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Ribosomal protein S6 kinase alpha-3 (S6K-alpha-3) (EC 2.7.11.1) (90 kDa ribosomal protein S6 kinase 3) (p90-RSK 3) (p90RSK3) (Insulin-stimulated protein kinase 1) (ISPK-1) (MAP kinase-activated protein kinase 1b) (MAPK-activated protein kinase 1b) (MAPKAP kinase 1b) (MAPKAPK-1b) (Ribosomal S6 kinase 2) (RSK-2) (pp90RSK2)

 KS6A3_HUMAN             Reviewed;         740 AA.
P51812; B2R9V4; Q4VAP3; Q59H26; Q5JPK8; Q7Z3Z7;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
01-OCT-1996, sequence version 1.
22-NOV-2017, entry version 187.
RecName: Full=Ribosomal protein S6 kinase alpha-3;
Short=S6K-alpha-3;
EC=2.7.11.1;
AltName: Full=90 kDa ribosomal protein S6 kinase 3;
Short=p90-RSK 3;
Short=p90RSK3;
AltName: Full=Insulin-stimulated protein kinase 1;
Short=ISPK-1;
AltName: Full=MAP kinase-activated protein kinase 1b;
Short=MAPK-activated protein kinase 1b;
Short=MAPKAP kinase 1b;
Short=MAPKAPK-1b;
AltName: Full=Ribosomal S6 kinase 2;
Short=RSK-2;
AltName: Full=pp90RSK2;
Name=RPS6KA3; Synonyms=ISPK1, MAPKAPK1B, RSK2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Placenta, and T-cell;
PubMed=7813820; DOI=10.2337/diab.44.1.90;
Bjoerbaek C., Vik T.A., Echwald S.M., Webb G.C., Wang J.P.,
Yang P.-Y., Vestergaard H., Richmond K., Hansen T., Erikson R.L.,
Miklos G.L.G., Cohen P.T.W., Pedersen O.;
"Cloning of a human insulin-stimulated protein kinase (ISPK-1) gene
and analysis of coding regions and mRNA levels of the ISPK-1 and the
protein phosphatase-1 genes in muscle from NIDDM patients.";
Diabetes 44:90-97(1995).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
Ohara O., Nagase T., Kikuno R.F.;
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15772651; DOI=10.1038/nature03440;
Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A.,
Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G.,
Jones M.C., Hurles M.E., Andrews T.D., Scott C.E., Searle S.,
Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R.,
Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L.,
Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A.,
Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S.,
Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R.,
Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M.,
Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N.,
Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D.,
Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W.,
Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C.,
Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C.,
Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
Corby N., Connor R.E., David R., Davies J., Davis C., Davis J.,
Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S.,
Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I.,
Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L.,
Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P.,
Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S.,
Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A.,
Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J.,
Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J.,
Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S.,
de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z.,
Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C.,
Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W.,
Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T.,
Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I.,
Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N.,
Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J.,
Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E.,
Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S.,
Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T.,
Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S.,
Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L.,
Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A.,
Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L.,
Williams G., Williams L., Williamson A., Williamson H., Wilming L.,
Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H.,
Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A.,
Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A.,
Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T.,
Gibbs R.A., Beck S., Rogers J., Bentley D.R.;
"The DNA sequence of the human X chromosome.";
Nature 434:325-337(2005).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 2-582.
TISSUE=Skeletal muscle;
PubMed=8141249;
Moller D.E., Xia C.-H., Tang W., Zhu A.X., Jakubowski M.;
"Human rsk isoforms: cloning and characterization of tissue-specific
expression.";
Am. J. Physiol. 266:C351-C359(1994).
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 15-735.
PubMed=12777533; DOI=10.1093/molbev/msg134;
Kitano T., Schwarz C., Nickel B., Paeaebo S.;
"Gene diversity patterns at 10 X-chromosomal loci in humans and
chimpanzees.";
Mol. Biol. Evol. 20:1281-1289(2003).
[8]
FUNCTION IN PHOSPHORYLATION OF GSK3B.
PubMed=8250835; DOI=10.1042/bj2960015;
Sutherland C., Leighton I.A., Cohen P.;
"Inactivation of glycogen synthase kinase-3 beta by phosphorylation:
new kinase connections in insulin and growth-factor signalling.";
Biochem. J. 296:15-19(1993).
[9]
FUNCTION IN PHOSPHORYLATION OF CREB1.
PubMed=9770464; DOI=10.1073/pnas.95.21.12202;
De Cesare D., Jacquot S., Hanauer A., Sassone-Corsi P.;
"Rsk-2 activity is necessary for epidermal growth factor-induced
phosphorylation of CREB protein and transcription of c-fos gene.";
Proc. Natl. Acad. Sci. U.S.A. 95:12202-12207(1998).
[10]
FUNCTION IN PHOSPHORYLATION OF HISTONE H3.
