GENTAUR Belgium BVBA BE0473327336 Voortstraat 49, 1910 Kampenhout BELGIUM Tel 0032 16 58 90 45
GENTAUR U.S.A Genprice Inc,Logistics 547 Yurok Circle, SanJose, CA 95123
Tel (408) 780-0908, Fax (408) 780-0908, [email protected]

Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, Gentaur another in time delivery

Tyrosine-protein kinase HCK (EC 2.7.10.2) (Hematopoietic cell kinase) (Hemopoietic cell kinase) (p59-HCK/p60-HCK) (p59Hck) (p61Hck)

 HCK_HUMAN               Reviewed;         526 AA.
P08631; A8K1I1; B4DQB6; E1P5M2; Q29RX1; Q2VPE2; Q504R5; Q5T7K1; Q5T7K2;
Q96CC0; Q9H5Y5; Q9NUA4; Q9UMJ5;
01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 5.
11-DEC-2019, entry version 249.
RecName: Full=Tyrosine-protein kinase HCK;
EC=2.7.10.2;
AltName: Full=Hematopoietic cell kinase;
AltName: Full=Hemopoietic cell kinase;
AltName: Full=p59-HCK/p60-HCK;
AltName: Full=p59Hck;
AltName: Full=p61Hck;
Name=HCK;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=3496523; DOI=10.1128/mcb.7.6.2267;
Quintrell N., Lebo R., Varmus H., Bishop J.M., Pettenati M.J.,
le Beau M.M., Diaz M.O., Rowley J.D.;
"Identification of a human gene (HCK) that encodes a protein-tyrosine
kinase and is expressed in hemopoietic cells.";
Mol. Cell. Biol. 7:2267-2275(1987).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND TISSUE SPECIFICITY.
PubMed=3453117; DOI=10.1128/mcb.7.6.2276;
Ziegler S.F., Marth J.D., Lewis D.B., Perlmutter R.M.;
"Novel protein-tyrosine kinase gene (hck) preferentially expressed in cells
of hematopoietic origin.";
Mol. Cell. Biol. 7:2276-2285(1987).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 4), AND VARIANT
LEU-105.
TISSUE=Corpus callosum, and Ileal mucosa;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=11780052; DOI=10.1038/414865a;
Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
"The DNA sequence and comparative analysis of human chromosome 20.";
Nature 414:865-871(2001).
[5]
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.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
TISSUE=B-cell, and 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).
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-21 (ISOFORM 1), AND ALTERNATIVE INITIATION.
TISSUE=Bone marrow;
PubMed=1875927; DOI=10.1128/mcb.11.9.4363;
Lock P., Ralph S., Stanley E., Boulet I., Ramsay R., Dunn A.R.;
"Two isoforms of murine hck, generated by utilization of alternative
translational initiation codons, exhibit different patterns of subcellular
localization.";
Mol. Cell. Biol. 11:4363-4370(1991).
[8]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 178-526.
TISSUE=Spleen;
PubMed=1572549; DOI=10.1016/0378-1119(92)90407-g;
Hradetzky D., Strebhardt K., Ruesamen-Waigmann H.;
"The genomic locus of the human hemopoietic-specific cell protein tyrosine
kinase (PTK)-encoding gene (HCK) confirms conservation of exon-intron
structure among human PTKs of the src family.";
Gene 113:275-280(1992).
[9]
INTERACTION WITH FCGR2A, CATALYTIC ACTIVITY, AND FUNCTION IN
PHOSPHORYLATION OF FCGR2A.
PubMed=8132624;
Ghazizadeh S., Bolen J.B., Fleit H.B.;
"Physical and functional association of Src-related protein tyrosine
kinases with Fc gamma RII in monocytic THP-1 cells.";
J. Biol. Chem. 269:8878-8884(1994).
[10]
INTERACTION WITH FCGR1A, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, AND
PHOSPHORYLATION.
PubMed=8064233; DOI=10.1084/jem.180.3.1165;
Wang A.V., Scholl P.R., Geha R.S.;
"Physical and functional association of the high affinity immunoglobulin G
receptor (Fc gamma RI) with the kinases Hck and Lyn.";
J. Exp. Med. 180:1165-1170(1994).
[11]
FUNCTION IN FCGR1A SIGNALING, CATALYTIC ACTIVITY, AUTOPHOSPHORYLATION, AND
ACTIVITY REGULATION.
PubMed=7535819;
Durden D.L., Kim H.M., Calore B., Liu Y.;
"The Fc gamma RI receptor signals through the activation of hck and MAP
kinase.";
J. Immunol. 154:4039-4047(1995).
[12]
SUBCELLULAR LOCATION, ALTERNATIVE INITIATION, MYRISTOYLATION AT GLY-2,
MYRISTOYLATION AT GLY-2 (ISOFORM 2), PALMITOYLATION AT CYS-3 (ISOFORM 2),
AND MUTAGENESIS OF GLY-3; GLY-23 AND CYS-24.
PubMed=7791757; DOI=10.1128/mcb.15.7.3507;
Robbins S.M., Quintrell N.A., Bishop J.M.;
"Myristoylation and differential palmitoylation of the HCK protein-tyrosine
kinases govern their attachment to membranes and association with
caveolae.";
Mol. Cell. Biol. 15:3507-3515(1995).
[13]
FUNCTION, ACTIVITY REGULATION, PHOSPHORYLATION, AND INTERACTION WITH IL6ST.
PubMed=9406996;
Hallek M., Neumann C., Schaffer M., Danhauser-Riedl S., von Bubnoff N.,
de Vos G., Druker B.J., Yasukawa K., Griffin J.D., Emmerich B.;
"Signal transduction of interleukin-6 involves tyrosine phosphorylation of
multiple cytosolic proteins and activation of Src-family kinases Fyn, Hck,
and Lyn in multiple myeloma cell lines.";
Exp. Hematol. 25:1367-1377(1997).
[14]
INDUCTION, SUBCELLULAR LOCATION, CATALYTIC ACTIVITY, AND TISSUE
SPECIFICITY.
PubMed=8995234; DOI=10.1074/jbc.272.1.102;
Welch H., Maridonneau-Parini I.;
"Hck is activated by opsonized zymosan and A23187 in distinct subcellular
fractions of human granulocytes.";
J. Biol. Chem. 272:102-109(1997).
[15]
ACTIVITY REGULATION, AND INTERACTION WITH HIV-1 NEF (MICROBIAL INFECTION).
PubMed=9218412; DOI=10.1074/jbc.272.29.17899;
Briggs S.D., Sharkey M., Stevenson M., Smithgall T.E.;
"SH3-mediated Hck tyrosine kinase activation and fibroblast transformation
by the Nef protein of HIV-1.";
J. Biol. Chem. 272:17899-17902(1997).
[16]
FUNCTION IN PHOSPHORYLATION OF BCR, AND INTERACTION WITH BCR-ABL.
PubMed=9407116; DOI=10.1074/jbc.272.52.33260;
Warmuth M., Bergmann M., Priess A., Hauslmann K., Emmerich B., Hallek M.;
"The Src family kinase Hck interacts with Bcr-Abl by a kinase-independent
mechanism and phosphorylates the Grb2-binding site of Bcr.";
J. Biol. Chem. 272:33260-33270(1997).
[17]
FUNCTION IN CBL PHOSPHORYLATION; CELL PROLIFERATION AND REGULATION OF CELL
SHAPE, CATALYTIC ACTIVITY, AUTOPHOSPHORYLATION, MUTAGENESIS OF TYR-522, AND
INTERACTION WITH CBL.
PubMed=10092522; DOI=10.1006/bbrc.1999.0427;
Howlett C.J., Bisson S.A., Resek M.E., Tigley A.W., Robbins S.M.;
"The proto-oncogene p120(Cbl) is a downstream substrate of the Hck protein-
tyrosine kinase.";
Biochem. Biophys. Res. Commun. 257:129-138(1999).
[18]
FUNCTION IN IL2 SIGNALING, CATALYTIC ACTIVITY, INDUCTION, ACTIVITY
REGULATION, AND PHOSPHORYLATION.
PubMed=10779760; DOI=10.4049/jimmunol.164.9.4575;
Bosco M.C., Curiel R.E., Zea A.H., Malabarba M.G., Ortaldo J.R.,
Espinoza-Delgado I.;
"IL-2 signaling in human monocytes involves the phosphorylation and
activation of p59hck.";
J. Immunol. 164:4575-4585(2000).
[19]
PHOSPHORYLATION AT TYR-411 AND TYR-522, IDENTIFICATION BY MASS
SPECTROMETRY, ACTIVITY REGULATION, AND MUTAGENESIS OF GLU-305 AND TYR-411.
PubMed=10644735; DOI=10.1074/jbc.275.4.2721;
Porter M., Schindler T., Kuriyan J., Miller W.T.;
"Reciprocal regulation of Hck activity by phosphorylation of Tyr(527) and
Tyr(416). Effect of introducing a high affinity intramolecular SH2
ligand.";
J. Biol. Chem. 275:2721-2726(2000).
[20]
FUNCTION IN IL8-MEDIATED DEGRANULATION, ACTIVITY REGULATION, AND
INTERACTION WITH ARRB1 AND ARRB2.
PubMed=10973280; DOI=10.1038/79767;
Barlic J., Andrews J.D., Kelvin A.A., Bosinger S.E., DeVries M.E., Xu L.,
Dobransky T., Feldman R.D., Ferguson S.S., Kelvin D.J.;
"Regulation of tyrosine kinase activation and granule release through beta-
arrestin by CXCRI.";
Nat. Immunol. 1:227-233(2000).
