ID   SBK2_RAT                Reviewed;         362 AA.
AC   B1WBU5;
DT   16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 1.
DT   03-AUG-2022, entry version 82.
DE   RecName: Full=Serine/threonine-protein kinase SBK2;
DE            EC=2.7.11.1;
DE   AltName: Full=SH3-binding domain kinase family member 2;
GN   Name=Sbk2;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Heart;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
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   -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC       kinase family. STKL subfamily. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR   EMBL; CH474075; EDL75876.1; -; Genomic_DNA.
DR   EMBL; BC161893; AAI61893.1; -; mRNA.
DR   RefSeq; NP_001121011.1; NM_001127539.2.
DR   RefSeq; XP_017445240.1; XM_017589751.1.
DR   AlphaFoldDB; B1WBU5; -.
DR   SMR; B1WBU5; -.
DR   STRING; 10116.ENSRNOP00000055736; -.
DR   PaxDb; B1WBU5; -.
DR   Ensembl; ENSRNOT00000058956; ENSRNOP00000055736; ENSRNOG00000038625.
DR   GeneID; 691411; -.
DR   KEGG; rno:691411; -.
DR   UCSC; RGD:1563279; rat.
DR   CTD; 646643; -.
DR   RGD; 1563279; Sbk2.
DR   eggNOG; KOG1345; Eukaryota.
DR   GeneTree; ENSGT00940000161663; -.
DR   HOGENOM; CLU_000288_10_0_1; -.
DR   InParanoid; B1WBU5; -.
DR   OMA; HRQKGTT; -.
DR   OrthoDB; 1221624at2759; -.
DR   PhylomeDB; B1WBU5; -.
DR   TreeFam; TF326736; -.
DR   PRO; PR:B1WBU5; -.
DR   Proteomes; UP000002494; Chromosome 1.
DR   Proteomes; UP000234681; Chromosome 1.
DR   Bgee; ENSRNOG00000038625; Expressed in esophagus and 3 other tissues.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004708; F:MAP kinase kinase activity; IBA:GO_Central.
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:0000165; P:MAPK cascade; IBA:GO_Central.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
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   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Kinase; Nucleotide-binding; Reference proteome; Repeat;
KW   Serine/threonine-protein kinase; Transferase.
FT   CHAIN           1..362
FT                   /note="Serine/threonine-protein kinase SBK2"
FT                   /id="PRO_0000376932"
FT   DOMAIN          62..330
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          317..362
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        331..352
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        183
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         68..76
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         91
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ   SEQUENCE   362 AA;  39773 MW;  D7FAB1FD9A219CC2 CRC64;
     MPGKQSEDRP MEVAAVEDGG DEGLGGLTVE ELQQGQEAAL ALEDMMALSA QTLVRTEVEE
     LYEEVRPLGQ GRFGRVLLVT HRQKGTPLAL KQLPKHSTSL RSFLYEFCVG LSLGTHPAIV
     AAYGIGIESA NSYSFLTEPV LHGDLITFIK PKVGLPQPAV QRCAAQLASA LEHIHSHGLV
     YRDLKPENVL VCDPACQRVK LTDFGHTRPR GTMLRLTGPP IPYTAPELCA PPPLPEGLPI
     QPALDAWALG VLIFCLLTGY FPWDQPLVEV DPFFEDFLIW QASGQPQDRP QPWYNLSPAA
     DTLLWGLLDP HPRKRNPVSS IKSYLGQPWK QREEGAEELT KELREDGSRG GQEAAKGEQP
     AC