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Ribosomal protein S6 kinase alpha-5 (S6K-alpha-5) (EC 2.7.11.1) (90 kDa ribosomal protein S6 kinase 5) (Nuclear mitogen- and stress-activated protein kinase 1) (RSK-like protein kinase) (RSKL)

 KS6A5_HUMAN             Reviewed;         802 AA.
O75582; B7Z2Y5; O95316; Q96AF7;
24-OCT-2003, integrated into UniProtKB/Swiss-Prot.
01-NOV-1998, sequence version 1.
25-OCT-2017, entry version 180.
RecName: Full=Ribosomal protein S6 kinase alpha-5;
Short=S6K-alpha-5;
EC=2.7.11.1;
AltName: Full=90 kDa ribosomal protein S6 kinase 5;
AltName: Full=Nuclear mitogen- and stress-activated protein kinase 1;
AltName: Full=RSK-like protein kinase;
Short=RSKL;
Name=RPS6KA5; Synonyms=MSK1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606 {ECO:0000312|EMBL:AAC69577.1};
[1] {ECO:0000305}
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, ENZYME REGULATION,
SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND MUTAGENESIS OF ASP-195
AND ASP-565.
TISSUE=Pancreas {ECO:0000269|PubMed:9687510};
PubMed=9687510; DOI=10.1093/emboj/17.15.4426;
Deak M., Clifton A.D., Lucocq J.M., Alessi D.R.;
"Mitogen- and stress-activated protein kinase-1 (MSK1) is directly
activated by MAPK and SAPK2/p38, and may mediate activation of CREB.";
EMBO J. 17:4426-4441(1998).
[2] {ECO:0000305}
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND TISSUE
SPECIFICITY.
TISSUE=Placenta {ECO:0000269|PubMed:9873047};
PubMed=9873047; DOI=10.1074/jbc.274.2.1026;
New L., Zhao M., Li Y., Bassett W.W., Feng Y., Ludwig S., Padova F.D.,
Gram H., Han J.;
"Cloning and characterization of RLPK, a novel RSK-related protein
kinase.";
J. Biol. Chem. 274:1026-1032(1999).
[3] {ECO:0000305}
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND CHROMOSOMAL LOCATION.
PubMed=10702687;
Jiang C., Yu L., Tu Q., Zhao Y., Zhang H., Zhao S.;
"Assignment of a member of the ribosomal protein S6 kinase family,
RPS6KA5, to human chromosome 14q31-q32.1 by radiation hybrid
mapping.";
Cytogenet. Cell Genet. 87:261-262(1999).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
TISSUE=Caudate nucleus;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=12508121; DOI=10.1038/nature01348;
Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S.,
Sun H., Du H., Pepin K., Artiguenave F., Robert C., Cruaud C.,
Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P.,
Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N.,
Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C.,
Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S.,
Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B.,
Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M.,
Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S.,
Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D.,
Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A.,
Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L.,
Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J.,
Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W.,
Quetier F., Waterston R., Hood L., Weissenbach J.;
"The DNA sequence and analysis of human chromosome 14.";
Nature 421:601-607(2003).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Placenta {ECO:0000312|EMBL:AAH17187.1};
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
FUNCTION.
PubMed=11909979; DOI=10.1128/MCB.22.8.2871-2881.2002;
Wiggin G.R., Soloaga A., Foster J.M., Murray-Tait V., Cohen P.,
Arthur J.S.;
"MSK1 and MSK2 are required for the mitogen- and stress-induced
phosphorylation of CREB and ATF1 in fibroblasts.";
Mol. Cell. Biol. 22:2871-2881(2002).
[8]
FUNCTION, AND INTERACTION WITH RELA.
PubMed=12628924; DOI=10.1093/emboj/cdg139;
Vermeulen L., De Wilde G., Van Damme P., Vanden Berghe W.,
Haegeman G.;
"Transcriptional activation of the NF-kappaB p65 subunit by
mitogen- and stress-activated protein kinase-1 (MSK1).";
EMBO J. 22:1313-1324(2003).
[9]
FUNCTION IN PHOSPHORYLATION OF HISTONE H3 AND HMGN1/HMG14.