[21]
INTERACTION WITH HIV-1 VIF (MICROBIAL INFECTION).
PubMed=11278465; DOI=10.1074/jbc.m009076200;
Hassaine G., Courcoul M., Bessou G., Barthalay Y., Picard C., Olive D.,
Collette Y., Vigne R., Decroly E.;
"The tyrosine kinase Hck is an inhibitor of HIV-1 replication counteracted
by the viral vif protein.";
J. Biol. Chem. 276:16885-16893(2001).
[22]
INTERACTION WITH HEV ORF3 PROTEIN (MICROBIAL INFECTION).
PubMed=11518702; DOI=10.1074/jbc.m101546200;
Korkaya H., Jameel S., Gupta D., Tyagi S., Kumar R., Zafrullah M.,
Mazumdar M., Lal S.K., Xiaofang L., Sehgal D., Das S.R., Sahal D.;
"The ORF3 protein of hepatitis E virus binds to Src homology 3 domains and
activates MAPK.";
J. Biol. Chem. 276:42389-42400(2001).
[23]
FUNCTION AS EFFECTOR OF THE BCR-ABL FUSION PROTEIN IN PHOSPHORYLATION OF
STAT5B, INTERACTION WITH STAT5B AND THE BCR-ABL FUSION PROTEIN, AND
PHOSPHORYLATION.
PubMed=12411494; DOI=10.1093/emboj/cdf562;
Klejman A., Schreiner S.J., Nieborowska-Skorska M., Slupianek A.,
Wilson M., Smithgall T.E., Skorski T.;
"The Src family kinase Hck couples BCR/ABL to STAT5 activation in myeloid
leukemia cells.";
EMBO J. 21:5766-5774(2002).
[24]
INTERACTION WITH ADAM15, AND FUNCTION IN PHOSPHORYLATION OF ADAM15.
PubMed=11741929; DOI=10.1074/jbc.m107430200;
Poghosyan Z., Robbins S.M., Houslay M.D., Webster A., Murphy G.,
Edwards D.R.;
"Phosphorylation-dependent interactions between ADAM15 cytoplasmic domain
and Src family protein-tyrosine kinases.";
J. Biol. Chem. 277:4999-5007(2002).
[25]
FUNCTION IN REORGANIZATION OF THE ACTIN CYTOSKELETON; FORMATION OF CELL
PROTRUSIONS AND PHAGOCYTOSIS (ISOFORM 2), SUBCELLULAR LOCATION (ISOFORM 2),
AND MUTAGENESIS OF GLY-3.
PubMed=11904303; DOI=10.1074/jbc.m201212200;
Carreno S., Caron E., Cougoule C., Emorine L.J., Maridonneau-Parini I.;
"p59Hck isoform induces F-actin reorganization to form protrusions of the
plasma membrane in a Cdc42- and Rac-dependent manner.";
J. Biol. Chem. 277:21007-21016(2002).
[26]
FUNCTION IN CELL PROLIFERATION, UBIQUITINATION, PHOSPHORYLATION AT TYR-51;
TYR-411 AND TYR-522, SUBCELLULAR LOCATION, INTERACTION WITH CBL (ISOFORM
2), AND MUTAGENESIS OF LYS-290 AND TYR-522.
PubMed=11896602; DOI=10.1038/sj.onc.1205228;
Howlett C.J., Robbins S.M.;
"Membrane-anchored Cbl suppresses Hck protein-tyrosine kinase mediated
cellular transformation.";
Oncogene 21:1707-1716(2002).
[27]
FUNCTION IN IL6 SIGNALING CASCADE AND IN PHOSPHORYLATION OF GAB1 AND GAB2.
PubMed=15010462; DOI=10.1074/jbc.m305783200;
Podar K., Mostoslavsky G., Sattler M., Tai Y.T., Hayashi T., Catley L.P.,
Hideshima T., Mulligan R.C., Chauhan D., Anderson K.C.;
"Critical role for hematopoietic cell kinase (Hck)-mediated phosphorylation
of Gab1 and Gab2 docking proteins in interleukin 6-induced proliferation
and survival of multiple myeloma cells.";
J. Biol. Chem. 279:21658-21665(2004).
[28]
FUNCTION IN PHOSPHORYLATION OF ELMO1, AND INTERACTION WITH ELMO1.
PubMed=15952790; DOI=10.1021/bi0500832;
Yokoyama N., deBakker C.D., Zappacosta F., Huddleston M.J., Annan R.S.,
Ravichandran K.S., Miller W.T.;
"Identification of tyrosine residues on ELMO1 that are phosphorylated by
the Src-family kinase Hck.";
Biochemistry 44:8841-8849(2005).
[29]
FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
ASP-381.
PubMed=15998323; DOI=10.1111/j.1600-0854.2005.00307.x;
Cougoule C., Carreno S., Castandet J., Labrousse A., Astarie-Dequeker C.,
Poincloux R., Le Cabec V., Maridonneau-Parini I.;
"Activation of the lysosome-associated p61Hck isoform triggers the
biogenesis of podosomes.";
Traffic 6:682-694(2005).
[30]
INTERACTION WITH HIV-1 NEF (MICROBIAL INFECTION), AND ACTIVITY REGULATION.
PubMed=16849330; DOI=10.1074/jbc.m601128200;
Trible R.P., Emert-Sedlak L., Smithgall T.E.;
"HIV-1 Nef selectively activates Src family kinases Hck, Lyn, and c-Src
through direct SH3 domain interaction.";
J. Biol. Chem. 281:27029-27038(2006).
[31]
FUNCTION IN PHOSPHORYLATION AND INHIBITION OF TP73 ACTIVITY, SUBCELLULAR
LOCATION, AND INTERACTION WITH TP73 AND YAP1.
PubMed=17535448; DOI=10.1186/1471-2199-8-45;
Paliwal P., Radha V., Swarup G.;
"Regulation of p73 by Hck through kinase-dependent and independent
mechanisms.";
BMC Mol. Biol. 8:45-45(2007).
[32]
FUNCTION, AND INTERACTION WITH IL6ST.
PubMed=17310994; DOI=10.1038/sj.onc.1210306;
Hausherr A., Tavares R., Schaffer M., Obermeier A., Miksch C., Mitina O.,
Ellwart J., Hallek M., Krause G.;
"Inhibition of IL-6-dependent growth of myeloma cells by an acidic peptide
repressing the gp130-mediated activation of Src family kinases.";
Oncogene 26:4987-4998(2007).
[33]
INTERACTION WITH FASLG.
PubMed=19807924; DOI=10.1186/1471-2172-10-53;
Voss M., Lettau M., Janssen O.;
"Identification of SH3 domain interaction partners of human FasL (CD178) by
phage display screening.";
BMC Immunol. 10:53-53(2009).
[34]
FUNCTION IN REORGANIZATION OF ACTIN CYTOSKELETON AND CELL PROLIFERATION,
AND ROLE IN DISEASE.
PubMed=19114024; DOI=10.1016/j.ejca.2008.11.020;
Poincloux R., Al Saati T., Maridonneau-Parini I., Le Cabec V.;
"The oncogenic activity of the Src family kinase Hck requires the
cooperative action of the plasma membrane- and lysosome-associated
isoforms.";
Eur. J. Cancer 45:321-327(2009).
[35]
INTERACTION WITH ADAM15.
PubMed=19718658; DOI=10.1002/jcb.22317;
Kleino I., Ortiz R.M., Yritys M., Huovila A.P., Saksela K.;
"Alternative splicing of ADAM15 regulates its interactions with cellular
SH3 proteins.";
J. Cell. Biochem. 108:877-885(2009).
[36]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-202 AND SER-462, 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]
FUNCTION IN ABL1-MEDIATED CELL MIGRATION, AND IDENTIFICATION IN A COMPLEX
WITH ITGB1 AND WITH ABL1.
PubMed=19903482; DOI=10.1016/j.febslet.2009.11.009;
Baruzzi A., Iacobucci I., Soverini S., Lowell C.A., Martinelli G.,
Berton G.;
"c-Abl and Src-family kinases cross-talk in regulation of myeloid cell
migration.";
FEBS Lett. 584:15-21(2010).
[38]
ROLE IN DISEASE, AND FUNCTION IN PHOSPHORYLATION OF THE BCR-ABL FUSION
PROTEIN.
PubMed=20452982; DOI=10.1074/jbc.m109.090043;
Pene-Dumitrescu T., Smithgall T.E.;
"Expression of a Src family kinase in chronic myelogenous leukemia cells
induces resistance to imatinib in a kinase-dependent manner.";
J. Biol. Chem. 285:21446-21457(2010).
[39]
REVIEW ON ROLE IN PHAGOCYTOSIS AND SUBSTRATES.
PubMed=18538446; DOI=10.1016/j.ejcb.2008.03.008;
Guiet R., Poincloux R., Castandet J., Marois L., Labrousse A., Le Cabec V.,
Maridonneau-Parini I.;
"Hematopoietic cell kinase (Hck) isoforms and phagocyte duties - from
signaling and actin reorganization to migration and phagocytosis.";
Eur. J. Cell Biol. 87:527-542(2008).
[40]
ROLE IN NEUTROPHIL FUNCTION, AND SIGNALING.
PubMed=21338576; DOI=10.1016/j.abb.2011.02.009;
Zarbock A., Ley K.;
"Protein tyrosine kinases in neutrophil activation and recruitment.";
Arch. Biochem. Biophys. 510:112-119(2011).
[41]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-36, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
phosphoproteome.";
J. Proteomics 96:253-262(2014).
[42]
INTERACTION WITH WDCP.
