SGK1_MOUSE
ID SGK1_MOUSE Reviewed; 431 AA.
AC Q9WVC6; Q3TJN4; Q3UKD0; Q3UKF2; Q3V1V1; Q6NS85;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=Serine/threonine-protein kinase Sgk1;
DE EC=2.7.11.1;
DE AltName: Full=Serum/glucocorticoid-regulated kinase 1;
GN Name=Sgk1; Synonyms=Sgk;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=10358046; DOI=10.1074/jbc.274.24.16973;
RA Naray-Fejes-Toth A., Canessa C., Cleaveland E.S., Aldrich G.,
RA Fejes-Toth G.;
RT "sgk is an aldosterone-induced kinase in the renal collecting duct. Effects
RT on epithelial Na+ channels.";
RL J. Biol. Chem. 274:16973-16978(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Placenta;
RX PubMed=10751222; DOI=10.1152/ajprenal.2000.278.4.f613;
RA Shigaev A., Asher C., Latter H., Garty H., Reuveny E.;
RT "Regulation of sgk by aldosterone and its effects on the epithelial Na(+)
RT channel.";
RL Am. J. Physiol. 278:F613-F619(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC STRAIN=C57BL/6J; TISSUE=Brain, and Placenta;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J, and FVB/N; TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP REGULATION BY P53.
RC TISSUE=Mammary epithelium;
RX PubMed=8647846; DOI=10.1074/jbc.271.21.12414;
RA Maiyar A.C., Huang A.J., Phu P.T., Cha H.H., Firestone G.L.;
RT "p53 stimulates promoter activity of the sgk. serum/glucocorticoid-
RT inducible serine/threonine protein kinase gene in rodent mammary epithelial
RT cells.";
RL J. Biol. Chem. 271:12414-12422(1996).
RN [7]
RP FUNCTION.
RX PubMed=12488318; DOI=10.1074/jbc.m211649200;
RA Leong M.L.L., Maiyar A.C., Kim B., O'Keeffe B.A., Firestone G.L.;
RT "Expression of the serum- and glucocorticoid-inducible protein kinase, Sgk,
RT is a cell survival response to multiple types of environmental stress
RT stimuli in mammary epithelial cells.";
RL J. Biol. Chem. 278:5871-5882(2003).
RN [8]
RP FUNCTION IN PHOSPHORYLATION OF KCNJ1/ROMK1.
RX PubMed=12684516; DOI=10.1074/jbc.m212301200;
RA Yoo D., Kim B.Y., Campo C., Nance L., King A., Maouyo D., Welling P.A.;
RT "Cell surface expression of the ROMK (Kir 1.1) channel is regulated by the
RT aldosterone-induced kinase, SGK-1, and protein kinase A.";
RL J. Biol. Chem. 278:23066-23075(2003).
RN [9]
RP FUNCTION IN REGULATION OF GRIK2/GLUR6.
RX PubMed=15774535; DOI=10.1113/jphysiol.2004.079624;
RA Strutz-Seebohm N., Seebohm G., Shumilina E., Mack A.F., Wagner H.J.,
RA Lampert A., Grahammer F., Henke G., Just L., Skutella T., Hollmann M.,
RA Lang F.;
RT "Glucocorticoid adrenal steroids and glucocorticoid-inducible kinase
RT isoforms in the regulation of GluR6 expression.";
RL J. Physiol. (Lond.) 565:391-401(2005).
RN [10]
RP FUNCTION IN PHOSPHORYLATION OF MDM2.
RX PubMed=19756449; DOI=10.1007/s00109-009-0525-5;
RA Amato R., D'Antona L., Porciatti G., Agosti V., Menniti M., Rinaldo C.,
RA Costa N., Bellacchio E., Mattarocci S., Fuiano G., Soddu S., Paggi M.G.,
RA Lang F., Perrotti N.;
RT "Sgk1 activates MDM2-dependent p53 degradation and affects cell
RT proliferation, survival, and differentiation.";
RL J. Mol. Med. 87:1221-1239(2009).
RN [11]
RP FUNCTION.
RX PubMed=20568246; DOI=10.1002/dvdy.22345;
RA Catela C., Kratsios P., Hede M., Lang F., Rosenthal N.;
RT "Serum and glucocorticoid-inducible kinase 1 (SGK1) is necessary for
RT vascular remodeling during angiogenesis.";
RL Dev. Dyn. 239:2149-2160(2010).
