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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.
25-OCT-2017, entry version 228.
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 ENZYME 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, ENZYME 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]
ENZYME REGULATION, AND INTERACTION WITH HIV-1 NEF.
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, ENZYME
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, ENZYME 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, ENZYME 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.
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.
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, AND ENZYME 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, ENZYME 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, ENZYME 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.
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.
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: ATP + a [protein]-L-tyrosine = ADP + a
[protein]-L-tyrosine phosphate. {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}.
-!- ENZYME 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). Interacts (via SH3 domain) with HIV-1 Nef and Vif.
This interaction stimulates its tyrosine-kinase activity.
Interacts (via SH3 domain) with HEV ORF3 protein. 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:11278465, ECO:0000269|PubMed:11518702,
ECO:0000269|PubMed:11741929, ECO:0000269|PubMed:12411494,
ECO:0000269|PubMed:15952790, ECO:0000269|PubMed:16849330,
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:21477083,
ECO:0000269|PubMed:21625496, ECO:0000269|PubMed:25469238,
ECO:0000269|PubMed:8064233, ECO:0000269|PubMed:8132624,
ECO:0000269|PubMed:9024658, ECO:0000269|PubMed:9218412,
ECO:0000269|PubMed:9406996, ECO:0000269|PubMed:9407116}.
-!- 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:NOTCH2NL; 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;
Note=Initiates from a CTG codon.;
Name=2; Synonyms=p59-HCK, p59Hck;
IsoId=P08631-2; Sequence=VSP_018858;
Note=Initiator Met-1 is removed. Contains a N-myristoyl glycine
at position 2. Contains a S-palmitoyl cysteine at position 3.
{ECO:0000269|PubMed:7791757};
Name=3;
IsoId=P08631-3; Sequence=VSP_018858, VSP_041926;
Name=4;
IsoId=P08631-4; Sequence=VSP_041926;
Note=Initiates from a CTG codon.;
-!- 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.
-!- 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; Positions=20; Evidence={ECO:0000305};
Sequence=BAF82585.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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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]
UniGene; Hs.655210; -.
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; 5HCK; NMR; -; A=72-143.
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; 5HCK; -.
ProteinModelPortal; P08631; -.
SMR; P08631; -.
BioGrid; 109305; 63.
DIP; DIP-1051N; -.
ELM; P08631; -.
IntAct; P08631; 99.
MINT; MINT-135300; -.
STRING; 9606.ENSP00000365012; -.
BindingDB; P08631; -.
ChEMBL; CHEMBL3234; -.
DrugBank; DB06616; Bosutinib.
DrugBank; DB01962; Phosphonotyrosine.
DrugBank; DB04216; Quercetin.
GuidetoPHARMACOLOGY; 2032; -.
iPTMnet; P08631; -.
PhosphoSitePlus; P08631; -.
SwissPalm; P08631; -.
BioMuta; HCK; -.
DMDM; 20141296; -.
MaxQB; P08631; -.
PaxDb; P08631; -.
PeptideAtlas; P08631; -.
PRIDE; P08631; -.
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; ENSGT00760000118938; -.
HOGENOM; HOG000233858; -.
HOVERGEN; HBG008761; -.
InParanoid; P08631; -.
KO; K08893; -.
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.
SignaLink; P08631; -.
SIGNOR; P08631; -.
ChiTaRS; HCK; human.
EvolutionaryTrace; P08631; -.
GeneWiki; HCK; -.
GenomeRNAi; 3055; -.
PRO; PR:P08631; -.
Proteomes; UP000005640; Chromosome 20.
Bgee; ENSG00000101336; -.
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: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 proliferation; IMP:UniProtKB.
GO; GO:0046777; P:protein autophosphorylation; IMP:UniProtKB.
GO; GO:0006468; P:protein phosphorylation; TAS:ProtInc.
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: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:0051090; P:regulation of sequence-specific DNA binding transcription factor activity; IMP: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.
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.
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;
Complete proteome; 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 1 Removed.
CHAIN 2 526 Tyrosine-protein kinase HCK.
/FTId=PRO_0000024433.