PubMed=12773393; DOI=10.1093/emboj/cdg273;
Soloaga A., Thomson S., Wiggin G.R., Rampersaud N., Dyson M.H.,
Hazzalin C.A., Mahadevan L.C., Arthur J.S.;
"MSK2 and MSK1 mediate the mitogen- and stress-induced phosphorylation
of histone H3 and HMG-14.";
EMBO J. 22:2788-2797(2003).
[10]
FUNCTION IN PHOSPHORYLATION OF STAT3.
PubMed=12763138; DOI=10.1016/S0301-472X(03)00045-6;
Wierenga A.T., Vogelzang I., Eggen B.J., Vellenga E.;
"Erythropoietin-induced serine 727 phosphorylation of STAT3 in
erythroid cells is mediated by a MEK-, ERK-, and MSK1-dependent
pathway.";
Exp. Hematol. 31:398-405(2003).
[11]
FUNCTION IN PHOSPHORYLATION OF ETV1/ER81, AND INTERACTION WITH CREBBP
AND EP300.
PubMed=12569367; DOI=10.1038/sj.onc.1206185;
Janknecht R.;
"Regulation of the ER81 transcription factor and its coactivators by
mitogen- and stress-activated protein kinase 1 (MSK1).";
Oncogene 22:746-755(2003).
[12]
FUNCTION IN PHOSPHORYLATION OF HISTONE H2A.
PubMed=15010469; DOI=10.1074/jbc.M400099200;
Zhang Y., Griffin K., Mondal N., Parvin J.D.;
"Phosphorylation of histone H2A inhibits transcription on chromatin
templates.";
J. Biol. Chem. 279:21866-21872(2004).
[13]
ENZYME REGULATION, PHOSPHORYLATION AT SER-212; SER-360; SER-376;
SER-381; THR-581; SER-750; SER-752 AND SER-758, AND MUTAGENESIS OF
SER-212; SER-360; SER-376 AND THR-581.
PubMed=15568999; DOI=10.1042/BJ20041501;
McCoy C.E., Campbell D.G., Deak M., Bloomberg G.B., Arthur J.S.C.;
"MSK1 activity is controlled by multiple phosphorylation sites.";
Biochem. J. 387:507-517(2005).
[14]
PHOSPHORYLATION AT SER-647; SER-657; SER-695 AND THR-700, AND
MUTAGENESIS OF THR-700.
PubMed=17117922; DOI=10.1042/BJ20061183;
McCoy C.E., Macdonald A., Morrice N.A., Campbell D.G., Deak M.,
Toth R., McIlrath J., Arthur J.S.;
"Identification of novel phosphorylation sites in MSK1 by precursor
ion scanning MS.";
Biochem. J. 402:491-501(2007).
[15]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=18511904; DOI=10.1038/emboj.2008.95;
Beck I.M., Vanden Berghe W., Vermeulen L., Bougarne N.,
Vander Cruyssen B., Haegeman G., De Bosscher K.;
"Altered subcellular distribution of MSK1 induced by glucocorticoids
contributes to NF-kappaB inhibition.";
EMBO J. 27:1682-1693(2008).
[16]
REVIEW ON FUNCTION.
PubMed=18508628; DOI=10.2741/3122;
Arthur J.S.;
"MSK activation and physiological roles.";
Front. Biosci. 13:5866-5879(2008).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-376, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[18]
REVIEW ON FUNCTION.
PubMed=19464896; DOI=10.1016/j.tibs.2009.02.007;
Vermeulen L., Vanden Berghe W., Beck I.M., De Bosscher K.,
Haegeman G.;
"The versatile role of MSKs in transcriptional regulation.";
Trends Biochem. Sci. 34:311-318(2009).
[19]
UBIQUITINATION.
PubMed=20596523; DOI=10.1371/journal.pone.0011332;
Del Rincon S.V., Rogers J., Widschwendter M., Sun D., Sieburg H.B.,
Spruck C.;
"Development and validation of a method for profiling post-
translational modification activities using protein microarrays.";
PLoS ONE 5:E11332-E11332(2010).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-376 AND SER-381, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[21]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[22]
FUNCTION IN PHOSPHORYLATION OF TRIM7.
