ID   LYN_HUMAN      STANDARD;      PRT;   511 AA.
AC   P07948;
DT   01-AUG-1988 (Rel. 08, Created)
DT   01-JUN-1994 (Rel. 29, Last sequence update)
DT   30-MAY-2000 (Rel. 39, Last annotation update)
DE   TYROSINE-PROTEIN KINASE LYN (EC 2.7.1.112).
GN   LYN.
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 FROM N.A.
RX   MEDLINE=87172710; PubMed=3561390;
RA   Yamanashi Y., Fukushige S.-I., Semba K., Sukegawa J., Miyajima N.,
RA   Matsubara K.-I., Yamamoto T., Toyoshima K.;
RT   "The yes-related cellular gene lyn encodes a possible tyrosine kinase
RT   similar to p56lck.";
RL   Mol. Cell. Biol. 7:237-243(1987).
RN   [2]
RP   SEQUENCE FROM N.A.
RX   MEDLINE=94171041; PubMed=8125304;
RA   Rider L.G., Raben N., Miller L., Jelsema C.;
RT   "The cDNAs encoding two forms of the LYN protein tyrosine kinase are
RT   expressed in rat mast cells and human myeloid cells.";
RL   Gene 138:219-222(1994).
CC   -!- CATALYTIC ACTIVITY: ATP + A PROTEIN TYROSINE = ADP +
CC       PROTEIN TYROSINE PHOSPHATE.
CC   -!- ALTERNATIVE PRODUCTS: 2 ISOFORMS; LYN A (SHOWN HERE) AND LYN B;
CC       ARE PRODUCED BY ALTERNATIVE SPLICING.
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.
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DR   EMBL; M16038; AAA59540.1; -.
DR   EMBL; M79321; AAB50019.1; -.
DR   PIR; A26719; TVHULY.
DR   HSSP; P08631; 2HCK.
DR   MIM; 165120; -.
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; 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   Proto-oncogene; Tyrosine-protein kinase; Phosphorylation;
KW   Transferase; ATP-binding; Myristate; SH2 domain; SH3 domain;
KW   Palmitate; Lipoprotein; Alternative splicing.
FT   INIT_MET      0      0       BY SIMILARITY.
FT   LIPID         1      1       MYRISTATE (BY SIMILARITY).
FT   LIPID         2      2       PALMITATE (BY SIMILARITY).
FT   DOMAIN       62    122       SH3.
FT   DOMAIN      128    225       SH2.
FT   DOMAIN      246    500       PROTEIN KINASE.
FT   NP_BIND     252    260       ATP (BY SIMILARITY).
FT   BINDING     274    274       ATP (BY SIMILARITY).
FT   ACT_SITE    366    366       BY SIMILARITY.
FT   MOD_RES     396    396       PHOSPHORYLATION (AUTO-) (BY SIMILARITY).
FT   MOD_RES     507    507       PHOSPHORYLATION (BY SIMILARITY).
FT   VARSPLIC     22     42       MISSING (IN ISOFORM LYN B).
SQ   SEQUENCE   511 AA;  58442 MW;  8419CD461204E364 CRC64;
     GCIKSKGKDS LSDDGVDLKT QPVRNTERTI YVRDPTSNKQ QRPVPESQLL PGQRFQTKDP
     EEQGDIVVAL YPYDGIHPDD LSFKKGEKMK VLEEHGEWWK AKSLLTKKEG FIPSNYVAKL
     NTLETEEWFF KDITRKDAER QLLAPGNSAG AFLIRESETL KGSFSLSVRD FDPVHGDVIK
     HYKIRSLDNG GYYISPRITF PCISDMIKHY QKQADGLCRR LEKACISPKP QKPWDKDAWE
     IPRESIKLVK RLGAGQFGEV WMGYYNNSTK VAVKTLKPGT MSVQAFLEEA NLMKTLQHDK
     LVRLYAVVTR EEPIYIITEY MAKGSLLDFL KSDEGGKVLL PKLIDFSAQI AEGMAYIERK
     NYIHRDLRAA NVLVSESLMC KIADFGLARV IEDNEYTARE GAKFPIKWTA PEAINFGCFT
     IKSDVWSFGI LLYEIVTYGK IPYPGRTNAD VMTALSQGYR MPRVENCPDE LYDIMKMCWK
     EKAEERPTFD YLQSVLDDFY TATEGQYQQQ P
//