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Serine/threonine-protein kinase Sgk1 (EC 2.7.11.1) (Serum/glucocorticoid-regulated kinase 1)

 SGK1_HUMAN              Reviewed;         431 AA.
O00141; B7UUP7; B7UUP8; B7UUP9; B7Z5B2; E1P583; Q5TCN2; Q5TCN3;
Q5TCN4; Q5VY65; Q9UN56;
15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
07-MAR-2006, sequence version 2.
30-AUG-2017, entry version 178.
RecName: Full=Serine/threonine-protein kinase Sgk1;
EC=2.7.11.1;
AltName: Full=Serum/glucocorticoid-regulated kinase 1;
Name=SGK1; Synonyms=SGK;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=9114008; DOI=10.1073/pnas.94.9.4440;
Waldegger S., Barth P., Raber G., Lang F.;
"Cloning and characterization of a putative human serine/threonine
protein kinase transcriptionally modified during anisotonic and
isotonic alterations of cell volume.";
Proc. Natl. Acad. Sci. U.S.A. 94:4440-4445(1997).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING (ISOFORM
1).
PubMed=9722955; DOI=10.1006/geno.1998.5258;
Waldegger S., Erdel M., Nagl U.O., Barth P., Raber G., Steuer S.,
Utermann G., Paulmichl M., Lang F.;
"Genomic organization and chromosomal localization of the human SGK
protein kinase gene.";
Genomics 51:299-302(1998).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, ALTERNATIVE PROMOTER
USAGE, INDUCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
TISSUE=Brain;
PubMed=18753299; DOI=10.1152/ajprenal.90239.2008;
Raikwar N.S., Snyder P.M., Thomas C.P.;
"An evolutionarily conserved N-terminal Sgk1 variant with enhanced
stability and improved function.";
Am. J. Physiol. 295:F1440-F1448(2008).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3; 4 AND 5), AND ALTERNATIVE
PROMOTER USAGE.
TISSUE=Glioblastoma, Hippocampus, and Skin;
Hall B.A., Blakeley S., Daniels N.A., Jamieson D., Brickley D.,
Reynolds N.J., Conzen S.D., Jackson T.R.;
"Transcriptional variants of serum/glucocorticoid regulated kinase 1
show differential localisation and regulation.";
Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Hair follicle dermal papilla;
Kim M.K., Kim Y.H., Seo J.M., Lee H.M., Chung H.J., Sohn M.Y.,
Hwang S.Y., Im S.U., Jung E.J., Lee J.H., Kim J.C.;
"A catalogue of genes in the human dermal papilla cells as identified
by expressed sequence tags.";
Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
TISSUE=Brain;
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).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=14574404; DOI=10.1038/nature02055;
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
"The DNA sequence and analysis of human chromosome 6.";
Nature 425:805-811(2003).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Cervix;
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).
[10]
TISSUE SPECIFICITY.
PubMed=10548550; DOI=10.1042/bj3440189;
Kobayashi T., Deak M., Morrice N., Cohen P.;
"Characterization of the structure and regulation of two novel
isoforms of serum- and glucocorticoid-induced protein kinase.";
Biochem. J. 344:189-197(1999).
[11]
PHOSPHORYLATION AT THR-256 AND SER-422, AND MUTAGENESIS OF THR-256 AND
SER-422.
TISSUE=Brain;
PubMed=10191262; DOI=10.1042/bj3390319;
Kobayashi T., Cohen P.;
"Activation of serum- and glucocorticoid-regulated protein kinase by
agonists that activate phosphatidylinositide 3-kinase is mediated by
3-phosphoinositide-dependent protein kinase-1 (PDK1) and PDK2.";
Biochem. J. 339:319-328(1999).
[12]
CHARACTERIZATION.
PubMed=10884438; DOI=10.1073/pnas.97.14.8157;
Lang F., Klingel K., Wagner C.A., Stegen C., Waerntges S.,
Friedrich B., Lanzendoerfer M., Melzig J., Moschen I., Steuer S.,
Waldegger S., Sauter M., Paulmichl M., Gerke V., Risler T., Gamba G.,
Capasso G., Kandolf R., Hebert S.C., Massry S.G., Broer S.;
"Deranged transcriptional regulation of cell-volume-sensitive kinase
hSGK in diabetic nephropathy.";
Proc. Natl. Acad. Sci. U.S.A. 97:8157-8162(2000).
[13]
PHOSPHORYLATION AT SER-78 BY MAPK7, AND INTERACTION WITH MAPK7.
PubMed=11254654; DOI=10.1074/jbc.C000838200;
Hayashi M., Tapping R.I., Chao T.H., Lo J.F., King C.C., Yang Y.,
Lee J.D.;
"BMK1 mediates growth factor-induced cell proliferation through direct
cellular activation of serum and glucocorticoid-inducible kinase.";
J. Biol. Chem. 276:8631-8634(2001).
[14]
PHOSPHORYLATION AT THR-369 BY PKA.
PubMed=11096081; DOI=10.1074/jbc.M007052200;
Perrotti N., He R.A., Phillips S.A., Haft C.R., Taylor S.I.;
"Activation of serum- and glucocorticoid-induced protein kinase (Sgk)
by cyclic AMP and insulin.";
J. Biol. Chem. 276:9406-9412(2001).
[15]
FUNCTION IN PHOSPHORYLATION OF BRAF.
PubMed=11410590; DOI=10.1074/jbc.M102808200;
Zhang B.H., Tang E.D., Zhu T., Greenberg M.E., Vojtek A.B., Guan K.L.;
"Serum- and glucocorticoid-inducible kinase SGK phosphorylates and
negatively regulates B-Raf.";
J. Biol. Chem. 276:31620-31626(2001).
[16]
FUNCTION.
PubMed=11154281; DOI=10.1128/MCB.21.3.952-965.2001;
Brunet A., Park J., Tran H., Hu L.S., Hemmings B.A., Greenberg M.E.;
"Protein kinase SGK mediates survival signals by phosphorylating the
forkhead transcription factor FKHRL1 (FOXO3a).";
Mol. Cell. Biol. 21:952-965(2001).
[17]
INTERACTION WITH NEDD4 AND NEDD4L, MUTAGENESIS OF LYS-127; TYR-298 AND
SER-422, AND FUNCTION.
PubMed=11696533; DOI=10.1074/jbc.C100623200;
Snyder P.M., Olson D.R., Thomas B.C.;
"Serum and glucocorticoid-regulated kinase modulates Nedd4-2-mediated
inhibition of the epithelial Na+ channel.";
J. Biol. Chem. 277:5-8(2002).
[18]
FUNCTION IN REGULATION OF NA(+)/K(+) ATPASE.