PubMed=25469238; DOI=10.3892/br.2014.374;
Yokoyama N., Miller W.T.;
"Molecular characterization of WDCP, a novel fusion partner for the
anaplastic lymphoma tyrosine kinase ALK.";
Biomed. Rep. 3:9-13(2015).
[43]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[44]
STRUCTURE BY NMR OF 140-245.
PubMed=9109402; DOI=10.1016/s0014-5793(97)00255-x;
Zhang W., Smithgall T.E., Gmeiner W.H.;
"Sequential assignment and secondary structure determination for the Src
homology 2 domain of hematopoietic cellular kinase.";
FEBS Lett. 406:131-135(1997).
[45]
X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 78-526 IN COMPLEX WITH CALCIUM,
AND PHOSPHORYLATION AT TYR-522.
PubMed=9024658; DOI=10.1038/385602a0;
Sicheri F., Moarefi I., Kuriyan J.;
"Crystal structure of the Src family tyrosine kinase Hck.";
Nature 385:602-609(1997).
[46]
X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 81-137.
PubMed=9778343; DOI=10.1021/bi980989q;
Arold S., O'Brien R., Franken P., Strub M.-P., Hoh F., Dumas C.,
Ladbury J.E.;
"RT loop flexibility enhances the specificity of Src family SH3 domains for
HIV-1 Nef.";
Biochemistry 37:14683-14691(1998).
[47]
STRUCTURE BY NMR OF 72-143.
PubMed=9571048; DOI=10.1006/jmbi.1998.1690;
Horita D.A., Baldisseri D.M., Zhang W., Altieri A.S., Smithgall T.E.,
Gmeiner W.H., Byrd R.A.;
"Solution structure of the human Hck SH3 domain and identification of its
ligand binding site.";
J. Mol. Biol. 278:253-265(1998).
[48]
X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 81-522 IN COMPLEX WITH THE
PYRAZOLO PYRIMIDINE-TYPE INHIBITOR PP1, AND PHOSPHORYLATION AT TYR-522.
PubMed=10360180; DOI=10.1016/s1097-2765(00)80357-3;
Schindler T., Sicheri F., Pico A., Gazit A., Levitzki A., Kuriyan J.;
"Crystal structure of Hck in complex with a Src family-selective tyrosine
kinase inhibitor.";
Mol. Cell 3:639-648(1999).
[49]
X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 81-522 IN COMPLEXES WITH
INHIBITORS A-420983; A-641359 AND A-770041, ACTIVITY REGULATION, AND
PHOSPHORYLATION AT TYR-522.
PubMed=16216497; DOI=10.1016/j.bmcl.2005.09.039;
Burchat A., Borhani D.W., Calderwood D.J., Hirst G.C., Li B.,
Stachlewitz R.F.;
"Discovery of A-770041, a src-family selective orally active lck inhibitor
that prevents organ allograft rejection.";
Bioorg. Med. Chem. Lett. 16:118-122(2006).
[50]
X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 247-513 IN COMPLEX WITH INHIBITOR
PG-1009247.
PubMed=16997556; DOI=10.1016/j.bmcl.2006.08.132;
Sabat M., VanRens J.C., Laufersweiler M.J., Brugel T.A., Maier J.,
Golebiowski A., De B., Easwaran V., Hsieh L.C., Walter R.L., Mekel M.J.,
Evdokimov A., Janusz M.J.;
"The development of 2-benzimidazole substituted pyrimidine based inhibitors
of lymphocyte specific kinase (Lck).";
Bioorg. Med. Chem. Lett. 16:5973-5977(2006).
[51]
STRUCTURE BY NMR OF 61-140 IN COMPLEX WITH PROLINE-RICH SYNTHETIC PEPTIDE.
PubMed=17141806; DOI=10.1016/j.jmb.2006.11.013;
Schmidt H., Hoffmann S., Tran T., Stoldt M., Stangler T., Wiesehan K.,
Willbold D.;
"Solution structure of a Hck SH3 domain ligand complex reveals novel
interaction modes.";
J. Mol. Biol. 365:1517-1532(2007).
[52]
X-RAY CRYSTALLOGRAPHY (2.61 ANGSTROMS) OF 72-256, ACTIVITY REGULATION, AND
CATALYTIC ACTIVITY.
PubMed=20810664; DOI=10.1074/jbc.m110.145102;
Alvarado J.J., Betts L., Moroco J.A., Smithgall T.E., Yeh J.I.;
"Crystal structure of the Src family kinase Hck SH3-SH2 linker regulatory
region supports an SH3-dominant activation mechanism.";
J. Biol. Chem. 285:35455-35461(2010).
[53]
X-RAY CRYSTALLOGRAPHY (3.45 ANGSTROMS) OF 79-138 IN COMPLEX WITH HIV-1 NEF,
AND INTERACTION WITH HIV-1 NEF (MICROBIAL INFECTION).
PubMed=21625496; DOI=10.1371/journal.pone.0020033;
Breuer S., Schievink S.I., Schulte A., Blankenfeldt W., Fackler O.T.,
Geyer M.;
"Molecular design, functional characterization and structural basis of a
protein inhibitor against the HIV-1 pathogenicity factor Nef.";
PLoS ONE 6:E20033-E20033(2011).
[54]
X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 79-138 IN COMPLEX WITH HIV-1 NEF,
AND INTERACTION WITH HIV-1 NEF (MICROBIAL INFECTION).
PubMed=21477083; DOI=10.1111/j.1600-0854.2011.01205.x;
Horenkamp F.A., Breuer S., Schulte A., Lulf S., Weyand M., Saksela K.,
Geyer M.;
"Conformation of the dileucine-based sorting motif in HIV-1 Nef revealed by
intermolecular domain assembly.";
Traffic 12:867-877(2011).
[55]
VARIANTS [LARGE SCALE ANALYSIS] THR-44; LEU-105 AND GLY-399.
PubMed=17344846; DOI=10.1038/nature05610;
Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G.,
Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S.,
Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.,
Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K.,
Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D.,
Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R.,
Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A.,
Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F.,
Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F.,
Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G.,
Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R.,
Futreal P.A., Stratton M.R.;
"Patterns of somatic mutation in human cancer genomes.";
Nature 446:153-158(2007).
-!- FUNCTION: Non-receptor tyrosine-protein kinase found in hematopoietic
cells that transmits signals from cell surface receptors and plays an
important role in the regulation of innate immune responses, including
neutrophil, monocyte, macrophage and mast cell functions, phagocytosis,
cell survival and proliferation, cell adhesion and migration. Acts
downstream of receptors that bind the Fc region of immunoglobulins,
such as FCGR1A and FCGR2A, but also CSF3R, PLAUR, the receptors for
IFNG, IL2, IL6 and IL8, and integrins, such as ITGB1 and ITGB2. During
the phagocytic process, mediates mobilization of secretory lysosomes,
degranulation, and activation of NADPH oxidase to bring about the
respiratory burst. Plays a role in the release of inflammatory
molecules. Promotes reorganization of the actin cytoskeleton and actin
polymerization, formation of podosomes and cell protrusions. Inhibits
TP73-mediated transcription activation and TP73-mediated apoptosis.
Phosphorylates CBL in response to activation of immunoglobulin gamma Fc
region receptors. Phosphorylates ADAM15, BCR, ELMO1, FCGR2A, GAB1,
GAB2, RAPGEF1, STAT5B, TP73, VAV1 and WAS.
{ECO:0000269|PubMed:10092522, ECO:0000269|PubMed:10779760,
ECO:0000269|PubMed:10973280, ECO:0000269|PubMed:11741929,
ECO:0000269|PubMed:11896602, ECO:0000269|PubMed:12411494,
ECO:0000269|PubMed:15010462, ECO:0000269|PubMed:15952790,
ECO:0000269|PubMed:15998323, ECO:0000269|PubMed:17310994,
ECO:0000269|PubMed:17535448, ECO:0000269|PubMed:19114024,
ECO:0000269|PubMed:19903482, ECO:0000269|PubMed:20452982,
ECO:0000269|PubMed:21338576, ECO:0000269|PubMed:7535819,
ECO:0000269|PubMed:8132624, ECO:0000269|PubMed:9406996,
ECO:0000269|PubMed:9407116}.
-!- CATALYTIC ACTIVITY:
Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.2;
Evidence={ECO:0000255|PROSITE-ProRule:PRU10028,
ECO:0000269|PubMed:10092522, ECO:0000269|PubMed:10779760,
ECO:0000269|PubMed:15998323, ECO:0000269|PubMed:20810664,
ECO:0000269|PubMed:7535819, ECO:0000269|PubMed:8064233,
ECO:0000269|PubMed:8132624, ECO:0000269|PubMed:8995234};
-!- ACTIVITY REGULATION: Subject to autoinhibition, mediated by
intramolecular interactions involving the SH2 and SH3 domains. Kinase
activity is also regulated by phosphorylation at regulatory tyrosine
residues. Phosphorylation at Tyr-411 is required for optimal activity.
Phosphorylation at Tyr-522 inhibits kinase activity. Inhibited by PP1
and A-770041. {ECO:0000269|PubMed:10644735,
ECO:0000269|PubMed:10779760, ECO:0000269|PubMed:10973280,
ECO:0000269|PubMed:16216497, ECO:0000269|PubMed:16849330,
ECO:0000269|PubMed:20810664, ECO:0000269|PubMed:7535819,
ECO:0000269|PubMed:9218412, ECO:0000269|PubMed:9406996}.
-!- SUBUNIT: Interacts (via SH2 domain) with FLT3 (tyrosine
phosphorylated). Interacts with VAV1, WAS and RAPGEF1 (By similarity).
This interaction stimulates its tyrosine-kinase activity. Interacts
with ARRB1 and ARRB2. Interacts with ADAM15. Interacts with FASLG.