RN [12]
RP ACTIVITY REGULATION.
RX PubMed=20525693; DOI=10.1074/jbc.m110.103432;
RA Heise C.J., Xu B.E., Deaton S.L., Cha S.K., Cheng C.J., Earnest S.,
RA Sengupta S., Juang Y.C., Stippec S., Xu Y., Zhao Y., Huang C.L., Cobb M.H.;
RT "Serum and glucocorticoid-induced kinase (SGK) 1 and the epithelial sodium
RT channel are regulated by multiple with no lysine (WNK) family members.";
RL J. Biol. Chem. 285:25161-25167(2010).
RN [13]
RP FUNCTION IN PHOSPHORYLATION OF FOXO1.
RX PubMed=19965929; DOI=10.1210/me.2009-0265;
RA Di Pietro N., Panel V., Hayes S., Bagattin A., Meruvu S., Pandolfi A.,
RA Hugendubler L., Fejes-Toth G., Naray-Fejes-Toth A., Mueller E.;
RT "Serum- and glucocorticoid-inducible kinase 1 (SGK1) regulates adipocyte
RT differentiation via forkhead box O1.";
RL Mol. Endocrinol. 24:370-380(2010).
RN [14]
RP FUNCTION.
RX PubMed=21385992; DOI=10.1096/fj.10-178210;
RA Eylenstein A., Gehring E.M., Heise N., Shumilina E., Schmidt S., Szteyn K.,
RA Muenzer P., Nurbaeva M.K., Eichenmueller M., Tyan L., Regel I., Foeller M.,
RA Kuhl D., Soboloff J., Penner R., Lang F.;
RT "Stimulation of Ca2+-channel Orai1/STIM1 by serum- and glucocorticoid-
RT inducible kinase 1 (SGK1).";
RL FASEB J. 25:2012-2021(2011).
RN [15]
RP FUNCTION, AND INTERACTION WITH MAPKAP1/SIN1.
RX PubMed=21757730; DOI=10.1074/jbc.m111.257592;
RA Lu M., Wang J., Ives H.E., Pearce D.;
RT "mSIN1 protein mediates SGK1 protein interaction with mTORC2 protein
RT complex and is required for selective activation of the epithelial sodium
RT channel.";
RL J. Biol. Chem. 286:30647-30654(2011).
RN [16]
RP FUNCTION IN PHOSPHORYLATION OF FBXW7, AND INTERACTION WITH NOTCH1 AND
RP FBXW7.
RX PubMed=21147854; DOI=10.1242/jcs.073924;
RA Mo J.S., Ann E.J., Yoon J.H., Jung J., Choi Y.H., Kim H.Y., Ahn J.S.,
RA Kim S.M., Kim M.Y., Hong J.A., Seo M.S., Lang F., Choi E.J., Park H.S.;
RT "Serum- and glucocorticoid-inducible kinase 1 (SGK1) controls Notch1
RT signaling by downregulation of protein stability through Fbw7 ubiquitin
RT ligase.";
RL J. Cell Sci. 124:100-112(2011).
RN [17]
RP FUNCTION IN REGULATION OF SLC9A3/NHE3, AND SUBCELLULAR LOCATION.
RX PubMed=21865597; DOI=10.1091/mbc.e11-04-0328;
RA He P., Lee S.J., Lin S., Seidler U., Lang F., Fejes-Toth G.,
RA Naray-Fejes-Toth A., Yun C.C.;
RT "Serum- and glucocorticoid-induced kinase 3 in recycling endosomes mediates
RT acute activation of Na+/H+ exchanger NHE3 by glucocorticoids.";
RL Mol. Biol. Cell 22:3812-3825(2011).