PubMed=12590200; DOI=10.1159/000068699;
Henke G., Setiawan I., Boehmer C., Lang F.;
"Activation of Na+/K+-ATPase by the serum and glucocorticoid-dependent
kinase isoforms.";
Kidney Blood Press. Res. 25:370-374(2002).
[19]
FUNCTION.
PubMed=12397388; DOI=10.1007/s00424-002-0873-2;
Gamper N., Fillon S., Feng Y., Friedrich B., Lang P.A., Henke G.,
Huber S.M., Kobayashi T., Cohen P., Lang F.;
"K(+) channel activation by all three isoforms of serum- and
glucocorticoid-dependent protein kinase SGK.";
Pflugers Arch. 445:60-66(2002).
[20]
FUNCTION, AND INTERACTION WITH SLC9A3R2/NHERF2 AND KCNJ1/ROMK1.
PubMed=14623317; DOI=10.1016/j.bbrc.2003.10.037;
Palmada M., Embark H.M., Yun C., Bohmer C., Lang F.;
"Molecular requirements for the regulation of the renal outer
medullary K(+) channel ROMK1 by the serum- and glucocorticoid-
inducible kinase SGK1.";
Biochem. Biophys. Res. Commun. 311:629-634(2003).
[21]
FUNCTION IN REGULATION OF SCN5A.
PubMed=12650886; DOI=10.1016/S0008-6363(02)00837-4;
Boehmer C., Wilhelm V., Palmada M., Wallisch S., Henke G.,
Brinkmeier H., Cohen P., Pieske B., Lang F.;
"Serum and glucocorticoid inducible kinases in the regulation of the
cardiac sodium channel SCN5A.";
Cardiovasc. Res. 57:1079-1084(2003).
[22]
FUNCTION IN PHOSPHORYLATION OF MAP3K3/MEKK3.
PubMed=12761204; DOI=10.1093/jb/mvg010;
Chun J., Kwon T., Kim D.J., Park I., Chung G., Lee E.J., Hong S.K.,
Chang S.I., Kim H.Y., Kang S.S.;
"Inhibition of mitogen-activated kinase kinase kinase 3 activity
through phosphorylation by the serum- and glucocorticoid-induced
kinase 1.";
J. Biochem. 133:103-108(2003).
[23]
FUNCTION IN REGULATION OF KCNA3/KV1.3, AND MUTAGENESIS OF LYS-127 AND
SER-422.
PubMed=12911626;
Boehmer C., Henke G., Schniepp R., Palmada M., Rothstein J.D.,
Broeer S., Lang F.;
"Regulation of the glutamate transporter EAAT1 by the ubiquitin ligase
Nedd4-2 and the serum and glucocorticoid-inducible kinase isoforms
SGK1/3 and protein kinase B.";
J. Neurochem. 86:1181-1188(2003).
[24]
NUCLEAR LOCALIZATION SIGNAL.
PubMed=12631736; DOI=10.1091/mbc.E02-03-0170;
Maiyar A.C., Leong M.L., Firestone G.L.;
"Importin-alpha mediates the regulated nuclear targeting of serum- and
glucocorticoid-inducible protein kinase (Sgk) by recognition of a
nuclear localization signal in the kinase central domain.";
Mol. Biol. Cell 14:1221-1239(2003).
[25]
FUNCTION IN REGULATION OF KCNE1 AND KCNQ1.
PubMed=12634932; DOI=10.1007/s00424-002-0982-y;
Embark H.M., Boehmer C., Vallon V., Luft F., Lang F.;
"Regulation of KCNE1-dependent K(+) current by the serum and
glucocorticoid-inducible kinase (SGK) isoforms.";
Pflugers Arch. 445:601-606(2003).
[26]
FUNCTION IN REGULATION OF SLC34A2/NAPI-2B, AND FUNCTION IN
PHOSPHORYLATION OF NEDD4L.
PubMed=15044175; DOI=10.1152/ajpgi.00121.2003;
Palmada M., Dieter M., Speil A., Boehmer C., Mack A.F., Wagner H.J.,
Klingel K., Kandolf R., Murer H., Biber J., Closs E.I., Lang F.;
"Regulation of intestinal phosphate cotransporter NaPi IIb by
ubiquitin ligase Nedd4-2 and by serum- and glucocorticoid-dependent
kinase 1.";
Am. J. Physiol. 287:G143-G150(2004).
[27]
FUNCTION IN REGULATION OF SLC13A2/NADC1.
PubMed=14706641; DOI=10.1016/j.bbrc.2003.12.011;
Boehmer C., Embark H.M., Bauer A., Palmada M., Yun C.H., Weinman E.J.,
Endou H., Cohen P., Lahme S., Bichler K.H., Lang F.;
"Stimulation of renal Na+ dicarboxylate cotransporter 1 by Na+/H+
exchanger regulating factor 2, serum and glucocorticoid inducible
kinase isoforms, and protein kinase B.";
Biochem. Biophys. Res. Commun. 313:998-1003(2004).
[28]
FUNCTION IN REGULATION OF TRPV5.
PubMed=15319523; DOI=10.1159/000080329;
Embark H.M., Setiawan I., Poppendieck S., van de Graaf S.F.,
Boehmer C., Palmada M., Wieder T., Gerstberger R., Cohen P., Yun C.C.,
Bindels R.J., Lang F.;
"Regulation of the epithelial Ca2+ channel TRPV5 by the NHE regulating
factor NHERF2 and the serum and glucocorticoid inducible kinase
isoforms SGK1 and SGK3 expressed in Xenopus oocytes.";
Cell. Physiol. Biochem. 14:203-212(2004).
[29]
FUNCTION.
PubMed=15234985; DOI=10.1074/jbc.M403260200;
Diakov A., Korbmacher C.;
"A novel pathway of epithelial sodium channel activation involves a
serum- and glucocorticoid-inducible kinase consensus motif in the C
terminus of the channel's alpha-subunit.";
J. Biol. Chem. 279:38134-38142(2004).
[30]
FUNCTION, AND MUTAGENESIS OF LYS-127 AND SER-422.
PubMed=15040001; DOI=10.1002/jcp.10430;
Henke G., Maier G., Wallisch S., Boehmer C., Lang F.;
"Regulation of the voltage gated K+ channel Kv1.3 by the ubiquitin
ligase Nedd4-2 and the serum and glucocorticoid inducible kinase
SGK1.";
J. Cell. Physiol. 199:194-199(2004).
[31]
FUNCTION IN REGULATION OF BSND.