Interacts with CBL. Interacts with FCGR1A; the interaction may be
indirect. Interacts with IL6ST. Interacts (via SH3 domain) with ELMO1.
Interacts (via SH3 domain) with TP73. Interacts with YAP1. Interacts
with ABL1 and ITGB1, and thereby recruits ABL1 to activated ITGB1.
Interacts (via SH3 domain) with WDCP. {ECO:0000250,
ECO:0000269|PubMed:10092522, ECO:0000269|PubMed:10360180,
ECO:0000269|PubMed:10973280, ECO:0000269|PubMed:11741929,
ECO:0000269|PubMed:12411494, ECO:0000269|PubMed:15952790,
ECO:0000269|PubMed:16997556, ECO:0000269|PubMed:17141806,
ECO:0000269|PubMed:17310994, ECO:0000269|PubMed:17535448,
ECO:0000269|PubMed:19718658, ECO:0000269|PubMed:19807924,
ECO:0000269|PubMed:19903482, ECO:0000269|PubMed:25469238,
ECO:0000269|PubMed:8064233, ECO:0000269|PubMed:8132624,
ECO:0000269|PubMed:9024658, ECO:0000269|PubMed:9406996,
ECO:0000269|PubMed:9407116}.
-!- SUBUNIT: (Microbial infection) Interacts (via SH3 domain) with HEV ORF3
protein. {ECO:0000269|PubMed:11518702}.
-!- SUBUNIT: (Microbial infection) Interacts (via SH3 domain) with HIV-1
Nef and Vif. {ECO:0000269|PubMed:11278465, ECO:0000269|PubMed:16849330,
ECO:0000269|PubMed:21477083, ECO:0000269|PubMed:21625496,
ECO:0000269|PubMed:9218412}.
-!- INTERACTION:
O92972:- (xeno); NbExp=2; IntAct=EBI-346340, EBI-710506;
P27958:- (xeno); NbExp=5; IntAct=EBI-346340, EBI-706378;
Q13444:ADAM15; NbExp=3; IntAct=EBI-346340, EBI-77818;
P09917:ALOX5; NbExp=2; IntAct=EBI-346340, EBI-79934;
Q9ULH1:ASAP1; NbExp=2; IntAct=EBI-346340, EBI-346622;
P22681:CBL; NbExp=2; IntAct=EBI-9834454, EBI-518228;
P00533:EGFR; NbExp=2; IntAct=EBI-346340, EBI-297353;
Q92556:ELMO1; NbExp=4; IntAct=EBI-346340, EBI-346417;
P21860:ERBB3; NbExp=2; IntAct=EBI-346340, EBI-720706;
P17948:FLT1; NbExp=2; IntAct=EBI-346340, EBI-1026718;
O43559:FRS3; NbExp=2; IntAct=EBI-9834454, EBI-725515;
Q9HD26:GOPC; NbExp=3; IntAct=EBI-346340, EBI-349832;
Q07666:KHDRBS1; NbExp=4; IntAct=EBI-346340, EBI-1364;
P10721:KIT; NbExp=2; IntAct=EBI-346340, EBI-1379503;
Q6A162:KRT40; NbExp=3; IntAct=EBI-346340, EBI-10171697;
P60411:KRTAP10-9; NbExp=3; IntAct=EBI-346340, EBI-10172052;
Q5JR59:MTUS2; NbExp=3; IntAct=EBI-346340, EBI-742948;
P03406:nef (xeno); NbExp=2; IntAct=EBI-346340, EBI-15672419;
Q90VU7:nef (xeno); NbExp=2; IntAct=EBI-346340, EBI-7460704;
Q7Z3S9:NOTCH2NLA; NbExp=3; IntAct=EBI-346340, EBI-945833;
Q8TAK6:OLIG1; NbExp=2; IntAct=EBI-9834454, EBI-3867416;
Q13177:PAK2; NbExp=2; IntAct=EBI-346340, EBI-1045887;
Q8WUM4:PDCD6IP; NbExp=4; IntAct=EBI-346340, EBI-310624;
P42338:PIK3CB; NbExp=2; IntAct=EBI-346340, EBI-2609540;
Q92569:PIK3R3; NbExp=4; IntAct=EBI-9834454, EBI-79893;
P19174:PLCG1; NbExp=2; IntAct=EBI-346340, EBI-79387;
Q05397:PTK2; NbExp=2; IntAct=EBI-9834454, EBI-702142;
Q07889:SOS1; NbExp=4; IntAct=EBI-346340, EBI-297487;
P12504:vif (xeno); NbExp=3; IntAct=EBI-346340, EBI-779991;
P42768:WAS; NbExp=9; IntAct=EBI-346340, EBI-346375;
O43516:WIPF1; NbExp=3; IntAct=EBI-346340, EBI-346356;
-!- SUBCELLULAR LOCATION: [Isoform 1]: Lysosome. Membrane; Lipid-anchor.
Cell projection, podosome membrane; Lipid-anchor. Cytoplasm, cytosol.
Note=Associated with specialized secretory lysosomes called azurophil
granules. At least half of this isoform is found in the cytoplasm, some
of this fraction is myristoylated.
-!- SUBCELLULAR LOCATION: [Isoform 2]: Cell membrane
{ECO:0000269|PubMed:11904303}; Lipid-anchor
{ECO:0000269|PubMed:11904303}. Membrane, caveola
{ECO:0000269|PubMed:11904303}; Lipid-anchor
{ECO:0000269|PubMed:11904303}. Cell junction, focal adhesion
{ECO:0000269|PubMed:11904303}. Cytoplasm, cytoskeleton
{ECO:0000269|PubMed:11904303}. Golgi apparatus
{ECO:0000269|PubMed:11904303}. Cytoplasmic vesicle
{ECO:0000269|PubMed:11904303}. Lysosome {ECO:0000269|PubMed:11904303}.
Nucleus {ECO:0000269|PubMed:11904303}. Note=20% of this isoform is
associated with caveolae. Localization at the cell membrane and at
caveolae requires palmitoylation at Cys-3. Colocalizes with the actin
cytoskeleton at focal adhesions.
-!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle.
Cytoplasm, cytosol.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing, Alternative initiation; Named isoforms=4;
Name=1; Synonyms=p60-HCK, p61Hck;
IsoId=P08631-1; Sequence=Displayed;
Name=2; Synonyms=p59-HCK, p59Hck;
IsoId=P08631-2; Sequence=VSP_018858;
Name=3;
IsoId=P08631-3; Sequence=VSP_018858, VSP_041926;
Name=4;
IsoId=P08631-4; Sequence=VSP_041926;
-!- TISSUE SPECIFICITY: Detected in monocytes and neutrophils (at protein
level). Expressed predominantly in cells of the myeloid and B-lymphoid
lineages. Highly expressed in granulocytes. Detected in tonsil.
{ECO:0000269|PubMed:3453117, ECO:0000269|PubMed:8064233,
ECO:0000269|PubMed:8995234}.
-!- INDUCTION: Up-regulated during myeloid cell differentiation. The
highest levels are detected in fully differentiated phagocytes. Up-
regulated by IL2. {ECO:0000269|PubMed:10779760,
ECO:0000269|PubMed:8995234}.
-!- DOMAIN: The SH3 domain mediates binding to HIV-1 Nef.
-!- PTM: Phosphorylated on several tyrosine residues. Autophosphorylated.
Becomes rapidly phosphorylated upon activation of the immunoglobulin
receptors FCGR1A and FCGR2A. Phosphorylation by the BCR-ABL fusion
protein mediates activation of HCK. Phosphorylation at Tyr-411
increases kinase activity. Phosphorylation at Tyr-522 inhibits kinase
activity. Kinase activity is not required for phosphorylation at Tyr-
522, suggesting that this site is a target of other kinases.
{ECO:0000269|PubMed:10360180, ECO:0000269|PubMed:10644735,
ECO:0000269|PubMed:10779760, ECO:0000269|PubMed:11896602,
ECO:0000269|PubMed:12411494, ECO:0000269|PubMed:16216497,
ECO:0000269|PubMed:8064233, ECO:0000269|PubMed:9024658,
ECO:0000269|PubMed:9406996}.
-!- PTM: Ubiquitinated by CBL, leading to its degradation via the
proteasome. {ECO:0000269|PubMed:11896602}.
-!- PTM: Isoform 2 palmitoylation at position 2 requires prior
myristoylation. Palmitoylation at position 3 is required for caveolar
localization of isoform 2. {ECO:0000269|PubMed:7791757}.
-!- DISEASE: Note=Aberrant activation of HCK by HIV-1 protein Nef enhances
HIV-1 replication and contributes to HIV-1 pathogenicity.
-!- DISEASE: Note=Aberrant activation of HCK, e.g. by the BCR-ABL fusion
protein, promotes cancer cell proliferation.
-!- MISCELLANEOUS: [Isoform 1]: Initiates from a CTG codon.
-!- MISCELLANEOUS: [Isoform 4]: Initiates from a CTG codon. {ECO:0000305}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
kinase family. SRC subfamily. {ECO:0000255|PROSITE-ProRule:PRU00159}.
-!- SEQUENCE CAUTION:
Sequence=AAA52643.1; Type=Frameshift; Evidence={ECO:0000305};
Sequence=BAF82585.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
---------------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
---------------------------------------------------------------------------
EMBL; M16591; AAA52643.1; ALT_FRAME; mRNA.
EMBL; M16592; AAA52644.1; -; mRNA.
EMBL; AK026432; BAB15482.1; -; mRNA.
EMBL; AK289896; BAF82585.1; ALT_INIT; mRNA.