PubMed=10436156; DOI=10.1126/science.285.5429.886;
Sassone-Corsi P., Mizzen C.A., Cheung P., Crosio C., Monaco L.,
Jacquot S., Hanauer A., Allis C.D.;
"Requirement of Rsk-2 for epidermal growth factor-activated
phosphorylation of histone H3.";
Science 285:886-891(1999).
[11]
FUNCTION IN PHOSPHORYLATION OF DAPK1.
PubMed=16213824; DOI=10.1016/j.cub.2005.08.050;
Anjum R., Roux P.P., Ballif B.A., Gygi S.P., Blenis J.;
"The tumor suppressor DAP kinase is a target of RSK-mediated survival
signaling.";
Curr. Biol. 15:1762-1767(2005).
[12]
FUNCTION IN PHOSPHORYLATION OF NR4A1/NUR77.
PubMed=16223362; DOI=10.1042/BJ20050967;
Wingate A.D., Campbell D.G., Peggie M., Arthur J.S.;
"Nur77 is phosphorylated in cells by RSK in response to mitogenic
stimulation.";
Biochem. J. 393:715-724(2006).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-715, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=16964243; DOI=10.1038/nbt1240;
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
"A probability-based approach for high-throughput protein
phosphorylation analysis and site localization.";
Nat. Biotechnol. 24:1285-1292(2006).
[14]
INTERACTION WITH NFATC4.
PubMed=17213202; DOI=10.1074/jbc.M611322200;
Cho Y.-Y., Yao K., Bode A.M., Bergen H.R. III, Madden B.J., Oh S.-M.,
Ermakova S., Kang B.S., Choi H.S., Shim J.-H., Dong Z.;
"RSK2 mediates muscle cell differentiation through regulation of
NFAT3.";
J. Biol. Chem. 282:8380-8392(2007).
[15]
FUNCTION IN PHOSPHORYLATION OF RPS6.
PubMed=17360704; DOI=10.1074/jbc.M700906200;
Roux P.P., Shahbazian D., Vu H., Holz M.K., Cohen M.S., Taunton J.,
Sonenberg N., Blenis J.;
"RAS/ERK signaling promotes site-specific ribosomal protein S6
phosphorylation via RSK and stimulates cap-dependent translation.";
J. Biol. Chem. 282:14056-14064(2007).
[16]
FUNCTION IN MTOR SIGNALING.
PubMed=18722121; DOI=10.1016/j.cub.2008.07.078;
Carriere A., Cargnello M., Julien L.A., Gao H., Bonneil E.,
Thibault P., Roux P.P.;
"Oncogenic MAPK signaling stimulates mTORC1 activity by promoting RSK-
mediated raptor phosphorylation.";
Curr. Biol. 18:1269-1277(2008).
[17]
REVIEW ON FUNCTION, AND REVIEW ON ENZYME REGULATION.
PubMed=18508509; DOI=10.2741/3003;
Carriere A., Ray H., Blenis J., Roux P.P.;
"The RSK factors of activating the Ras/MAPK signaling cascade.";
Front. Biosci. 13:4258-4275(2008).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-365; SER-369; SER-375;
SER-386; SER-415; SER-556 AND SER-715, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[19]
REVIEW ON FUNCTION, AND REVIEW ON ENZYME REGULATION.
PubMed=18813292; DOI=10.1038/nrm2509;
Anjum R., Blenis J.;
"The RSK family of kinases: emerging roles in cellular signalling.";
Nat. Rev. Mol. Cell Biol. 9:747-758(2008).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-365; SER-369 AND
SER-375, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-365; SER-369; SER-375;
SER-386; SER-415 AND SER-715, AND IDENTIFICATION BY MASS SPECTROMETRY
[LARGE SCALE ANALYSIS].
PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
Mann M., Daub H.;
"Large-scale proteomics analysis of the human kinome.";
Mol. Cell. Proteomics 8:1751-1764(2009).
[22]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-415, 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).
[23]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-715, 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).
[24]
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).
[25]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-365 AND SER-369, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[26]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-365; SER-369; SER-415
AND SER-715, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[27]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-369; SER-386; SER-415
AND SER-715, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[28]
FUNCTION IN PHOSPHORYLATION OF EPHA2.
PubMed=26158630; DOI=10.1038/ncomms8679;
Zhou Y., Yamada N., Tanaka T., Hori T., Yokoyama S., Hayakawa Y.,
Yano S., Fukuoka J., Koizumi K., Saiki I., Sakurai H.;
"Crucial roles of RSK in cell motility by catalysing serine
phosphorylation of EphA2.";
Nat. Commun. 6:7679-7679(2015).
[29]
VARIANTS CLS VAL-75 AND ALA-227.
