
UCSC; uc001bux.3; human. [P06239-1]
CTD; 3932; -.
DisGeNET; 3932; -.
GeneCards; LCK; -.
H-InvDB; HIX0019954; -.
HGNC; HGNC:6524; LCK.
HPA; CAB003816; -.
HPA; HPA003494; -.
MalaCards; LCK; -.
MIM; 153390; gene.
MIM; 615758; phenotype.
neXtProt; NX_P06239; -.
OpenTargets; ENSG00000182866; -.
Orphanet; 280142; Severe combined immunodeficiency due to LCK deficiency.
PharmGKB; PA30307; -.
eggNOG; KOG0197; Eukaryota.
eggNOG; COG0515; LUCA.
GeneTree; ENSGT00760000118938; -.
HOVERGEN; HBG008761; -.
InParanoid; P06239; -.
KO; K05856; -.
OMA; NPEDDWM; -.
OrthoDB; EOG091G0D46; -.
PhylomeDB; P06239; -.
TreeFam; TF351634; -.
BRENDA; 2.7.10.2; 2681.
Reactome; R-HSA-114604; GPVI-mediated activation cascade.
Reactome; R-HSA-1257604; PIP3 activates AKT signaling.
Reactome; R-HSA-1433557; Signaling by SCF-KIT.
Reactome; R-HSA-1433559; Regulation of KIT signaling.
Reactome; R-HSA-164944; Nef and signal transduction.
Reactome; R-HSA-167590; Nef Mediated CD4 Down-regulation.
Reactome; R-HSA-202424; Downstream TCR signaling.
Reactome; R-HSA-202427; Phosphorylation of CD3 and TCR zeta chains.
Reactome; R-HSA-202430; Translocation of ZAP-70 to Immunological synapse.
Reactome; R-HSA-202433; Generation of second messenger molecules.
Reactome; R-HSA-210990; PECAM1 interactions.
Reactome; R-HSA-2219530; Constitutive Signaling by Aberrant PI3K in Cancer.
Reactome; R-HSA-2424491; DAP12 signaling.
Reactome; R-HSA-389356; CD28 co-stimulation.
Reactome; R-HSA-389357; CD28 dependent PI3K/Akt signaling.
Reactome; R-HSA-389359; CD28 dependent Vav1 pathway.
Reactome; R-HSA-389513; CTLA4 inhibitory signaling.
Reactome; R-HSA-389948; PD-1 signaling.
Reactome; R-HSA-451927; Interleukin-2 signaling.
Reactome; R-HSA-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
SignaLink; P06239; -.
SIGNOR; P06239; -.
ChiTaRS; LCK; human.
EvolutionaryTrace; P06239; -.
GeneWiki; Lck; -.
GenomeRNAi; 3932; -.
PRO; PR:P06239; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000182866; -.
CleanEx; HS_LCK; -.
ExpressionAtlas; P06239; baseline and differential.
Genevisible; P06239; HS.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; IBA:GO_Central.
GO; GO:0001772; C:immunological synapse; IDA:MGI.
GO; GO:0045121; C:membrane raft; IDA:UniProtKB.
GO; GO:0000242; C:pericentriolar material; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:BHF-UCL.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0051117; F:ATPase binding; IPI:UniProtKB.
GO; GO:0042609; F:CD4 receptor binding; IPI:UniProtKB.
GO; GO:0042610; F:CD8 receptor binding; IPI:UniProtKB.
GO; GO:0001948; F:glycoprotein binding; IPI:UniProtKB.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0016301; F:kinase activity; TAS:Reactome.
GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IBA:GO_Central.
GO; GO:0043548; F:phosphatidylinositol 3-kinase binding; IPI:UniProtKB.
GO; GO:0046934; F:phosphatidylinositol-4,5-bisphosphate 3-kinase activity; TAS:Reactome.
GO; GO:0001784; F:phosphotyrosine residue binding; IPI:CAFA.
GO; GO:0008022; F:protein C-terminus binding; IPI:UniProtKB.
GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
GO; GO:0019903; F:protein phosphatase binding; IPI:UniProtKB.