EMBL; AK298726; BAG60878.1; -; mRNA.
EMBL; AL353092; CAI19694.1; -; Genomic_DNA.
EMBL; AL049539; CAI19694.1; JOINED; Genomic_DNA.
EMBL; AL353092; CAI19695.1; -; Genomic_DNA.
EMBL; AL049539; CAI19695.1; JOINED; Genomic_DNA.
EMBL; AL049539; CAI22966.1; -; Genomic_DNA.
EMBL; AL353092; CAI22966.1; JOINED; Genomic_DNA.
EMBL; AL049539; CAI22967.1; -; Genomic_DNA.
EMBL; AL353092; CAI22967.1; JOINED; Genomic_DNA.
EMBL; CH471077; EAW76392.1; -; Genomic_DNA.
EMBL; CH471077; EAW76393.1; -; Genomic_DNA.
EMBL; BC014435; AAH14435.2; -; mRNA.
EMBL; BC094847; AAH94847.2; -; mRNA.
EMBL; BC108930; AAI08931.2; -; mRNA.
EMBL; BC108931; AAI08932.2; -; mRNA.
EMBL; BC113854; AAI13855.2; -; mRNA.
EMBL; BC114463; AAI14464.2; -; mRNA.
EMBL; X58741; CAA41565.2; -; Genomic_DNA.
EMBL; X58742; CAA41565.2; JOINED; Genomic_DNA.
EMBL; X58743; CAA41565.2; JOINED; Genomic_DNA.
CCDS; CCDS33460.1; -. [P08631-1]
CCDS; CCDS54453.1; -. [P08631-4]
CCDS; CCDS54455.1; -. [P08631-2]
CCDS; CCDS54456.1; -. [P08631-3]
PIR; A27811; TVHUHC.
PIR; A41263; A41263.
RefSeq; NP_001165600.1; NM_001172129.1. [P08631-2]
RefSeq; NP_001165601.1; NM_001172130.1. [P08631-4]
RefSeq; NP_001165602.1; NM_001172131.1. [P08631-3]
RefSeq; NP_001165604.1; NM_001172133.1. [P08631-2]
RefSeq; NP_002101.2; NM_002110.3. [P08631-1]
PDB; 1AD5; X-ray; 2.60 A; A/B=79-526.
PDB; 1BU1; X-ray; 2.60 A; A/B/C/D/E/F=81-137.
PDB; 1QCF; X-ray; 2.00 A; A=81-526.
PDB; 2C0I; X-ray; 2.30 A; A/B=81-526.
PDB; 2C0O; X-ray; 2.85 A; A/B=81-526.
PDB; 2C0T; X-ray; 2.15 A; A/B=81-526.
PDB; 2HCK; X-ray; 3.00 A; A/B=79-526.
PDB; 2HK5; X-ray; 2.00 A; A=247-514.
PDB; 2OI3; NMR; -; A=61-141.
PDB; 2OJ2; NMR; -; A=61-141.
PDB; 3HCK; NMR; -; A=140-245.
PDB; 3NHN; X-ray; 2.61 A; A=72-256.
PDB; 3RBB; X-ray; 2.35 A; B/D=79-138.
PDB; 3REA; X-ray; 2.00 A; B/D=79-138.
PDB; 3REB; X-ray; 3.45 A; B/D=79-138.
PDB; 3VRY; X-ray; 2.48 A; A/B=81-526.
PDB; 3VRZ; X-ray; 2.22 A; A/B=81-526.
PDB; 3VS0; X-ray; 2.93 A; A/B=81-526.
PDB; 3VS1; X-ray; 2.46 A; A/B=81-526.
PDB; 3VS2; X-ray; 2.61 A; A/B=81-526.
PDB; 3VS3; X-ray; 2.17 A; A/B=81-526.
PDB; 3VS4; X-ray; 2.75 A; A/B=81-526.
PDB; 3VS5; X-ray; 2.85 A; A/B=81-526.
PDB; 3VS6; X-ray; 2.37 A; A/B=81-526.
PDB; 3VS7; X-ray; 3.00 A; A/B=81-526.
PDB; 4HCK; NMR; -; A=72-143.
PDB; 4LUD; X-ray; 2.85 A; A/B=81-526.
PDB; 4LUE; X-ray; 3.04 A; A/B=81-526.
PDB; 4ORZ; X-ray; 2.00 A; A=77-138.
PDB; 4U5W; X-ray; 1.86 A; B/D=72-242.
PDB; 5H09; X-ray; 1.95 A; A=81-526.
PDB; 5H0B; X-ray; 1.65 A; A=81-526.
PDB; 5H0E; X-ray; 2.10 A; A=81-526.
PDB; 5H0G; X-ray; 1.80 A; A=81-526.
PDB; 5H0H; X-ray; 1.72 A; A=81-526.
PDB; 5HCK; NMR; -; A=72-143.
PDB; 5NUH; X-ray; 2.78 A; C/D=79-138.
PDB; 5ZJ6; X-ray; 1.70 A; A/B=242-521.
PDBsum; 1AD5; -.
PDBsum; 1BU1; -.
PDBsum; 1QCF; -.
PDBsum; 2C0I; -.
PDBsum; 2C0O; -.
PDBsum; 2C0T; -.
PDBsum; 2HCK; -.
PDBsum; 2HK5; -.
PDBsum; 2OI3; -.
PDBsum; 2OJ2; -.
PDBsum; 3HCK; -.
PDBsum; 3NHN; -.
PDBsum; 3RBB; -.
PDBsum; 3REA; -.
PDBsum; 3REB; -.
PDBsum; 3VRY; -.
PDBsum; 3VRZ; -.
PDBsum; 3VS0; -.
PDBsum; 3VS1; -.
PDBsum; 3VS2; -.
PDBsum; 3VS3; -.
PDBsum; 3VS4; -.
PDBsum; 3VS5; -.
PDBsum; 3VS6; -.
PDBsum; 3VS7; -.
PDBsum; 4HCK; -.
PDBsum; 4LUD; -.
PDBsum; 4LUE; -.
PDBsum; 4ORZ; -.
PDBsum; 4U5W; -.
PDBsum; 5H09; -.
PDBsum; 5H0B; -.
PDBsum; 5H0E; -.
PDBsum; 5H0G; -.
PDBsum; 5H0H; -.
PDBsum; 5HCK; -.
PDBsum; 5NUH; -.
PDBsum; 5ZJ6; -.
SMR; P08631; -.
BioGrid; 109305; 70.
DIP; DIP-1051N; -.
ELM; P08631; -.
IntAct; P08631; 103.
MINT; P08631; -.
STRING; 9606.ENSP00000444986; -.
BindingDB; P08631; -.
ChEMBL; CHEMBL3234; -.
DrugBank; DB01809; 1-Ter-Butyl-3-P-Tolyl-1h-Pyrazolo[3,4-D]Pyrimidin-4-Ylamine.
DrugBank; DB06616; Bosutinib.
DrugBank; DB12010; Fostamatinib.
DrugBank; DB01962; Phosphonotyrosine.
DrugBank; DB04216; Quercetin.
DrugCentral; P08631; -.
GuidetoPHARMACOLOGY; 2032; -.
iPTMnet; P08631; -.
PhosphoSitePlus; P08631; -.
SwissPalm; P08631; -.
BioMuta; HCK; -.
DMDM; 20141296; -.
jPOST; P08631; -.
MassIVE; P08631; -.
MaxQB; P08631; -.
PaxDb; P08631; -.
PeptideAtlas; P08631; -.
PRIDE; P08631; -.
ProteomicsDB; 52142; -. [P08631-1]
ProteomicsDB; 52143; -. [P08631-2]
ProteomicsDB; 52144; -. [P08631-3]
ProteomicsDB; 52145; -. [P08631-4]
DNASU; 3055; -.
Ensembl; ENST00000518730; ENSP00000427757; ENSG00000101336. [P08631-3]
Ensembl; ENST00000520553; ENSP00000429848; ENSG00000101336. [P08631-2]
Ensembl; ENST00000534862; ENSP00000444986; ENSG00000101336. [P08631-1]
Ensembl; ENST00000538448; ENSP00000441169; ENSG00000101336. [P08631-2]
Ensembl; ENST00000629881; ENSP00000486627; ENSG00000101336. [P08631-2]
Ensembl; ENST00000639405; ENSP00000491964; ENSG00000101336. [P08631-4]
GeneID; 3055; -.
KEGG; hsa:3055; -.
UCSC; uc002wxi.4; human. [P08631-1]
CTD; 3055; -.
DisGeNET; 3055; -.
EuPathDB; HostDB:ENSG00000101336.12; -.
GeneCards; HCK; -.
HGNC; HGNC:4840; HCK.
HPA; CAB005195; -.
HPA; HPA063768; -.
MIM; 142370; gene.
neXtProt; NX_P08631; -.
OpenTargets; ENSG00000101336; -.
PharmGKB; PA29216; -.
eggNOG; KOG0197; Eukaryota.
eggNOG; COG0515; LUCA.
GeneTree; ENSGT00940000158738; -.
HOGENOM; HOG000233858; -.
InParanoid; P08631; -.
KO; K08893; -.
OrthoDB; 539311at2759; -.
PhylomeDB; P08631; -.
BRENDA; 2.7.10.2; 2681.
Reactome; R-HSA-164944; Nef and signal transduction.
Reactome; R-HSA-2029481; FCGR activation.
Reactome; R-HSA-912631; Regulation of signaling by CBL.
Reactome; R-HSA-9607240; FLT3 Signaling.
SignaLink; P08631; -.
SIGNOR; P08631; -.
ChiTaRS; HCK; human.
