ID   SBK1_DANRE              Reviewed;         385 AA.
AC   Q90ZY4;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 109.
DE   RecName: Full=Serine/threonine-protein kinase SBK1;
DE            EC=2.7.11.1;
DE   AltName: Full=Brain-specific protein kinase BSK146;
DE   AltName: Full=SH3-binding kinase 1;
GN   Name=sbk1; Synonyms=bsk146;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], MUTAGENESIS OF LYS-61, FUNCTION, TISSUE
RP   SPECIFICITY, AND SUBCELLULAR LOCATION.
RX   PubMed=16403448; DOI=10.1016/j.bbrc.2005.12.090;
RA   Chou C.-M., Chen Y.-C., Lee M.-T., Chen G.-D., Lu I.-C., Chen S.-T.,
RA   Huang C.-J.;
RT   "Expression and characterization of a brain-specific protein kinase BSK146
RT   from zebrafish.";
RL   Biochem. Biophys. Res. Commun. 340:767-775(2006).
CC   -!- FUNCTION: May be involved in the control of neuronal proliferation or
CC       migration in the brain of embryos. {ECO:0000269|PubMed:16403448}.
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   -!- 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;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Mainly expressed in brain.
CC       {ECO:0000269|PubMed:16403448}.
CC   -!- DEVELOPMENTAL STAGE: Expressed predominantly in the developing neural
CC       structures. Levels gradually increases from 36 to 144 hpf.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC       kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR   EMBL; AF265347; AAK52420.1; -; mRNA.
DR   RefSeq; NP_998006.1; NM_212841.1.
DR   AlphaFoldDB; Q90ZY4; -.
DR   SMR; Q90ZY4; -.
DR   STRING; 7955.ENSDARP00000109713; -.
DR   PaxDb; Q90ZY4; -.
DR   GeneID; 405767; -.
DR   KEGG; dre:405767; -.
DR   CTD; 405767; -.
DR   ZFIN; ZDB-GENE-060313-3; bsk146.
DR   eggNOG; KOG1345; Eukaryota.
DR   InParanoid; Q90ZY4; -.
DR   OrthoDB; 1221624at2759; -.
DR   PhylomeDB; Q90ZY4; -.
DR   PRO; PR:Q90ZY4; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004672; F:protein kinase activity; IDA:ZFIN.
DR   GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR   GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR   GO; GO:0018107; P:peptidyl-threonine phosphorylation; IBA:GO_Central.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   InterPro; IPR016234; Ser/Thr_kinase_Sbk1.
DR   Pfam; PF00069; Pkinase; 1.
DR   PIRSF; PIRSF000566; Ser/Thr_PK_Sbk1; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Cytoplasm; Kinase; Nucleotide-binding; Reference proteome;
KW   Serine/threonine-protein kinase; Transferase.
FT   CHAIN           1..385
FT                   /note="Serine/threonine-protein kinase SBK1"
FT                   /id="PRO_0000238454"
FT   DOMAIN          32..297
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          328..374
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        153
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         38..46
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         61
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   MUTAGEN         61
FT                   /note="K->R: Loss of activity."
FT                   /evidence="ECO:0000269|PubMed:16403448"
SQ   SEQUENCE   385 AA;  43913 MW;  54BE4E6D3819EBD2 CRC64;
     MSSSPVVSRD ILEELQLYTA QNLEKLEVNK YYEVIRELGK GTYGKVDLVI HKIRGSKMAL
     KFLKKKSTKL KSFLREYSIS LYLSPCPFII NMFGIAFETD EYYVFAQEYA PSGDLFDIIP
     PQVGLPEPVA KRCVHQVAIA LEYLHSKKLV HRDIKPENIL IFDKECRKVK LSDFGMTRRA
     GSPVKRVSGT IPYTAPELCD TSKHDGFCVD YSTDVWAFGV LLFCMLTGNF PWEKAMPSDT
     FYEEFVRWQK RRTGAVPSQW RRFTDESLRM FRKLLALEQE RRCSVKEVFA HLGHRWMLDG
     TSGNHHQSVL NSSSEEDELL VDRMKQQTLS PTANTSNAIE PGSANHFTSM STNSSVSSTN
     SYERSARDSP PTSRILVTTP IEICV