PubMed=8955270; DOI=10.1038/384567a0;
Trivier E., de Cesare D., Jacquot S., Pannetier S., Zackai E.,
Young I., Mandel J.-L., Sassone-Corsi P., Hanauer A.;
"Mutations in the kinase Rsk-2 associated with Coffin-Lowry
syndrome.";
Nature 384:567-570(1996).
[30]
VARIANTS CLS PHE-82; GLN-127; TYR-154; VAL-225 AND ASP-431, AND
VARIANT SER-38.
PubMed=9837815; DOI=10.1086/302153;
Jacquot S., Merienne K., de Cesare D., Pannetier S., Mandel J.-L.,
Sassone-Corsi P., Hanauer A.;
"Mutation analysis of the RSK2 gene in Coffin-Lowry patients:
extensive allelic heterogeneity and a high rate of De novo
mutations.";
Am. J. Hum. Genet. 63:1631-1640(1998).
[31]
VARIANTS CLS TRP-114 AND GLN-729.
PubMed=10094187; DOI=10.1038/sj.ejhg.5200231;
Abidi F., Jacquot S., Lassiter C., Trivier E., Hanauer A.,
Schwartz C.E.;
"Novel mutations in Rsk-2, the gene for Coffin-Lowry syndrome (CLS).";
Eur. J. Hum. Genet. 7:20-26(1999).
[32]
VARIANT CLS LYS-189.
PubMed=10528858; DOI=10.1136/jmg.36.10.775;
Manouvrier-Hanu S., Amiel J., Jacquot S., Merienne K., Moerman A.,
Coeslier A., Labarriere F., Vallee L., Croquette M.F., Hanauer A.;
"Unreported RSK2 missense mutation in two male sibs with an unusually
mild form of Coffin-Lowry syndrome.";
J. Med. Genet. 36:775-778(1999).
[33]
VARIANT MRX19 TRP-383, AND CHARACTERIZATION OF VARIANT MRX19 TRP-383.
PubMed=10319851; DOI=10.1038/8719;
Merienne K., Jacquot S., Pannetier S., Zeniou M., Bankier A., Gecz J.,
Mandel J.L., Mulley J., Sassone-Corsi P., Hanauer A.;
"A missense mutation in RPS6KA3 (RSK2) responsible for non-specific
mental retardation.";
Nat. Genet. 22:13-14(1999).
[34]
VARIANT CLS SER-268.
PubMed=14986828; DOI=10.1046/j.1399-0004.2003.00166.x;
Martinez-Garay I., Ballesta M.J., Oltra S., Orellana C., Palomeque A.,
Molto M.D., Prieto F., Martinez F.;
"Intronic L1 insertion and F268S, novel mutations in RPS6KA3 (RSK2)
causing Coffin-Lowry syndrome.";
Clin. Genet. 64:491-496(2003).
[35]
VARIANT CLS ILE-477 DEL.
PubMed=15214012; DOI=10.1002/ajmg.a.30056;
Facher J.J., Regier E.J., Jacobs G.H., Siwik E., Delaunoy J.P.,
Robin N.H.;
"Cardiomyopathy in Coffin-Lowry syndrome.";
Am. J. Med. Genet. A 128:176-178(2004).
[36]
VARIANTS MRX19 SER-115; GLY-152 DEL AND ASP-202 DEL.
PubMed=17100996; DOI=10.1111/j.1399-0004.2006.00723.x;
Field M., Tarpey P., Boyle J., Edkins S., Goodship J., Luo Y.,
Moon J., Teague J., Stratton M.R., Futreal P.A., Wooster R.,
Raymond F.L., Turner G.;
"Mutations in the RSK2(RPS6KA3) gene cause Coffin-Lowry syndrome and
nonsyndromic X-linked mental retardation.";
Clin. Genet. 70:509-515(2006).
[37]
VARIANT [LARGE SCALE ANALYSIS] VAL-416.
PubMed=16959974; DOI=10.1126/science.1133427;
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal
cancers.";
Science 314:268-274(2006).
[38]
VARIANTS [LARGE SCALE ANALYSIS] SER-38; CYS-483; PHE-608 AND CYS-723.
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 acts downstream of
ERK (MAPK1/ERK2 and MAPK3/ERK1) signaling and mediates mitogenic
and stress-induced activation of the transcription factors CREB1,
ETV1/ER81 and NR4A1/NUR77, regulates translation through RPS6 and
EIF4B phosphorylation, and mediates cellular proliferation,
survival, and differentiation by modulating mTOR signaling and
repressing pro-apoptotic function of BAD and DAPK1. In fibroblast,
is required for EGF-stimulated phosphorylation of CREB1 and
histone H3 at 'Ser-10', which results in the subsequent
transcriptional activation of several immediate-early genes. In
response to mitogenic stimulation (EGF and PMA), phosphorylates
and activates NR4A1/NUR77 and ETV1/ER81 transcription factors and
the cofactor CREBBP. Upon insulin-derived signal, acts indirectly
on the transcription regulation of several genes by
phosphorylating GSK3B at 'Ser-9' and inhibiting its activity.
