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Database: UniProt
Entry: F7G4I3_MACMU
LinkDB: F7G4I3_MACMU
Original site: F7G4I3_MACMU 
ID   F7G4I3_MACMU            Unreviewed;       728 AA.
AC   F7G4I3;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   11-DEC-2019, sequence version 3.
DT   27-MAR-2024, entry version 78.
DE   RecName: Full=Ribosomal protein S6 kinase {ECO:0000256|PIRNR:PIRNR000606};
DE            EC=2.7.11.1 {ECO:0000256|PIRNR:PIRNR000606};
GN   Name=RPS6KA5 {ECO:0000313|Ensembl:ENSMMUP00000007383.4,
GN   ECO:0000313|VGNC:VGNC:76931};
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544 {ECO:0000313|Ensembl:ENSMMUP00000007383.4, ECO:0000313|Proteomes:UP000006718};
RN   [1] {ECO:0000313|Proteomes:UP000006718}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=17573 {ECO:0000313|Proteomes:UP000006718};
RX   PubMed=17431167; DOI=10.1126/science.1139247;
RA   Gibbs R.A., Rogers J., Katze M.G., Bumgarner R., Weinstock G.M.,
RA   Mardis E.R., Remington K.A., Strausberg R.L., Venter J.C., Wilson R.K.,
RA   Batzer M.A., Bustamante C.D., Eichler E.E., Hahn M.W., Hardison R.C.,
RA   Makova K.D., Miller W., Milosavljevic A., Palermo R.E., Siepel A.,
RA   Sikela J.M., Attaway T., Bell S., Bernard K.E., Buhay C.J.,
RA   Chandrabose M.N., Dao M., Davis C., Delehaunty K.D., Ding Y., Dinh H.H.,
RA   Dugan-Rocha S., Fulton L.A., Gabisi R.A., Garner T.T., Godfrey J.,
RA   Hawes A.C., Hernandez J., Hines S., Holder M., Hume J., Jhangiani S.N.,
RA   Joshi V., Khan Z.M., Kirkness E.F., Cree A., Fowler R.G., Lee S.,
RA   Lewis L.R., Li Z., Liu Y.-S., Moore S.M., Muzny D., Nazareth L.V.,
RA   Ngo D.N., Okwuonu G.O., Pai G., Parker D., Paul H.A., Pfannkoch C.,
RA   Pohl C.S., Rogers Y.-H.C., Ruiz S.J., Sabo A., Santibanez J.,
RA   Schneider B.W., Smith S.M., Sodergren E., Svatek A.F., Utterback T.R.,
RA   Vattathil S., Warren W., White C.S., Chinwalla A.T., Feng Y., Halpern A.L.,
RA   Hillier L.W., Huang X., Minx P., Nelson J.O., Pepin K.H., Qin X.,
RA   Sutton G.G., Venter E., Walenz B.P., Wallis J.W., Worley K.C., Yang S.-P.,
RA   Jones S.M., Marra M.A., Rocchi M., Schein J.E., Baertsch R., Clarke L.,
RA   Csuros M., Glasscock J., Harris R.A., Havlak P., Jackson A.R., Jiang H.,
RA   Liu Y., Messina D.N., Shen Y., Song H.X.-Z., Wylie T., Zhang L., Birney E.,
RA   Han K., Konkel M.K., Lee J., Smit A.F.A., Ullmer B., Wang H., Xing J.,
RA   Burhans R., Cheng Z., Karro J.E., Ma J., Raney B., She X., Cox M.J.,
RA   Demuth J.P., Dumas L.J., Han S.-G., Hopkins J., Karimpour-Fard A.,
RA   Kim Y.H., Pollack J.R., Vinar T., Addo-Quaye C., Degenhardt J., Denby A.,
RA   Hubisz M.J., Indap A., Kosiol C., Lahn B.T., Lawson H.A., Marklein A.,
RA   Nielsen R., Vallender E.J., Clark A.G., Ferguson B., Hernandez R.D.,
RA   Hirani K., Kehrer-Sawatzki H., Kolb J., Patil S., Pu L.-L., Ren Y.,
RA   Smith D.G., Wheeler D.A., Schenck I., Ball E.V., Chen R., Cooper D.N.,
RA   Giardine B., Hsu F., Kent W.J., Lesk A., Nelson D.L., O'brien W.E.,
RA   Pruefer K., Stenson P.D., Wallace J.C., Ke H., Liu X.-M., Wang P.,
RA   Xiang A.P., Yang F., Barber G.P., Haussler D., Karolchik D., Kern A.D.,
RA   Kuhn R.M., Smith K.E., Zwieg A.S.;
RT   "Evolutionary and biomedical insights from the rhesus macaque genome.";
RL   Science 316:222-234(2007).
RN   [2] {ECO:0000313|Ensembl:ENSMMUP00000007383.4}
RP   IDENTIFICATION.
