KS6B2_MOUSE
ID KS6B2_MOUSE Reviewed; 485 AA.
AC Q9Z1M4;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 183.
DE RecName: Full=Ribosomal protein S6 kinase beta-2;
DE Short=S6K-beta-2;
DE Short=S6K2;
DE EC=2.7.11.1;
DE AltName: Full=70 kDa ribosomal protein S6 kinase 2;
DE AltName: Full=p70 ribosomal S6 kinase beta;
DE Short=p70 S6 kinase beta;
DE Short=p70 S6K-beta;
DE Short=p70 S6KB;
GN Name=Rps6kb2;
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 [MRNA].
RX PubMed=9822608; DOI=10.1093/emboj/17.22.6649;
RA Shima H., Pende M., Chen Y., Fumagalli S., Thomas G., Kozma S.C.;
RT "Disruption of the p70(s6k)/p85(s6k) gene reveals a small mouse phenotype
RT and a new functional S6 kinase.";
RL EMBO J. 17:6649-6659(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Placenta;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-420 AND SER-423, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Phosphorylates specifically ribosomal protein S6. Seems to
CC act downstream of mTOR signaling in response to growth factors and
CC nutrients to promote cell proliferation, cell growth and cell cycle
CC progression in an alternative pathway regulated by MEAK7.
CC {ECO:0000250|UniProtKB:Q9UBS0}.
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}. Nucleus {ECO:0000250}.
CC -!- PTM: Phosphorylated and activated by MTOR. Phosphorylation by PKC
CC within the NLS in response to mitogenic stimuli causes cytoplasmic
CC retention.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC protein kinase family. S6 kinase subfamily. {ECO:0000305}.
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DR EMBL; AJ007938; CAA07774.1; -; mRNA.
DR EMBL; AK014412; BAB29335.1; -; mRNA.
DR CCDS; CCDS29419.1; -.
DR RefSeq; NP_067460.1; NM_021485.2.
DR AlphaFoldDB; Q9Z1M4; -.
DR SMR; Q9Z1M4; -.
DR STRING; 10090.ENSMUSP00000025749; -.
DR iPTMnet; Q9Z1M4; -.
DR PhosphoSitePlus; Q9Z1M4; -.
DR EPD; Q9Z1M4; -.
DR jPOST; Q9Z1M4; -.
DR MaxQB; Q9Z1M4; -.
DR PaxDb; Q9Z1M4; -.
DR PRIDE; Q9Z1M4; -.
DR ProteomicsDB; 263470; -.
DR Antibodypedia; 1546; 805 antibodies from 39 providers.
DR DNASU; 58988; -.
DR Ensembl; ENSMUST00000025749; ENSMUSP00000025749; ENSMUSG00000024830.
DR GeneID; 58988; -.
DR KEGG; mmu:58988; -.
DR UCSC; uc008fzb.1; mouse.
DR CTD; 6199; -.
DR MGI; MGI:1927343; Rps6kb2.
DR VEuPathDB; HostDB:ENSMUSG00000024830; -.
DR eggNOG; KOG0598; Eukaryota.
DR GeneTree; ENSGT00940000155062; -.
DR InParanoid; Q9Z1M4; -.
DR OMA; CVIYDMM; -.
DR OrthoDB; 1132245at2759; -.
DR PhylomeDB; Q9Z1M4; -.
DR TreeFam; TF313438; -.
DR BRENDA; 2.7.11.1; 3474.
DR Reactome; R-MMU-198693; AKT phosphorylates targets in the nucleus.
DR BioGRID-ORCS; 58988; 0 hits in 74 CRISPR screens.
DR ChiTaRS; Rps6kb2; mouse.
DR PRO; PR:Q9Z1M4; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q9Z1M4; protein.
DR Bgee; ENSMUSG00000024830; Expressed in bone marrow and 72 other tissues.
DR ExpressionAtlas; Q9Z1M4; baseline and differential.
DR Genevisible; Q9Z1M4; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; ISO:MGI.
DR GO; GO:0042277; F:peptide binding; ISO:MGI.
DR GO; GO:0004672; F:protein kinase activity; IDA:MGI.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0004711; F:ribosomal protein S6 kinase activity; ISO:MGI.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR GO; GO:0045948; P:positive regulation of translational initiation; ISO:MGI.
DR GO; GO:0043491; P:protein kinase B signaling; IGI:MGI.
DR GO; GO:0006468; P:protein phosphorylation; IDA:MGI.
DR GO; GO:0031929; P:TOR signaling; ISS:UniProtKB.
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; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00433; Pkinase_C; 1.
DR SMART; SM00133; S_TK_X; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 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; Nucleus;
KW Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
KW Transferase.
FT CHAIN 1..485
FT /note="Ribosomal protein S6 kinase beta-2"
FT /id="PRO_0000086215"
FT DOMAIN 67..328
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 329..399
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00618"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 407..485
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 474..480
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250"
FT COMPBIAS 409..423
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 433..466
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 194
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 73..81
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 99
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 15
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UBS0"
FT MOD_RES 417
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UBS0"
FT MOD_RES 420
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17242355"
FT MOD_RES 423
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355"
FT MOD_RES 476
FT /note="Phosphoserine; by PKC"
FT /evidence="ECO:0000250|UniProtKB:Q9UBS0"
SQ SEQUENCE 485 AA; 53538 MW; 396929ADAB0F6CB6 CRC64;
MAAVFDLDLE TEEGSEGEGE PEFSPADVCP LGELRAAGLE TVGHYEEVEL TESSVNLGPE
RIGPHCFELL SVLGKGGYGK VFQVRKVQGT NLGKIYAMKV LRKAKIVCSA KDTAHTRAER
NILESVKHPF IVELAYAFQT GGKLYLILEC LSGGELFTHL EREGIFLEDT ACFYLAEITL
ALGHLHSHGI IYRDLKPENI MLSSQGHIKL TDFGLCKESI HEGAITHTFC GTIEYMAPEI
LVRTGHNRAV DWWSLGALMY DMLTGSPPFT AENRKKTMDK IIKGKLVLPP YLTPDARDLA
KKFLKRNPTQ RIGGGLGDAA DVQRHPFFRH INWDDLLARR VDPPFRPSLQ SEEDVSQFDA
RFTRQTPVDS PDDTALSESA NQAFLGFTYV APSVLDSIKE GFSFQPKLRS PRRLNSSPRT
PISPLKFSPF EGFRPSPGPP EPMEPSLPPL LPSPPSPPPT STAPLPIRPP SGTKKSKKGR
GRSGR