Phosphorylates RPS6 in response to serum or EGF via an mTOR-
independent mechanism and promotes translation initiation by
facilitating assembly of the preinitiation complex. In response to
insulin, phosphorylates EIF4B, enhancing EIF4B affinity for the
EIF3 complex and stimulating cap-dependent translation. Is
involved in the mTOR nutrient-sensing pathway by directly
phosphorylating TSC2 at 'Ser-1798', which potently inhibits TSC2
ability to suppress mTOR signaling, and mediates phosphorylation
of RPTOR, which regulates mTORC1 activity and may promote
rapamycin-sensitive signaling independently of the PI3K/AKT
pathway. Mediates cell survival by phosphorylating the pro-
apoptotic proteins BAD and DAPK1 and suppressing their pro-
apoptotic function. Promotes the survival of hepatic stellate
cells by phosphorylating CEBPB in response to the hepatotoxin
carbon tetrachloride (CCl4). Is involved in cell cycle regulation
by phosphorylating the CDK inhibitor CDKN1B, which promotes CDKN1B
association with 14-3-3 proteins and prevents its translocation to
the nucleus and inhibition of G1 progression. In LPS-stimulated
dendritic cells, is involved in TLR4-induced macropinocytosis, and
in myeloma cells, acts as effector of FGFR3-mediated
transformation signaling, after direct phosphorylation at Tyr-529
by FGFR3. Negatively regulates EGF-induced MAPK1/3 phosphorylation
via phosphorylation of SOS1. Phosphorylates SOS1 at 'Ser-1134' and
'Ser-1161' that create YWHAB and YWHAE binding sites and which
contribute to the negative regulation of MAPK1/3 phosphorylation
(By similarity). Phosphorylates EPHA2 at 'Ser-897', the RPS6KA-
EPHA2 signaling pathway controls cell migration (PubMed:26158630).
{ECO:0000250|UniProtKB:P18654, ECO:0000269|PubMed:10436156,
ECO:0000269|PubMed:16213824, ECO:0000269|PubMed:16223362,
ECO:0000269|PubMed:17360704, ECO:0000269|PubMed:18722121,
ECO:0000269|PubMed:26158630, ECO:0000269|PubMed:8250835,
ECO:0000269|PubMed:9770464}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
-!- ENZYME REGULATION: Upon extracellular signal or mitogen
stimulation, phosphorylated at Thr-577 in the C-terminal kinase
domain (CTKD) by MAPK1/ERK2 and MAPK3/ERK1. The activated CTKD
then autophosphorylates Ser-386, allowing binding of PDPK1, which
in turn phosphorylates Ser-227 in the N-terminal kinase domain
(NTDK) leading to the full activation of the protein and
subsequent phosphorylation of the substrates by the NTKD.
-!- SUBUNIT: Forms a complex with either MAPK1/ERK2 or MAPK3/ERK1 in
quiescent cells. Transiently dissociates following mitogenic
stimulation (By similarity). Interacts with NFATC4, ETV1/ER81 and
FGFR1. {ECO:0000250, ECO:0000269|PubMed:17213202}.
-!- INTERACTION:
P28482:MAPK1; NbExp=3; IntAct=EBI-1046616, EBI-959949;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm
{ECO:0000250}.
-!- TISSUE SPECIFICITY: Expressed in many tissues, highest levels in
skeletal muscle.
-!- PTM: Activated by phosphorylation at Ser-227 by PDPK1.
Autophosphorylated on Ser-386, as part of the activation process.
May be phosphorylated at Thr-365 and Ser-369 by MAPK1/ERK2 and
MAPK3/ERK1. Can also be activated via phosphorylation at Ser-386
by MAPKAPK2.
-!- PTM: N-terminal myristoylation results in an activated kinase in
the absence of added growth factors.
-!- DISEASE: Coffin-Lowry syndrome (CLS) [MIM:303600]: A X-linked
mental retardation associated with facial and digital
dysmorphisms, progressive skeletal malformations, growth
retardation, hearing deficit and paroxysmal movement disorders.
{ECO:0000269|PubMed:10094187, ECO:0000269|PubMed:10528858,
ECO:0000269|PubMed:14986828, ECO:0000269|PubMed:15214012,
ECO:0000269|PubMed:8955270, ECO:0000269|PubMed:9837815}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- DISEASE: Mental retardation, X-linked 19 (MRX19) [MIM:300844]: A
non-syndromic form of mild to moderate mental retardation. Mental
retardation is characterized by significantly below average
general intellectual functioning associated with impairments in
adaptive behavior and manifested during the developmental period.