PubMed=15496163; DOI=10.1111/j.1523-1755.2004.00966.x;
Embark H.M., Boehmer C., Palmada M., Rajamanickam J., Wyatt A.W.,
Wallisch S., Capasso G., Waldegger P., Seyberth H.W., Waldegger S.,
Lang F.;
"Regulation of CLC-Ka/barttin by the ubiquitin ligase Nedd4-2 and the
serum- and glucocorticoid-dependent kinases.";
Kidney Int. 66:1918-1925(2004).
[32]
FUNCTION IN PHOSPHORYLATION OF SLC9A3/NHE3.
PubMed=15888551; DOI=10.1152/ajpcell.00597.2004;
Wang D., Sun H., Lang F., Yun C.C.;
"Activation of NHE3 by dexamethasone requires phosphorylation of NHE3
at Ser663 by SGK1.";
Am. J. Physiol. 289:C802-C810(2005).
[33]
FUNCTION IN REGULATION OF SLC1A5/ASCT2.
PubMed=15845389; DOI=10.1016/j.bbrc.2005.03.159;
Palmada M., Speil A., Jeyaraj S., Boehmer C., Lang F.;
"The serine/threonine kinases SGK1, 3 and PKB stimulate the amino acid
transporter ASCT2.";
Biochem. Biophys. Res. Commun. 331:272-277(2005).
[34]
FUNCTION IN REGULATION OF SLC1A7/EAAT5.
PubMed=15737648; DOI=10.1016/j.bbrc.2005.02.035;
Boehmer C., Rajamanickam J., Schniepp R., Kohler K., Wulff P.,
Kuhl D., Palmada M., Lang F.;
"Regulation of the excitatory amino acid transporter EAAT5 by the
serum and glucocorticoid dependent kinases SGK1 and SGK3.";
Biochem. Biophys. Res. Commun. 329:738-742(2005).
[35]
FUNCTION IN REGULATION OF SLC6A8.
PubMed=16036218; DOI=10.1016/j.bbrc.2005.06.164;
Shojaiefard M., Christie D.L., Lang F.;
"Stimulation of the creatine transporter SLC6A8 by the protein kinases
SGK1 and SGK3.";
Biochem. Biophys. Res. Commun. 334:742-746(2005).
[36]
FUNCTION IN PHOSPHORYLATION OF CREB1, AND INTERACTION WITH CREB1.
PubMed=15733869; DOI=10.1016/j.febslet.2005.01.040;
David S., Kalb R.G.;
"Serum/glucocorticoid-inducible kinase can phosphorylate the cyclic
AMP response element binding protein, CREB.";
FEBS Lett. 579:1534-1538(2005).
[37]
UBIQUITINATION.
PubMed=15576372; DOI=10.1074/jbc.M411053200;
Zhou R., Snyder P.M.;
"Nedd4-2 phosphorylation induces serum and glucocorticoid-regulated
kinase (SGK) ubiquitination and degradation.";
J. Biol. Chem. 280:4518-4523(2005).
[38]
FUNCTION IN REGULATION OF SLC2A1/GLUT1.
PubMed=16443776; DOI=10.2337/diabetes.55.02.06.db05-0720;
Palmada M., Boehmer C., Akel A., Rajamanickam J., Jeyaraj S.,
Keller K., Lang F.;
"SGK1 kinase upregulates GLUT1 activity and plasma membrane
expression.";
Diabetes 55:421-427(2006).
[39]
FUNCTION IN PHOSPHORYLATION OF MAPT/TAU, AND INTERACTION WITH
MAPT/TAU.
PubMed=16982696; DOI=10.1128/MCB.01017-06;
Yang Y.C., Lin C.H., Lee E.H.;
"Serum- and glucocorticoid-inducible kinase 1 (SGK1) increases neurite
formation through microtubule depolymerization by SGK1 and by SGK1
phosphorylation of tau.";
Mol. Cell. Biol. 26:8357-8370(2006).
[40]
SUBCELLULAR LOCATION.
PubMed=17202226; DOI=10.1152/ajpcell.00399.2006;
Cordas E., Naray-Fejes-Toth A., Fejes-Toth G.;
"Subcellular location of serum- and glucocorticoid-induced kinase-1 in
renal and mammary epithelial cells.";
Am. J. Physiol. 292:C1971-C1981(2007).
[41]
FUNCTION IN PHOSPHORYLATION OF SLC2A4/GLUT4.
PubMed=17382906; DOI=10.1016/j.bbrc.2007.03.029;
Jeyaraj S., Boehmer C., Lang F., Palmada M.;
"Role of SGK1 kinase in regulating glucose transport via glucose
transporter GLUT4.";
Biochem. Biophys. Res. Commun. 356:629-635(2007).
[42]
FUNCTION IN REGULATION OF TRPV6.
PubMed=18005662; DOI=10.1016/j.febslet.2007.11.006;
Boehmer C., Palmada M., Kenngott C., Lindner R., Klaus F., Laufer J.,
Lang F.;
"Regulation of the epithelial calcium channel TRPV6 by the serum and
glucocorticoid-inducible kinase isoforms SGK1 and SGK3.";
FEBS Lett. 581:5586-5590(2007).
[43]
FUNCTION IN PHOSPHORYLATION OF APBB1/FE65.
PubMed=18304449; DOI=10.5483/BMBRep.2008.41.1.041;
Lee E.J., Chun J., Hyun S., Ahn H.R., Jeong J.M., Hong S.K.,
Hong J.T., Chang I.K., Jeon H.Y., Han Y.S., Auh C.K., Park J.I.,
Kang S.S.;
"Regulation Fe65 localization to the nucleus by SGK1 phosphorylation
of its Ser566 residue.";
BMB Rep. 41:41-47(2008).
[44]
PHOSPHORYLATION AT SER-422 BY MTORC2.
PubMed=18925875; DOI=10.1042/BJ20081668;
Garcia-Martinez J.M., Alessi D.R.;
"mTOR complex 2 (mTORC2) controls hydrophobic motif phosphorylation
and activation of serum- and glucocorticoid-induced protein kinase 1
(SGK1).";
Biochem. J. 416:375-385(2008).
[45]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-74; SER-397 AND SER-401,
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).
[46]
ALTERNATIVE PROMOTER USAGE (ISOFORMS 2 AND 3).
PubMed=18334630; DOI=10.1073/pnas.0800958105;
Arteaga M.F., Coric T., Straub C., Canessa C.M.;
"A brain-specific SGK1 splice isoform regulates expression of ASIC1 in
neurons.";
Proc. Natl. Acad. Sci. U.S.A. 105:4459-4464(2008).