RC   STRAIN=17573 {ECO:0000313|Ensembl:ENSMMUP00000007383.4};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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         Evidence={ECO:0000256|PIRNR:PIRNR000606};
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; Evidence={ECO:0000256|PIRNR:PIRNR000606};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946,
CC         ECO:0000256|PIRNR:PIRNR000606};
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC       protein kinase family. S6 kinase subfamily.
CC       {ECO:0000256|ARBA:ARBA00009804, ECO:0000256|PIRNR:PIRNR000606}.
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DR   AlphaFoldDB; F7G4I3; -.
DR   SMR; F7G4I3; -.
DR   Ensembl; ENSMMUT00000007856.4; ENSMMUP00000007383.4; ENSMMUG00000005586.4.
DR   VEuPathDB; HostDB:ENSMMUG00000005586; -.
DR   VGNC; VGNC:76931; RPS6KA5.
DR   GeneTree; ENSGT00940000156886; -.
DR   HOGENOM; CLU_000288_58_0_1; -.
DR   TreeFam; TF313438; -.
DR   Proteomes; UP000006718; Chromosome 7.
DR   Bgee; ENSMMUG00000005586; Expressed in Ammon's horn and 21 other cell types or tissues.
DR   ExpressionAtlas; F7G4I3; baseline.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
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:0035556; P:intracellular signal transduction; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd14179; STKc_MSK1_C; 1.
DR   CDD; cd05613; STKc_MSK1_N; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 2.
DR   InterPro; IPR000961; AGC-kinase_C.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR017892; Pkinase_C.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR016239; Ribosomal_S6_kinase_II.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR24351; RIBOSOMAL PROTEIN S6 KINASE; 1.
DR   PANTHER; PTHR24351:SF115; RIBOSOMAL PROTEIN S6 KINASE ALPHA-5; 1.
DR   Pfam; PF00069; Pkinase; 2.
DR   Pfam; PF00433; Pkinase_C; 1.
DR   PIRSF; PIRSF000606; Ribsml_S6_kin_2; 1.
DR   SMART; SM00133; S_TK_X; 1.
DR   SMART; SM00220; S_TKc; 2.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 2.
DR   PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 2.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 2.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 2.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRNR:PIRNR000606};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|PIRNR:PIRNR000606};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|PIRNR:PIRNR000606};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006718};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527,
KW   ECO:0000256|PIRNR:PIRNR000606};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000606}.
FT   DOMAIN          36..305
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          306..374
FT                   /note="AGC-kinase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51285"
FT   DOMAIN          413..674
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   ACT_SITE        164
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000606-50"
FT   ACT_SITE        531
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000606-50"
FT   BINDING         42..50
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000606-51"
FT   BINDING         68
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000606-51,
FT                   ECO:0000256|PROSITE-ProRule:PRU10141"
FT   BINDING         419..427
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000606-51"
FT   BINDING         442
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000606-51,
FT                   ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   728 AA;  82226 MW;  56399B0BEF63DB95 CRC64;
     MSLLPLPAQV THVCLRPVGA KANLTGHAEK VGIENFELLK VLGTGAYGKV FLVRKISGHD
     TGKLYAMKVL KKATIVQKAK TTEHTRTERQ VLEHIRQSPF LVTLHYAFQT ETKLHLILDY
     INGGELFTHL SQRERFTEHE VQIYVGEIVL ALEHLHKLGI IYRDIKLENI LLDSNGHVVL
     TDFGLSKEFV ADETERAYSF CGTIEYMAPD IVRGGDSGHD KAVDWWSLGV LMYELLTGAS
     PFTVDGEKNS QAEISRRILK SEPPYPQEMS ALAKDLIQRL LMKDPKKRLG CGPRDADEIK
     EHLFFQKINW DDLAAKKVPA PFKPVIRDEL DVSNFAEEFT EMDPTYSPAA LPQSSEKLFQ
     GYSFVAPSIL FKRNAAVIDP LQFHMGVERP GVTNVARSAM MKDSPFYQHY DLDLKDKPLG
     EGSFSICRKC VHKKSNQAFA VKIISKRMEA NTQKEITALK LCEGHPNIVK LHEVFHDQLH
     TFLVMELLNG GELFERIKRK KHFSETEASY IMRKLVSAVS HMHDVGVVHR DLKPENLLFT
     DENDNLEIKI IDFGFARLKP PDNQPLKTPC FTLHYAAPEL LNQNGYDESC DLWSLGVILY
     TMLSGQVPFQ SHDRSLTCTS AVEIMKKIKK GDFSFEGEAW KNVSQEAKDL IQGLLTVDPN
     KRLKMSGLRY NEWLQDGSQL SSNPLMTPDI LGSSGAAVHT CVKATFHAFN KYKREGFCLQ
     NVDKAPLA
//
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