GO; GO:0004722; F:protein serine/threonine phosphatase activity; IDA:UniProtKB.
GO; GO:0004713; F:protein tyrosine kinase activity; IDA:UniProtKB.
GO; GO:0042169; F:SH2 domain binding; IPI:UniProtKB.
GO; GO:0042608; F:T cell receptor binding; IPI:CAFA.
GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; IDA:UniProtKB.
GO; GO:0050853; P:B cell receptor signaling pathway; IBA:GO_Central.
GO; GO:0016477; P:cell migration; IBA:GO_Central.
GO; GO:0006882; P:cellular zinc ion homeostasis; IEP:UniProtKB.
GO; GO:0030097; P:hemopoiesis; NAS:UniProtKB.
GO; GO:0045087; P:innate immune response; IBA:GO_Central.
GO; GO:0050900; P:leukocyte migration; TAS:Reactome.
GO; GO:0038083; P:peptidyl-tyrosine autophosphorylation; IBA:GO_Central.
GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; IMP:CAFA.
GO; GO:0048015; P:phosphatidylinositol-mediated signaling; TAS:Reactome.
GO; GO:0030168; P:platelet activation; TAS:Reactome.
GO; GO:2001244; P:positive regulation of intrinsic apoptotic signaling pathway; IMP:UniProtKB.
GO; GO:0050870; P:positive regulation of T cell activation; IDA:UniProtKB.
GO; GO:0050862; P:positive regulation of T cell receptor signaling pathway; NAS:UniProtKB.
GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
GO; GO:0042127; P:regulation of cell proliferation; IBA:GO_Central.
GO; GO:0050690; P:regulation of defense response to virus by virus; TAS:Reactome.
GO; GO:0051249; P:regulation of lymphocyte activation; NAS:UniProtKB.
GO; GO:0014066; P:regulation of phosphatidylinositol 3-kinase signaling; TAS:Reactome.
GO; GO:0051209; P:release of sequestered calcium ion into cytosol; ISS:UniProtKB.
GO; GO:0042493; P:response to drug; IDA:UniProtKB.
GO; GO:0031295; P:T cell costimulation; TAS:Reactome.
GO; GO:0030217; P:T cell differentiation; IMP:UniProtKB.
GO; GO:0050852; P:T cell receptor signaling pathway; TAS:Reactome.
GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA:GO_Central.
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;
3D-structure; Alternative splicing; ATP-binding; Cell membrane;
Chromosomal rearrangement; Complete proteome; Cytoplasm;
Disease mutation; Host-virus interaction; Kinase; Lipoprotein;
Membrane; Myristate; Nucleotide-binding; Palmitate; Phosphoprotein;
Polymorphism; Proto-oncogene; Reference proteome; SH2 domain;
SH3 domain; Transferase; Tyrosine-protein kinase.
INIT_MET 1 1 Removed.
CHAIN 2 509 Tyrosine-protein kinase Lck.
/FTId=PRO_0000088124.
DOMAIN 61 121 SH3. {ECO:0000255|PROSITE-
ProRule:PRU00192}.
DOMAIN 127 224 SH2. {ECO:0000255|PROSITE-
ProRule:PRU00191}.
DOMAIN 245 498 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 251 259 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
REGION 2 72 Interactions with CD4 and CD8.
{ECO:0000250}.
REGION 154 242 Interaction with PTPRH.
{ECO:0000269|PubMed:12837766}.
ACT_SITE 364 364 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10028}.
BINDING 273 273 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 102 102 Phosphoserine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 159 159 Phosphothreonine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 162 162 Phosphoserine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 192 192 Phosphotyrosine.
{ECO:0000250|UniProtKB:P06240}.
MOD_RES 194 194 Phosphoserine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 394 394 Phosphotyrosine; by autocatalysis.
{ECO:0000269|PubMed:8139546}.
MOD_RES 505 505 Phosphotyrosine; by CSK.
{ECO:0000244|PubMed:15592455,
ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:19369195,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:21406692,
ECO:0000269|PubMed:1639064,
ECO:0000269|PubMed:8139546,
ECO:0000269|PubMed:8631775}.