PubMed=25851810; DOI=10.1038/ncomms7782;
Chakraborty A., Diefenbacher M.E., Mylona A., Kassel O., Behrens A.;
"The E3 ubiquitin ligase Trim7 mediates c-Jun/AP-1 activation by Ras
signalling.";
Nat. Commun. 6:6782-6782(2015).
[23]
X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 2-348.
PubMed=15274926; DOI=10.1016/j.str.2004.02.040;
Smith K.J., Carter P.S., Bridges A., Horrocks P., Lewis C.,
Pettman G., Clarke A., Brown M., Hughes J., Wilkinson M., Bax B.,
Reith A.;
"The structure of MSK1 reveals a novel autoinhibitory conformation for
a dual kinase protein.";
Structure 12:1067-1077(2004).
[24]
X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 414-738.
PubMed=20382163; DOI=10.1016/j.jmb.2010.03.064;
Malakhova M., D'Angelo I., Kim H.G., Kurinov I., Bode A.M., Dong Z.;
"The crystal structure of the active form of the C-terminal kinase
domain of mitogen- and stress-activated protein kinase 1.";
J. Mol. Biol. 399:41-52(2010).
[25]
VARIANTS [LARGE SCALE ANALYSIS] ASN-554; LEU-574 AND CYS-599.
PubMed=17344846; DOI=10.1038/nature05610;
Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C.,
Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S.,
O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S.,
Bhamra G., Buck G., Choudhury B., Clements J., Cole J., Dicks E.,
Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J.,
Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K.,
Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T.,
West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P.,
Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E.,
DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E.,
Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T.,
Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.;
"Patterns of somatic mutation in human cancer genomes.";
Nature 446:153-158(2007).
-!- FUNCTION: Serine/threonine-protein kinase that is required for the
mitogen or stress-induced phosphorylation of the transcription
factors CREB1 and ATF1 and for the regulation of the transcription
factors RELA, STAT3 and ETV1/ER81, and that contributes to gene
activation by histone phosphorylation and functions in the
regulation of inflammatory genes (PubMed:11909979,
PubMed:12569367, PubMed:12763138, PubMed:9687510, PubMed:18511904,
PubMed:9873047). Phosphorylates CREB1 and ATF1 in response to
mitogenic or stress stimuli such as UV-C irradiation, epidermal
growth factor (EGF) and anisomycin (PubMed:11909979,
PubMed:9873047). Plays an essential role in the control of RELA
transcriptional activity in response to TNF and upon
glucocorticoid, associates in the cytoplasm with the
glucocorticoid receptor NR3C1 and contributes to RELA inhibition
and repression of inflammatory gene expression (PubMed:12628924,
PubMed:18511904). In skeletal myoblasts is required for
phosphorylation of RELA at 'Ser-276' during oxidative stress
(PubMed:12628924). In erythropoietin-stimulated cells, is
necessary for the 'Ser-727' phosphorylation of STAT3 and
regulation of its transcriptional potential (PubMed:12763138).
Phosphorylates ETV1/ER81 at 'Ser-191' and 'Ser-216', and thereby
regulates its ability to stimulate transcription, which may be
important during development and breast tumor formation
(PubMed:12569367). Directly represses transcription via
phosphorylation of 'Ser-1' of histone H2A (PubMed:15010469).