In contrast to syndromic or specific X-linked mental retardation
which also present with associated physical, neurological and/or
psychiatric manifestations, intellectual deficiency is the only
primary symptom of non-syndromic X-linked mental retardation.
{ECO:0000269|PubMed:10319851, ECO:0000269|PubMed:17100996}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
protein kinase family. S6 kinase subfamily. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAD92170.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; U08316; AAA81952.1; -; mRNA.
EMBL; AK313932; BAG36651.1; -; mRNA.
EMBL; AB208933; BAD92170.1; ALT_INIT; mRNA.
EMBL; AL732366; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL807772; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC096301; AAH96301.1; -; mRNA.
EMBL; BC096302; AAH96302.1; -; mRNA.
EMBL; BC096303; AAH96303.1; -; mRNA.
EMBL; L07599; AAC82495.1; -; mRNA.
EMBL; AB102662; BAC81131.1; -; mRNA.
CCDS; CCDS14197.1; -.
PIR; I38556; I38556.
RefSeq; NP_004577.1; NM_004586.2.
UniGene; Hs.445387; -.
PDB; 4D9T; X-ray; 2.40 A; A=399-740.
PDB; 4D9U; X-ray; 2.40 A; A=399-740.
PDB; 4JG6; X-ray; 2.60 A; A=399-740.
PDB; 4JG7; X-ray; 3.00 A; A=399-740.
PDB; 4JG8; X-ray; 3.10 A; A=399-740.
PDB; 4NUS; X-ray; 2.39 A; A=39-359.
PDB; 4NW5; X-ray; 1.94 A; A=39-359.
PDB; 4NW6; X-ray; 1.74 A; A=39-359.
PDB; 5D9K; X-ray; 2.55 A; A/B=39-366.
PDB; 5D9L; X-ray; 2.15 A; A=39-359.
PDBsum; 4D9T; -.
PDBsum; 4D9U; -.
PDBsum; 4JG6; -.
PDBsum; 4JG7; -.
PDBsum; 4JG8; -.
PDBsum; 4NUS; -.
PDBsum; 4NW5; -.
PDBsum; 4NW6; -.
PDBsum; 5D9K; -.
PDBsum; 5D9L; -.
ProteinModelPortal; P51812; -.
SMR; P51812; -.
BioGrid; 112111; 58.
DIP; DIP-38247N; -.
IntAct; P51812; 22.
MINT; MINT-1542962; -.
STRING; 9606.ENSP00000368884; -.
BindingDB; P51812; -.
ChEMBL; CHEMBL2345; -.
DrugBank; DB00945; Acetylsalicylic acid.
GuidetoPHARMACOLOGY; 1528; -.
iPTMnet; P51812; -.
PhosphoSitePlus; P51812; -.
BioMuta; RPS6KA3; -.
DMDM; 1730070; -.
EPD; P51812; -.
MaxQB; P51812; -.
PaxDb; P51812; -.
PeptideAtlas; P51812; -.
PRIDE; P51812; -.
DNASU; 6197; -.
Ensembl; ENST00000379565; ENSP00000368884; ENSG00000177189.
GeneID; 6197; -.
KEGG; hsa:6197; -.
UCSC; uc004czu.4; human.
CTD; 6197; -.
DisGeNET; 6197; -.
EuPathDB; HostDB:ENSG00000177189.12; -.
GeneCards; RPS6KA3; -.
GeneReviews; RPS6KA3; -.
HGNC; HGNC:10432; RPS6KA3.
HPA; CAB003853; -.
HPA; CAB013520; -.
HPA; HPA003221; -.
MalaCards; RPS6KA3; -.
MIM; 300075; gene.
MIM; 300844; phenotype.
MIM; 303600; phenotype.
neXtProt; NX_P51812; -.
OpenTargets; ENSG00000177189; -.
Orphanet; 192; Coffin-Lowry syndrome.
Orphanet; 777; X-linked non-syndromic intellectual disability.
PharmGKB; PA34847; -.
eggNOG; KOG0598; Eukaryota.
eggNOG; ENOG410XNPH; LUCA.
GeneTree; ENSGT00890000139324; -.
HOGENOM; HOG000233033; -.
HOVERGEN; HBG108317; -.
InParanoid; P51812; -.
KO; K04373; -.
OMA; YTLNRQD; -.
OrthoDB; EOG091G05Z7; -.
PhylomeDB; P51812; -.
TreeFam; TF313438; -.
BRENDA; 2.7.11.1; 2681.
Reactome; R-HSA-198753; ERK/MAPK targets.
