ID   B7ZA00_HUMAN            Unreviewed;       314 AA.
AC   B7ZA00;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   27-MAR-2024, entry version 79.
DE   RecName: Full=cAMP-dependent protein kinase {ECO:0000256|ARBA:ARBA00012444};
DE            EC=2.7.11.11 {ECO:0000256|ARBA:ARBA00012444};
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606 {ECO:0000313|EMBL:BAH14486.1};
RN   [1] {ECO:0000313|EMBL:BAH14486.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Thalamus {ECO:0000313|EMBL:BAH14486.1};
RA   Wakamatsu A., Yamamoto J., Kimura K., Ishii S., Watanabe K., Sugiyama A.,
RA   Murakawa K., Kaida T., Tsuchiya K., Fukuzumi Y., Kumagai A., Oishi Y.,
RA   Yamamoto S., Ono Y., Komori Y., Yamazaki M., Kisu Y., Nishikawa T.,
RA   Sugano S., Nomura N., Isogai T.;
RT   "NEDO human cDNA sequencing project.";
RL   Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC         [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC         COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.11;
CC         Evidence={ECO:0000256|ARBA:ARBA00001036};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC         threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC         Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC         EC=2.7.11.11; Evidence={ECO:0000256|ARBA:ARBA00000541};
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC       protein kinase family. cAMP subfamily. {ECO:0000256|ARBA:ARBA00007115}.
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DR   EMBL; AK316115; BAH14486.1; -; mRNA.
DR   RefSeq; NP_001229791.1; NM_001242862.2.
DR   AlphaFoldDB; B7ZA00; -.
DR   PeptideAtlas; B7ZA00; -.
DR   DNASU; 5567; -.
DR   GeneID; 5567; -.
DR   CTD; 5567; -.
DR   OrthoDB; 10768at2759; -.
DR   BioGRID-ORCS; 5567; 20 hits in 1191 CRISPR screens.
DR   GenomeRNAi; 5567; -.
DR   GO; GO:0004679; F:AMP-activated protein kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004691; F:cAMP-dependent protein kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd14209; STKc_PKA; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR000961; AGC-kinase_C.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   InterPro; IPR044109; STKc_PKA.
DR   PANTHER; PTHR24353:SF116; CAMP-DEPENDENT PROTEIN KINASE CATALYTIC SUBUNIT BETA; 1.
DR   PANTHER; PTHR24353; CYCLIC NUCLEOTIDE-DEPENDENT PROTEIN KINASE; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00133; S_TK_X; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR   Genevisible; B7ZA00; HS.
PE   2: Evidence at transcript level;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; cAMP {ECO:0000256|ARBA:ARBA00023149};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:BAH14486.1};
KW   Lipoprotein {ECO:0000256|ARBA:ARBA00022707};
KW   Myristate {ECO:0000256|ARBA:ARBA00022707};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527,
KW   ECO:0000256|RuleBase:RU000304};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          7..261
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          262..314
FT                   /note="AGC-kinase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51285"
FT   BINDING         36
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   314 AA;  36479 MW;  F56E02B8C211B94A CRC64;
     MPDLKILKGK KTLGTGSFGR VMLVKHKATE QYYAMKILDK QKVVKLKQIE HTLNEKRILQ
     AVNFPFLVRL EYAFKDNSNL YMVMEYVPGG EMFSHLRRIG RFSEPHARFY AAQIVLTFEY
     LHSLDLIYRD LKPENLLIDH QGYIQVTDFG FAKRVKGRTW TLCGTPEYLA PEIILSKGYN
     KAVDWWALGV LIYEMAAGYP PFFADQPIQI YEKIVSGKVR FPSHFSSDLK DLLRNLLQVD
     LTKRFGNLKN GVSDIKTHKW FATTDWIAIY QRKVEAPFIP KFRGSGDTSN FDDYEEEDIR
     VSITEKCAKE FGEF
//