KS6A5_MOUSE
ID KS6A5_MOUSE Reviewed; 863 AA.
AC Q8C050; Q8CI92;
DT 24-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 24-OCT-2003, sequence version 2.
DT 03-AUG-2022, entry version 183.
DE RecName: Full=Ribosomal protein S6 kinase alpha-5;
DE Short=S6K-alpha-5;
DE EC=2.7.11.1;
DE AltName: Full=90 kDa ribosomal protein S6 kinase 5;
DE AltName: Full=Nuclear mitogen- and stress-activated protein kinase 1;
DE AltName: Full=RSK-like protein kinase;
DE Short=RLSK;
GN Name=Rps6ka5; Synonyms=Msk1;
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 {ECO:0000312|EMBL:BAC27809.1};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J;
RA Zhou G., Wang J., Xu W.;
RT "Cloning of mouse ribosomal protein S6 kinase, 90kDa, polypeptide 5
RT (RPS6KA5).";
RL Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Mammary gland;
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).
RN [4]
RP FUNCTION IN PHOSPHORYLATION OF HISTONE H3.
RX PubMed=11441012; DOI=10.1074/jbc.m103973200;
RA Zhong S., Jansen C., She Q.-B., Goto H., Inagaki M., Bode A.M., Ma W.-Y.,
RA Dong Z.;
RT "Ultraviolet B-induced phosphorylation of histone H3 at serine 28 is
RT mediated by MSK1.";
RL J. Biol. Chem. 276:33213-33219(2001).
RN [5]
RP FUNCTION IN PHOSPHORYLATION OF STAT3.
RX PubMed=11553624; DOI=10.1074/jbc.m106044200;
RA Zhang Y., Liu G., Dong Z.;
RT "MSK1 and JNKs mediate phosphorylation of STAT3 in UVA-irradiated mouse
RT epidermal JB6 cells.";
RL J. Biol. Chem. 276:42534-42542(2001).
RN [6]
RP FUNCTION IN PHOSPHORYLATION OF CREB1 AND ATF1.
RX PubMed=11909979; DOI=10.1128/mcb.22.8.2871-2881.2002;
RA Wiggin G.R., Soloaga A., Foster J.M., Murray-Tait V., Cohen P.,
RA Arthur J.S.;
RT "MSK1 and MSK2 are required for the mitogen- and stress-induced
RT phosphorylation of CREB and ATF1 in fibroblasts.";
RL Mol. Cell. Biol. 22:2871-2881(2002).
RN [7] {ECO:0000305}
RP FUNCTION.
RX PubMed=12628924; DOI=10.1093/emboj/cdg139;
RA Vermeulen L., De Wilde G., Van Damme P., Vanden Berghe W., Haegeman G.;
RT "Transcriptional activation of the NF-kappaB p65 subunit by mitogen- and
RT stress-activated protein kinase-1 (MSK1).";
RL EMBO J. 22:1313-1324(2003).
RN [8]
RP FUNCTION IN CELL DEATH.
RX PubMed=12807421; DOI=10.1046/j.1471-4159.2003.01830.x;
RA Hughes J.P., Staton P.C., Wilkinson M.G., Strijbos P.J., Skaper S.D.,
RA Arthur J.S., Reith A.D.;
RT "Mitogen and stress response kinase-1 (MSK1) mediates excitotoxic induced
RT death of hippocampal neurones.";
RL J. Neurochem. 86:25-32(2003).
RN [9]
RP FUNCTION IN PHOSPHORYLATION OF HISTONE H3.
RX PubMed=15870105; DOI=10.1242/jcs.02373;
RA Dyson M.H., Thomson S., Inagaki M., Goto H., Arthur S.J., Nightingale K.,
RA Iborra F.J., Mahadevan L.C.;
RT "MAP kinase-mediated phosphorylation of distinct pools of histone H3 at S10
RT or S28 via mitogen- and stress-activated kinase 1/2.";
RL J. Cell Sci. 118:2247-2259(2005).
