SBK1_MOUSE
ID SBK1_MOUSE Reviewed; 417 AA.
AC Q8QZX0;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Serine/threonine-protein kinase SBK1;
DE EC=2.7.11.1;
DE AltName: Full=SH3-binding kinase 1;
GN Name=Sbk1; Synonyms=Sbk;
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 MRNA].
RC STRAIN=FVB/N; TISSUE=Liver;
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 -!- FUNCTION: May be involved in signal-transduction pathways related to
CC the control of brain development. {ECO:0000250}.
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 -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; BC024114; AAH24114.1; -; mRNA.
DR EMBL; BC025837; AAH25837.1; -; mRNA.
DR EMBL; BC031759; AAH31759.1; -; mRNA.
DR CCDS; CCDS21824.1; -.
DR RefSeq; NP_663562.1; NM_145587.2.
DR RefSeq; XP_017177409.1; XM_017321920.1.
DR AlphaFoldDB; Q8QZX0; -.
DR SMR; Q8QZX0; -.
DR STRING; 10090.ENSMUSP00000060907; -.
DR PhosphoSitePlus; Q8QZX0; -.
DR MaxQB; Q8QZX0; -.
DR PaxDb; Q8QZX0; -.
DR PRIDE; Q8QZX0; -.
DR ProteomicsDB; 256839; -.
DR Antibodypedia; 55882; 22 antibodies from 13 providers.
DR DNASU; 104175; -.
DR Ensembl; ENSMUST00000056028; ENSMUSP00000060907; ENSMUSG00000042978.
DR GeneID; 104175; -.
DR KEGG; mmu:104175; -.
DR UCSC; uc009jqw.1; mouse.
DR CTD; 388228; -.
DR MGI; MGI:2135937; Sbk1.
DR VEuPathDB; HostDB:ENSMUSG00000042978; -.
DR eggNOG; KOG1345; Eukaryota.
DR GeneTree; ENSGT00940000154852; -.
DR HOGENOM; CLU_000288_10_1_1; -.
DR InParanoid; Q8QZX0; -.
DR OMA; IFCFIKY; -.
DR OrthoDB; 1221624at2759; -.
DR PhylomeDB; Q8QZX0; -.
DR TreeFam; TF326736; -.
DR BioGRID-ORCS; 104175; 1 hit in 76 CRISPR screens.
DR ChiTaRS; Sbk1; mouse.
DR PRO; PR:Q8QZX0; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q8QZX0; protein.
DR Bgee; ENSMUSG00000042978; Expressed in rostral migratory stream and 249 other tissues.
DR ExpressionAtlas; Q8QZX0; baseline and differential.
DR Genevisible; Q8QZX0; MM.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; ISO:MGI.
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 2: Evidence at transcript level;
KW ATP-binding; Cytoplasm; Kinase; Nucleotide-binding; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..417
FT /note="Serine/threonine-protein kinase SBK1"
FT /id="PRO_0000238452"
FT DOMAIN 53..318
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 321..405
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 366..390
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 174
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 59..67
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 82
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ SEQUENCE 417 AA; 45696 MW; C6A79A28EE6D2EC7 CRC64;
MSVGCPEPEP LHSLPCCGPG AAPVPGAGVP LLTEDMQALT LRTLAASDVT KHYELVRELG
KGTYGKVDLV AYKGTGTKMA LKFVNKSKTK LKNFLREVSI TNSLSSSPFI IKVFDVVFET
EECYVFAQEY APAGDLFDII PPQVGLPEDT VKRCVQQLGL ALDFMHSRQL VHRDIKPENV
LLFDRECRRV KLADFGMTRR VGCRVKRVSG TIPYTAPEVC QAGRADGFAV DTGVDVWAFG
VLIFCVLTGN FPWEAASGAD AFFEEFVRWQ RGRLPGLPSQ WRRFTEPALR MFQRLLALEP
ERRGPAKEVF RFLKHELTSE LRRRPSHRAR KPPGDRLPGS LRLEAPGPLK RTVLTESGSG
SRPSPPSVGP VVPVPVPVPV PVPEAGLAPP APPGRTDGRT DKSKGQVVLA TAIEICV