CC -!- FUNCTION: Serine/threonine-protein kinase which is involved in the
CC regulation of a wide variety of ion channels, membrane transporters,
CC cellular enzymes, transcription factors, neuronal excitability, cell
CC growth, proliferation, survival, migration and apoptosis. Plays an
CC important role in cellular stress response. Contributes to regulation
CC of renal Na(+) retention, renal K(+) elimination, salt appetite,
CC gastric acid secretion, intestinal Na(+)/H(+) exchange and nutrient
CC transport, insulin-dependent salt sensitivity of blood pressure, salt
CC sensitivity of peripheral glucose uptake, cardiac repolarization and
CC memory consolidation. Up-regulates Na(+) channels: SCNN1A/ENAC, SCN5A
CC and ASIC1/ACCN2, K(+) channels: KCNJ1/ROMK1, KCNA1-5, KCNQ1-5 and
CC KCNE1, epithelial Ca(2+) channels: TRPV5 and TRPV6, chloride channels:
CC BSND, CLCN2 and CFTR, glutamate transporters: SLC1A3/EAAT1, SLC1A2
CC /EAAT2, SLC1A1/EAAT3, SLC1A6/EAAT4 and SLC1A7/EAAT5, amino acid
CC transporters: SLC1A5/ASCT2, SLC38A1/SN1 and SLC6A19, creatine
CC transporter: SLC6A8, Na(+)/dicarboxylate cotransporter: SLC13A2/NADC1,
CC Na(+)-dependent phosphate cotransporter: SLC34A2/NAPI-2B, glutamate
CC receptor: GRIK2/GLUR6. Up-regulates carriers: SLC9A3/NHE3,
CC SLC12A1/NKCC2, SLC12A3/NCC, SLC5A3/SMIT, SLC2A1/GLUT1, SLC5A1/SGLT1 and
CC SLC15A2/PEPT2. Regulates enzymes: GSK3A/B, PMM2 and Na(+)/K(+) ATPase,
CC and transcription factors: CTNNB1 and nuclear factor NF-kappa-B.
CC Stimulates sodium transport into epithelial cells by enhancing the
CC stability and expression of SCNN1A/ENAC. This is achieved by
CC phosphorylating the NEDD4L ubiquitin E3 ligase, promoting its
CC interaction with 14-3-3 proteins, thereby preventing it from binding to
CC SCNN1A/ENAC and targeting it for degradation. Regulates store-operated
CC Ca(+2) entry (SOCE) by stimulating ORAI1 and STIM1. Regulates
CC KCNJ1/ROMK1 directly via its phosphorylation or indirectly via
CC increased interaction with SLC9A3R2/NHERF2. Phosphorylates MDM2 and
CC activates MDM2-dependent ubiquitination of p53/TP53. Phosphorylates
CC MAPT/TAU and mediates microtubule depolymerization and neurite
CC formation in hippocampal neurons. Phosphorylates SLC2A4/GLUT4 and up-
CC regulates its activity. Phosphorylates APBB1/FE65 and promotes its
CC localization to the nucleus. Phosphorylates MAPK1/ERK2 and activates it
CC by enhancing its interaction with MAP2K1/MEK1 and MAP2K2/MEK2.
CC Phosphorylates FBXW7 and plays an inhibitory role in the NOTCH1
CC signaling. Phosphorylates FOXO1 resulting in its relocalization from
CC the nucleus to the cytoplasm. Phosphorylates FOXO3, promoting its exit
CC from the nucleus and interference with FOXO3-dependent transcription.
CC Phosphorylates BRAF and MAP3K3/MEKK3 and inhibits their activity.
CC Phosphorylates SLC9A3/NHE3 in response to dexamethasone, resulting in
CC its activation and increased localization at the cell membrane.
CC Phosphorylates CREB1. Necessary for vascular remodeling during
CC angiogenesis. {ECO:0000269|PubMed:12488318,
CC ECO:0000269|PubMed:12684516, ECO:0000269|PubMed:15774535,
CC ECO:0000269|PubMed:19756449, ECO:0000269|PubMed:19965929,
CC ECO:0000269|PubMed:20568246, ECO:0000269|PubMed:21147854,
CC ECO:0000269|PubMed:21385992, ECO:0000269|PubMed:21757730,
CC ECO:0000269|PubMed:21865597}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1;
CC -!- ACTIVITY REGULATION: Two specific sites, one in the kinase domain (Thr-
CC 256) and the other in the C-terminal regulatory region (Ser-422), need
CC to be phosphorylated for its full activation. Phosphorylation at Ser-
CC 397 and Ser-401 are also essential for its activity. Activated by WNK1,
CC WNK2, WNK3 and WNK4. {ECO:0000269|PubMed:20525693}.