Phosphorylates 'Ser-10' of histone H3 in response to mitogenics,
stress stimuli and EGF, which results in the transcriptional
activation of several immediate early genes, including proto-
oncogenes c-fos/FOS and c-jun/JUN (PubMed:12773393). May also
phosphorylate 'Ser-28' of histone H3 (PubMed:12773393). Mediates
the mitogen- and stress-induced phosphorylation of high mobility
group protein 1 (HMGN1/HMG14) (PubMed:12773393). In
lipopolysaccharide-stimulated primary macrophages, acts downstream
of the Toll-like receptor TLR4 to limit the production of pro-
inflammatory cytokines (By similarity). Functions probably by
inducing transcription of the MAP kinase phosphatase DUSP1 and the
anti-inflammatory cytokine interleukin 10 (IL10), via CREB1 and
ATF1 transcription factors (By similarity). Plays a role in
neuronal cell death by mediating the downstream effects of
excitotoxic injury (By similarity). Phosphorylates TRIM7 at 'Ser-
107' in response to growth factor signaling via the MEK/ERK
pathway, thereby stimulating its ubiquitin ligase activity
(PubMed:25851810). {ECO:0000250|UniProtKB:Q8C050,
ECO:0000269|PubMed:11909979, ECO:0000269|PubMed:12569367,
ECO:0000269|PubMed:12628924, ECO:0000269|PubMed:12763138,
ECO:0000269|PubMed:12773393, ECO:0000269|PubMed:15010469,
ECO:0000269|PubMed:18511904, ECO:0000269|PubMed:25851810,
ECO:0000269|PubMed:9687510, ECO:0000269|PubMed:9873047}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
{ECO:0000269|PubMed:12628924, ECO:0000269|PubMed:9687510,
ECO:0000269|PubMed:9873047}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000269|PubMed:12628924,
ECO:0000269|PubMed:9687510, ECO:0000269|PubMed:9873047};
-!- ENZYME REGULATION: Activated by phosphorylation at Ser-360, Thr-
581 and Thr-700 by MAPK1/ERK2, MAPK3/ERK1 and MAPK14/p38-alpha,
and by further autophosphorylation of Ser-212, Ser-376 and Ser-381
by the activated C-terminal kinase domain. The active N-terminal
kinase domain finally phosphorylates downstream substrates, as
well as Ser-750, Ser-752 and Ser-758 in its own C-terminal region.
{ECO:0000269|PubMed:15568999, ECO:0000269|PubMed:9687510}.
-!- SUBUNIT: Forms a complex with either MAPK1/ERK2 or MAPK3/ERK1 in
quiescent cells which transiently dissociates following mitogenic
stimulation. Also associates with MAPK14/p38-alpha. Activated
RPS6KA5 associates with and phosphorylates the NF-kappa-B p65
subunit RELA. Interacts with CREBBP and EP300.
{ECO:0000269|PubMed:12569367, ECO:0000269|PubMed:12628924}.
-!- INTERACTION:
Q9Y4C1:KDM3A; NbExp=3; IntAct=EBI-16135973, EBI-2515339;
Q9NYL2:MAP3K20; NbExp=4; IntAct=EBI-73869, EBI-602273;
Q04206:RELA; NbExp=2; IntAct=EBI-73869, EBI-73886;
-!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Predominantly
nuclear. Exported into cytoplasm in response to glucocorticoid.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=O75582-1; Sequence=Displayed;
Name=2;
IsoId=O75582-2; Sequence=VSP_041837, VSP_041838;
Name=3;
IsoId=O75582-3; Sequence=VSP_057410;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Widely expressed with high levels in heart,
brain and placenta. Less abundant in lung, kidney and liver.
{ECO:0000269|PubMed:9687510, ECO:0000269|PubMed:9873047}.
-!- PTM: Ser-376 and Thr-581 phosphorylation is required for kinase
activity. Ser-376 and Ser-212 are autophosphorylated by the C-
terminal kinase domain, and their phosphorylation is essential for
the catalytic activity of the N-terminal kinase domain.
Phosphorylated at Ser-360, Thr-581 and Thr-700 by MAPK1/ERK2,
MAPK3/ERK1 and MAPK14/p38-alpha. Autophosphorylated at Ser-750,
Ser-752 and Ser-758 by the N-terminal kinase domain.
{ECO:0000269|PubMed:15568999, ECO:0000269|PubMed:17117922}.
-!- PTM: Ubiquitinated. {ECO:0000269|PubMed:20596523}.
-!- MISCELLANEOUS: Enzyme activity requires the presence of both
kinase domains. {ECO:0000269|PubMed:9687510}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
protein kinase family. S6 kinase subfamily. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAC69577.1; Type=Frameshift; Positions=Several; Evidence={ECO:0000305};
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EMBL; AF074393; AAC31171.1; -; mRNA.
EMBL; AF080000; AAD23915.1; -; mRNA.
EMBL; AF090421; AAC69577.1; ALT_FRAME; mRNA.
EMBL; AK295266; BAH12021.1; -; mRNA.
EMBL; AL121784; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL133454; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL159191; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC017187; AAH17187.1; -; mRNA.