EvolutionaryTrace; P08631; -.
GeneWiki; HCK; -.
GenomeRNAi; 3055; -.
Pharos; P08631; Tclin.
PRO; PR:P08631; -.
Proteomes; UP000005640; Chromosome 20.
RNAct; P08631; protein.
Bgee; ENSG00000101336; Expressed in 200 organ(s), highest expression level in blood.
ExpressionAtlas; P08631; baseline and differential.
Genevisible; P08631; HS.
GO; GO:0005901; C:caveola; IDA:UniProtKB.
GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW.
GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; IMP:UniProtKB.
GO; GO:0005925; C:focal adhesion; IMP:UniProtKB.
GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
GO; GO:0005764; C:lysosome; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005886; C:plasma membrane; IDA:HPA.
GO; GO:0030133; C:transport vesicle; IEA:UniProtKB-SubCell.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IBA:GO_Central.
GO; GO:0001784; F:phosphotyrosine residue binding; IPI:CAFA.
GO; GO:0004713; F:protein tyrosine kinase activity; IMP:UniProtKB.
GO; GO:0005102; F:signaling receptor binding; IBA:GO_Central.
GO; GO:0007155; P:cell adhesion; TAS:UniProtKB.
GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
GO; GO:0019221; P:cytokine-mediated signaling pathway; TAS:UniProtKB.
GO; GO:0038096; P:Fc-gamma receptor signaling pathway involved in phagocytosis; TAS:Reactome.
GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
GO; GO:0002758; P:innate immune response-activating signal transduction; TAS:UniProtKB.
GO; GO:0007229; P:integrin-mediated signaling pathway; TAS:UniProtKB.
GO; GO:0060333; P:interferon-gamma-mediated signaling pathway; TAS:UniProtKB.
GO; GO:0043299; P:leukocyte degranulation; TAS:UniProtKB.
GO; GO:0002522; P:leukocyte migration involved in immune response; TAS:UniProtKB.
GO; GO:0031663; P:lipopolysaccharide-mediated signaling pathway; TAS:UniProtKB.
GO; GO:0007498; P:mesoderm development; TAS:ProtInc.
GO; GO:0043066; P:negative regulation of apoptotic process; IMP:UniProtKB.
GO; GO:0038083; P:peptidyl-tyrosine autophosphorylation; IBA:GO_Central.
GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; IMP:UniProtKB.
GO; GO:2000251; P:positive regulation of actin cytoskeleton reorganization; IDA:UniProtKB.
GO; GO:0030838; P:positive regulation of actin filament polymerization; TAS:UniProtKB.
GO; GO:0008284; P:positive regulation of cell population proliferation; IMP:UniProtKB.
GO; GO:0046777; P:protein autophosphorylation; IMP:UniProtKB.
GO; GO:0006468; P:protein phosphorylation; TAS:ProtInc.
GO; GO:0042127; P:regulation of cell population proliferation; IBA:GO_Central.
GO; GO:0008360; P:regulation of cell shape; IMP:UniProtKB.
GO; GO:0050690; P:regulation of defense response to virus by virus; TAS:Reactome.
GO; GO:0051090; P:regulation of DNA-binding transcription factor activity; IMP:UniProtKB.
GO; GO:0050727; P:regulation of inflammatory response; TAS:UniProtKB.
GO; GO:0050764; P:regulation of phagocytosis; IMP:UniProtKB.
GO; GO:0071801; P:regulation of podosome assembly; IDA:UniProtKB.
GO; GO:0045728; P:respiratory burst after phagocytosis; TAS:UniProtKB.
GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA:GO_Central.
CDD; cd10363; SH2_Src_HCK; 1.
Gene3D; 3.30.505.10; -; 1.
InterPro; IPR035851; HCK_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.
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 initiation; Alternative splicing; ATP-binding;
Cell junction; Cell membrane; Cell projection; Cytoplasm;
Cytoplasmic vesicle; Cytoskeleton; Exocytosis; Golgi apparatus;
Host-virus interaction; Immunity; Inflammatory response; Innate immunity;
Kinase; Lipoprotein; Lysosome; Membrane; Myristate; Nucleotide-binding;
Nucleus; Palmitate; Phagocytosis; Phosphoprotein; Polymorphism;
Proto-oncogene; Reference proteome; SH2 domain; SH3 domain; Transferase;
Tyrosine-protein kinase; Ubl conjugation.
INIT_MET 1
/note="Removed"
CHAIN 2..526
/note="Tyrosine-protein kinase HCK"
/id="PRO_0000024433"
DOMAIN 78..138
/note="SH3"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
DOMAIN 144..241
/note="SH2"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
DOMAIN 262..515
/note="Protein kinase"
/evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
NP_BIND 268..276
/note="ATP"
ACT_SITE 381
/note="Proton acceptor"
BINDING 290
/note="ATP"
MOD_RES 36
/note="Phosphothreonine"
/evidence="ECO:0000244|PubMed:24275569"
MOD_RES 51
/note="Phosphotyrosine; by autocatalysis"
/evidence="ECO:0000269|PubMed:11896602"
MOD_RES 202
/note="Phosphothreonine"
/evidence="ECO:0000244|PubMed:19369195"
MOD_RES 209
/note="Phosphotyrosine"
/evidence="ECO:0000250|UniProtKB:P08103"
MOD_RES 411
/note="Phosphotyrosine; by autocatalysis"
/evidence="ECO:0000269|PubMed:10644735,
ECO:0000269|PubMed:11896602"
MOD_RES 462
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:19369195"
MOD_RES 522
/note="Phosphotyrosine"
/evidence="ECO:0000269|PubMed:10360180,
ECO:0000269|PubMed:10644735, ECO:0000269|PubMed:11896602,
ECO:0000269|PubMed:16216497, ECO:0000269|PubMed:9024658"
LIPID 2
/note="N-myristoyl glycine"
/evidence="ECO:0000269|PubMed:7791757"
VAR_SEQ 1..21
/note="Missing (in isoform 2 and isoform 3)"
/evidence="ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:3453117"
/id="VSP_018858"
VAR_SEQ 76
/note="Missing (in isoform 3 and isoform 4)"
/evidence="ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334"
/id="VSP_041926"
VARIANT 44
/note="A -> T (in dbSNP:rs56029200)"
/evidence="ECO:0000269|PubMed:17344846"
/id="VAR_041707"
VARIANT 105
/note="M -> L (in dbSNP:rs55722810)"
/evidence="ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:17344846"
/id="VAR_041708"
VARIANT 399
/note="D -> G (in an ovarian mucinous carcinoma sample;
somatic mutation)"
/evidence="ECO:0000269|PubMed:17344846"
/id="VAR_041709"
VARIANT 502
/note="P -> Q (in dbSNP:rs17093828)"
/id="VAR_033836"
MUTAGEN 3
/note="G->C: Slight palmitoylation, cytoplasmic and
caveolar localization; in isoform 1;."
/evidence="ECO:0000269|PubMed:11904303,
ECO:0000269|PubMed:7791757"
MUTAGEN 3
/note="G->S: Abolishes palmitoylation and localization at
the cell membrane."
/evidence="ECO:0000269|PubMed:11904303,
ECO:0000269|PubMed:7791757"
MUTAGEN 23
/note="G->A: Myristoylation and palmitoylation are
abolished, leading to entirely cytoplasmic localization; in
isoform 2."
/evidence="ECO:0000269|PubMed:7791757"
MUTAGEN 24
/note="C->S: Palmitoylation is abolished, some cytoplasmic
and no calveolar localization; in isoform 2."
/evidence="ECO:0000269|PubMed:7791757"
MUTAGEN 290
/note="K->E: Loss of kinase activity."
/evidence="ECO:0000269|PubMed:11896602"
MUTAGEN 305
/note="E->A: Loss of kinase activity."
/evidence="ECO:0000269|PubMed:10644735"
MUTAGEN 381
/note="D->E: Loss of kinase activity."
/evidence="ECO:0000269|PubMed:15998323"
MUTAGEN 411
/note="Y->A: Reduced catalytic activity and higher affinity
for target peptides."
/evidence="ECO:0000269|PubMed:10644735"
MUTAGEN 522
/note="Y->F: Constitutively activated kinase, leading to
cellular transformation."