[47]
PHOSPHORYLATION AT SER-397 AND SER-401.
PubMed=19068477; DOI=10.1074/jbc.M807502200;
Chen W., Chen Y., Xu B.E., Juang Y.C., Stippec S., Zhao Y., Cobb M.H.;
"Regulation of a third conserved phosphorylation site in SGK1.";
J. Biol. Chem. 284:3453-3460(2009).
[48]
FUNCTION IN PHOSPHORYLATION OF MAPK1/ERK2, AND INTERACTION WITH
MAPK3/ERK1; MAPK1/ERK2; MAP2K1/MEK1 AND MAP2K2/MEK2.
PubMed=19447520; DOI=10.1016/j.jhep.2009.02.027;
Won M., Park K.A., Byun H.S., Kim Y.R., Choi B.L., Hong J.H., Park J.,
Seok J.H., Lee Y.H., Cho C.H., Song I.S., Kim Y.K., Shen H.M.,
Hur G.M.;
"Protein kinase SGK1 enhances MEK/ERK complex formation through the
phosphorylation of ERK2: implication for the positive regulatory role
of SGK1 on the ERK function during liver regeneration.";
J. Hepatol. 51:67-76(2009).
[49]
FUNCTION IN PHOSPHORYLATION OF MDM2.
PubMed=19756449; DOI=10.1007/s00109-009-0525-5;
Amato R., D'Antona L., Porciatti G., Agosti V., Menniti M.,
Rinaldo C., Costa N., Bellacchio E., Mattarocci S., Fuiano G.,
Soddu S., Paggi M.G., Lang F., Perrotti N.;
"Sgk1 activates MDM2-dependent p53 degradation and affects cell
proliferation, survival, and differentiation.";
J. Mol. Med. 87:1221-1239(2009).
[50]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-74; SER-397 AND SER-401,
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).
[51]
FUNCTION IN REGULATION OF SLC6A19.
PubMed=20511718; DOI=10.1159/000315092;
Boehmer C., Sopjani M., Klaus F., Lindner R., Laufer J., Jeyaraj S.,
Lang F., Palmada M.;
"The serum and glucocorticoid inducible kinases SGK1-3 stimulate the
neutral amino acid transporter SLC6A19.";
Cell. Physiol. Biochem. 25:723-732(2010).
[52]
PHOSPHORYLATION AT SER-422 BY MTORC2, AND INTERACTION WITH MTORC2.
PubMed=20338997; DOI=10.1681/ASN.2009111168;
Lu M., Wang J., Jones K.T., Ives H.E., Feldman M.E., Yao L.J.,
Shokat K.M., Ashrafi K., Pearce D.;
"mTOR complex-2 activates ENaC by phosphorylating SGK1.";
J. Am. Soc. Nephrol. 21:811-818(2010).
[53]
FUNCTION.
PubMed=20730100; DOI=10.1371/journal.pone.0012163;
Wiemuth D., Lott J.S., Ly K., Ke Y., Teesdale-Spittle P., Snyder P.M.,
McDonald F.J.;
"Interaction of serum- and glucocorticoid regulated kinase 1 (SGK1)
with the WW-domains of Nedd4-2 is required for epithelial sodium
channel regulation.";
PLoS ONE 5:E12163-E12163(2010).
[54]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-397, 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).
[55]
FUNCTION IN REGULATION OF SLC9A3/NHE3, AND SUBCELLULAR LOCATION.
PubMed=21865597; DOI=10.1091/mbc.E11-04-0328;
He P., Lee S.J., Lin S., Seidler U., Lang F., Fejes-Toth G.,
Naray-Fejes-Toth A., Yun C.C.;
"Serum- and glucocorticoid-induced kinase 3 in recycling endosomes
mediates acute activation of Na+/H+ exchanger NHE3 by
glucocorticoids.";
Mol. Biol. Cell 22:3812-3825(2011).
[56]
REVIEW.
PubMed=12649597; DOI=10.1159/000070244;
Firestone G.L., Giampaolo J.R., O'Keeffe B.A.;
"Stimulus-dependent regulation of serum and glucocorticoid inducible
protein kinase (SGK) transcription, subcellular localization and
enzymatic activity.";
Cell. Physiol. Biochem. 13:1-12(2003).
[57]
REVIEW.
PubMed=16460280; DOI=10.1146/annurev.physiol.68.040104.131654;
Loffing J., Flores S.Y., Staub O.;
"Sgk kinases and their role in epithelial transport.";
Annu. Rev. Physiol. 68:461-490(2006).
[58]
REVIEW ON FUNCTION.
PubMed=20919962; DOI=10.3109/08977194.2010.518616;
Bruhn M.A., Pearson R.B., Hannan R.D., Sheppard K.E.;
"Second AKT: the rise of SGK in cancer signalling.";
Growth Factors 28:394-408(2010).
[59]
REVIEW ON FUNCTION.
PubMed=20530112; DOI=10.1113/jphysiol.2010.190926;
Lang F., Strutz-Seebohm N., Seebohm G., Lang U.E.;
"Significance of SGK1 in the regulation of neuronal function.";
J. Physiol. (Lond.) 588:3349-3354(2010).
[60]
X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 60-431, SUBUNIT, AND
DISULFIDE BOND.
PubMed=17965184; DOI=10.1110/ps.073161707;
Zhao B., Lehr R., Smallwood A.M., Ho T.F., Maley K., Randall T.,
Head M.S., Koretke K.K., Schnackenberg C.G.;
"Crystal structure of the kinase domain of serum and glucocorticoid-
regulated kinase 1 in complex with AMP PNP.";
Protein Sci. 16:2761-2769(2007).
[61]
VARIANTS [LARGE SCALE ANALYSIS] ILE-219 AND VAL-342.
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 which is involved in the
regulation of a wide variety of ion channels, membrane
transporters, cellular enzymes, transcription factors, neuronal
excitability, cell growth, proliferation, survival, migration and
apoptosis. Plays an important role in cellular stress response.
Contributes to regulation of renal Na(+) retention, renal K(+)
elimination, salt appetite, gastric acid secretion, intestinal
Na(+)/H(+) exchange and nutrient transport, insulin-dependent salt
sensitivity of blood pressure, salt sensitivity of peripheral
glucose uptake, cardiac repolarization and memory consolidation.