CCDS; CCDS45149.1; -. [O75582-2]
CCDS; CCDS81839.1; -. [O75582-3]
CCDS; CCDS9893.1; -. [O75582-1]
PIR; T13149; T13149.
RefSeq; NP_001309164.1; NM_001322235.1. [O75582-3]
RefSeq; NP_001309166.1; NM_001322237.1. [O75582-3]
RefSeq; NP_004746.2; NM_004755.3. [O75582-1]
RefSeq; NP_872198.1; NM_182398.2. [O75582-2]
UniGene; Hs.510225; -.
PDB; 1VZO; X-ray; 1.80 A; A=2-348.
PDB; 3KN5; X-ray; 2.40 A; A/B=414-738.
PDB; 3KN6; X-ray; 2.00 A; A/B=414-738.
PDBsum; 1VZO; -.
PDBsum; 3KN5; -.
PDBsum; 3KN6; -.
ProteinModelPortal; O75582; -.
SMR; O75582; -.
BioGrid; 114676; 55.
DIP; DIP-30894N; -.
ELM; O75582; -.
IntAct; O75582; 37.
MINT; MINT-261060; -.
STRING; 9606.ENSP00000261991; -.
BindingDB; O75582; -.
ChEMBL; CHEMBL4237; -.
GuidetoPHARMACOLOGY; 1523; -.
iPTMnet; O75582; -.
PhosphoSitePlus; O75582; -.
BioMuta; RPS6KA5; -.
EPD; O75582; -.
MaxQB; O75582; -.
PaxDb; O75582; -.
PeptideAtlas; O75582; -.
PRIDE; O75582; -.
DNASU; 9252; -.
Ensembl; ENST00000418736; ENSP00000402787; ENSG00000100784. [O75582-2]
Ensembl; ENST00000536315; ENSP00000442803; ENSG00000100784. [O75582-3]
Ensembl; ENST00000614987; ENSP00000479667; ENSG00000100784. [O75582-1]
GeneID; 9252; -.
KEGG; hsa:9252; -.
UCSC; uc001xys.4; human. [O75582-1]
UCSC; uc010twi.3; human.
CTD; 9252; -.
DisGeNET; 9252; -.
EuPathDB; HostDB:ENSG00000100784.9; -.
GeneCards; RPS6KA5; -.
HGNC; HGNC:10434; RPS6KA5.
HPA; CAB025458; -.
HPA; HPA001274; -.
HPA; HPA001780; -.
MIM; 603607; gene.
neXtProt; NX_O75582; -.
OpenTargets; ENSG00000100784; -.
PharmGKB; PA34849; -.
eggNOG; KOG0598; Eukaryota.
eggNOG; ENOG410XNPH; LUCA.
GeneTree; ENSGT00890000139324; -.
HOGENOM; HOG000233033; -.
HOVERGEN; HBG108317; -.
InParanoid; O75582; -.
KO; K04445; -.
OMA; APSILFK; -.
PhylomeDB; O75582; -.
TreeFam; TF313438; -.
Reactome; R-HSA-198753; ERK/MAPK targets.
Reactome; R-HSA-199920; CREB phosphorylation.
Reactome; R-HSA-375165; NCAM signaling for neurite out-growth.
Reactome; R-HSA-437239; Recycling pathway of L1.
Reactome; R-HSA-5621575; CD209 (DC-SIGN) signaling.
SABIO-RK; O75582; -.
SignaLink; O75582; -.
SIGNOR; O75582; -.
ChiTaRS; RPS6KA5; human.
EvolutionaryTrace; O75582; -.
GeneWiki; RPS6KA5; -.
GenomeRNAi; 9252; -.
PRO; PR:O75582; -.
Proteomes; UP000005640; Chromosome 14.
Bgee; ENSG00000100784; -.
CleanEx; HS_RPS6KA5; -.
ExpressionAtlas; O75582; baseline and differential.
Genevisible; O75582; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
GO; GO:0004672; F:protein kinase activity; IDA:UniProtKB.
GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
GO; GO:0007411; P:axon guidance; TAS:Reactome.
GO; GO:0007173; P:epidermal growth factor receptor signaling pathway; TAS:UniProtKB.