/evidence="ECO:0000269|PubMed:10092522,
ECO:0000269|PubMed:11896602"
CONFLICT 24
/note="C -> S (in Ref. 1; AAA52643)"
/evidence="ECO:0000305"
CONFLICT 69
/note="N -> D (in Ref. 3; BAF82585)"
/evidence="ECO:0000305"
CONFLICT 144
/note="W -> R (in Ref. 3; BAB15482)"
/evidence="ECO:0000305"
CONFLICT 168
/note="F -> Y (in Ref. 3; BAF82585)"
/evidence="ECO:0000305"
CONFLICT 378
/note="I -> T (in Ref. 6; AAI13855)"
/evidence="ECO:0000305"
CONFLICT 488
/note="N -> S (in Ref. 3; BAF82585)"
/evidence="ECO:0000305"
STRAND 82..85
/evidence="ECO:0000244|PDB:5H0B"
STRAND 93..96
/evidence="ECO:0000244|PDB:5H0B"
STRAND 99..102
/evidence="ECO:0000244|PDB:5H0H"
STRAND 104..111
/evidence="ECO:0000244|PDB:5H0B"
STRAND 114..122
/evidence="ECO:0000244|PDB:5H0B"
STRAND 127..129
/evidence="ECO:0000244|PDB:5H0B"
HELIX 130..132
/evidence="ECO:0000244|PDB:5H0B"
STRAND 133..135
/evidence="ECO:0000244|PDB:5H0B"
HELIX 136..138
/evidence="ECO:0000244|PDB:2OI3"
HELIX 139..141
/evidence="ECO:0000244|PDB:5H0B"
STRAND 145..148
/evidence="ECO:0000244|PDB:3VS2"
HELIX 151..159
/evidence="ECO:0000244|PDB:5H0B"
STRAND 168..172
/evidence="ECO:0000244|PDB:5H0B"
STRAND 174..176
/evidence="ECO:0000244|PDB:5H0B"
STRAND 180..188
/evidence="ECO:0000244|PDB:5H0B"
TURN 189..191
/evidence="ECO:0000244|PDB:5H0B"
STRAND 192..202
/evidence="ECO:0000244|PDB:5H0B"
STRAND 204..206
/evidence="ECO:0000244|PDB:4U5W"
STRAND 208..211
/evidence="ECO:0000244|PDB:5H0B"
STRAND 215..218
/evidence="ECO:0000244|PDB:5H0B"
HELIX 219..228
/evidence="ECO:0000244|PDB:5H0B"
STRAND 233..235
/evidence="ECO:0000244|PDB:5H0B"
TURN 252..255
/evidence="ECO:0000244|PDB:2HCK"
HELIX 259..261
/evidence="ECO:0000244|PDB:5H0B"
STRAND 262..270
/evidence="ECO:0000244|PDB:5H0B"
STRAND 272..281
/evidence="ECO:0000244|PDB:5H0B"
TURN 282..284
/evidence="ECO:0000244|PDB:5H0B"
STRAND 285..292
/evidence="ECO:0000244|PDB:5H0B"
STRAND 294..297
/evidence="ECO:0000244|PDB:3VS3"
HELIX 299..309
/evidence="ECO:0000244|PDB:5H0B"
STRAND 320..324
/evidence="ECO:0000244|PDB:5H0B"
STRAND 326..328
/evidence="ECO:0000244|PDB:5H0B"
STRAND 330..333
/evidence="ECO:0000244|PDB:5H0B"
HELIX 341..345
/evidence="ECO:0000244|PDB:5H0B"
HELIX 350..352
/evidence="ECO:0000244|PDB:5H0B"
HELIX 355..374
/evidence="ECO:0000244|PDB:5H0B"
HELIX 384..386
/evidence="ECO:0000244|PDB:5H0B"
STRAND 387..389
/evidence="ECO:0000244|PDB:5H0B"
STRAND 395..397
/evidence="ECO:0000244|PDB:5H0B"
HELIX 402..405
/evidence="ECO:0000244|PDB:5H0B"
HELIX 410..413
/evidence="ECO:0000244|PDB:5H0B"
STRAND 416..419
/evidence="ECO:0000244|PDB:1QCF"
HELIX 421..423
/evidence="ECO:0000244|PDB:5H0B"
HELIX 426..431
/evidence="ECO:0000244|PDB:5H0B"
HELIX 436..451
/evidence="ECO:0000244|PDB:5H0B"
TURN 452..454
/evidence="ECO:0000244|PDB:2HK5"
STRAND 457..460
/evidence="ECO:0000244|PDB:1AD5"
HELIX 463..471
/evidence="ECO:0000244|PDB:5H0B"
STRAND 480..482
/evidence="ECO:0000244|PDB:3VS6"
HELIX 484..493
/evidence="ECO:0000244|PDB:5H0B"
HELIX 498..500
/evidence="ECO:0000244|PDB:5H0B"
HELIX 504..512
/evidence="ECO:0000244|PDB:5H0B"
TURN 513..518
/evidence="ECO:0000244|PDB:5H0B"
STRAND 521..523
/evidence="ECO:0000244|PDB:1QCF"
INIT_MET P08631-2:1
/note="Removed"
/evidence="ECO:0000305"
LIPID P08631-2:2
/note="N-myristoyl glycine"
/evidence="ECO:0000269|PubMed:7791757"
LIPID P08631-2:3
/note="S-palmitoyl cysteine"
/evidence="ECO:0000269|PubMed:7791757"
SEQUENCE 526 AA; 59600 MW; 847E877A0A641725 CRC64;
MGGRSSCEDP GCPRDEERAP RMGCMKSKFL QVGGNTFSKT ETSASPHCPV YVPDPTSTIK
PGPNSHNSNT PGIREAGSED IIVVALYDYE AIHHEDLSFQ KGDQMVVLEE SGEWWKARSL
ATRKEGYIPS NYVARVDSLE TEEWFFKGIS RKDAERQLLA PGNMLGSFMI RDSETTKGSY
SLSVRDYDPR QGDTVKHYKI RTLDNGGFYI SPRSTFSTLQ ELVDHYKKGN DGLCQKLSVP
CMSSKPQKPW EKDAWEIPRE SLKLEKKLGA GQFGEVWMAT YNKHTKVAVK TMKPGSMSVE
AFLAEANVMK TLQHDKLVKL HAVVTKEPIY IITEFMAKGS LLDFLKSDEG SKQPLPKLID
FSAQIAEGMA FIEQRNYIHR DLRAANILVS ASLVCKIADF GLARVIEDNE YTAREGAKFP
IKWTAPEAIN FGSFTIKSDV WSFGILLMEI VTYGRIPYPG MSNPEVIRAL ERGYRMPRPE
NCPEELYNIM MRCWKNRPEE RPTFEYIQSV LDDFYTATES QYQQQP


Related products :

Catalog number Product name Quantity
32-168 Hemopoietic cell kinase.The protein encoded by this gene is a protein-tyrosine kinase that is predominantly expressed in hemopoietic cell types. The encoded protein may help couple the Fc receptor to 0.1 mL
32-169 Hemopoietic cell kinase.The protein encoded by this gene is a protein-tyrosine kinase that is predominantly expressed in hemopoietic cell types. The encoded protein may help couple the Fc receptor to 0.1 mL
FP-0036 Hemopoietic cell kinase isoform p61HCK 10 ug
FP-0036 Hemopoietic cell kinase isoform p61HCK 10ug
FP-0036 Hemopoietic cell kinase isoform p61HCK; SH2-Domain: HCK 10ug
10-782-55036 Tyrosine-protein kinase HCK - EC 2.7.10.2; p59-HCK_p60-HCK; Hemopoietic cell kinase N_A 0.02 mg
10-782-55036 Tyrosine-protein kinase HCK - EC 2.7.10.2; p59-HCK_p60-HCK; Hemopoietic cell kinase N_A 0.001 mg
10-782-55036 Tyrosine-protein kinase HCK - EC 2.7.10.2; p59-HCK_p60-HCK; Hemopoietic cell kinase N_A 0.01 mg
10-782-55036 Tyrosine-protein kinase HCK - EC 2.7.10.2; p59-HCK_p60-HCK; Hemopoietic cell kinase N_A 0.005 mg
FP-0036 Fusion proteins: Hemopoietic cell kinase isoform p61HCK, HCK 10ug
U1915m CLIA Agammaglobulinaemia tyrosine kinase,ATK,B-cell progenitor kinase,BPK,Bpk,Bruton tyrosine kinase,Btk,Kinase EMB,Mouse,Mus musculus,Tyrosine-protein kinase BTK 96T
U1915m CLIA kit Agammaglobulinaemia tyrosine kinase,ATK,B-cell progenitor kinase,BPK,Bpk,Bruton tyrosine kinase,Btk,Kinase EMB,Mouse,Mus musculus,Tyrosine-protein kinase BTK 96T
E1915m ELISA kit Agammaglobulinaemia tyrosine kinase,ATK,B-cell progenitor kinase,BPK,Bpk,Bruton tyrosine kinase,Btk,Kinase EMB,Mouse,Mus musculus,Tyrosine-protein kinase BTK 96T
E1915m ELISA Agammaglobulinaemia tyrosine kinase,ATK,B-cell progenitor kinase,BPK,Bpk,Bruton tyrosine kinase,Btk,Kinase EMB,Mouse,Mus musculus,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
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
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
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
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
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
EIAAB14370 CADTK,CAK-beta,Calcium-dependent tyrosine kinase,Cell adhesion kinase beta,FADK 2,FAK2,Focal adhesion kinase 2,Homo sapiens,Human,Proline-rich tyrosine kinase 2,Protein-tyrosine kinase 2-beta,PTK2B,PY
EIAAB14368 CADTK,CAK-beta,Calcium-dependent tyrosine kinase,Cell adhesion kinase beta,FADK 2,Fak2,Focal adhesion kinase 2,Mouse,Mus musculus,Proline-rich tyrosine kinase 2,Protein-tyrosine kinase 2-beta,Ptk2b,Py
18-003-42265 Protein tyrosine kinase 2 beta - EC 2.7.10.2; Focal adhesion kinase 2; FADK 2; Proline-rich tyrosine kinase 2; Cell adhesion kinase beta; CAK beta; Calcium-dependent tyrosine kinase; CADTK; Related ad 0.1 mg Protein A
18-003-42266 Protein tyrosine kinase 2 beta - EC 2.7.10.2; Focal adhesion kinase 2; FADK 2; Proline-rich tyrosine kinase 2; Cell adhesion kinase beta; CAK beta; Calcium-dependent tyrosine kinase; CADTK; Related ad 0.05 mg Aff Pur