CC -!- SUBUNIT: Homodimer; disulfide-linked. Interacts with MAPK3/ERK1,
CC MAPK1/ERK2, MAP2K1/MEK1, MAP2K2/MEK2, NEDD4, NEDD4L, MAPT/TAU, MAPK7,
CC CREB1, SLC9A3R2/NHERF2 and KCNJ1/ROMK1 (By similarity). Forms a
CC trimeric complex with FBXW7 and NOTCH1 Associates with the mammalian
CC target of rapamycin complex 2 (mTORC2) via an interaction with
CC MAPKAP1/SIN1. {ECO:0000250, ECO:0000269|PubMed:21147854,
CC ECO:0000269|PubMed:21757730}.
CC -!- INTERACTION:
CC Q9WVC6; Q99N57: Raf1; NbExp=2; IntAct=EBI-15591730, EBI-397757;
CC Q9WVC6; Q9Z2S7-3: Tsc22d3; NbExp=2; IntAct=EBI-15591730, EBI-15771036;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC Endoplasmic reticulum membrane {ECO:0000250}. Cell membrane
CC {ECO:0000250}. Mitochondrion {ECO:0000250}. Note=The subcellular
CC localization is controlled by the cell cycle, as well as by exposure to
CC specific hormones and environmental stress stimuli. In proliferating
CC cells, it shuttles between the nucleus and cytoplasm in synchrony with
CC the cell cycle, and in serum/growth factor-stimulated cells it resides
CC in the nucleus. In contrast, after exposure to environmental stress or
CC treatment with glucocorticoids, it is detected in the cytoplasm and
CC with certain stress conditions is associated with the mitochondria. In
CC osmoregulation through the epithelial sodium channel, it can be
CC localized to the cytoplasmic surface of the cell membrane. Nuclear,
CC upon phosphorylation (By similarity). {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9WVC6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9WVC6-2; Sequence=VSP_037788;
CC Name=3;
CC IsoId=Q9WVC6-3; Sequence=VSP_037789;
CC -!- INDUCTION: Up-regulated by tumor suppressor p53 in mammary epithelial
CC tumor cells.
CC -!- PTM: Regulated by phosphorylation. Activated by phosphorylation on Ser-
CC 422 by mTORC2, transforming it into a substrate for PDPK1 which
CC phosphorylates it on Thr-256. Phosphorylation on Ser-397 and Ser-401
CC are also essential for its activity. Phosphorylation on Ser-78 by MAPK7
CC is required for growth factor-induced cell cycle progression (By
CC similarity). {ECO:0000250}.
CC -!- PTM: Ubiquitinated by NEDD4L; which promotes proteasomal degradation.
CC Ubiquitinated by SYVN1 at the endoplasmic reticulum; which promotes
CC rapid proteasomal degradation and maintains a high turnover rate in
CC resting cells (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC protein kinase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH70401.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF139638; AAD43302.1; -; mRNA.
DR EMBL; AF205855; AAF19429.1; -; mRNA.
DR EMBL; AK132234; BAE21048.1; -; mRNA.
DR EMBL; AK146037; BAE26849.1; -; mRNA.
DR EMBL; AK146062; BAE26871.1; -; mRNA.
DR EMBL; AK159131; BAE34843.1; -; mRNA.
DR EMBL; AK167364; BAE39461.1; -; mRNA.
DR EMBL; CH466562; EDL03408.1; -; Genomic_DNA.
DR EMBL; BC005720; AAH05720.1; -; mRNA.
DR EMBL; BC070401; AAH70401.1; ALT_INIT; mRNA.
DR CCDS; CCDS23726.1; -. [Q9WVC6-1]
DR CCDS; CCDS48515.1; -. [Q9WVC6-2]
DR CCDS; CCDS48517.1; -. [Q9WVC6-3]
DR RefSeq; NP_001155317.2; NM_001161845.2. [Q9WVC6-2]
DR RefSeq; NP_001155319.1; NM_001161847.2.
DR RefSeq; NP_001155320.1; NM_001161848.2.
DR RefSeq; NP_001155321.1; NM_001161849.2.