Up-regulates Na(+) channels: SCNN1A/ENAC, SCN5A and ASIC1/ACCN2,
K(+) channels: KCNJ1/ROMK1, KCNA1-5, KCNQ1-5 and KCNE1, epithelial
Ca(2+) channels: TRPV5 and TRPV6, chloride channels: BSND, CLCN2
and CFTR, glutamate transporters: SLC1A3/EAAT1, SLC1A2 /EAAT2,
SLC1A1/EAAT3, SLC1A6/EAAT4 and SLC1A7/EAAT5, amino acid
transporters: SLC1A5/ASCT2, SLC38A1/SN1 and SLC6A19, creatine
transporter: SLC6A8, Na(+)/dicarboxylate cotransporter:
SLC13A2/NADC1, Na(+)-dependent phosphate cotransporter:
SLC34A2/NAPI-2B, glutamate receptor: GRIK2/GLUR6. Up-regulates
carriers: SLC9A3/NHE3, SLC12A1/NKCC2, SLC12A3/NCC, SLC5A3/SMIT,
SLC2A1/GLUT1, SLC5A1/SGLT1 and SLC15A2/PEPT2. Regulates enzymes:
GSK3A/B, PMM2 and Na(+)/K(+) ATPase, and transcription factors:
CTNNB1 and nuclear factor NF-kappa-B. Stimulates sodium transport
into epithelial cells by enhancing the stability and expression of
SCNN1A/ENAC. This is achieved by phosphorylating the NEDD4L
ubiquitin E3 ligase, promoting its interaction with 14-3-3
proteins, thereby preventing it from binding to SCNN1A/ENAC and
targeting it for degradation. Regulates store-operated Ca(+2)
entry (SOCE) by stimulating ORAI1 and STIM1. Regulates KCNJ1/ROMK1
directly via its phosphorylation or indirectly via increased
interaction with SLC9A3R2/NHERF2. Phosphorylates MDM2 and
activates MDM2-dependent ubiquitination of p53/TP53.
Phosphorylates MAPT/TAU and mediates microtubule depolymerization
and neurite formation in hippocampal neurons. Phosphorylates
SLC2A4/GLUT4 and up-regulates its activity. Phosphorylates
APBB1/FE65 and promotes its localization to the nucleus.
Phosphorylates MAPK1/ERK2 and activates it by enhancing its
interaction with MAP2K1/MEK1 and MAP2K2/MEK2. Phosphorylates FBXW7
and plays an inhibitory role in the NOTCH1 signaling.
Phosphorylates FOXO1 resulting in its relocalization from the
nucleus to the cytoplasm. Phosphorylates FOXO3, promoting its exit
from the nucleus and interference with FOXO3-dependent
transcription. Phosphorylates BRAF and MAP3K3/MEKK3 and inhibits
their activity. Phosphorylates SLC9A3/NHE3 in response to
dexamethasone, resulting in its activation and increased
localization at the cell membrane. Phosphorylates CREB1. Necessary
for vascular remodeling during angiogenesis. Sustained high levels
and activity may contribute to conditions such as hypertension and
diabetic nephropathy. Isoform 2 exhibited a greater effect on cell
plasma membrane expression of SCNN1A/ENAC and Na(+) transport than
isoform 1. {ECO:0000269|PubMed:11154281,
ECO:0000269|PubMed:11410590, ECO:0000269|PubMed:11696533,
ECO:0000269|PubMed:12397388, ECO:0000269|PubMed:12590200,
ECO:0000269|PubMed:12634932, ECO:0000269|PubMed:12650886,
ECO:0000269|PubMed:12761204, ECO:0000269|PubMed:12911626,
ECO:0000269|PubMed:14623317, ECO:0000269|PubMed:14706641,
ECO:0000269|PubMed:15040001, ECO:0000269|PubMed:15044175,
ECO:0000269|PubMed:15234985, ECO:0000269|PubMed:15319523,
ECO:0000269|PubMed:15496163, ECO:0000269|PubMed:15733869,
ECO:0000269|PubMed:15737648, ECO:0000269|PubMed:15845389,
ECO:0000269|PubMed:15888551, ECO:0000269|PubMed:16036218,
ECO:0000269|PubMed:16443776, ECO:0000269|PubMed:16982696,
ECO:0000269|PubMed:17382906, ECO:0000269|PubMed:18005662,
ECO:0000269|PubMed:18304449, ECO:0000269|PubMed:18753299,
ECO:0000269|PubMed:19447520, ECO:0000269|PubMed:19756449,
ECO:0000269|PubMed:20511718, ECO:0000269|PubMed:20730100,
ECO:0000269|PubMed:21865597}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
-!- ENZYME REGULATION: Two specific sites, one in the kinase domain
(Thr-256) and the other in the C-terminal regulatory region (Ser-
422), need to be phosphorylated for its full activation.
Phosphorylation at Ser-397 and Ser-401 are also essential for its
activity. Activated by WNK1, WNK2, WNK3 and WNK4.
-!- SUBUNIT: Homodimer; disulfide-linked. Forms a trimeric complex
with FBXW7 and NOTCH1. Interacts with MAPK3/ERK1, MAPK1/ERK2,
MAP2K1/MEK1, MAP2K2/MEK2, NEDD4, NEDD4L, MAPT/TAU, MAPK7, CREB1,
SLC9A3R2/NHERF2 and KCNJ1/ROMK1. Associates with the mammalian
target of rapamycin complex 2 (mTORC2) via an interaction with
MAPKAP1/SIN1. {ECO:0000269|PubMed:11254654,
ECO:0000269|PubMed:11696533, ECO:0000269|PubMed:14623317,
ECO:0000269|PubMed:15733869, ECO:0000269|PubMed:16982696,
ECO:0000269|PubMed:17965184, ECO:0000269|PubMed:19447520,
ECO:0000269|PubMed:20338997}.
-!- INTERACTION:
P49815:TSC2; NbExp=4; IntAct=EBI-1042854, EBI-396587;
-!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Endoplasmic reticulum
membrane. Cell membrane. Mitochondrion. Note=The subcellular
localization is controlled by the cell cycle, as well as by
exposure to specific hormones and environmental stress stimuli. In
proliferating cells, it shuttles between the nucleus and cytoplasm
in synchrony with the cell cycle, and in serum/growth factor-
stimulated cells it resides in the nucleus. In contrast, after
exposure to environmental stress or treatment with
glucocorticoids, it is detected in the cytoplasm and with certain
stress conditions is associated with the mitochondria. In
osmoregulation through the epithelial sodium channel, it can be
localized to the cytoplasmic surface of the cell membrane.
Nuclear, upon phosphorylation.