Reactome; R-HSA-199920; CREB phosphorylation.
Reactome; R-HSA-2559582; Senescence-Associated Secretory Phenotype (SASP).
Reactome; R-HSA-437239; Recycling pathway of L1.
Reactome; R-HSA-442742; CREB phosphorylation through the activation of Ras.
Reactome; R-HSA-444257; RSK activation.
Reactome; R-HSA-881907; Gastrin-CREB signalling pathway via PKC and MAPK.
SignaLink; P51812; -.
SIGNOR; P51812; -.
ChiTaRS; RPS6KA3; human.
GeneWiki; RPS6KA3; -.
GenomeRNAi; 6197; -.
PRO; PR:P51812; -.
Proteomes; UP000005640; Chromosome X.
Bgee; ENSG00000177189; -.
CleanEx; HS_RPS6KA3; -.
ExpressionAtlas; P51812; baseline and differential.
Genevisible; P51812; HS.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IBA:GO_Central.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0043027; F:cysteine-type endopeptidase inhibitor activity involved in apoptotic process; IDA:UniProtKB.
GO; GO:0016301; F:kinase activity; TAS:Reactome.
GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
GO; GO:0004672; F:protein kinase activity; TAS:ProtInc.
GO; GO:0019901; F:protein kinase binding; IEA:Ensembl.
GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
GO; GO:0007417; P:central nervous system development; TAS:ProtInc.
GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
GO; GO:0043066; P:negative regulation of apoptotic process; TAS:UniProtKB.
GO; GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; IDA:UniProtKB.
GO; GO:0018105; P:peptidyl-serine phosphorylation; TAS:ARUK-UCL.
GO; GO:0045597; P:positive regulation of cell differentiation; TAS:UniProtKB.
GO; GO:0030307; P:positive regulation of cell growth; TAS:UniProtKB.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IMP:BHF-UCL.
GO; GO:0043620; P:regulation of DNA-templated transcription in response to stress; TAS:UniProtKB.
GO; GO:0043555; P:regulation of translation in response to stress; TAS:UniProtKB.
GO; GO:0032496; P:response to lipopolysaccharide; ISS:UniProtKB.
GO; GO:0007165; P:signal transduction; TAS:ProtInc.
GO; GO:0001501; P:skeletal system development; TAS:ProtInc.
GO; GO:0002224; P:toll-like receptor signaling pathway; ISS:UniProtKB.
InterPro; IPR000961; AGC-kinase_C.
InterPro; IPR011009; Kinase-like_dom_sf.
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; ATP-binding; Cell cycle; Complete proteome; Cytoplasm;
Disease mutation; Kinase; Magnesium; Mental retardation;
Metal-binding; Nucleotide-binding; Nucleus; Phosphoprotein;
Polymorphism; Reference proteome; Repeat;
Serine/threonine-protein kinase; Stress response; Transferase.
CHAIN 1 740 Ribosomal protein S6 kinase alpha-3.
/FTId=PRO_0000086203.
DOMAIN 68 327 Protein kinase 1. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
DOMAIN 328 397 AGC-kinase C-terminal.
DOMAIN 422 679 Protein kinase 2. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 74 82 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 428 436 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
ACT_SITE 193 193 Proton acceptor. {ECO:0000250}.
ACT_SITE 539 539 Proton acceptor. {ECO:0000250}.
BINDING 100 100 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
BINDING 451 451 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 227 227 Phosphoserine; by PDPK1.
{ECO:0000250|UniProtKB:P18654,
ECO:0000305}.
MOD_RES 365 365 Phosphothreonine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:19369195,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 369 369 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:19369195,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 375 375 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:19369195}.
MOD_RES 386 386 Phosphoserine; by autocatalysis and
MAPKAPK2. {ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:19369195,
ECO:0000244|PubMed:24275569}.
MOD_RES 415 415 Phosphoserine.
{ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:19369195,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 529 529 Phosphotyrosine; by FGFR3.
{ECO:0000250|UniProtKB:P18654}.
MOD_RES 556 556 Phosphoserine.
{ECO:0000244|PubMed:18691976}.
MOD_RES 715 715 Phosphoserine.
{ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:19369195,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
VARIANT 38 38 I -> S (in dbSNP:rs56218010).
{ECO:0000269|PubMed:17344846,
ECO:0000269|PubMed:9837815}.
/FTId=VAR_006188.
VARIANT 75 75 G -> V (in CLS; dbSNP:rs122454124).
{ECO:0000269|PubMed:8955270}.
/FTId=VAR_006189.
VARIANT 82 82 V -> F (in CLS; dbSNP:rs122454126).
{ECO:0000269|PubMed:9837815}.
/FTId=VAR_006190.
