ID KAPA_HUMAN STANDARD; PRT; 350 AA. AC P17612; DT 01-AUG-1990 (Rel. 15, Created) DT 01-AUG-1990 (Rel. 15, Last sequence update) DT 30-MAY-2000 (Rel. 39, Last annotation update) DE CAMP-DEPENDENT PROTEIN KINASE, ALPHA-CATALYTIC SUBUNIT (EC 2.7.1.37) DE (PKA C-ALPHA). GN PRKACA. 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=88335571; PubMed=2843813; RA Maldonado F., Hanks S.K.; RT "A cDNA clone encoding human cAMP-dependent protein kinase catalytic RT subunit C alpha."; RL Nucleic Acids Res. 16:8189-8190(1988). CC -!- CATALYTIC ACTIVITY: ATP + A PROTEIN = ADP + A PHOSPHOPROTEIN. CC -!- ENZYME REGULATION: THIS ENZYME IS ACTIVATED BY CAMP. CC -!- SUBUNIT: COMPOSED OF TWO REGULATORY CHAINS AND TWO CATALYTIC CC CHAINS. CC -!- SIMILARITY: BELONGS TO THE SER/THR FAMILY OF PROTEIN KINASES. CC CAMP SUBFAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X07767; CAA30597.1; -. DR PIR; S01404; OKHU2C. DR HSSP; P05132; 1CTP. DR MIM; 601639; -. DR INTERPRO; IPR000719; -. DR INTERPRO; IPR000961; -. DR INTERPRO; IPR002290; -. DR PFAM; PF00069; pkinase; 1. DR PFAM; PF00433; pkinase_C; 1. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. KW Transferase; Serine/threonine-protein kinase; ATP-binding; cAMP; KW Phosphorylation; Myristate; Multigene family. FT INIT_MET 0 0 FT LIPID 1 1 MYRISTATE (BY SIMILARITY). FT DOMAIN 43 297 PROTEIN KINASE. FT NP_BIND 49 57 ATP (BY SIMILARITY). FT BINDING 72 72 ATP (BY SIMILARITY). FT ACT_SITE 166 166 BY SIMILARITY. FT MOD_RES 197 197 PHOSPHORYLATION (BY SIMILARITY). FT MOD_RES 338 338 PHOSPHORYLATION (BY SIMILARITY). SQ SEQUENCE 350 AA; 40458 MW; 15A28BEAA820F3C0 CRC64; GNAAAAKKGS EQESVKEFLA KAKEDFLKKW ESPAQNTAHL DQFERIKTLG TGSFGRVMLV KHKETGNHYA MKILDKQKVV KLKQIEHTLN EKRILQAVNF PFLVKLEFSF KDNSNLYMVM EYVPGGEMFS HLRRIGRFSE PHARFYAAQI VLTFEYLHSL DLIYRDLKPE NLLIDQQGYI QVTDFGFAKR VKGRTWTLCG TPEYLAPEII LSKGYNKAVD WWALGVLIYE MAAGYPPFFA DQPIQIYEKI VSGKVRFPSH FSSDLKDLLR NLLQVDLTKR FGNLKNGVND IKNHKWFATT DWIAIYQRKV EAPFIPKFKG PGDTSNFDDY EEEEIRVSIN EKCGKEFSEF //