E0039h ELISA kit CD135,Fetal liver kinase-2,FL cytokine receptor,FLK2,FLK-2,FLT3,FLT-3,Fms-like tyrosine kinase 3,Homo sapiens,Human,Receptor-type tyrosine-protein kinase FLT3,Stem cell tyrosine kinase 1,ST 96T
Pathways :
WP1493: Carbon assimilation C4 pathway
WP32: Translation Factors
WP1653: Galactose metabolism
WP2341: vitamin B1 (thiamin) biosynthesis and salvage pathway
WP1703: Streptomycin biosynthesis
WP1681: Pantothenate and CoA biosynthesis
WP1701: Starch and sucrose metabolism
WP2340: Thiamine (vitamin B1) biosynthesis and salvage
WP1567: Glycolysis and Gluconeogenesis
WP1619: Amino sugar and nucleotide sugar metabolism
WP1946: Cori Cycle
WP253: Glycolysis
WP1844: MAP kinase cascade
WP2006: Squamous cell TarBase
WP274: B Cell Receptor Signaling Pathway
WP844: Cell cycle
WP1011: T Cell Receptor Signaling Pathway
WP1793: Cell junction organization
WP2226: Cell engulfment
WP480: T Cell Receptor Signaling Pathway
WP1354: B Cell Receptor Signaling Pathway
WP1833: Integrin cell surface interactions
WP1386: Integrin-mediated cell adhesion
WP2029: Cell Differentiation - Index
WP923: Calcium Regulation in the Cardiac Cell

Related Genes :
[Fyn] Tyrosine-protein kinase Fyn (EC 2.7.10.2) (Proto-oncogene c-Fyn) (p59-Fyn)
[ERBB3 HER3] Receptor tyrosine-protein kinase erbB-3 (EC 2.7.10.1) (Proto-oncogene-like protein c-ErbB-3) (Tyrosine kinase-type cell surface receptor HER3)
[FLT3 CD135 FLK2 STK1] Receptor-type tyrosine-protein kinase FLT3 (EC 2.7.10.1) (FL cytokine receptor) (Fetal liver kinase-2) (FLK-2) (Fms-like tyrosine kinase 3) (FLT-3) (Stem cell tyrosine kinase 1) (STK-1) (CD antigen CD135)
[Fgr] Tyrosine-protein kinase Fgr (EC 2.7.10.2) (Proto-oncogene c-Fgr) (p55-Fgr)
[KIT SCFR] Mast/stem cell growth factor receptor Kit (SCFR) (EC 2.7.10.1) (Piebald trait protein) (PBT) (Proto-oncogene c-Kit) (Tyrosine-protein kinase Kit) (p145 c-kit) (v-kit Hardy-Zuckerman 4 feline sarcoma viral oncogene homolog) (CD antigen CD117)
[SRC] Proto-oncogene tyrosine-protein kinase Src (EC 2.7.10.2) (Proto-oncogene c-Src) (pp60c-src) (p60-Src)
[Lck Lsk-t] Proto-oncogene tyrosine-protein kinase LCK (EC 2.7.10.2) (Leukocyte C-terminal Src kinase) (LSK) (Lymphocyte cell-specific protein-tyrosine kinase) (p56-LCK)
[ABL1 ABL JTK7] Tyrosine-protein kinase ABL1 (EC 2.7.10.2) (Abelson murine leukemia viral oncogene homolog 1) (Abelson tyrosine-protein kinase 1) (Proto-oncogene c-Abl) (p150)
[SRC SRC1] Proto-oncogene tyrosine-protein kinase Src (EC 2.7.10.2) (Proto-oncogene c-Src) (pp60c-src) (p60-Src)
[Csk] Tyrosine-protein kinase CSK (EC 2.7.10.2) (C-Src kinase) (Protein-tyrosine kinase MPK-2) (p50CSK)
[Flt3 Flk-2 Flt-3] Receptor-type tyrosine-protein kinase FLT3 (EC 2.7.10.1) (FL cytokine receptor) (Fetal liver kinase 2) (FLK-2) (Fms-like tyrosine kinase 3) (FLT-3) (Tyrosine-protein kinase receptor flk-2) (CD antigen CD135)
[Lyn] Tyrosine-protein kinase Lyn (EC 2.7.10.2) (V-yes-1 Yamaguchi sarcoma viral related oncogene homolog) (p53Lyn) (p56Lyn)
[Ptk2b Fak2 Pyk2 Raftk] Protein-tyrosine kinase 2-beta (EC 2.7.10.2) (Calcium-dependent tyrosine kinase) (CADTK) (Calcium-regulated non-receptor proline-rich tyrosine kinase) (Cell adhesion kinase beta) (CAK-beta) (CAKB) (Focal adhesion kinase 2) (FADK 2) (Proline-rich tyrosine kinase 2) (Related adhesion focal tyrosine kinase) (RAFTK)
[DDR1 CAK EDDR1 NEP NTRK4 PTK3A RTK6 TRKE] Epithelial discoidin domain-containing receptor 1 (Epithelial discoidin domain receptor 1) (EC 2.7.10.1) (CD167 antigen-like family member A) (Cell adhesion kinase) (Discoidin receptor tyrosine kinase) (HGK2) (Mammary carcinoma kinase 10) (MCK-10) (Protein-tyrosine kinase 3A) (Protein-tyrosine kinase RTK-6) (TRK E) (Tyrosine kinase DDR) (Tyrosine-protein kinase CAK) (CD antigen CD167a)
[Tek Hyk Tie-2 Tie2] Angiopoietin-1 receptor (EC 2.7.10.1) (Endothelial tyrosine kinase) (HYK) (STK1) (Tunica interna endothelial cell kinase) (Tyrosine kinase with Ig and EGF homology domains-2) (Tyrosine-protein kinase receptor TEK) (Tyrosine-protein kinase receptor TIE-2) (mTIE2) (p140 TEK) (CD antigen CD202b)
[Itk Emt Tlk Tsk] Tyrosine-protein kinase ITK/TSK (EC 2.7.10.2) (IL-2-inducible T-cell kinase) (Kinase EMT) (Kinase TLK) (T-cell-specific kinase)
[LYN JTK8] Tyrosine-protein kinase Lyn (EC 2.7.10.2) (Lck/Yes-related novel protein tyrosine kinase) (V-yes-1 Yamaguchi sarcoma viral related oncogene homolog) (p53Lyn) (p56Lyn)
[Abl1 Abl] Tyrosine-protein kinase ABL1 (EC 2.7.10.2) (Abelson murine leukemia viral oncogene homolog 1) (Abelson tyrosine-protein kinase 1) (Proto-oncogene c-Abl) (p150)
[Csk] Tyrosine-protein kinase CSK (EC 2.7.10.2) (C-Src kinase)
[FLT1 FLT FRT VEGFR1] Vascular endothelial growth factor receptor 1 (VEGFR-1) (EC 2.7.10.1) (Fms-like tyrosine kinase 1) (FLT-1) (Tyrosine-protein kinase FRT) (Tyrosine-protein kinase receptor FLT) (FLT) (Vascular permeability factor receptor)
[EGFR ERBB ERBB1 HER1] Epidermal growth factor receptor (EC 2.7.10.1) (Proto-oncogene c-ErbB-1) (Receptor tyrosine-protein kinase erbB-1)
[ITK EMT LYK] Tyrosine-protein kinase ITK/TSK (EC 2.7.10.2) (Interleukin-2-inducible T-cell kinase) (IL-2-inducible T-cell kinase) (Kinase EMT) (T-cell-specific kinase) (Tyrosine-protein kinase Lyk)
[Src] Neuronal proto-oncogene tyrosine-protein kinase Src (EC 2.7.10.2) (Proto-oncogene c-Src) (pp60c-src) (p60-Src)
[Src] Proto-oncogene tyrosine-protein kinase Src (EC 2.7.10.2) (Proto-oncogene c-Src) (pp60c-src) (p60-Src)
[LCK] 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)
[PTK2B FAK2 PYK2 RAFTK] Protein-tyrosine kinase 2-beta (EC 2.7.10.2) (Calcium-dependent tyrosine kinase) (CADTK) (Calcium-regulated non-receptor proline-rich tyrosine kinase) (Cell adhesion kinase beta) (CAK-beta) (CAKB) (Focal adhesion kinase 2) (FADK 2) (Proline-rich tyrosine kinase 2) (Related adhesion focal tyrosine kinase) (RAFTK)
[Eif2ak2 Pkr Prkr Tik] Interferon-induced, double-stranded RNA-activated protein kinase (EC 2.7.11.1) (Eukaryotic translation initiation factor 2-alpha kinase 2) (eIF-2A protein kinase 2) (Interferon-inducible RNA-dependent protein kinase) (P1/eIF-2A protein kinase) (Protein kinase RNA-activated) (PKR) (Protein kinase R) (Serine/threonine-protein kinase TIK) (Tyrosine-protein kinase EIF2AK2) (EC 2.7.10.2) (p68 kinase)
[TEK TIE2 VMCM VMCM1] Angiopoietin-1 receptor (EC 2.7.10.1) (Endothelial tyrosine kinase) (Tunica interna endothelial cell kinase) (Tyrosine kinase with Ig and EGF homology domains-2) (Tyrosine-protein kinase receptor TEK) (Tyrosine-protein kinase receptor TIE-2) (hTIE2) (p140 TEK) (CD antigen CD202b)
[Ptk2b Fak2 Pyk2] Protein-tyrosine kinase 2-beta (EC 2.7.10.2) (Calcium-dependent tyrosine kinase) (CADTK) (Calcium-regulated non-receptor proline-rich tyrosine kinase) (Cell adhesion kinase beta) (CAK-beta) (CAKB) (Focal adhesion kinase 2) (FADK 2) (Proline-rich tyrosine kinase 2)
[EPHA2 ECK] Ephrin type-A receptor 2 (EC 2.7.10.1) (Epithelial cell kinase) (Tyrosine-protein kinase receptor ECK)

Bibliography :
No related Items