Q9WVC6 (SGK1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Serine/threonine-protein kinase Sgk1
EC=2.7.11.1

Alternative name(s):
Serum/glucocorticoid-regulated kinase 1

Gene names

Name:	Sgk1
Synonyms:	Sgk

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	431 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

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 Ca2+ 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. Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17
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. Ref.12
Subunit structure	Homodimer; disulfide-linked. Interacts with MAPK3/ERK1, MAPK1/ERK2, MAP2K1/MEK1, MAP2K2/MEK2, NEDD4, NEDD4L, MAPT/TAU, MAPK7, CREB1, SLC9A3R2/NHERF2 and KCNJ1/ROMK1 By similarity. Forms a trimeric complex with FBXW7 and NOTCH1 Associates with the mammalian target of rapamycin complex 2 (mTORC2) via an interaction with MAPKAP1/SIN1. Ref.15 Ref.16
Subcellular location	Cytoplasm By similarity. Nucleus By similarity. Endoplasmic reticulum membrane By similarity. Cell membrane By similarity. Mitochondrion By similarity. 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 By similarity. Ref.17
Induction	Up-regulated by tumor suppressor p53 in mammary epithelial tumor cells. Ref.6 Ref.12
Post-translational modification	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 By similarity. 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 By similarity.
Sequence similarities	Belongs to the protein kinase superfamily. AGC Ser/Thr protein kinase family. Contains 1 AGC-kinase C-terminal domain. Contains 1 protein kinase domain.
Sequence caution	The sequence AAH70401.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Apoptosis Stress response
Cellular component	Cell membrane Cytoplasm Endoplasmic reticulum Membrane Mitochondrion Nucleus
Coding sequence diversity	Alternative splicing
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Disulfide bond Phosphoprotein Ubl conjugation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	apoptotic process Inferred from electronic annotation. Source: UniProtKB-KW response to DNA damage stimulus Inferred from direct assay PubMed 15383658. Source: MGI
Cellular_component	endoplasmic reticulum membrane Inferred from electronic annotation. Source: UniProtKB-SubCell mitochondrion Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW protein kinase activity Inferred from direct assay PubMed 15383658. Source: MGI protein serine/threonine kinase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9WVC6-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q9WVC6-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-25: MTVKAEAARSTLTYSRMRGMVAILI → MVNKDMNGFP...PRTFWTNDDA

Isoform 3 (identifier: Q9WVC6-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-25: MTVKAEAARSTLTYSRMRGMVAILI → MGEMQGALARARLESLLRPRHKKRAEAQKRSESVLLSGL