GO; GO:0043990; P:histone H2A-S1 phosphorylation; IDA:UniProtKB.
GO; GO:0043987; P:histone H3-S10 phosphorylation; IMP:UniProtKB.
GO; GO:0043988; P:histone H3-S28 phosphorylation; IMP:UniProtKB.
GO; GO:0016572; P:histone phosphorylation; IDA:UniProtKB.
GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
GO; GO:0070498; P:interleukin-1-mediated signaling pathway; IMP:BHF-UCL.
GO; GO:0035556; P:intracellular signal transduction; IDA:UniProtKB.
GO; GO:0001818; P:negative regulation of cytokine production; TAS:UniProtKB.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0032793; P:positive regulation of CREB transcription factor activity; TAS:UniProtKB.
GO; GO:0035066; P:positive regulation of histone acetylation; IMP:BHF-UCL.
GO; GO:0033129; P:positive regulation of histone phosphorylation; IMP:BHF-UCL.
GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IMP:UniProtKB.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IMP:BHF-UCL.
GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0002223; P:stimulatory C-type lectin receptor signaling pathway; TAS:Reactome.
InterPro; IPR000961; AGC-kinase_C.
InterPro; IPR011009; Kinase-like_dom.
InterPro; IPR017892; Pkinase_C.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR016239; Ribosomal_S6_kinase_II.
InterPro; IPR008271; Ser/Thr_kinase_AS.
Pfam; PF00069; Pkinase; 2.
Pfam; PF00433; Pkinase_C; 1.
PIRSF; PIRSF000606; Ribsml_S6_kin_2; 1.
SMART; SM00133; S_TK_X; 1.
SMART; SM00220; S_TKc; 2.
SUPFAM; SSF56112; SSF56112; 2.
PROSITE; PS51285; AGC_KINASE_CTER; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 2.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 2.
PROSITE; PS00108; PROTEIN_KINASE_ST; 2.
1: Evidence at protein level;
3D-structure; Alternative splicing; ATP-binding; Complete proteome;
Cytoplasm; Inflammatory response; Kinase; Magnesium; Metal-binding;
Nucleotide-binding; Nucleus; Phosphoprotein; Polymorphism;
Reference proteome; Repeat; Serine/threonine-protein kinase;
Stress response; Transferase; Ubl conjugation.
CHAIN 1 802 Ribosomal protein S6 kinase alpha-5.
/FTId=PRO_0000086207.
DOMAIN 49 318 Protein kinase 1. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
DOMAIN 319 387 AGC-kinase C-terminal.
DOMAIN 426 687 Protein kinase 2. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 55 63 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 432 440 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
ACT_SITE 177 177 Proton acceptor. {ECO:0000250}.
ACT_SITE 544 544 Proton acceptor. {ECO:0000250}.
BINDING 81 81 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
BINDING 455 455 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 212 212 Phosphoserine; by autocatalysis.
{ECO:0000269|PubMed:15568999}.
MOD_RES 360 360 Phosphoserine; by MAPK1, MAPK3 and
MAPK14. {ECO:0000269|PubMed:15568999}.
MOD_RES 376 376 Phosphoserine; by autocatalysis.
{ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000269|PubMed:15568999}.
MOD_RES 381 381 Phosphoserine; by autocatalysis.
{ECO:0000244|PubMed:20068231,
ECO:0000269|PubMed:15568999}.
MOD_RES 581 581 Phosphothreonine; by MAPK1, MAPK3 and
MAPK14. {ECO:0000269|PubMed:15568999}.
MOD_RES 647 647 Phosphoserine.
{ECO:0000269|PubMed:17117922}.
MOD_RES 657 657 Phosphoserine.
{ECO:0000269|PubMed:17117922}.
MOD_RES 691 691 Phosphoserine.
{ECO:0000250|UniProtKB:Q8C050}.
MOD_RES 695 695 Phosphoserine.
{ECO:0000269|PubMed:17117922}.
MOD_RES 700 700 Phosphothreonine; by MAPK1, MAPK3 and
MAPK14. {ECO:0000269|PubMed:17117922}.
MOD_RES 750 750 Phosphoserine; by autocatalysis.