-!- SUBCELLULAR LOCATION: Isoform 2: Cell membrane.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative promoter usage, Alternative splicing; Named isoforms=5;
Name=1;
IsoId=O00141-1; Sequence=Displayed;
Name=2; Synonyms=Sgk1.1, Sgk1_v2;
IsoId=O00141-2; Sequence=VSP_037784;
Note=Produced by alternative promoter usage.;
Name=3; Synonyms=Sgk1.2;
IsoId=O00141-3; Sequence=VSP_037785;
Note=Produced by alternative promoter usage.;
Name=4;
IsoId=O00141-4; Sequence=VSP_037786;
Note=Produced by alternative splicing of isoform 1.;
Name=5;
IsoId=O00141-5; Sequence=VSP_037787;
Note=Produced by alternative promoter usage.;
-!- TISSUE SPECIFICITY: Expressed in most tissues with highest levels
in the pancreas, followed by placenta, kidney and lung. Isoform 2
is strongly expressed in brain and pancreas, weaker in heart,
placenta, lung, liver and skeletal muscle.
{ECO:0000269|PubMed:10548550, ECO:0000269|PubMed:18753299}.
-!- INDUCTION: Induced by a very large spectrum of stimuli distinct
from glucocorticoids and serum. These include aldosterone, cell
shrinkage, cell swelling, TGF-beta, ischemic injury of the brain,
neuronal excitotoxicity memory consolidation, chronic viral
hepatitis, DNA-damaging agents, vitamin D3 psychophysiological
stress, iron, glucose, EDN1, CSF2, fibroblast growth factor,
platelet-derived growth factor, phorbolesters, follicle-
stimulating hormone, sorbitol, heat shock, oxidative stress, UV
irradiation, and p53/TP53. Many of these stimuli are highly cell-
specific, as is the case, for example for aldosterone, which has
been found to stimulate its expression only in cells derived from
aldosterone-responsive epithelia. Isoform 2 is not induced by
glucocorticoids but by excessive extracellular glucose and by
TGFB1, in cultured cells. {ECO:0000269|PubMed:18753299}.
-!- DOMAIN: Isoform 2 subcellular localization at the cell membrane
and resistance to proteasomal degradation is mediated by the
sequences within the first 120 amino acids.
-!- PTM: Regulated by phosphorylation. Activated by phosphorylation on
Ser-422 by mTORC2, transforming it into a substrate for PDPK1
which phosphorylates it on Thr-256. Phosphorylation on Ser-397 and
Ser-401 are also essential for its activity. Phosphorylation on
Ser-78 by MAPK7 is required for growth factor-induced cell cycle
progression. {ECO:0000269|PubMed:10191262,
ECO:0000269|PubMed:11096081, ECO:0000269|PubMed:11254654,
ECO:0000269|PubMed:18925875, ECO:0000269|PubMed:19068477,
ECO:0000269|PubMed:20338997}.
-!- PTM: Ubiquitinated by NEDD4L; which promotes proteasomal
degradation. Ubiquitinated by SYVN1 at the endoplasmic reticulum;
which promotes rapid proteasomal degradation and maintains a high
turnover rate in resting cells. Isoform 2 shows enhanced
stability. {ECO:0000269|PubMed:15576372}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
protein kinase family. {ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; Y10032; CAA71138.1; -; mRNA.
EMBL; AJ000512; CAA04146.1; -; Genomic_DNA.
EMBL; EU518415; ACD35864.1; -; mRNA.
EMBL; FM205707; CAR58095.1; -; mRNA.
EMBL; FM205708; CAR58096.1; -; mRNA.
EMBL; FM205709; CAR58097.1; -; mRNA.
EMBL; FM205710; CAR58098.1; -; mRNA.
EMBL; AF153609; AAD41091.1; -; mRNA.
EMBL; AK055077; BAG51463.1; -; mRNA.
EMBL; AK298688; BAH12848.1; -; mRNA.
EMBL; AL355881; CAH72579.1; -; Genomic_DNA.
EMBL; AL135839; CAH72579.1; JOINED; Genomic_DNA.
EMBL; Z84486; CAH72579.1; JOINED; Genomic_DNA.
EMBL; AL135839; CAI19718.1; -; Genomic_DNA.
EMBL; AL135839; CAI19719.1; -; Genomic_DNA.
EMBL; AL135839; CAI19720.1; -; Genomic_DNA.
EMBL; AL135839; CAI19721.1; -; Genomic_DNA.
EMBL; AL355881; CAI19721.1; JOINED; Genomic_DNA.
EMBL; Z84486; CAI19721.1; JOINED; Genomic_DNA.
EMBL; Z84486; CAI21678.1; -; Genomic_DNA.
EMBL; AL135839; CAI21678.1; JOINED; Genomic_DNA.
EMBL; AL355881; CAI21678.1; JOINED; Genomic_DNA.
EMBL; CH471051; EAW47991.1; -; Genomic_DNA.
EMBL; CH471051; EAW47992.1; -; Genomic_DNA.
EMBL; CH471051; EAW47993.1; -; Genomic_DNA.
EMBL; BC001263; AAH01263.1; -; mRNA.
CCDS; CCDS47476.1; -. [O00141-2]
CCDS; CCDS47477.1; -. [O00141-5]
CCDS; CCDS47478.1; -. [O00141-3]
CCDS; CCDS5170.1; -. [O00141-1]
RefSeq; NP_001137148.1; NM_001143676.1. [O00141-2]
RefSeq; NP_001137149.1; NM_001143677.1. [O00141-5]
RefSeq; NP_001137150.1; NM_001143678.1. [O00141-3]
RefSeq; NP_001278924.1; NM_001291995.1.
RefSeq; NP_005618.2; NM_005627.3. [O00141-1]
RefSeq; XP_011534373.1; XM_011536071.1. [O00141-2]
UniGene; Hs.510078; -.
PDB; 2R5T; X-ray; 1.90 A; A=60-431.
PDB; 3HDM; X-ray; 2.60 A; A=60-431.
PDB; 3HDN; X-ray; 3.10 A; A=60-431.
PDBsum; 2R5T; -.
PDBsum; 3HDM; -.
PDBsum; 3HDN; -.
ProteinModelPortal; O00141; -.
SMR; O00141; -.
BioGrid; 112344; 61.
DIP; DIP-42464N; -.
ELM; O00141; -.
IntAct; O00141; 13.
MINT; MINT-1338693; -.
STRING; 9606.ENSP00000356832; -.
BindingDB; O00141; -.
ChEMBL; CHEMBL2343; -.
DrugBank; DB03247; Riboflavin Monophosphate.
GuidetoPHARMACOLOGY; 1534; -.
iPTMnet; O00141; -.
PhosphoSitePlus; O00141; -.
