ID   HCK_HUMAN      STANDARD;      PRT;   526 AA.
AC   P08631;
DT   01-AUG-1988 (Rel. 08, Created)
DT   01-NOV-1995 (Rel. 32, Last sequence update)
DT   30-MAY-2000 (Rel. 39, Last annotation update)
DE   TYROSINE-PROTEIN KINASE HCK (EC 2.7.1.112) (P59-HCK AND P60-HCK)
DE   (HEMOPOIETIC CELL KINASE).
GN   HCK.
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   SEQUENCE OF 22-526 FROM N.A.
RX   MEDLINE=87257942; PubMed=3496523;
RA   Quintrell N., Lebo R., Varmus H., Bishop J.M., Pettenati M.J.,
RA   le Beau M.M., Diaz M.O., Rowley J.D.;
RT   "Identification of a human gene (HCK) that encodes a protein-tyrosine
RT   kinase and is expressed in hemopoietic cells.";
RL   Mol. Cell. Biol. 7:2267-2275(1987).
RN   [2]
RP   SEQUENCE OF 22-526 FROM N.A.
RX   MEDLINE=87257943; PubMed=3453117;
RA   Ziegler S.F., Marth J.D., Lewis D.B., Perlmutter R.M.;
RT   "Novel protein-tyrosine kinase gene (hck) preferentially expressed in
RT   cells of hematopoietic origin.";
RL   Mol. Cell. Biol. 7:2276-2285(1987).
RN   [3]
RP   SEQUENCE OF 1-22 FROM N.A., AND ALTERNATIVE INITIATION.
RX   MEDLINE=91342636; PubMed=1875927;
RA   Lock P., Ralph S., Stanley E., Boulet I., Ramsay R., Dunn A.R.;
RT   "Two isoforms of murine hck, generated by utilization of alternative
RT   translational initiation codons, exhibit different patterns of
RT   subcellular localization.";
RL   Mol. Cell. Biol. 11:4363-4370(1991).
RN   [4]
RP   X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 78-526.
RX   MEDLINE=97177106; PubMed=9024658;
RA   Sicheri F., Moarefi I., Kuriyan J.;
RT   "Crystal structure of the Src family tyrosine kinase Hck.";
RL   Nature 385:602-609(1997).
RN   [5]
RP   STRUCTURE BY NMR OF 78-138.
RX   MEDLINE=98239731; PubMed=9571048;
RA   Horita D.A., Baldisseri D.M., Zhang W., Altieri A.S., Smithgall T.E.,
RA   Gmeiner W.H., Byrd R.A.;
RT   "Solution structure of the human Hck SH3 domain and identification of
RT   its ligand binding site.";
RL   J. Mol. Biol. 278:253-265(1998).
RN   [6]
RP   STRUCTURE BY NMR OF 139-245.
RX   MEDLINE=97263487; PubMed=9109402;
RA   Zhang W., Smithgall T.E., Gmeiner W.H.;
RT   "Sequential assignment and secondary structure determination for the
RT   Src homology 2 domain of hematopoietic cellular kinase.";
RL   FEBS Lett. 406:131-135(1997).
RN   [7]
RP   X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 81-137.
RX   MEDLINE=98453315; PubMed=9778343;
RA   Arold S., O'Brien R., Franken P., Strub M.P., Hoh F., Dumas C.,
RA   Ladbury J.E.;
RT   "RT loop flexibility enhances the specificity of Src family SH3
RT   domains for HIV-1 Nef.";
RL   Biochemistry 37:14683-14691(1998).
CC   -!- FUNCTION: MAY SERVE AS PART OF A SIGNALING PATHWAY COUPLING THE FC
CC       RECEPTOR TO THE ACTIVATION OF THE RESPIRATORY BURST. MAY ALSO
CC       CONTRIBUTE TO NEUTROPHIL MIGRATION AND MAY REGULATE THE
CC       DEGRANULATION PROCESS OF NEUTROPHILS.
CC   -!- CATALYTIC ACTIVITY: ATP + A PROTEIN TYROSINE = ADP +
CC       PROTEIN TYROSINE PHOSPHATE.
CC   -!- SUBCELLULAR LOCATION: P60-HCK AND P59-HCK ARE ASSOCIATED WITH
CC       MEMBRANES. P60-HCK IS ALSO CYTOPLASMIC (BY SIMILARITY).
CC   -!- ALTERNATIVE PRODUCTS: THE P60-HCK AND P59-HCK ARE PRODUCED BY THE
CC       USE OF ALTERNATIVE INITIATION SITES.
CC   -!- TISSUE SPECIFICITY: EXPRESSED PREDOMINANTLY IN CELLS OF THE
CC       MYELOID AND B-LYMPHOID LINEAGES.
CC   -!- SIMILARITY: CONTAINS 1 SH2 DOMAIN.
CC   -!- SIMILARITY: CONTAINS 1 SH3 DOMAIN.
CC   -!- SIMILARITY: TO OTHER PROTEIN-TYROSINE KINASES IN THE CATALYTIC
CC       DOMAIN. BELONGS TO THE SRC SUBFAMILY.
CC   --------------------------------------------------------------------------
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DR   EMBL; M16591; AAA52643.1; -.
DR   EMBL; M16592; AAA52644.1; -.
DR   PIR; A27812; TVHUHC.
DR   PDB; 2HCK; 20-AUG-97.
DR   PDB; 3HCK; 15-OCT-97.
DR   PDB; 4HCK; 17-JUN-98.
DR   PDB; 5HCK; 17-JUN-98.
DR   PDB; 1AD5; 15-MAY-97.
DR   PDB; 1BU1; 11-NOV-98.
DR   MIM; 142370; -.
DR   INTERPRO; IPR000719; -.
DR   INTERPRO; IPR000980; -.
DR   INTERPRO; IPR001245; -.
DR   INTERPRO; IPR001452; -.
DR   PFAM; PF00017; SH2; 1.
DR   PFAM; PF00018; SH3; 1.
DR   PFAM; PF00069; pkinase; 1.
DR   PRINTS; PR00109; TYRKINASE.
DR   PRINTS; PR00401; SH2DOMAIN.
DR   PRINTS; PR00452; SH3DOMAIN.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS50001; SH2; 1.
DR   PROSITE; PS50002; SH3; 1.
KW   Transferase; Tyrosine-protein kinase; Phosphorylation; ATP-binding;
KW   Myristate; SH2 domain; SH3 domain; Alternative initiation;
KW   3D-structure.
FT   CHAIN         1    526       TYROSINE-PROTEIN KINASE P60-HCK.
FT   CHAIN        22    526       TYROSINE-PROTEIN KINASE P59-HCK.
FT   INIT_MET     22     22       FOR P59-HCK.
FT   LIPID         2      2       MYRISTATE (BY SIMILARITY).
FT   LIPID        23     23       MYRISTATE (BY SIMILARITY).
FT   DOMAIN       78    138       SH3.
FT   DOMAIN      144    241       SH2.
FT   DOMAIN      262    515       PROTEIN KINASE.
FT   NP_BIND     268    276       ATP.
FT   BINDING     290    290       ATP.
FT   ACT_SITE    381    381
FT   MOD_RES     411    411       PHOSPHORYLATION (AUTO-) (BY SIMILARITY).
FT   CONFLICT     24     24       S -> C (IN AAA52644).
SQ   SEQUENCE   526 AA;  59583 MW;  347E877A0A6412B3 CRC64;
     MGGRSSCEDP GCPRDEERAP RMGSMKSKFL 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
//