DR RefSeq; NP_001155322.1; NM_001161850.2. [Q9WVC6-3]
DR RefSeq; NP_035491.1; NM_011361.3. [Q9WVC6-1]
DR AlphaFoldDB; Q9WVC6; -.
DR SMR; Q9WVC6; -.
DR BioGRID; 203197; 6.
DR DIP; DIP-48845N; -.
DR IntAct; Q9WVC6; 5.
DR STRING; 10090.ENSMUSP00000114074; -.
DR BindingDB; Q9WVC6; -.
DR ChEMBL; CHEMBL3988610; -.
DR iPTMnet; Q9WVC6; -.
DR PhosphoSitePlus; Q9WVC6; -.
DR MaxQB; Q9WVC6; -.
DR PaxDb; Q9WVC6; -.
DR PRIDE; Q9WVC6; -.
DR ProteomicsDB; 261009; -. [Q9WVC6-1]
DR ProteomicsDB; 261010; -. [Q9WVC6-2]
DR ProteomicsDB; 261011; -. [Q9WVC6-3]
DR Antibodypedia; 19734; 919 antibodies from 47 providers.
DR DNASU; 20393; -.
DR Ensembl; ENSMUST00000020145; ENSMUSP00000020145; ENSMUSG00000019970. [Q9WVC6-1]
DR Ensembl; ENSMUST00000092673; ENSMUSP00000090343; ENSMUSG00000019970. [Q9WVC6-3]
DR Ensembl; ENSMUST00000120509; ENSMUSP00000114074; ENSMUSG00000019970. [Q9WVC6-2]
DR GeneID; 20393; -.
DR KEGG; mmu:20393; -.
DR UCSC; uc007eov.2; mouse. [Q9WVC6-2]
DR UCSC; uc007eow.2; mouse. [Q9WVC6-3]
DR UCSC; uc007eox.2; mouse. [Q9WVC6-1]
DR CTD; 6446; -.
DR MGI; MGI:1340062; Sgk1.
DR VEuPathDB; HostDB:ENSMUSG00000019970; -.
DR eggNOG; KOG0598; Eukaryota.
DR GeneTree; ENSGT00940000155726; -.
DR InParanoid; Q9WVC6; -.
DR OMA; HICITDF; -.
DR OrthoDB; 614710at2759; -.
DR PhylomeDB; Q9WVC6; -.
DR TreeFam; TF320906; -.
DR BRENDA; 2.7.11.1; 3474.
DR Reactome; R-MMU-2672351; Stimuli-sensing channels.
DR Reactome; R-MMU-6804757; Regulation of TP53 Degradation.
DR Reactome; R-MMU-9031628; NGF-stimulated transcription.
DR BioGRID-ORCS; 20393; 2 hits in 74 CRISPR screens.
DR ChiTaRS; Sgk1; mouse.
DR PRO; PR:Q9WVC6; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q9WVC6; protein.
DR Bgee; ENSMUSG00000019970; Expressed in seminal vesicle and 294 other tissues.
DR ExpressionAtlas; Q9WVC6; baseline and differential.
DR Genevisible; Q9WVC6; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0043005; C:neuron projection; ISO:MGI.
DR GO; GO:0016607; C:nuclear speck; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0043423; F:3-phosphoinositide-dependent protein kinase binding; ISO:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0015459; F:potassium channel regulator activity; IBA:GO_Central.
DR GO; GO:0004672; F:protein kinase activity; IDA:MGI.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; ISO:MGI.
DR GO; GO:0004712; F:protein serine/threonine/tyrosine kinase activity; ISO:MGI.
DR GO; GO:0048156; F:tau protein binding; ISO:MGI.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:1904045; P:cellular response to aldosterone; IDA:MGI.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IDA:MGI.
DR GO; GO:0032869; P:cellular response to insulin stimulus; ISO:MGI.
DR GO; GO:0006883; P:cellular sodium ion homeostasis; ISO:MGI.
DR GO; GO:0043402; P:glucocorticoid mediated signaling pathway; ISO:MGI.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0007616; P:long-term memory; ISO:MGI.
DR GO; GO:0007019; P:microtubule depolymerization; ISO:MGI.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISO:MGI.
DR GO; GO:0031115; P:negative regulation of microtubule polymerization; ISO:MGI.
DR GO; GO:0048812; P:neuron projection morphogenesis; ISO:MGI.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; ISO:MGI.