LIPID 2 2 N-myristoyl glycine. {ECO:0000250}.
LIPID 3 3 S-palmitoyl cysteine. {ECO:0000250}.
LIPID 5 5 S-palmitoyl cysteine. {ECO:0000250}.
VAR_SEQ 321 321 N -> NDTLLDSQLEEKGLGASPWGNLGQQLLLLPT (in
isoform 3).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_016049.
VAR_SEQ 348 363 IAEGMAFIEERNYIHR -> VRRLGRGAGQGNRPVT (in
isoform Short).
{ECO:0000303|PubMed:7495859}.
/FTId=VSP_005000.
VAR_SEQ 364 509 Missing (in isoform Short).
{ECO:0000303|PubMed:7495859}.
/FTId=VSP_005001.
VARIANT 28 28 V -> L (found in leukemia).
{ECO:0000269|PubMed:8139546}.
/FTId=VAR_013463.
VARIANT 201 201 G -> S (in dbSNP:rs11567841).
/FTId=VAR_051697.
VARIANT 232 232 P -> PQKP (in leukemia).
/FTId=VAR_013464.
VARIANT 341 341 L -> P (in IMD22; dbSNP:rs587777335).
{ECO:0000269|PubMed:22985903}.
/FTId=VAR_071291.
VARIANT 353 353 A -> V (found in leukemia).
{ECO:0000269|PubMed:8139546}.
/FTId=VAR_013465.
VARIANT 447 447 P -> L (found in leukemia).
{ECO:0000269|PubMed:8139546}.
/FTId=VAR_013466.
MUTAGEN 59 59 S->E: Allows interaction with SQSTM1.
{ECO:0000269|PubMed:8618896}.
MUTAGEN 154 154 R->K: No effect on interaction with
SQSTM1. {ECO:0000269|PubMed:8618896}.
CONFLICT 29 29 P -> R (in Ref. 2; AAA59502).
{ECO:0000305}.
CONFLICT 35 35 T -> R (in Ref. 2; AAA59502).
{ECO:0000305}.
CONFLICT 87 87 Q -> P (in Ref. 2; CAA31884/AAA59502).
{ECO:0000305}.
CONFLICT 206 211 VRHYTN -> ASAITPI (in Ref. 1; CAA28691).
{ECO:0000305}.
CONFLICT 254 254 G -> A (in Ref. 2; AAA59502).
{ECO:0000305}.
CONFLICT 258 267 EVWMGYYNGH -> RCGWGTTTGT (in Ref. 1;
CAA28691). {ECO:0000305}.
CONFLICT 282 286 PDAFL -> AGRLP (in Ref. 1; CAA28691).
{ECO:0000305}.
CONFLICT 375 375 T -> A (in Ref. 14; CAA28165).
{ECO:0000305}.
CONFLICT 472 472 L -> H (in Ref. 13; CAA29667).
{ECO:0000305}.
CONFLICT 504 509 QYQPQP -> STA (in Ref. 1; CAA28691).
{ECO:0000305}.
HELIX 12 15 {ECO:0000244|PDB:1Q68}.
STRAND 21 23 {ECO:0000244|PDB:1Q68}.
STRAND 24 27 {ECO:0000244|PDB:1Q69}.
TURN 60 63 {ECO:0000244|PDB:2IIM}.
STRAND 65 70 {ECO:0000244|PDB:2IIM}.
STRAND 76 79 {ECO:0000244|PDB:4D8K}.
STRAND 87 92 {ECO:0000244|PDB:2IIM}.
STRAND 95 102 {ECO:0000244|PDB:2IIM}.
TURN 103 105 {ECO:0000244|PDB:2IIM}.
STRAND 108 112 {ECO:0000244|PDB:2IIM}.
HELIX 113 115 {ECO:0000244|PDB:2IIM}.
STRAND 116 118 {ECO:0000244|PDB:2IIM}.
STRAND 128 131 {ECO:0000244|PDB:1CWD}.
HELIX 134 141 {ECO:0000244|PDB:1LKK}.
STRAND 151 155 {ECO:0000244|PDB:1LKK}.
STRAND 157 159 {ECO:0000244|PDB:1LKK}.