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 431	431	Serine/threonine-protein kinase Sgk1		PRO_0000086643
Regions
	Domain	98 – 355	258	Protein kinase
	Domain	356 – 431	76	AGC-kinase C-terminal
	Nucleotide binding	104 – 112	9	ATP By similarity
	Region	1 – 60	60	Necessary for localization to the mitochondria By similarity
	Motif	131 – 141	11	Nuclear localization signal By similarity
	Compositional bias	131 – 141	11	Glu/Lys-rich
Sites
	Active site	222	1	Proton acceptor By similarity
	Binding site	127	1	ATP By similarity
Amino acid modifications
	Modified residue	74	1	Phosphoserine By similarity
	Modified residue	78	1	Phosphoserine; by MAPK7 By similarity
	Modified residue	256	1	Phosphothreonine; by PDPK1 By similarity
	Modified residue	369	1	Phosphothreonine; by PKA By similarity
	Modified residue	397	1	Phosphoserine By similarity
	Modified residue	401	1	Phosphoserine By similarity
	Modified residue	422	1	Phosphoserine By similarity
	Disulfide bond	193		Interchain (with C-258) By similarity
	Disulfide bond	258		Interchain (with C-193) By similarity
Natural variations
	Alternative sequence	1 – 25	25	MTVKA…VAILI → MVNKDMNGFPVKKCSAFQFF KKRVRRWIKSPMVSVDKHQS PNLKYTGPAGVHLPPGESDF EAMCQSCLGDHAFQRGMLPP EESCSWEIQPGCEVKEQCNH ANILTKPDPRTFWTNDDA in isoform 2.		VSP_037788
	Alternative sequence	1 – 25	25	MTVKA…VAILI → MGEMQGALARARLESLLRPR HKKRAEAQKRSESVLLSGL in isoform 3.		VSP_037789
Experimental info
	Sequence conflict	87	1	P → L in BAE26849. Ref.3
	Sequence conflict	347	1	M → V in BAE26849. Ref.3
	Sequence conflict	347	1	M → V in BAE26871. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified November 1, 1999. Version 1. Checksum: 6DF5B8464A4C2754	FASTA	431	48,928
	10 20 30 40 50 60 MTVKAEAARS TLTYSRMRGM VAILIAFMKQ RRMGLNDFIQ KIASNTYACK HAEVQSILKM 70 80 90 100 110 120 SHPQEPELMN 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 NGTTSTFCGT PEYLAPEVLH KQPYDRTVDW WCLGAVLYEM LYGLPPFYSR 310 320 330 340 350 360 NTAEMYDNIL NKPLQLKPNI TNSARHLLEG LLQKDRTKRL GAKDDFMEIK SHIFFSLINW 370 380 390 400 410 420 DDLINKKITP PFNPNVSGPS DLRHFDPEFT EEPVPSSIGR SPDSILVTAS VKEAAEAFLG 430 FSYAPPVDSF L
	Isoform 2 [UniParc]. Checksum: 5AB3CBA333DA87D1	FASTA	524	59,571
	10 20 30 40 50 60 MVNKDMNGFP VKKCSAFQFF KKRVRRWIKS PMVSVDKHQS PNLKYTGPAG VHLPPGESDF 70 80 90 100 110 120 EAMCQSCLGD HAFQRGMLPP EESCSWEIQP GCEVKEQCNH ANILTKPDPR TFWTNDDAAF 130 140 150 160 170 180 MKQRRMGLND FIQKIASNTY ACKHAEVQSI LKMSHPQEPE LMNANPSPPP SPSQQINLGP 190 200 210 220 230 240 SSNPHAKPSD FHFLKVIGKG SFGKVLLARH KAEEVFYAVK VLQKKAILKK KEEKHIMSER 250 260 270 280 290 300 NVLLKNVKHP FLVGLHFSFQ TADKLYFVLD YINGGELFYH LQRERCFLEP RARFYAAEIA 310 320 330 340 350 360 SALGYLHSLN IVYRDLKPEN ILLDSQGHIV LTDFGLCKEN IEHNGTTSTF CGTPEYLAPE 370 380 390 400 410 420 VLHKQPYDRT VDWWCLGAVL YEMLYGLPPF YSRNTAEMYD NILNKPLQLK PNITNSARHL 430 440 450 460 470 480 LEGLLQKDRT KRLGAKDDFM EIKSHIFFSL INWDDLINKK ITPPFNPNVS GPSDLRHFDP 490 500 510 520 EFTEEPVPSS IGRSPDSILV TASVKEAAEA FLGFSYAPPV DSFL
	Isoform 3 [UniParc]. Checksum: 275D16D8FD41AEEC	FASTA	445	50,533
	10 20 30 40 50 60 MGEMQGALAR ARLESLLRPR HKKRAEAQKR SESVLLSGLA FMKQRRMGLN DFIQKIASNT 70 80 90 100 110 120 YACKHAEVQS ILKMSHPQEP ELMNANPSPP PSPSQQINLG PSSNPHAKPS DFHFLKVIGK 130 140 150 160 170 180 GSFGKVLLAR HKAEEVFYAV KVLQKKAILK KKEEKHIMSE RNVLLKNVKH PFLVGLHFSF 190 200 210 220 230 240 QTADKLYFVL DYINGGELFY HLQRERCFLE PRARFYAAEI ASALGYLHSL NIVYRDLKPE 250 260 270 280 290 300 NILLDSQGHI VLTDFGLCKE NIEHNGTTST FCGTPEYLAP EVLHKQPYDR TVDWWCLGAV 310 320 330 340 350 360 LYEMLYGLPP FYSRNTAEMY DNILNKPLQL KPNITNSARH LLEGLLQKDR TKRLGAKDDF 370 380 390 400 410 420 MEIKSHIFFS LINWDDLINK KITPPFNPNV SGPSDLRHFD PEFTEEPVPS SIGRSPDSIL 430 440 VTASVKEAAE AFLGFSYAPP VDSFL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"sgk is an aldosterone-induced kinase in the renal collecting duct. Effects on epithelial Na+ channels." Naray-Fejes-Toth A., Canessa C., Cleaveland E.S., Aldrich G., Fejes-Toth G. J. Biol. Chem. 274:16973-16978(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]	"Regulation of sgk by aldosterone and its effects on the epithelial Na(+) channel." Shigaev A., Asher C., Latter H., Garty H., Reuveny E. Am. J. Physiol. 278:F613-F619(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Strain: C57BL/6J. Tissue: Placenta.