BioMuta; SGK1; -.
MaxQB; O00141; -.
PaxDb; O00141; -.
PeptideAtlas; O00141; -.
PRIDE; O00141; -.
DNASU; 6446; -.
Ensembl; ENST00000237305; ENSP00000237305; ENSG00000118515. [O00141-1]
Ensembl; ENST00000367857; ENSP00000356831; ENSG00000118515. [O00141-4]
Ensembl; ENST00000367858; ENSP00000356832; ENSG00000118515. [O00141-2]
Ensembl; ENST00000413996; ENSP00000396242; ENSG00000118515. [O00141-3]
Ensembl; ENST00000528577; ENSP00000434450; ENSG00000118515. [O00141-5]
GeneID; 6446; -.
KEGG; hsa:6446; -.
UCSC; uc003qen.5; human. [O00141-1]
CTD; 6446; -.
DisGeNET; 6446; -.
GeneCards; SGK1; -.
HGNC; HGNC:10810; SGK1.
HPA; CAB022085; -.
HPA; CAB025148; -.
HPA; HPA051251; -.
MIM; 602958; gene.
neXtProt; NX_O00141; -.
OpenTargets; ENSG00000118515; -.
PharmGKB; PA162403013; -.
eggNOG; KOG0598; Eukaryota.
eggNOG; ENOG410XNPH; LUCA.
GeneTree; ENSGT00890000139324; -.
HOVERGEN; HBG108317; -.
InParanoid; O00141; -.
KO; K13302; -.
OMA; EVKEPCN; -.
OrthoDB; EOG091G06FF; -.
PhylomeDB; O00141; -.
TreeFam; TF320906; -.
BRENDA; 2.7.11.1; 2681.
Reactome; R-HSA-2672351; Stimuli-sensing channels.
Reactome; R-HSA-6804757; Regulation of TP53 Degradation.
SignaLink; O00141; -.
SIGNOR; O00141; -.
ChiTaRS; SGK1; human.
EvolutionaryTrace; O00141; -.
GeneWiki; SGK; -.
GenomeRNAi; 6446; -.
PRO; PR:O00141; -.
Proteomes; UP000005640; Chromosome 6.
Bgee; ENSG00000118515; -.
CleanEx; HS_SGK1; -.
ExpressionAtlas; O00141; baseline and differential.
Genevisible; O00141; HS.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
GO; GO:0016607; C:nuclear speck; IDA:HPA.
GO; GO:0005634; C:nucleus; IBA:GO_Central.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0005246; F:calcium channel regulator activity; TAS:UniProtKB.
GO; GO:0017081; F:chloride channel regulator activity; TAS:UniProtKB.
GO; GO:0015459; F:potassium channel regulator activity; TAS:UniProtKB.
GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
GO; GO:0004712; F:protein serine/threonine/tyrosine kinase activity; IDA:MGI.
GO; GO:0017080; F:sodium channel regulator activity; TAS:UniProtKB.
GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
GO; GO:0006974; P:cellular response to DNA damage stimulus; IEA:Ensembl.
GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
GO; GO:0034220; P:ion transmembrane transport; TAS:Reactome.
GO; GO:0007616; P:long-term memory; TAS:UniProtKB.
GO; GO:0048812; P:neuron projection morphogenesis; IBA:GO_Central.
GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
GO; GO:0032411; P:positive regulation of transporter activity; TAS:UniProtKB.
GO; GO:0006468; P:protein phosphorylation; TAS:ProtInc.
GO; GO:0042981; P:regulation of apoptotic process; TAS:UniProtKB.
GO; GO:0008217; P:regulation of blood pressure; TAS:UniProtKB.
GO; GO:0050790; P:regulation of catalytic activity; TAS:UniProtKB.
GO; GO:0001558; P:regulation of cell growth; TAS:UniProtKB.
GO; GO:0030334; P:regulation of cell migration; TAS:UniProtKB.
GO; GO:0042127; P:regulation of cell proliferation; TAS:UniProtKB.
GO; GO:0060453; P:regulation of gastric acid secretion; TAS:UniProtKB.
GO; GO:0051090; P:regulation of sequence-specific DNA binding transcription factor activity; TAS:UniProtKB.
GO; GO:0070294; P:renal sodium ion absorption; TAS:UniProtKB.
GO; GO:0006950; P:response to stress; TAS:ProtInc.
GO; GO:0006814; P:sodium ion transport; TAS:ProtInc.
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; IPR008271; Ser/Thr_kinase_AS.
Pfam; PF00069; Pkinase; 1.
Pfam; PF00433; Pkinase_C; 1.
SMART; SM00133; S_TK_X; 1.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS51285; AGC_KINASE_CTER; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
1: Evidence at protein level;
3D-structure; Alternative promoter usage; Alternative splicing;
Apoptosis; ATP-binding; Cell membrane; Complete proteome; Cytoplasm;
Disulfide bond; Endoplasmic reticulum; Kinase; Membrane;
Mitochondrion; Nucleotide-binding; Nucleus; Phosphoprotein;
Polymorphism; Reference proteome; Serine/threonine-protein kinase;
Stress response; Transferase; Ubl conjugation.
CHAIN 1 431 Serine/threonine-protein kinase Sgk1.
/FTId=PRO_0000086642.
DOMAIN 98 355 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
DOMAIN 356 431 AGC-kinase C-terminal.
NP_BIND 104 112 ATP.
REGION 1 60 Necessary for localization to the
mitochondria.
MOTIF 131 141 Nuclear localization signal.
{ECO:0000269|PubMed:12631736}.
COMPBIAS 131 141 Glu/Lys-rich.
ACT_SITE 222 222 Proton acceptor.
BINDING 127 127 ATP.
MOD_RES 74 74 Phosphoserine.
{ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:19369195}.
MOD_RES 78 78 Phosphoserine; by MAPK7.
{ECO:0000269|PubMed:11254654}.
MOD_RES 256 256 Phosphothreonine; by PDPK1.
{ECO:0000269|PubMed:10191262}.
MOD_RES 369 369 Phosphothreonine; by PKA.
{ECO:0000269|PubMed:11096081}.
MOD_RES 397 397 Phosphoserine.
{ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:19369195,
ECO:0000244|PubMed:20068231,
ECO:0000269|PubMed:19068477}.
MOD_RES 401 401 Phosphoserine.
{ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:19369195,
ECO:0000269|PubMed:19068477}.
MOD_RES 422 422 Phosphoserine.
{ECO:0000269|PubMed:10191262,
ECO:0000269|PubMed:18925875,
ECO:0000269|PubMed:20338997}.