{ECO:0000269|PubMed:15568999}.
MOD_RES 752 752 Phosphoserine; by autocatalysis.
{ECO:0000269|PubMed:15568999}.
MOD_RES 758 758 Phosphoserine; by autocatalysis.
{ECO:0000269|PubMed:15568999}.
MOD_RES 798 798 Phosphoserine.
{ECO:0000250|UniProtKB:Q8C050}.
VAR_SEQ 1 79 Missing (in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_057410.
VAR_SEQ 549 549 N -> V (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_041837.
VAR_SEQ 550 802 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_041838.
VARIANT 190 190 H -> R (in dbSNP:rs34699345).
/FTId=VAR_051634.
VARIANT 554 554 D -> N (in dbSNP:rs55911249).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_040634.
VARIANT 574 574 P -> L (in dbSNP:rs34604933).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_040635.
VARIANT 599 599 Y -> C (in dbSNP:rs55968863).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_040636.
MUTAGEN 195 195 D->A: Loss of kinase activity.
{ECO:0000269|PubMed:9687510}.
MUTAGEN 212 212 S->A: Inactivates the N-terminal kinase
domain. {ECO:0000269|PubMed:15568999}.
MUTAGEN 360 360 S->A: Decreases kinase activity by 60% in
response to PMA and UV-C.
{ECO:0000269|PubMed:15568999}.
MUTAGEN 376 376 S->A: Loss of kinase activity, and
decreases the phosphorylation of S-360
and T-581. {ECO:0000269|PubMed:15568999}.
MUTAGEN 565 565 D->A: Loss of kinase activity.
{ECO:0000269|PubMed:9687510}.
MUTAGEN 581 581 T->A: Loss of kinase activity, and blocks
phosphorylation of S-212; S-376 and S-381
in response to PMA and UV-C.
{ECO:0000269|PubMed:15568999}.
MUTAGEN 700 700 T->A,D: Strongly reduces phosphorylation
of T-581 in response to PMA and UV-C.
{ECO:0000269|PubMed:17117922}.
CONFLICT 452 453 FA -> LQ (in Ref. 3; AAC69577).
{ECO:0000305}.
CONFLICT 532 532 V -> L (in Ref. 3; AAC69577).
{ECO:0000305}.
CONFLICT 538 538 V -> L (in Ref. 3; AAC69577).
{ECO:0000305}.
CONFLICT 757 758 SS -> RG (in Ref. 3; AAC69577).
{ECO:0000305}.
STRAND 26 31 {ECO:0000244|PDB:1VZO}.
HELIX 46 48 {ECO:0000244|PDB:1VZO}.
STRAND 49 57 {ECO:0000244|PDB:1VZO}.
TURN 58 60 {ECO:0000244|PDB:1VZO}.
STRAND 61 68 {ECO:0000244|PDB:1VZO}.
TURN 72 75 {ECO:0000244|PDB:1VZO}.
STRAND 77 94 {ECO:0000244|PDB:1VZO}.
HELIX 95 97 {ECO:0000244|PDB:1VZO}.
HELIX 101 109 {ECO:0000244|PDB:1VZO}.
STRAND 117 123 {ECO:0000244|PDB:1VZO}.
STRAND 126 131 {ECO:0000244|PDB:1VZO}.
HELIX 139 146 {ECO:0000244|PDB:1VZO}.
HELIX 151 170 {ECO:0000244|PDB:1VZO}.
HELIX 180 182 {ECO:0000244|PDB:1VZO}.
STRAND 183 185 {ECO:0000244|PDB:1VZO}.
STRAND 191 194 {ECO:0000244|PDB:1VZO}.
STRAND 196 201 {ECO:0000244|PDB:1VZO}.
HELIX 204 210 {ECO:0000244|PDB:1VZO}.
HELIX 212 214 {ECO:0000244|PDB:1VZO}.
HELIX 222 225 {ECO:0000244|PDB:1VZO}.
HELIX 235 250 {ECO:0000244|PDB:1VZO}.
HELIX 264 273 {ECO:0000244|PDB:1VZO}.
HELIX 284 293 {ECO:0000244|PDB:1VZO}.
HELIX 298 300 {ECO:0000244|PDB:1VZO}.