DOMAIN 78 138 SH3. {ECO:0000255|PROSITE-
ProRule:PRU00192}.
DOMAIN 144 241 SH2. {ECO:0000255|PROSITE-
ProRule:PRU00191}.
DOMAIN 262 515 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 268 276 ATP.
ACT_SITE 381 381 Proton acceptor.
BINDING 290 290 ATP.
MOD_RES 36 36 Phosphothreonine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 51 51 Phosphotyrosine; by autocatalysis.
{ECO:0000269|PubMed:11896602}.
MOD_RES 202 202 Phosphothreonine.
{ECO:0000244|PubMed:19369195}.
MOD_RES 209 209 Phosphotyrosine.
{ECO:0000250|UniProtKB:P08103}.
MOD_RES 411 411 Phosphotyrosine; by autocatalysis.
{ECO:0000269|PubMed:10644735,
ECO:0000269|PubMed:11896602}.
MOD_RES 462 462 Phosphoserine.
{ECO:0000244|PubMed:19369195}.
MOD_RES 522 522 Phosphotyrosine.
{ECO:0000269|PubMed:10360180,
ECO:0000269|PubMed:10644735,
ECO:0000269|PubMed:11896602,
ECO:0000269|PubMed:16216497,
ECO:0000269|PubMed:9024658}.
LIPID 2 2 N-myristoyl glycine.
{ECO:0000269|PubMed:7791757}.
VAR_SEQ 1 21 Missing (in isoform 2 and isoform 3).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:3453117}.
/FTId=VSP_018858.
VAR_SEQ 76 76 Missing (in isoform 3 and isoform 4).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_041926.
VARIANT 44 44 A -> T (in dbSNP:rs56029200).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041707.
VARIANT 105 105 M -> L (in dbSNP:rs55722810).
{ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:17344846}.
/FTId=VAR_041708.
VARIANT 399 399 D -> G (in an ovarian mucinous carcinoma
sample; somatic mutation).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041709.
VARIANT 502 502 P -> Q (in dbSNP:rs17093828).
/FTId=VAR_033836.
MUTAGEN 3 3 G->C: Slight palmitoylation, cytoplasmic
and caveolar localization; in isoform 1;.
{ECO:0000269|PubMed:11904303,
ECO:0000269|PubMed:7791757}.
MUTAGEN 3 3 G->S: Abolishes palmitoylation and
localization at the cell membrane.
{ECO:0000269|PubMed:11904303,
ECO:0000269|PubMed:7791757}.
MUTAGEN 23 23 G->A: Myristoylation and palmitoylation
are abolished, leading to entirely
cytoplasmic localization; in isoform 2.
{ECO:0000269|PubMed:7791757}.
MUTAGEN 24 24 C->S: Palmitoylation is abolished, some
cytoplasmic and no calveolar
localization; in isoform 2.
{ECO:0000269|PubMed:7791757}.
MUTAGEN 290 290 K->E: Loss of kinase activity.
{ECO:0000269|PubMed:11896602}.
MUTAGEN 305 305 E->A: Loss of kinase activity.
{ECO:0000269|PubMed:10644735}.
MUTAGEN 381 381 D->E: Loss of kinase activity.
{ECO:0000269|PubMed:15998323}.
MUTAGEN 411 411 Y->A: Reduced catalytic activity and
higher affinity for target peptides.
{ECO:0000269|PubMed:10644735}.
MUTAGEN 522 522 Y->F: Constitutively activated kinase,
leading to cellular transformation.
{ECO:0000269|PubMed:10092522,
ECO:0000269|PubMed:11896602}.
CONFLICT 24 24 C -> S (in Ref. 1; AAA52643).
{ECO:0000305}.
CONFLICT 69 69 N -> D (in Ref. 3; BAF82585).
{ECO:0000305}.
CONFLICT 144 144 W -> R (in Ref. 3; BAB15482).
{ECO:0000305}.
CONFLICT 168 168 F -> Y (in Ref. 3; BAF82585).
{ECO:0000305}.
CONFLICT 378 378 I -> T (in Ref. 6; AAI13855).