RN [10]
RP FUNCTION IN PHOSPHORYLATION OF RELA/NFKB3.
RX PubMed=16806820; DOI=10.1016/j.cellsig.2006.05.004;
RA Kefaloyianni E., Gaitanaki C., Beis I.;
RT "ERK1/2 and p38-MAPK signalling pathways, through MSK1, are involved in NF-
RT kappaB transactivation during oxidative stress in skeletal myoblasts.";
RL Cell. Signal. 18:2238-2251(2006).
RN [11]
RP FUNCTION IN PHOSPHORYLATION OF HISTONE H3.
RX PubMed=16517600; DOI=10.1074/jbc.m513333200;
RA Duncan E.A., Anest V., Cogswell P., Baldwin A.S.;
RT "The kinases MSK1 and MSK2 are required for epidermal growth factor-
RT induced, but not tumor necrosis factor-induced, histone H3 Ser10
RT phosphorylation.";
RL J. Biol. Chem. 281:12521-12525(2006).
RN [12]
RP FUNCTION IN PHOSPHORYLATION OF CREB1; ATF1 AND HISTONE H3.
RX PubMed=18690222; DOI=10.1038/ni.1644;
RA Ananieva O., Darragh J., Johansen C., Carr J.M., McIlrath J., Park J.M.,
RA Wingate A., Monk C.E., Toth R., Santos S.G., Iversen L., Arthur J.S.;
RT "The kinases MSK1 and MSK2 act as negative regulators of Toll-like receptor
RT signaling.";
RL Nat. Immunol. 9:1028-1036(2008).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-755; THR-764 AND SER-862, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Lung, Spleen, and Testis;
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: Serine/threonine-protein kinase that is required for the
CC mitogen or stress-induced phosphorylation of the transcription factors
CC CREB1 and ATF1 and for the regulation of the transcription factors
CC RELA, STAT3 and ETV1/ER81, and that contributes to gene activation by
CC histone phosphorylation and functions in the regulation of inflammatory
CC genes (By similarity)(PubMed:11553624, PubMed:11909979,
CC PubMed:16806820). Phosphorylates CREB1 and ATF1 in response to
CC mitogenic or stress stimuli such as UV-C irradiation, epidermal growth
CC factor (EGF) and anisomycin (PubMed:11909979). Plays an essential role
CC in the control of RELA transcriptional activity in response to TNF and
CC upon glucocorticoid, associates in the cytoplasm with the
CC glucocorticoid receptor NR3C1 and contributes to RELA inhibition and
CC repression of inflammatory gene expression (PubMed:12628924,
CC PubMed:16806820). In skeletal myoblasts is required for phosphorylation
CC of RELA at 'Ser-276' during oxidative stress (PubMed:12628924). In
CC erythropoietin-stimulated cells, is necessary for the 'Ser-727'
CC phosphorylation of STAT3 and regulation of its transcriptional
CC potential (PubMed:11553624). Phosphorylates ETV1/ER81 at 'Ser-191' and
CC 'Ser-216', and thereby regulates its ability to stimulate
CC transcription, which may be important during development and breast
CC tumor formation (By similarity). Directly represses transcription via
CC phosphorylation of 'Ser-1' of histone H2A (By similarity).
CC Phosphorylates 'Ser-10' of histone H3 in response to mitogenics, stress
CC stimuli and EGF, which results in the transcriptional activation of
CC several immediate early genes, including proto-oncogenes c-fos/FOS and
CC c-jun/JUN (PubMed:15870105, PubMed:16517600). May also phosphorylate
CC 'Ser-28' of histone H3 (PubMed:11441012, PubMed:15870105). Mediates the
CC mitogen- and stress-induced phosphorylation of high mobility group
CC protein 1 (HMGN1/HMG14) (By similarity). In lipopolysaccharide-
CC stimulated primary macrophages, acts downstream of the Toll-like
CC receptor TLR4 to limit the production of pro-inflammatory cytokines
CC (PubMed:18690222). Functions probably by inducing transcription of the
CC MAP kinase phosphatase DUSP1 and the anti-inflammatory cytokine
CC interleukin 10 (IL10), via CREB1 and ATF1 transcription factors
CC (PubMed:18690222). Plays a role in neuronal cell death by mediating the
CC downstream effects of excitotoxic injury (PubMed:12807421).
