ID   YRK_CHICK      STANDARD;      PRT;   535 AA.
AC   Q02977;
DT   01-FEB-1994 (Rel. 28, Created)
DT   01-FEB-1994 (Rel. 28, Last sequence update)
DT   01-OCT-1996 (Rel. 34, Last annotation update)
DE   PROTO-ONCOGENE TYROSINE-PROTEIN KINASE YRK (EC 2.7.1.112) (P60-YRK)
DE   (YES RELATED KINASE).
GN   YRK.
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archosauria; Aves; Neognathae; Galliformes; Phasianidae; Phasianinae;
OC   Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   SEQUENCE FROM N.A.
RC   STRAIN=WHITE LEGHORN; TISSUE=BRAIN, AND KIDNEY;
RX   MEDLINE=93205395; PubMed=8455940;
RA   Sudol M., Greulich H., Newman L., Sarkar A., Sukegawa J., Yamamoto T.;
RT   "A novel Yes-related kinase, Yrk, is expressed at elevated levels in
RT   neural and hematopoietic tissues.";
RL   Oncogene 8:823-831(1993).
CC   -!- FUNCTION: MAY PARTICIPATE IN SIGNALING PATHWAYS.
CC   -!- CATALYTIC ACTIVITY: ATP + A PROTEIN TYROSINE = ADP +
CC       PROTEIN TYROSINE PHOSPHATE.
CC   -!- TISSUE SPECIFICITY: THERE ARE ELEVATED LEVELS OF THIS PROTEIN IN
CC       NEURAL AND HEMATOPOIETIC TISSUES.
CC   -!- PTM: PHOSPHORYLATED.
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; X67786; CAA47996.1; -.
DR   PIR; S29553; S29553.
DR   PIR; S29626; S29626.
DR   PIR; S33569; S33569.
DR   HSSP; P06241; 1AOT.
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   Proto-oncogene; Transferase; Tyrosine-protein kinase; Phosphorylation;
KW   ATP-binding; Myristate; SH3 domain; SH2 domain; Palmitate;
KW   Lipoprotein.
FT   INIT_MET      0      0       BY SIMILARITY.
FT   LIPID         1      1       MYRISTATE (BY SIMILARITY).
FT   LIPID         2      2       PALMITATE (BY SIMILARITY).
FT   LIPID         5      5       PALMITATE (BY SIMILARITY).
FT   DOMAIN       80    141       SH3.
FT   DOMAIN      147    244       SH2.
FT   DOMAIN      269    522       PROTEIN KINASE.
FT   NP_BIND     275    283       ATP (BY SIMILARITY).
FT   BINDING     297    297       ATP (BY SIMILARITY).
FT   ACT_SITE    388    388       BY SIMILARITY.
FT   MOD_RES     418    418       PHOSPHORYLATION (AUTO-) (BY SIMILARITY).
FT   MOD_RES     529    529       PHOSPHORYLATION (BY SIMILARITY).
SQ   SEQUENCE   535 AA;  59871 MW;  FC994293000EE987 CRC64;
     GCVHCKEKIS GKGQGGSGTG TPAHPPSQYD PDPTQLSGAF THIPDFNNFH AAAVSPPVPF
     SGPGFYPCNT LQAHSSITGG GVTLFIALYD YEARTEDDLS FQKGEKFHII NNTEGDWWEA
     RSLSSGATGY IPSNYVAPVD SIQAEEWYFG KIGRKDAERQ LLCHGNCRGT FLIRESETTK
     GAYSLSIRDW DEAKGDHVKH YKIRKLDSGG YYITTRAQFD TIQQLVQHYI ERAAGLCCRL
     AVPCPKGTPK LADLSVKTKD VWEIPRESLQ LLQKLGNGQF GEVWMGTWNG TTKVAVKTLK
     PGTMSPEAFL EEAQIMKRLR HDKLVQLYAV VSEEPIYIVT EFMSQGSLLD FLKDGDGRYL
     KLPQLVDMAA QIAAGMAYIE RMNYIHRDLR AANILVGDNL VCKIADFGLA RLIEDNEYTA
     RQGAKFPIKW TAPEAALFGK FTIKSDVWSF GILLTELVTK GRVPYPGMNN REVLEQVERG
     YRMQCPGGCP PSLHDVMVQC WKREPEERPT FEYLQSFLED YFTATEPQYQ PGDNQ
//