{ECO:0000305}.
CONFLICT 488 488 N -> S (in Ref. 3; BAF82585).
{ECO:0000305}.
STRAND 81 87 {ECO:0000244|PDB:4U5W}.
STRAND 93 96 {ECO:0000244|PDB:2C0T}.
STRAND 104 109 {ECO:0000244|PDB:4U5W}.
STRAND 114 119 {ECO:0000244|PDB:4U5W}.
TURN 120 122 {ECO:0000244|PDB:4U5W}.
STRAND 125 129 {ECO:0000244|PDB:4U5W}.
HELIX 130 132 {ECO:0000244|PDB:4U5W}.
STRAND 133 135 {ECO:0000244|PDB:4U5W}.
HELIX 136 138 {ECO:0000244|PDB:2OI3}.
HELIX 139 141 {ECO:0000244|PDB:4U5W}.
STRAND 145 148 {ECO:0000244|PDB:3VS2}.
HELIX 151 159 {ECO:0000244|PDB:4U5W}.
STRAND 168 172 {ECO:0000244|PDB:4U5W}.
STRAND 174 176 {ECO:0000244|PDB:4U5W}.
STRAND 180 188 {ECO:0000244|PDB:4U5W}.
TURN 189 191 {ECO:0000244|PDB:4U5W}.
STRAND 192 202 {ECO:0000244|PDB:4U5W}.
STRAND 204 206 {ECO:0000244|PDB:4U5W}.
STRAND 208 211 {ECO:0000244|PDB:4U5W}.
STRAND 214 218 {ECO:0000244|PDB:4U5W}.
HELIX 219 228 {ECO:0000244|PDB:4U5W}.
STRAND 233 235 {ECO:0000244|PDB:4U5W}.
TURN 252 255 {ECO:0000244|PDB:2HCK}.
HELIX 259 261 {ECO:0000244|PDB:1QCF}.
STRAND 262 269 {ECO:0000244|PDB:1QCF}.
STRAND 272 281 {ECO:0000244|PDB:1QCF}.
TURN 282 284 {ECO:0000244|PDB:1QCF}.
STRAND 285 292 {ECO:0000244|PDB:1QCF}.
STRAND 294 297 {ECO:0000244|PDB:3VS3}.
HELIX 299 309 {ECO:0000244|PDB:1QCF}.
STRAND 320 324 {ECO:0000244|PDB:1QCF}.
STRAND 326 328 {ECO:0000244|PDB:1QCF}.
STRAND 330 333 {ECO:0000244|PDB:1QCF}.
HELIX 341 346 {ECO:0000244|PDB:1QCF}.
HELIX 348 351 {ECO:0000244|PDB:1QCF}.
HELIX 355 374 {ECO:0000244|PDB:1QCF}.
HELIX 384 386 {ECO:0000244|PDB:1QCF}.
STRAND 387 389 {ECO:0000244|PDB:1QCF}.
STRAND 395 397 {ECO:0000244|PDB:1QCF}.
HELIX 402 405 {ECO:0000244|PDB:1QCF}.
HELIX 409 412 {ECO:0000244|PDB:1QCF}.
STRAND 416 419 {ECO:0000244|PDB:1QCF}.
HELIX 421 423 {ECO:0000244|PDB:1QCF}.
HELIX 426 431 {ECO:0000244|PDB:1QCF}.
HELIX 436 451 {ECO:0000244|PDB:1QCF}.
TURN 452 454 {ECO:0000244|PDB:2HK5}.
STRAND 457 460 {ECO:0000244|PDB:1AD5}.
HELIX 463 472 {ECO:0000244|PDB:1QCF}.
STRAND 480 482 {ECO:0000244|PDB:3VS6}.
HELIX 484 493 {ECO:0000244|PDB:1QCF}.
HELIX 498 500 {ECO:0000244|PDB:1QCF}.
HELIX 504 512 {ECO:0000244|PDB:1QCF}.
STRAND 514 518 {ECO:0000244|PDB:1QCF}.
STRAND 521 523 {ECO:0000244|PDB:1QCF}.
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


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