CC Phosphorylates TRIM7 at 'Ser-106' in response to growth factor
CC signaling via the MEK/ERK pathway, thereby stimulating its ubiquitin
CC ligase activity (By similarity). {ECO:0000250|UniProtKB:O75582,
CC ECO:0000269|PubMed:11441012, ECO:0000269|PubMed:11553624,
CC ECO:0000269|PubMed:11909979, ECO:0000269|PubMed:12628924,
CC ECO:0000269|PubMed:12807421, ECO:0000269|PubMed:15870105,
CC ECO:0000269|PubMed:16517600, ECO:0000269|PubMed:16806820,
CC ECO:0000269|PubMed:18690222}.
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:0000269|PubMed:12628924};
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:0000269|PubMed:12628924};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- ACTIVITY REGULATION: Activated by phosphorylation at Ser-359, Thr-645
CC and Thr-764 by MAPK1/ERK2, MAPK3/ERK1 and MAPK14/p38-alpha, and by
CC further autophosphorylation of Ser-211, Ser-375 and Ser-380 by the
CC activated C-terminal kinase domain. The active N-terminal kinase domain
CC finally phosphorylates downstream substrates, as well as Ser-814, Ser-
CC 816 and Ser-822 in its own C-terminal region.
CC -!- SUBUNIT: Forms a complex with either MAPK1/ERK2 or MAPK3/ERK1 in
CC quiescent cells which transiently dissociates following mitogenic
CC stimulation. Also associates with MAPK14/p38-alpha. Activated RPS6KA5
CC associates with and phosphorylates the NF-kappa-B p65 subunit RELA.
CC Interacts with CREBBP and EP300 (By similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC Q8C050; P11416: Rara; NbExp=2; IntAct=EBI-8391218, EBI-346736;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=2 {ECO:0000305};
CC IsoId=Q8C050-1; Sequence=Displayed;
CC Name=1 {ECO:0000305}; Synonyms=5 {ECO:0000305};
CC IsoId=Q8C050-2; Sequence=VSP_050613;
CC -!- PTM: Ser-375 and Thr-645 phosphorylation is required for kinase
CC activity. Ser-375 and Ser-211 are autophosphorylated by the C-terminal
CC kinase domain, and their phosphorylation is essential for the catalytic
CC activity of the N-terminal kinase domain. Phosphorylated at Ser-359,
CC Thr-645 and Thr-764 by MAPK1/ERK2, MAPK3/ERK1 and MAPK14/p38-alpha.
CC Autophosphorylated at Ser-814, Ser-816 and Ser-822 by the N-terminal
CC kinase domain (By similarity). {ECO:0000250}.
CC -!- PTM: Ubiquitinated. {ECO:0000250}.
CC -!- MISCELLANEOUS: Enzyme activity requires the presence of both kinase
CC domains. {ECO:0000250|UniProtKB:O75582}.
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; AY341873; AAQ24158.1; -; mRNA.
DR EMBL; AY341881; AAQ24165.1; -; mRNA.
DR EMBL; AK032316; BAC27809.1; -; mRNA.
DR EMBL; BC035298; AAH35298.1; -; mRNA.
DR CCDS; CCDS26107.1; -. [Q8C050-1]
DR CCDS; CCDS88388.1; -. [Q8C050-2]
DR RefSeq; NP_001317631.1; NM_001330702.1. [Q8C050-2]
DR RefSeq; NP_705815.1; NM_153587.3. [Q8C050-1]
DR AlphaFoldDB; Q8C050; -.
DR SMR; Q8C050; -.
DR BioGRID; 215759; 11.