TURN 306 308 {ECO:0000244|PDB:1VZO}.
HELIX 309 313 {ECO:0000244|PDB:1VZO}.
HELIX 316 318 {ECO:0000244|PDB:1VZO}.
HELIX 323 327 {ECO:0000244|PDB:1VZO}.
HELIX 418 422 {ECO:0000244|PDB:3KN6}.
STRAND 423 425 {ECO:0000244|PDB:3KN6}.
STRAND 432 435 {ECO:0000244|PDB:3KN6}.
STRAND 438 445 {ECO:0000244|PDB:3KN6}.
TURN 446 448 {ECO:0000244|PDB:3KN6}.
STRAND 451 458 {ECO:0000244|PDB:3KN6}.
HELIX 459 461 {ECO:0000244|PDB:3KN6}.
HELIX 462 474 {ECO:0000244|PDB:3KN6}.
TURN 475 477 {ECO:0000244|PDB:3KN6}.
STRAND 484 489 {ECO:0000244|PDB:3KN6}.
STRAND 491 498 {ECO:0000244|PDB:3KN6}.
HELIX 506 512 {ECO:0000244|PDB:3KN6}.
HELIX 518 537 {ECO:0000244|PDB:3KN6}.
HELIX 547 549 {ECO:0000244|PDB:3KN6}.
STRAND 550 553 {ECO:0000244|PDB:3KN6}.
STRAND 560 563 {ECO:0000244|PDB:3KN6}.
HELIX 602 617 {ECO:0000244|PDB:3KN6}.
HELIX 634 641 {ECO:0000244|PDB:3KN6}.
TURN 642 644 {ECO:0000244|PDB:3KN6}.
HELIX 651 654 {ECO:0000244|PDB:3KN6}.
HELIX 658 668 {ECO:0000244|PDB:3KN6}.
TURN 672 674 {ECO:0000244|PDB:3KN6}.
TURN 678 680 {ECO:0000244|PDB:3KN6}.
HELIX 685 687 {ECO:0000244|PDB:3KN6}.
HELIX 700 728 {ECO:0000244|PDB:3KN6}.
SEQUENCE 802 AA; 89865 MW; 76C27D0F6639BFA4 CRC64;
MEEEGGSSGG AAGTSADGGD GGEQLLTVKH ELRTANLTGH AEKVGIENFE LLKVLGTGAY
GKVFLVRKIS GHDTGKLYAM KVLKKATIVQ KAKTTEHTRT ERQVLEHIRQ SPFLVTLHYA
FQTETKLHLI LDYINGGELF THLSQRERFT EHEVQIYVGE IVLALEHLHK LGIIYRDIKL
ENILLDSNGH VVLTDFGLSK EFVADETERA YSFCGTIEYM APDIVRGGDS GHDKAVDWWS
LGVLMYELLT GASPFTVDGE KNSQAEISRR ILKSEPPYPQ EMSALAKDLI QRLLMKDPKK
RLGCGPRDAD EIKEHLFFQK INWDDLAAKK VPAPFKPVIR DELDVSNFAE EFTEMDPTYS
PAALPQSSEK LFQGYSFVAP SILFKRNAAV IDPLQFHMGV ERPGVTNVAR SAMMKDSPFY
QHYDLDLKDK PLGEGSFSIC RKCVHKKSNQ AFAVKIISKR MEANTQKEIT ALKLCEGHPN
IVKLHEVFHD QLHTFLVMEL LNGGELFERI KKKKHFSETE ASYIMRKLVS AVSHMHDVGV
VHRDLKPENL LFTDENDNLE IKIIDFGFAR LKPPDNQPLK TPCFTLHYAA PELLNQNGYD
ESCDLWSLGV ILYTMLSGQV PFQSHDRSLT CTSAVEIMKK IKKGDFSFEG EAWKNVSQEA
KDLIQGLLTV DPNKRLKMSG LRYNEWLQDG SQLSSNPLMT PDILGSSGAA VHTCVKATFH
AFNKYKREGF CLQNVDKAPL AKRRKMKKTS TSTETRSSSS ESSHSSSSHS HGKTTPTKTL
QPSNPADSNN PETLFQFSDS VA


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