VARIANT 114 114 R -> W (in CLS; dbSNP:rs122454127).
{ECO:0000269|PubMed:10094187}.
/FTId=VAR_006191.
VARIANT 115 115 T -> S (in MRX19; dbSNP:rs387906703).
{ECO:0000269|PubMed:17100996}.
/FTId=VAR_065892.
VARIANT 127 127 H -> Q (in CLS).
{ECO:0000269|PubMed:9837815}.
/FTId=VAR_006192.
VARIANT 152 152 Missing (in MRX19).
{ECO:0000269|PubMed:17100996}.
/FTId=VAR_065893.
VARIANT 154 154 D -> Y (in CLS).
{ECO:0000269|PubMed:9837815}.
/FTId=VAR_006193.
VARIANT 189 189 I -> K (in CLS; dbSNP:rs122454130).
{ECO:0000269|PubMed:10528858}.
/FTId=VAR_065894.
VARIANT 202 202 Missing (in MRX19).
{ECO:0000269|PubMed:17100996}.
/FTId=VAR_065895.
VARIANT 225 225 A -> V (in CLS; dbSNP:rs879027948).
{ECO:0000269|PubMed:9837815}.
/FTId=VAR_006194.
VARIANT 227 227 S -> A (in CLS; dbSNP:rs122454125).
{ECO:0000269|PubMed:8955270}.
/FTId=VAR_006195.
VARIANT 268 268 F -> S (in CLS; dbSNP:rs122454131).
{ECO:0000269|PubMed:14986828}.
/FTId=VAR_065896.
VARIANT 383 383 R -> W (in MRX19; kinase activity is
decreased but not abolished;
dbSNP:rs122454129).
{ECO:0000269|PubMed:10319851}.
/FTId=VAR_065897.
VARIANT 416 416 I -> V (in a breast cancer sample;
somatic mutation; dbSNP:rs148050184).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_035627.
VARIANT 431 431 G -> D (in CLS).
{ECO:0000269|PubMed:9837815}.
/FTId=VAR_006196.
VARIANT 477 477 Missing (in CLS).
{ECO:0000269|PubMed:15214012}.
/FTId=VAR_065898.
VARIANT 483 483 Y -> C (in a gastric adenocarcinoma
sample; somatic mutation).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_040629.
VARIANT 608 608 L -> F (in a glioblastoma multiforme
sample; somatic mutation).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_040630.
VARIANT 723 723 R -> C (in dbSNP:rs35026425).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_040631.
VARIANT 729 729 R -> Q (in CLS; dbSNP:rs28935171).
{ECO:0000269|PubMed:10094187}.
/FTId=VAR_006197.
CONFLICT 89 89 S -> L (in Ref. 5; AAH96303).
{ECO:0000305}.
CONFLICT 410 410 Missing (in Ref. 3; BAD92170).
{ECO:0000305}.
CONFLICT 424 424 V -> L (in Ref. 6; AAC82495).
{ECO:0000305}.
CONFLICT 480 480 K -> N (in Ref. 6; AAC82495).
{ECO:0000305}.
CONFLICT 494 494 Missing (in Ref. 6; AAC82495).
{ECO:0000305}.
HELIX 50 54 {ECO:0000244|PDB:5D9L}.
HELIX 65 67 {ECO:0000244|PDB:4NW6}.
STRAND 68 76 {ECO:0000244|PDB:4NW6}.
STRAND 78 87 {ECO:0000244|PDB:4NW6}.
TURN 91 94 {ECO:0000244|PDB:4NW6}.
STRAND 96 104 {ECO:0000244|PDB:4NW6}.
TURN 105 107 {ECO:0000244|PDB:4NW6}.
HELIX 109 124 {ECO:0000244|PDB:4NW6}.
STRAND 133 139 {ECO:0000244|PDB:4NW6}.
STRAND 142 148 {ECO:0000244|PDB:4NW6}.
STRAND 152 154 {ECO:0000244|PDB:5D9K}.
HELIX 155 162 {ECO:0000244|PDB:4NW6}.
HELIX 167 186 {ECO:0000244|PDB:4NW6}.
STRAND 189 192 {ECO:0000244|PDB:5D9L}.
HELIX 196 198 {ECO:0000244|PDB:4NW6}.
STRAND 199 201 {ECO:0000244|PDB:4NW6}.
STRAND 203 205 {ECO:0000244|PDB:4NUS}.
STRAND 207 209 {ECO:0000244|PDB:4NW6}.
STRAND 214 216 {ECO:0000244|PDB:5D9L}.
HELIX 217 223 {ECO:0000244|PDB:4NUS}.
TURN 224 226 {ECO:0000244|PDB:4NUS}.
HELIX 232 234 {ECO:0000244|PDB:4NW6}.
