SBK1_RAT
ID SBK1_RAT Reviewed; 417 AA.
AC Q9Z335; A2RRT7;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 135.
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 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 [MRNA], MUTAGENESIS OF LYS-73, FUNCTION, TISSUE
RP SPECIFICITY, AND SUBCELLULAR LOCATION.
RC STRAIN=Wistar; TISSUE=Hippocampus;
RX PubMed=11322885; DOI=10.1046/j.1432-1327.2001.02157.x;
RA Nara K., Akasako Y., Matsuda Y., Fukazawa Y., Iwashita S., Kataoka M.,
RA Nagai Y.;
RT "Cloning and characterization of a novel serine/threonine protein kinase
RT gene expressed predominantly in developing brain.";
RL Eur. J. Biochem. 268:2642-2651(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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:0000269|PubMed:11322885}.
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:0000269|PubMed:11322885}.
CC -!- TISSUE SPECIFICITY: Mainly expressed in brain, with small amounts in
CC heart, liver, kidney and heart. {ECO:0000269|PubMed:11322885}.
CC -!- DEVELOPMENTAL STAGE: Detected in developing brain with a peak at E18.
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; AB010154; BAA36362.1; -; mRNA.
DR EMBL; BC131843; AAI31844.1; -; mRNA.
DR RefSeq; NP_671476.1; NM_147135.2.
DR RefSeq; XP_008757084.1; XM_008758862.2.
DR RefSeq; XP_008757086.1; XM_008758864.2.
DR RefSeq; XP_008758076.1; XM_008759854.2.
DR RefSeq; XP_017444131.1; XM_017588642.1.
DR AlphaFoldDB; Q9Z335; -.
DR SMR; Q9Z335; -.
DR STRING; 10116.ENSRNOP00000025808; -.
DR PhosphoSitePlus; Q9Z335; -.
DR PaxDb; Q9Z335; -.
DR Ensembl; ENSRNOT00000082228; ENSRNOP00000073472; ENSRNOG00000067387.
DR GeneID; 113907; -.
DR KEGG; rno:113907; -.
DR UCSC; RGD:628713; rat.
DR CTD; 388228; -.
DR RGD; 628713; Sbk1.
DR eggNOG; KOG1345; Eukaryota.
DR GeneTree; ENSGT00940000154852; -.
DR HOGENOM; CLU_000288_10_1_1; -.
DR InParanoid; Q9Z335; -.
DR OMA; IFCFIKY; -.
DR OrthoDB; 1221624at2759; -.
DR PhylomeDB; Q9Z335; -.
DR TreeFam; TF326736; -.
DR PRO; PR:Q9Z335; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000019082; Expressed in ovary and 19 other tissues.
DR Genevisible; Q9Z335; RN.
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; IDA:RGD.
DR GO; GO:0007420; P:brain development; IEP:RGD.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IDA:RGD.
DR GO; GO:0018107; P:peptidyl-threonine phosphorylation; IDA:RGD.
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..417
FT /note="Serine/threonine-protein kinase SBK1"
FT /id="PRO_0000238453"
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"
FT MUTAGEN 73
FT /note="K->M: Loss of activity."
FT /evidence="ECO:0000269|PubMed:11322885"
SQ SEQUENCE 417 AA; 45676 MW; C4D36608EE6EE208 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 KPPGDRLPGP LRLEAPGPLK RTVLTESGSG
SRPSPPSVGP VVPVPVPVPV PVPEAGLAPP APPGRTDGRA DKSKGQVVLA TAIEICV