[3]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). Strain: C57BL/6J. Tissue: Brain and Placenta.
[4]	Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). Strain: C57BL/6 and FVB/N. Tissue: Brain.
[6]	"p53 stimulates promoter activity of the sgk. serum/glucocorticoid-inducible serine/threonine protein kinase gene in rodent mammary epithelial cells." Maiyar A.C., Huang A.J., Phu P.T., Cha H.H., Firestone G.L. J. Biol. Chem. 271:12414-12422(1996) [PubMed] [Europe PMC] [Abstract] Cited for: REGULATION BY P53. Tissue: Mammary epithelium.
[7]	"Expression of the serum- and glucocorticoid-inducible protein kinase, Sgk, is a cell survival response to multiple types of environmental stress stimuli in mammary epithelial cells." Leong M.L.L., Maiyar A.C., Kim B., O'Keeffe B.A., Firestone G.L. J. Biol. Chem. 278:5871-5882(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[8]	"Cell surface expression of the ROMK (Kir 1.1) channel is regulated by the aldosterone-induced kinase, SGK-1, and protein kinase A." Yoo D., Kim B.Y., Campo C., Nance L., King A., Maouyo D., Welling P.A. J. Biol. Chem. 278:23066-23075(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN PHOSPHORYLATION OF KCNJ1/ROMK1.
[9]	"Glucocorticoid adrenal steroids and glucocorticoid-inducible kinase isoforms in the regulation of GluR6 expression." Strutz-Seebohm N., Seebohm G., Shumilina E., Mack A.F., Wagner H.J., Lampert A., Grahammer F., Henke G., Just L., Skutella T., Hollmann M., Lang F. J. Physiol. (Lond.) 565:391-401(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN REGULATION OF GRIK2/GLUR6.
[10]	"Sgk1 activates MDM2-dependent p53 degradation and affects cell proliferation, survival, and differentiation." 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. J. Mol. Med. 87:1221-1239(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN PHOSPHORYLATION OF MDM2.
[11]	"Serum and glucocorticoid-inducible kinase 1 (SGK1) is necessary for vascular remodeling during angiogenesis." Catela C., Kratsios P., Hede M., Lang F., Rosenthal N. Dev. Dyn. 239:2149-2160(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[12]	"Serum and glucocorticoid-induced kinase (SGK) 1 and the epithelial sodium channel are regulated by multiple with no lysine (WNK) family members." Heise C.J., Xu B.E., Deaton S.L., Cha S.K., Cheng C.J., Earnest S., Sengupta S., Juang Y.C., Stippec S., Xu Y., Zhao Y., Huang C.L., Cobb M.H. J. Biol. Chem. 285:25161-25167(2010) [PubMed] [Europe PMC] [Abstract] Cited for: ENZYME REGULATION.
[13]	"Serum- and glucocorticoid-inducible kinase 1 (SGK1) regulates adipocyte differentiation via forkhead box O1." Di Pietro N., Panel V., Hayes S., Bagattin A., Meruvu S., Pandolfi A., Hugendubler L., Fejes-Toth G., Naray-Fejes-Toth A., Mueller E. Mol. Endocrinol. 24:370-380(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN PHOSPHORYLATION OF FOXO1.
[14]	"Stimulation of Ca2+-channel Orai1/STIM1 by serum- and glucocorticoid-inducible kinase 1 (SGK1)." Eylenstein A., Gehring E.M., Heise N., Shumilina E., Schmidt S., Szteyn K., Muenzer P., Nurbaeva M.K., Eichenmueller M., Tyan L., Regel I., Foeller M., Kuhl D., Soboloff J., Penner R., Lang F. FASEB J. 25:2012-2021(2011) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[15]	"mSIN1 protein mediates SGK1 protein interaction with mTORC2 protein complex and is required for selective activation of the epithelial sodium channel." Lu M., Wang J., Ives H.E., Pearce D. J. Biol. Chem. 286:30647-30654(2011) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH MAPKAP1/SIN1.