HELIX 237 240 {ECO:0000244|PDB:4NW6}.
HELIX 249 263 {ECO:0000244|PDB:4NW6}.
HELIX 273 282 {ECO:0000244|PDB:4NW6}.
HELIX 293 302 {ECO:0000244|PDB:4NW6}.
HELIX 307 309 {ECO:0000244|PDB:4NW6}.
TURN 315 318 {ECO:0000244|PDB:4NW6}.
HELIX 319 322 {ECO:0000244|PDB:4NW6}.
HELIX 325 327 {ECO:0000244|PDB:4NW6}.
HELIX 332 336 {ECO:0000244|PDB:4NW6}.
HELIX 351 353 {ECO:0000244|PDB:5D9L}.
STRAND 409 411 {ECO:0000244|PDB:4JG7}.
HELIX 412 414 {ECO:0000244|PDB:4D9U}.
TURN 419 421 {ECO:0000244|PDB:4D9T}.
STRAND 422 430 {ECO:0000244|PDB:4D9T}.
STRAND 432 441 {ECO:0000244|PDB:4D9T}.
TURN 442 445 {ECO:0000244|PDB:4D9T}.
STRAND 446 454 {ECO:0000244|PDB:4D9T}.
TURN 455 457 {ECO:0000244|PDB:4D9T}.
HELIX 461 470 {ECO:0000244|PDB:4D9T}.
STRAND 479 484 {ECO:0000244|PDB:4D9T}.
STRAND 486 494 {ECO:0000244|PDB:4D9T}.
HELIX 501 506 {ECO:0000244|PDB:4D9T}.
HELIX 513 532 {ECO:0000244|PDB:4D9T}.
HELIX 542 544 {ECO:0000244|PDB:4D9T}.
STRAND 545 551 {ECO:0000244|PDB:4D9T}.
HELIX 554 556 {ECO:0000244|PDB:4D9T}.
STRAND 557 559 {ECO:0000244|PDB:4D9T}.
STRAND 571 573 {ECO:0000244|PDB:4JG8}.
HELIX 587 613 {ECO:0000244|PDB:4D9T}.
HELIX 626 635 {ECO:0000244|PDB:4D9T}.
HELIX 643 645 {ECO:0000244|PDB:4D9U}.
STRAND 646 648 {ECO:0000244|PDB:4JG6}.
HELIX 650 659 {ECO:0000244|PDB:4D9T}.
TURN 664 666 {ECO:0000244|PDB:4D9T}.
HELIX 670 673 {ECO:0000244|PDB:4D9T}.
HELIX 677 680 {ECO:0000244|PDB:4D9T}.
HELIX 682 684 {ECO:0000244|PDB:4D9T}.
HELIX 696 710 {ECO:0000244|PDB:4D9T}.
HELIX 711 713 {ECO:0000244|PDB:4JG8}.
SEQUENCE 740 AA; 83736 MW; 486AE8357CEAB6C8 CRC64;
MPLAQLADPW QKMAVESPSD SAENGQQIMD EPMGEEEINP QTEEVSIKEI AITHHVKEGH
EKADPSQFEL LKVLGQGSFG KVFLVKKISG SDARQLYAMK VLKKATLKVR DRVRTKMERD
ILVEVNHPFI VKLHYAFQTE GKLYLILDFL RGGDLFTRLS KEVMFTEEDV KFYLAELALA
LDHLHSLGII YRDLKPENIL LDEEGHIKLT DFGLSKESID HEKKAYSFCG TVEYMAPEVV
NRRGHTQSAD WWSFGVLMFE MLTGTLPFQG KDRKETMTMI LKAKLGMPQF LSPEAQSLLR
MLFKRNPANR LGAGPDGVEE IKRHSFFSTI DWNKLYRREI HPPFKPATGR PEDTFYFDPE
FTAKTPKDSP GIPPSANAHQ LFRGFSFVAI TSDDESQAMQ TVGVHSIVQQ LHRNSIQFTD
GYEVKEDIGV GSYSVCKRCI HKATNMEFAV KIIDKSKRDP TEEIEILLRY GQHPNIITLK
DVYDDGKYVY VVTELMKGGE LLDKILRQKF FSEREASAVL FTITKTVEYL HAQGVVHRDL
KPSNILYVDE SGNPESIRIC DFGFAKQLRA ENGLLMTPCY TANFVAPEVL KRQGYDAACD
IWSLGVLLYT MLTGYTPFAN GPDDTPEEIL ARIGSGKFSL SGGYWNSVSD TAKDLVSKML
HVDPHQRLTA ALVLRHPWIV HWDQLPQYQL NRQDAPHLVK GAMAATYSAL NRNQSPVLEP
VGRSTLAQRR GIKKITSTAL


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