DR IntAct; Q8C050; 2.
DR MINT; Q8C050; -.
DR STRING; 10090.ENSMUSP00000042987; -.
DR iPTMnet; Q8C050; -.
DR PhosphoSitePlus; Q8C050; -.
DR EPD; Q8C050; -.
DR MaxQB; Q8C050; -.
DR PaxDb; Q8C050; -.
DR PeptideAtlas; Q8C050; -.
DR PRIDE; Q8C050; -.
DR ProteomicsDB; 264876; -. [Q8C050-1]
DR ProteomicsDB; 264877; -. [Q8C050-2]
DR Antibodypedia; 83; 973 antibodies from 42 providers.
DR DNASU; 73086; -.
DR Ensembl; ENSMUST00000043599; ENSMUSP00000042987; ENSMUSG00000021180. [Q8C050-1]
DR Ensembl; ENSMUST00000222731; ENSMUSP00000152481; ENSMUSG00000021180. [Q8C050-2]
DR GeneID; 73086; -.
DR KEGG; mmu:73086; -.
DR UCSC; uc007ost.1; mouse. [Q8C050-1]
DR UCSC; uc007osu.1; mouse. [Q8C050-2]
DR CTD; 9252; -.
DR MGI; MGI:1920336; Rps6ka5.
DR VEuPathDB; HostDB:ENSMUSG00000021180; -.
DR eggNOG; KOG0603; Eukaryota.
DR GeneTree; ENSGT00940000156886; -.
DR HOGENOM; CLU_000288_58_0_1; -.
DR InParanoid; Q8C050; -.
DR OMA; IMQRICR; -.
DR PhylomeDB; Q8C050; -.
DR TreeFam; TF313438; -.
DR Reactome; R-MMU-198753; ERK/MAPK targets.
DR Reactome; R-MMU-199920; CREB phosphorylation.
DR Reactome; R-MMU-375165; NCAM signaling for neurite out-growth.
DR Reactome; R-MMU-5621575; CD209 (DC-SIGN) signaling.
DR BioGRID-ORCS; 73086; 3 hits in 77 CRISPR screens.
DR ChiTaRS; Rps6ka5; mouse.
DR PRO; PR:Q8C050; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; Q8C050; protein.
DR Bgee; ENSMUSG00000021180; Expressed in dorsal striatum and 219 other tissues.
DR ExpressionAtlas; Q8C050; baseline and differential.
DR Genevisible; Q8C050; MM.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
DR GO; GO:0044024; F:histone kinase activity (H2A-S1 specific); ISS:UniProtKB.
DR GO; GO:0035175; F:histone kinase activity (H3-S10 specific); ISS:UniProtKB.
DR GO; GO:0044022; F:histone kinase activity (H3-S28 specific); ISS:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0004672; F:protein kinase activity; ISO:MGI.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
DR GO; GO:0004713; F:protein tyrosine kinase activity; IEA:Ensembl.
DR GO; GO:0043990; P:histone H2A-S1 phosphorylation; ISO:MGI.
DR GO; GO:0043987; P:histone H3-S10 phosphorylation; ISO:MGI.
DR GO; GO:0043988; P:histone H3-S28 phosphorylation; ISO:MGI.
DR GO; GO:0016572; P:histone phosphorylation; ISO:MGI.
DR GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
DR GO; GO:0070498; P:interleukin-1-mediated signaling pathway; ISO:MGI.
DR GO; GO:0035556; P:intracellular signal transduction; IDA:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR GO; GO:0035066; P:positive regulation of histone acetylation; ISO:MGI.
DR GO; GO:0033129; P:positive regulation of histone phosphorylation; ISO:MGI.
DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0043687; P:post-translational protein modification; ISS:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA: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; IPR016239; Ribosomal_S6_kinase_II.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 3.
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; SSF56112; 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 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Inflammatory response; Kinase;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Serine/threonine-protein kinase; Stress response; Transferase;
KW Ubl conjugation.