[16]	"Serum- and glucocorticoid-inducible kinase 1 (SGK1) controls Notch1 signaling by downregulation of protein stability through Fbw7 ubiquitin ligase." Mo J.S., Ann E.J., Yoon J.H., Jung J., Choi Y.H., Kim H.Y., Ahn J.S., Kim S.M., Kim M.Y., Hong J.A., Seo M.S., Lang F., Choi E.J., Park H.S. J. Cell Sci. 124:100-112(2011) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN PHOSPHORYLATION OF FBXW7, INTERACTION WITH NOTCH1 AND FBXW7.
[17]	"Serum- and glucocorticoid-induced kinase 3 in recycling endosomes mediates acute activation of Na+/H+ exchanger NHE3 by glucocorticoids." He P., Lee S.J., Lin S., Seidler U., Lang F., Fejes-Toth G., Naray-Fejes-Toth A., Yun C.C. Mol. Biol. Cell 22:3812-3825(2011) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN REGULATION OF SLC9A3/NHE3, SUBCELLULAR LOCATION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF139638 mRNA. Translation: AAD43302.1. AF205855 mRNA. Translation: AAF19429.1. AK132234 mRNA. Translation: BAE21048.1. AK146037 mRNA. Translation: BAE26849.1. AK146062 mRNA. Translation: BAE26871.1. AK159131 mRNA. Translation: BAE34843.1. AK167364 mRNA. Translation: BAE39461.1. CH466562 Genomic DNA. Translation: EDL03408.1. BC005720 mRNA. Translation: AAH05720.1. BC070401 mRNA. Translation: AAH70401.1. Different initiation.
IPI	IPI00125834. IPI00462411. IPI00652180.
RefSeq	NP_001155317.2. NM_001161845.2. NP_001155319.1. NM_001161847.2. NP_001155320.1. NM_001161848.2. NP_001155321.1. NM_001161849.2. NP_001155322.1. NM_001161850.2. NP_035491.1. NM_011361.3.
UniGene	Mm.28405.
3D structure databases
ProteinModelPortal	Q9WVC6.
SMR	Q9WVC6. Positions 36-426.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-48845N.
STRING	10090.ENSMUSP00000114074.
PTM databases
PhosphoSite	Q9WVC6.
Proteomic databases
PRIDE	Q9WVC6.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000020145; ENSMUSP00000020145; ENSMUSG00000019970. ENSMUST00000092673; ENSMUSP00000090343; ENSMUSG00000019970. ENSMUST00000120509; ENSMUSP00000114074; ENSMUSG00000019970.
GeneID	20393.
KEGG	mmu:20393.
UCSC	uc007eov.2. mouse. uc007eow.2. mouse. uc007eox.2. mouse.
Organism-specific databases
CTD	6446.
MGI	MGI:1340062. Sgk1.
Phylogenomic databases
eggNOG	COG0515.
GeneTree	ENSGT00700000104132.
HOGENOM	HOG000233033.
HOVERGEN	HBG108317.
InParanoid	Q6NS85.
KO	K13302.
OMA	QFYAVKV.
Enzyme and pathway databases
BRENDA	2.7.11.1. 3474.
Gene expression databases
ArrayExpress	Q9WVC6.
Bgee	Q9WVC6.
CleanEx	MM_SGK1.
Genevestigator	Q9WVC6.
GermOnline	ENSMUSG00000019970. Mus musculus.
Family and domain databases
InterPro	IPR000961. AGC-kinase_C. IPR011009. Kinase-like_dom. IPR017892. Pkinase_C. IPR000719. Prot_kinase_cat_dom. IPR017441. Protein_kinase_ATP_BS. IPR002290. Ser/Thr_dual-sp_kinase_dom. IPR008271. Ser/Thr_kinase_AS. [Graphical view]
Pfam	PF00069. Pkinase. 1 hit. PF00433. Pkinase_C. 1 hit. [Graphical view]
SMART	SM00133. S_TK_X. 1 hit. SM00220. S_TKc. 1 hit. [Graphical view]
SUPFAM	SSF56112. Kinase_like. 1 hit.
PROSITE	PS51285. AGC_KINASE_CTER. 1 hit. PS00107. PROTEIN_KINASE_ATP. 1 hit. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00108. PROTEIN_KINASE_ST. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	298338.
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Entry information

Entry name

SGK1_MOUSE

Accession

Primary (citable) accession number: Q9WVC6
Secondary accession number(s): Q3TJN4 , Q3UKD0, Q3UKF2, Q3V1V1, Q6NS85

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 27, 2001
Last sequence update:	November 1, 1999
Last modified:	May 1, 2013
This is version 113 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program