ID   KS6R_MOUSE              Reviewed;         278 AA.
AC   Q5SYL1;
DT   03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 121.
DE   RecName: Full=Ribosomal protein S6 kinase-related protein {ECO:0000305};
DE            EC=2.7.11.1 {ECO:0000255|PROSITE-ProRule:PRU00159};
GN   Name=Rskr {ECO:0000250|UniProtKB:Q96LW2};
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. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR   EMBL; AL591070; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; Q5SYL1; -.
DR   SMR; Q5SYL1; -.
DR   STRING; 10090.ENSMUSP00000038139; -.
DR   PhosphoSitePlus; Q5SYL1; -.
DR   PaxDb; Q5SYL1; -.
DR   PRIDE; Q5SYL1; -.
DR   Antibodypedia; 26388; 53 antibodies from 13 providers.
DR   Ensembl; ENSMUST00000046361; ENSMUSP00000038139; ENSMUSG00000037593.
DR   UCSC; uc033fyn.1; mouse.
DR   MGI; MGI:2652869; Rskr.
DR   VEuPathDB; HostDB:ENSMUSG00000037593; -.
DR   eggNOG; KOG0694; Eukaryota.
DR   GeneTree; ENSGT00940000160082; -.
DR   HOGENOM; CLU_000288_63_0_1; -.
DR   InParanoid; Q5SYL1; -.
DR   PhylomeDB; Q5SYL1; -.
DR   TreeFam; TF331546; -.
DR   ChiTaRS; Rskr; mouse.
DR   PRO; PR:Q5SYL1; -.
DR   Proteomes; UP000000589; Chromosome 11.
DR   RNAct; Q5SYL1; protein.
DR   Bgee; ENSMUSG00000037593; Expressed in retinal neural layer and 65 other tissues.
DR   ExpressionAtlas; Q5SYL1; baseline and differential.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004672; F:protein 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:0006468; P:protein 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   Pfam; PF00069; Pkinase; 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   3: Inferred from homology;
KW   ATP-binding; Kinase; Nucleotide-binding; Reference proteome;
KW   Serine/threonine-protein kinase; Transferase.
FT   CHAIN           1..278
FT                   /note="Ribosomal protein S6 kinase-related protein"
FT                   /id="PRO_0000250647"
FT   DOMAIN          100..278
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   ACT_SITE        222
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         106..114
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         129
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ   SEQUENCE   278 AA;  31682 MW;  00DF615E93861F68 CRC64;
     MGAVSCRQGQ HTRVSAPQKG DNIQGHWVQG WKSLWCGMGT IRSGLEELWG LQRHQCLHQE
     LLQPAPLLLE KPQSEWPVPQ FISLFLPEFP VRPVREQQEL KILGLVAKGS FGTVLKVLDC
     AQKAVFAVKV VPKVKVLQRD TLRQCKEEVS IQRQINHPFV HSLGDSWQGK QHLFIMCSYC
     SMDLYSLWST VGWFPEDSIR LFAAELVLVL CYLHDLGIIH RDVKMENILL DERGHLKVTD
     FGLSRHLSQG ARAYTICGTL QYMGEREAKV GREGDLRM