FT CHAIN 1..863
FT /note="Ribosomal protein S6 kinase alpha-5"
FT /id="PRO_0000086208"
FT DOMAIN 48..317
FT /note="Protein kinase 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 318..386
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00618"
FT DOMAIN 428..675
FT /note="Protein kinase 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 805..863
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 816..863
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 176
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 608
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 54..62
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 80
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 431..440
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 454
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 211
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:O75582"
FT MOD_RES 359
FT /note="Phosphoserine; by MAPK1, MAPK3 and MAPK14"
FT /evidence="ECO:0000250|UniProtKB:O75582"
FT MOD_RES 375
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:O75582"
FT MOD_RES 380
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:O75582"
FT MOD_RES 645
FT /note="Phosphothreonine; by MAPK1, MAPK3 and MAPK14"
FT /evidence="ECO:0000250|UniProtKB:O75582"
FT MOD_RES 711
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75582"
FT MOD_RES 721
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75582"
FT MOD_RES 755
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 759
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75582"
FT MOD_RES 764
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 814
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:O75582"
FT MOD_RES 816
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:O75582"
FT MOD_RES 822
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:O75582"
FT MOD_RES 862
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 490..554
FT /note="Missing (in isoform 1)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072, ECO:0000303|Ref.1"
FT /id="VSP_050613"
FT CONFLICT 2..15
FT /note="EGEGGGSGGAGTSG -> GGRAAAAAARAPAE (in Ref. 1;
FT AAQ24165)"
FT /evidence="ECO:0000305"
FT CONFLICT 117
FT /note="H -> N (in Ref. 2; BAC27809)"
FT /evidence="ECO:0000305"
FT CONFLICT 376
FT /note="F -> Y (in Ref. 2; BAC27809)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 863 AA; 96583 MW; 7A3C76D4036EA3EA CRC64;
MEGEGGGSGG AGTSGDSGDG GEQLLTVKHE LRTANLTGHA EKVGIENFEL LKVLGTGAYG
KVFLVRKISG HDAGKLYAMK VLKKATIVQK AKTTEHTRTE RQVLEHIRQS PFLVTLHYAF
QTETKLHLIL DYINGGELFT HLSQRERFTE HEVQIYVGEI VLALEHLHKL GIIYRDIKLE
NILLDSNGHV VLTDFGLSKE FVADETERAY SFCGTIEYMA PDIVRGGDSG HDKAVDWWSL
GVLMYELLTG ASPFTVDGEK NSQAEISRRI LKSEPPYPQE MSTVAKDLLQ RLLMKDPKKR
LGCGPRDAEE IKEHLFFEKI KWDDLAAKKV PAPFKPVIRD ELDVSNFAEE FTEMDPTYSP
AALPQSSERL FQGYSFVAPS ILFKRNAAVI DPLQFHMGVD RPGVTNVARS AMMKDSPFYQ
HYDLDLKDKP LGEGSFSICR KCVHKKTNQA FAVKIISKRM EANTQKEITA LKLCEGHPNI
VKLHEVFHDQ VAASAQPPGQ VVLCSLLLLA LLFNRSLTRK PVTWTWLVHS TSQLPPLPPP
MPEIVLFILL SDNGQLHTFL VMELLNGGEL FERIKRKKHF SETEASYIMR KLVSAVSHMH
DVGVVHRDLK PENLLFTDEN DNLEIKVIDF GFARLKPPDN QPLKTPCFTL HYAAPELLTH
NGYDESCDLW SLGVILYTML SGQVPFQSHD RSLTCTSAVE IMKKIKKGDF SFEGEAWKNV
SQEAKDLIQG LLTVDPNKRL KMSGLRYNEW LQDGSQLSSN PLMTPDILGS SGAAVHTCVK
ATFHAFNKYK REGFCLQNVD KAPLAKRRKM KRTSTSTETR SSSSESSRSS SSQSHGKTTP
TKTLQPSNPT EGSNPDTLFQ FSD