DISULFID 193 193 Interchain (with C-258).
{ECO:0000269|PubMed:17965184}.
DISULFID 258 258 Interchain (with C-193).
{ECO:0000269|PubMed:17965184}.
VAR_SEQ 1 25 MTVKTEAAKGTLTYSRMRGMVAILI -> MVNKDMNGFPVK
KCSAFQFFKKRVRRWIKSPMVSVDKHQSPSLKYTGSSMVHI
PPGEPDFESSLCQTCLGEHAFQRGVLPQENESCSWETQSGC
EVREPCNHANILTKPDPRTFWTNDDP (in isoform
2). {ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:18753299,
ECO:0000303|Ref.4}.
/FTId=VSP_037784.
VAR_SEQ 1 25 MTVKTEAAKGTLTYSRMRGMVAILI -> MGEMQGALARAR
LESLLRPRHKKRAEAQKRSESFLLSGL (in isoform
3). {ECO:0000303|PubMed:14702039,
ECO:0000303|Ref.4}.
/FTId=VSP_037785.
VAR_SEQ 1 25 MTVKTEAAKGTLTYSRMRGMVAILI -> MKPSKRFFISPP
SST (in isoform 4). {ECO:0000303|Ref.4}.
/FTId=VSP_037786.
VAR_SEQ 1 25 MTVKTEAAKGTLTYSRMRGMVAILI -> MSSQSSSLSEAC
SREAYSSHNWALPPASRSNPQPAYPWATRRMKEEAIKPPLK
(in isoform 5). {ECO:0000303|Ref.4}.
/FTId=VSP_037787.
VARIANT 219 219 V -> I (in dbSNP:rs34133418).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041071.
VARIANT 342 342 A -> V (in dbSNP:rs55932330).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041072.
MUTAGEN 127 127 K->M: Abolishes enzymatic activity.
{ECO:0000269|PubMed:11696533,
ECO:0000269|PubMed:12911626,
ECO:0000269|PubMed:15040001}.
MUTAGEN 256 256 T->A: Low activity.
{ECO:0000269|PubMed:10191262}.
MUTAGEN 256 256 T->D: Low activity.
{ECO:0000269|PubMed:10191262}.
MUTAGEN 256 256 T->E: Low activity.
{ECO:0000269|PubMed:10191262}.
MUTAGEN 298 298 Y->A: Abolishes interaction with NEDD4
and NEDD4L.
{ECO:0000269|PubMed:11696533}.
MUTAGEN 422 422 S->A: Low activity.
{ECO:0000269|PubMed:10191262,
ECO:0000269|PubMed:11696533,
ECO:0000269|PubMed:12911626,
ECO:0000269|PubMed:15040001}.
MUTAGEN 422 422 S->D: 10-fold activation.
{ECO:0000269|PubMed:10191262,
ECO:0000269|PubMed:11696533,
ECO:0000269|PubMed:12911626,
ECO:0000269|PubMed:15040001}.
CONFLICT 62 62 Q -> E (in Ref. 4; CAR58097).
{ECO:0000305}.
CONFLICT 152 152 K -> R (in Ref. 4; CAR58096).
{ECO:0000305}.
CONFLICT 196 196 E -> G (in Ref. 4; CAR58095).
{ECO:0000305}.
CONFLICT 228 228 I -> V (in Ref. 6; BAH12848).
{ECO:0000305}.
CONFLICT 371 371 P -> R (in Ref. 4; CAR58097).
{ECO:0000305}.
CONFLICT 381 381 D -> E (in Ref. 1; CAA71138 and 2;
CAA04146). {ECO:0000305}.
HELIX 95 97 {ECO:0000244|PDB:2R5T}.
STRAND 98 105 {ECO:0000244|PDB:2R5T}.
STRAND 111 117 {ECO:0000244|PDB:2R5T}.
TURN 118 120 {ECO:0000244|PDB:2R5T}.
STRAND 123 130 {ECO:0000244|PDB:2R5T}.
HELIX 131 133 {ECO:0000244|PDB:2R5T}.
STRAND 162 167 {ECO:0000244|PDB:2R5T}.
STRAND 169 177 {ECO:0000244|PDB:2R5T}.
HELIX 184 191 {ECO:0000244|PDB:2R5T}.
HELIX 196 215 {ECO:0000244|PDB:2R5T}.
HELIX 225 227 {ECO:0000244|PDB:2R5T}.
STRAND 228 230 {ECO:0000244|PDB:2R5T}.
STRAND 232 234 {ECO:0000244|PDB:3HDN}.
STRAND 236 238 {ECO:0000244|PDB:2R5T}.
HELIX 245 247 {ECO:0000244|PDB:2R5T}.
STRAND 256 258 {ECO:0000244|PDB:2R5T}.
HELIX 266 269 {ECO:0000244|PDB:2R5T}.
HELIX 277 292 {ECO:0000244|PDB:2R5T}.
HELIX 302 311 {ECO:0000244|PDB:2R5T}.
STRAND 318 320 {ECO:0000244|PDB:2R5T}.
HELIX 322 331 {ECO:0000244|PDB:2R5T}.
HELIX 336 338 {ECO:0000244|PDB:2R5T}.
TURN 340 345 {ECO:0000244|PDB:2R5T}.
HELIX 346 350 {ECO:0000244|PDB:2R5T}.
HELIX 353 355 {ECO:0000244|PDB:2R5T}.
HELIX 360 364 {ECO:0000244|PDB:2R5T}.
SEQUENCE 431 AA; 48942 MW; F3697C63AB1F499D CRC64;
MTVKTEAAKG TLTYSRMRGM VAILIAFMKQ RRMGLNDFIQ KIANNSYACK HPEVQSILKI
SQPQEPELMN ANPSPPPSPS QQINLGPSSN PHAKPSDFHF LKVIGKGSFG KVLLARHKAE
EVFYAVKVLQ KKAILKKKEE KHIMSERNVL LKNVKHPFLV GLHFSFQTAD KLYFVLDYIN
GGELFYHLQR ERCFLEPRAR FYAAEIASAL GYLHSLNIVY RDLKPENILL DSQGHIVLTD
FGLCKENIEH NSTTSTFCGT PEYLAPEVLH KQPYDRTVDW WCLGAVLYEM LYGLPPFYSR
NTAEMYDNIL NKPLQLKPNI TNSARHLLEG LLQKDRTKRL GAKDDFMEIK SHVFFSLINW
DDLINKKITP PFNPNVSGPN DLRHFDPEFT EEPVPNSIGK SPDSVLVTAS VKEAAEAFLG
FSYAPPTDSF L


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