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UniProtKB/Swiss-Prot entry O00141


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name SGK1_HUMAN
Primary accession number O00141
Secondary accession numbers Q5TCN3 Q9UN56
Integrated into Swiss-Prot on December 15, 1998
Sequence was last modified on March 7, 2006 (Sequence version 2)
Annotations were last modified on    June 16, 2009 (Entry version 92)
Name and origin of the protein
Protein name Serine/threonine-protein kinase Sgk1
Synonyms EC 2.7.11.1
Serum/glucocorticoid-regulated kinase 1
Gene name
Name: SGK1
Synonyms: SGK
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
DOI=10.1073/pnas.94.9.4440; PubMed=9114008 [NCBI, ExPASy, EBI, Israel, Japan]
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].
DOI=10.1006/geno.1998.5258; PubMed=9722955 [NCBI, ExPASy, EBI, Israel, Japan]
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 [LARGE SCALE MRNA].
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.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/nature02055; PubMed=14574404 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Cervix;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
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]
TISSUE SPECIFICITY.
DOI=10.1042/0264-6021:3440189; PubMed=10548550 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[7]
PHOSPHORYLATION AT THR-256 AND SER-422, AND MUTAGENESIS OF THR-256 AND SER-422.
TISSUE=Brain;
DOI=10.1042/0264-6021:3390319; PubMed=10191262 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[8]
CHARACTERIZATION.
DOI=10.1073/pnas.97.14.8157; PubMed=10884438 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[9]
FUNCTION.
DOI=10.1128/MCB.21.3.952-965.2001; PubMed=11154281 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[10]
INTERACTION WITH NEDD4 AND NEDD4L, MUTAGENESIS OF LYS-127; TYR-298 AND SER-422, AND FUNCTION.
DOI=10.1074/jbc.C100623200; PubMed=11696533 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[11]
FUNCTION.
DOI=10.1007/s00424-002-0873-2; PubMed=12397388 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[12]
FUNCTION, AND MUTAGENESIS OF LYS-127 AND SER-422.
PubMed=12911626 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[13]
NUCLEAR LOCALIZATION SIGNAL.
DOI=10.1091/mbc.E02-03-0170; PubMed=12631736 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[14]
FUNCTION, AND MUTAGENESIS OF LYS-127 AND SER-422.
DOI=10.1002/jcp.10430; PubMed=15040001 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[15]
UBIQUITINATION.
DOI=10.1074/jbc.M411053200; PubMed=15576372 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-74; SER-78; SER-397 AND SER-401, AND MASS SPECTROMETRY.
DOI=10.1016/j.molcel.2008.07.007; PubMed=18691976 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[17]
VARIANTS [LARGE SCALE ANALYSIS] ILE-219 AND VAL-342.
DOI=10.1038/nature05610; PubMed=17344846 [NCBI, ExPASy, EBI, Israel, Japan]
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).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
Y10032; CAA71138.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ000512; CAA04146.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF153609; AAD41091.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL135839; CAI19719.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC001263; AAH01263.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00297590; -.
RefSeq NP_005618.2; -.
UniGene Hs.510078
3D structure databases
PDB
2R5T; X-ray; 1.90 A; A=60-431.[ExPASy / RCSB / EBI]
PDBsum 2R5T; -.
ModBase O00141.
Protein-protein interaction databases
IntAct O00141; 47.
PTM databases
PhosphoSite O00141; -.
Enzyme and pathway databases
BRENDA 2.7.11.1; 247.
Pathway_Interaction_DB pi3kcipathway; Class I PI3K signaling events.
foxopathway; FoxO family signaling.
insulin_pathway; Insulin Pathway.
Organism-specific databases
GeneCards GC06M134533; -.
H-InvDB HIX0006234; -.
HGNC HGNC:10810; SGK1.
GenAtlas SGK1.
MIM 602958; gene. [NCBI / EBI]
PharmGKB PA35721; -.
Gene expression databases
ArrayExpress O00141; -.
Bgee O00141; -.
CleanEx HS_SGK1; -.
GermOnline ENSG00000118515; Homo sapiens.
Ontologies
GO
GO:0005783; Cellular component: endoplasmic reticulum (inferred from electronic annotation from UniProtKB-SubCell).
GO:0005634; Cellular component: nucleus (inferred from electronic annotation from UniProtKB-SubCell).
