ID   B4DG79_HUMAN            Unreviewed;       419 AA.
AC   B4DG79;
DT   23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   23-SEP-2008, sequence version 1.
DT   27-MAR-2024, entry version 100.
DE   RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE            EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
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:BAG57690.1};
RN   [1] {ECO:0000313|EMBL:BAG57690.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Amygdala {ECO:0000313|EMBL:BAG57690.1};
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 focused on splicing variants.";
RL   Submitted (OCT-2007) 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=2.7.11.1;
CC         Evidence={ECO:0000256|ARBA:ARBA00001433};
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=2.7.11.1; Evidence={ECO:0000256|ARBA:ARBA00000775};
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC       protein kinase family. RAC subfamily. {ECO:0000256|ARBA:ARBA00006935}.
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DR   EMBL; AK294453; BAG57690.1; -; mRNA.
DR   RefSeq; NP_001229956.1; NM_001243027.2.
DR   RefSeq; NP_001229957.1; NM_001243028.2.
DR   AlphaFoldDB; B4DG79; -.
DR   SMR; B4DG79; -.
DR   PeptideAtlas; B4DG79; -.
DR   DNASU; 208; -.
DR   GeneID; 208; -.
DR   CTD; 208; -.
DR   OrthoDB; 3028764at2759; -.
DR   BioGRID-ORCS; 208; 39 hits in 1204 CRISPR screens.
DR   GenomeRNAi; 208; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd05595; STKc_PKB_beta; 1.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR000961; AGC-kinase_C.
DR   InterPro; IPR034677; Akt2.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR001849; PH_domain.
DR   InterPro; IPR017892; Pkinase_C.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR24351:SF192; PROTEIN KINASE C; 1.
DR   PANTHER; PTHR24351; RIBOSOMAL PROTEIN S6 KINASE; 1.
DR   Pfam; PF00169; PH; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   Pfam; PF00433; Pkinase_C; 1.
DR   SMART; SM00133; S_TK_X; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR   Genevisible; B4DG79; HS.
PE   2: Evidence at transcript level;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU10141};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:BAG57690.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527,
KW   ECO:0000256|RuleBase:RU000304};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          1..46
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   DOMAIN          90..347
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          348..419
FT                   /note="AGC-kinase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51285"
FT   BINDING         129
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   419 AA;  48502 MW;  67AEDEBB2CDC2D53 CRC64;
     MKTERPRPNT FVIRCLQWTT VIERTFHVDS PDEREEWMRA IQMVANSLKQ RAPGEDPMDY
     KCGSPSDSST TEEMEVAVSK ARAKVTMNDF DYLKLLGKGT FGKVILVREK ATGRYYAMKI
     LRKEVIIAKD EVAHTVTESR VLQNTRHPFL TALKYAFQTH DRLCFVMEYA NGGELFFHLS
     RERVFTEERA RFYGAEIVSA LEYLHSRDVV YRDIKLENLM LDKDGHIKIT DFGLCKEGIS
     DGATMKTFCG TPEYLAPEVL EDNDYGRAVD WWGLGVVMYE MMCGRLPFYN QDHERLFELI
     LMEEIRFPRT LSPEAKSLLA GLLKKDPKQR LGGGPSDAKE VMEHRFFLSI NWQDVVQKKL
     LPPFKPQVTS EVDTRYFDDE FTAQSITITP PDRYDSLGLL ELDQRTHFPQ FSYSASIRE
//