DR GO; GO:0030307; P:positive regulation of cell growth; ISO:MGI.
DR GO; GO:0050775; P:positive regulation of dendrite morphogenesis; ISO:MGI.
DR GO; GO:0010765; P:positive regulation of sodium ion transport; ISO:MGI.
DR GO; GO:0006468; P:protein phosphorylation; IDA:MGI.
DR GO; GO:0051726; P:regulation of cell cycle; ISO:MGI.
DR GO; GO:0032880; P:regulation of protein localization; ISO:MGI.
DR GO; GO:0008542; P:visual learning; ISO:MGI.
DR InterPro; IPR000961; AGC-kinase_C.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR017892; Pkinase_C.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00433; Pkinase_C; 1.
DR SMART; SM00133; S_TK_X; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Apoptosis; ATP-binding; Cell membrane; Cytoplasm;
KW Disulfide bond; Endoplasmic reticulum; Kinase; Membrane; Mitochondrion;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Stress response; Transferase;
KW Ubl conjugation.
FT CHAIN 1..431
FT /note="Serine/threonine-protein kinase Sgk1"
FT /id="PRO_0000086643"
FT DOMAIN 98..355
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 356..431
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00618"
FT REGION 1..60
FT /note="Necessary for localization to the mitochondria"
FT /evidence="ECO:0000250"
FT REGION 65..92
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 131..141
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250"
FT ACT_SITE 222
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 104..112
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 127
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 74
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O00141"
FT MOD_RES 78
FT /note="Phosphoserine; by MAPK7"
FT /evidence="ECO:0000250|UniProtKB:O00141"
FT MOD_RES 256
FT /note="Phosphothreonine; by PDPK1"
FT /evidence="ECO:0000250|UniProtKB:O00141"
FT MOD_RES 369
FT /note="Phosphothreonine; by PKA"
FT /evidence="ECO:0000250|UniProtKB:O00141"
FT MOD_RES 397
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O00141"
FT MOD_RES 401
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O00141"
FT MOD_RES 422
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O00141"
FT DISULFID 193
FT /note="Interchain (with C-258)"
FT /evidence="ECO:0000250"
FT DISULFID 258
FT /note="Interchain (with C-193)"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..25
FT /note="MTVKAEAARSTLTYSRMRGMVAILI -> MVNKDMNGFPVKKCSAFQFFKKR
FT VRRWIKSPMVSVDKHQSPNLKYTGPAGVHLPPGESDFEAMCQSCLGDHAFQRGMLPPEE
FT SCSWEIQPGCEVKEQCNHANILTKPDPRTFWTNDDA (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_037788"
FT VAR_SEQ 1..25
FT /note="MTVKAEAARSTLTYSRMRGMVAILI -> MGEMQGALARARLESLLRPRHKK
FT RAEAQKRSESVLLSGL (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_037789"
FT CONFLICT 87
FT /note="P -> L (in Ref. 3; BAE26849)"
FT /evidence="ECO:0000305"
FT CONFLICT 347
FT /note="M -> V (in Ref. 3; BAE26849/BAE26871)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 431 AA; 48928 MW; 6DF5B8464A4C2754 CRC64;
MTVKAEAARS TLTYSRMRGM VAILIAFMKQ RRMGLNDFIQ KIASNTYACK HAEVQSILKM
SHPQEPELMN ANPSPPPSPS QQINLGPSSN PHAKPSDFHF LKVIGKGSFG KVLLARHKAE
EVFYAVKVLQ KKAILKKKEE KHIMSERNVL LKNVKHPFLV GLHFSFQTAD KLYFVLDYIN
GGELFYHLQR ERCFLEPRAR FYAAEIASAL GYLHSLNIVY RDLKPENILL DSQGHIVLTD
FGLCKENIEH NGTTSTFCGT PEYLAPEVLH KQPYDRTVDW WCLGAVLYEM LYGLPPFYSR
NTAEMYDNIL NKPLQLKPNI TNSARHLLEG LLQKDRTKRL GAKDDFMEIK SHIFFSLINW
DDLINKKITP PFNPNVSGPS DLRHFDPEFT EEPVPSSIGR SPDSILVTAS VKEAAEAFLG
FSYAPPVDSF L
