SBK2_MOUSE
ID SBK2_MOUSE Reviewed; 362 AA.
AC P0C5K1; E9QLZ2;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2013, sequence version 2.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Serine/threonine-protein kinase SBK2;
DE EC=2.7.11.1;
DE AltName: Full=SH3-binding domain kinase family member 2;
DE AltName: Full=Sugen kinase 69;
DE Short=SgK069;
GN Name=Sbk2; Synonyms=Sgk069;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
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; AC157563; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS51980.1; -.
DR RefSeq; NP_001139801.1; NM_001146329.1.
DR RefSeq; XP_006540202.1; XM_006540139.2.
DR AlphaFoldDB; P0C5K1; -.
DR SMR; P0C5K1; -.
DR STRING; 10090.ENSMUSP00000138504; -.
DR MaxQB; P0C5K1; -.
DR PaxDb; P0C5K1; -.
DR PRIDE; P0C5K1; -.
DR ProteomicsDB; 255461; -.
DR Antibodypedia; 33118; 50 antibodies from 16 providers.
DR DNASU; 381836; -.
DR Ensembl; ENSMUST00000032598; ENSMUSP00000032598; ENSMUSG00000030433.
DR Ensembl; ENSMUST00000182214; ENSMUSP00000138504; ENSMUSG00000030433.
DR GeneID; 381836; -.
DR KEGG; mmu:381836; -.
DR UCSC; uc012exa.1; mouse.
DR CTD; 646643; -.
DR MGI; MGI:2685925; Sbk2.
DR VEuPathDB; HostDB:ENSMUSG00000030433; -.
DR eggNOG; KOG1345; Eukaryota.
DR GeneTree; ENSGT00940000161663; -.
DR HOGENOM; CLU_000288_10_0_1; -.
DR InParanoid; P0C5K1; -.
DR OMA; HRQKGTT; -.
DR OrthoDB; 1221624at2759; -.
DR PhylomeDB; P0C5K1; -.
DR TreeFam; TF326736; -.
DR BioGRID-ORCS; 381836; 3 hits in 74 CRISPR screens.
DR PRO; PR:P0C5K1; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; P0C5K1; protein.
DR Bgee; ENSMUSG00000030433; Expressed in zone of skin and 23 other tissues.
DR ExpressionAtlas; P0C5K1; baseline and differential.
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 3: Inferred from homology;
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_0000308264"
FT DOMAIN 62..330
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 329..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; 39699 MW; 3E3A1B156C777F26 CRC64;
MPGKQSEDKP MEVSTVEDGG DEGLGGLTVE ELQQGQEAAL ALEDMMALSA QTLVQTEVEE
LYEEVRPLGQ GRFGRVLLVT HRQKGTPLAL KQLPKQSTSL RGFLYEFCVG LSLGTHSAIV
TAYGIGIESA NSYSFLTEPV LHGDLITFIQ PKVGLPQPAA QRCAAQLASA LEHIHSHGLV
YRDLKPENVL VCDPACQRVK LTDFGHTRPR GTLLRLTGPP IPYTAPELCA PPPLPEGLPI
QPSLDAWALG VLIFCLLTGY FPWDQPLVEV DPFFEDFLIW QASGQPQDRP QPWYSLSPAA
DTLLWGLLDP HPRKRNPVGS IKSYLGQPWK QREGEAEELA TELREDGWRG GQEAAKGEQP
AC