GO:0005524; Molecular function: ATP binding (inferred from electronic annotation from UniProtKB-KW).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0004674; Molecular function: protein serine/threonine kinase activity (traceable author statement from ProtInc).
GO:0006915; Biological process: apoptosis (inferred from electronic annotation from UniProtKB-KW).
GO:0006468; Biological process: protein amino acid phosphorylation (traceable author statement from ProtInc).
GO:0006950; Biological process: response to stress (traceable author statement from ProtInc).
GO:0006814; Biological process: sodium ion transport (traceable author statement from ProtInc).
QuickGo view.
Family and domain databases
InterPro IPR000961; AGC-kinase_C.
IPR017892; Pkinase_C.
IPR000719; Prot_kinase_core.
IPR017441; Protein_kinase_ATP_BS.
IPR017442; Se/Thr_pkinase-rel.
IPR008271; Ser_thr_pkin_AS.
IPR002290; Ser_thr_pkinase.
Graphical view of domain structure.
Pfam PF00069; Pkinase; 1.
PF00433; Pkinase_C; 1.
Pfam graphical view of domain structure.
ProDom PD000001; Prot_kinase; 1.
[Domain structure / List of seq. sharing at least 1 domain]
SMART SM00133; S_TK_X; 1.
SM00220; S_TKc; 1.
SMART graphical view of domain structure.
PROSITE PS51285; AGC_KINASE_CTER; 1.
PS00107; PROTEIN_KINASE_ATP; 1.
PS50011; PROTEIN_KINASE_DOM; 1.
PS00108; PROTEIN_KINASE_ST; 1.
PROSITE graphical view of domain structure (profiles).
Proteomic databases
PRIDE O00141; -.
Genome annotation databases
Ensembl ENSG00000118515; Homo sapiens. [Contig view]
GeneID 6446; -.
KEGG hsa:6446; -.
Phylogenomic databases
HOVERGEN O00141; -.
Other
NextBio 25053; -.
SOURCE SGK1; Homo sapiens.
ProtoNet O00141.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Apoptosis; ATP-binding; Cytoplasm; Endoplasmic reticulum; Kinase; Nucleotide-binding; Nucleus; Phosphoprotein; Polymorphism; Serine/threonine-protein kinase; Transferase; Ubl conjugation.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   431  431     Serine/threonine-protein kinase Sgk1. PRO_0000086642
DOMAIN   98   355  258     Protein kinase. 
DOMAIN   356   431  76     AGC-kinase C-terminal. 
NP_BIND   104   112  9     ATP (By similarity). 
MOTIF   131   141  11     Nuclear localization signal. 
COMPBIAS   131   141  11     Glu/Lys-rich. 
ACT_SITE   222   222        Proton acceptor (By similarity). 
BINDING   127   127        ATP (By similarity). 
MOD_RES   74    74        Phosphoserine. 
MOD_RES   78    78        Phosphoserine. 
MOD_RES   256   256        Phosphothreonine; by PDPK1. 
MOD_RES   397   397        Phosphoserine. 
MOD_RES   401   401        Phosphoserine. 
MOD_RES   422   422        Phosphoserine. 
VARIANT   219   219  1     V -> I. VAR_041071 
VARIANT   342   342  1     A -> V. VAR_041072 
MUTAGEN   127   127        K->M: Abolishes enzymatic activity. 
MUTAGEN   256   256        T->A: Low activity. 
MUTAGEN   256   256        T->D: Low activity. 
MUTAGEN   256   256        T->E: Low activity. 
MUTAGEN   298   298        Y->A: Abolishes interaction with NEDD4 and NEDD4L. 
MUTAGEN   422   422        S->A: Low activity. 
MUTAGEN   422   422        S->D: 10-fold activation. 
CONFLICT   381   381        D -> E (in Ref. 1 and 2). 
Sequence information
Length: 431 AA [This is the length of the unprocessed precursor] Molecular weight: 48942 Da [This is the MW of the unprocessed precursor] CRC64: F3697C63AB1F499D [This is a checksum on the sequence]
        10         20         30         40         50         60 
MTVKTEAAKG TLTYSRMRGM VAILIAFMKQ RRMGLNDFIQ KIANNSYACK HPEVQSILKI 

        70         80         90        100        110        120 
SQPQEPELMN ANPSPPPSPS QQINLGPSSN PHAKPSDFHF LKVIGKGSFG KVLLARHKAE 

       130        140        150        160        170        180 
EVFYAVKVLQ KKAILKKKEE KHIMSERNVL LKNVKHPFLV GLHFSFQTAD KLYFVLDYIN 

       190        200        210        220        230        240 
GGELFYHLQR ERCFLEPRAR FYAAEIASAL GYLHSLNIVY RDLKPENILL DSQGHIVLTD 

       250        260        270        280        290        300 
FGLCKENIEH NSTTSTFCGT PEYLAPEVLH KQPYDRTVDW WCLGAVLYEM LYGLPPFYSR 

       310        320        330        340        350        360 
NTAEMYDNIL NKPLQLKPNI TNSARHLLEG LLQKDRTKRL GAKDDFMEIK SHVFFSLINW 

       370        380        390        400        410        420 
DDLINKKITP PFNPNVSGPN DLRHFDPEFT EEPVPNSIGK SPDSVLVTAS VKEAAEAFLG 

       430 
FSYAPPTDSF L 

O00141 in FASTA format

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