STRAND 163 171 {ECO:0000244|PDB:1LKK}.
TURN 172 174 {ECO:0000244|PDB:1LKK}.
STRAND 175 185 {ECO:0000244|PDB:1LKK}.
TURN 187 189 {ECO:0000244|PDB:1LCJ}.
STRAND 191 194 {ECO:0000244|PDB:1LKK}.
STRAND 199 201 {ECO:0000244|PDB:1LKK}.
HELIX 202 211 {ECO:0000244|PDB:1LKK}.
STRAND 216 218 {ECO:0000244|PDB:1LKK}.
TURN 233 235 {ECO:0000244|PDB:1QPC}.
STRAND 237 239 {ECO:0000244|PDB:1QPE}.
HELIX 242 244 {ECO:0000244|PDB:1QPC}.
STRAND 245 254 {ECO:0000244|PDB:1QPC}.
STRAND 257 264 {ECO:0000244|PDB:1QPC}.
TURN 265 267 {ECO:0000244|PDB:1QPC}.
STRAND 268 275 {ECO:0000244|PDB:1QPC}.
TURN 277 279 {ECO:0000244|PDB:1QPD}.
HELIX 282 294 {ECO:0000244|PDB:1QPC}.
STRAND 303 307 {ECO:0000244|PDB:1QPC}.
STRAND 309 311 {ECO:0000244|PDB:1QPC}.
STRAND 313 317 {ECO:0000244|PDB:1QPC}.
HELIX 324 327 {ECO:0000244|PDB:1QPC}.
HELIX 331 334 {ECO:0000244|PDB:1QPC}.
HELIX 338 357 {ECO:0000244|PDB:1QPC}.
HELIX 367 369 {ECO:0000244|PDB:1QPC}.
STRAND 370 372 {ECO:0000244|PDB:1QPC}.
STRAND 378 380 {ECO:0000244|PDB:1QPC}.
HELIX 383 385 {ECO:0000244|PDB:1QPE}.
HELIX 386 389 {ECO:0000244|PDB:3B2W}.
STRAND 390 392 {ECO:0000244|PDB:1QPC}.
STRAND 393 395 {ECO:0000244|PDB:4C3F}.
TURN 404 406 {ECO:0000244|PDB:1QPC}.
HELIX 409 414 {ECO:0000244|PDB:1QPC}.
HELIX 419 434 {ECO:0000244|PDB:1QPC}.
TURN 435 437 {ECO:0000244|PDB:1QPC}.
HELIX 446 454 {ECO:0000244|PDB:1QPC}.
HELIX 467 476 {ECO:0000244|PDB:1QPC}.
HELIX 481 483 {ECO:0000244|PDB:1QPC}.
HELIX 487 500 {ECO:0000244|PDB:1QPC}.
SEQUENCE 509 AA; 58001 MW; 44BFF0D43FFB420D CRC64;
MGCGCSSHPE DDWMENIDVC ENCHYPIVPL DGKGTLLIRN GSEVRDPLVT YEGSNPPASP
LQDNLVIALH SYEPSHDGDL GFEKGEQLRI LEQSGEWWKA QSLTTGQEGF IPFNFVAKAN
SLEPEPWFFK NLSRKDAERQ LLAPGNTHGS FLIRESESTA GSFSLSVRDF DQNQGEVVKH
YKIRNLDNGG FYISPRITFP GLHELVRHYT NASDGLCTRL SRPCQTQKPQ KPWWEDEWEV
PRETLKLVER LGAGQFGEVW MGYYNGHTKV AVKSLKQGSM SPDAFLAEAN LMKQLQHQRL
VRLYAVVTQE PIYIITEYME NGSLVDFLKT PSGIKLTINK LLDMAAQIAE GMAFIEERNY
IHRDLRAANI LVSDTLSCKI ADFGLARLIE DNEYTAREGA KFPIKWTAPE AINYGTFTIK
SDVWSFGILL TEIVTHGRIP YPGMTNPEVI QNLERGYRMV RPDNCPEELY QLMRLCWKER
PEDRPTFDYL RSVLEDFFTA TEGQYQPQP


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