Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

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

 SGK1_MOUSE              Reviewed;         431 AA.
Q9WVC6; Q3TJN4; Q3UKD0; Q3UKF2; Q3V1V1; Q6NS85;
27-APR-2001, integrated into UniProtKB/Swiss-Prot.
01-NOV-1999, sequence version 1.
22-NOV-2017, entry version 152.
RecName: Full=Serine/threonine-protein kinase Sgk1;
EC=2.7.11.1;
AltName: Full=Serum/glucocorticoid-regulated kinase 1;
Name=Sgk1; Synonyms=Sgk;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=10358046; DOI=10.1074/jbc.274.24.16973;
Naray-Fejes-Toth A., Canessa C., Cleaveland E.S., Aldrich G.,
Fejes-Toth G.;
"sgk is an aldosterone-induced kinase in the renal collecting duct.
Effects on epithelial Na+ channels.";
J. Biol. Chem. 274:16973-16978(1999).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
STRAIN=C57BL/6J; TISSUE=Placenta;
PubMed=10751222;
Shigaev A., Asher C., Latter H., Garty H., Reuveny E.;
"Regulation of sgk by aldosterone and its effects on the epithelial
Na(+) channel.";
Am. J. Physiol. 278:F613-F619(2000).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
STRAIN=C57BL/6J; TISSUE=Brain, and Placenta;
PubMed=16141072; DOI=10.1126/science.1112014;
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.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
STRAIN=C57BL/6J, and FVB/N; TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
REGULATION BY P53.
TISSUE=Mammary epithelium;
PubMed=8647846; DOI=10.1074/jbc.271.21.12414;
Maiyar A.C., Huang A.J., Phu P.T., Cha H.H., Firestone G.L.;
"p53 stimulates promoter activity of the sgk. serum/glucocorticoid-
inducible serine/threonine protein kinase gene in rodent mammary
epithelial cells.";
J. Biol. Chem. 271:12414-12422(1996).
[7]
FUNCTION.
PubMed=12488318; DOI=10.1074/jbc.M211649200;
Leong M.L.L., Maiyar A.C., Kim B., O'Keeffe B.A., Firestone G.L.;
"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.";
J. Biol. Chem. 278:5871-5882(2003).
[8]
FUNCTION IN PHOSPHORYLATION OF KCNJ1/ROMK1.
PubMed=12684516; DOI=10.1074/jbc.M212301200;
Yoo D., Kim B.Y., Campo C., Nance L., King A., Maouyo D.,
Welling P.A.;
"Cell surface expression of the ROMK (Kir 1.1) channel is regulated by
the aldosterone-induced kinase, SGK-1, and protein kinase A.";
J. Biol. Chem. 278:23066-23075(2003).
[9]
FUNCTION IN REGULATION OF GRIK2/GLUR6.
PubMed=15774535; DOI=10.1113/jphysiol.2004.079624;
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.;
"Glucocorticoid adrenal steroids and glucocorticoid-inducible kinase
isoforms in the regulation of GluR6 expression.";
J. Physiol. (Lond.) 565:391-401(2005).
[10]
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).
[11]
FUNCTION.
PubMed=20568246; DOI=10.1002/dvdy.22345;
Catela C., Kratsios P., Hede M., Lang F., Rosenthal N.;
"Serum and glucocorticoid-inducible kinase 1 (SGK1) is necessary for
vascular remodeling during angiogenesis.";
Dev. Dyn. 239:2149-2160(2010).
[12]
ENZYME REGULATION.
PubMed=20525693; DOI=10.1074/jbc.M110.103432;
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.;
"Serum and glucocorticoid-induced kinase (SGK) 1 and the epithelial
sodium channel are regulated by multiple with no lysine (WNK) family
members.";
J. Biol. Chem. 285:25161-25167(2010).
[13]
FUNCTION IN PHOSPHORYLATION OF FOXO1.
PubMed=19965929; DOI=10.1210/me.2009-0265;
Di Pietro N., Panel V., Hayes S., Bagattin A., Meruvu S., Pandolfi A.,
Hugendubler L., Fejes-Toth G., Naray-Fejes-Toth A., Mueller E.;
"Serum- and glucocorticoid-inducible kinase 1 (SGK1) regulates
adipocyte differentiation via forkhead box O1.";
Mol. Endocrinol. 24:370-380(2010).
[14]
FUNCTION.
PubMed=21385992; DOI=10.1096/fj.10-178210;
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.;
"Stimulation of Ca2+-channel Orai1/STIM1 by serum- and glucocorticoid-
inducible kinase 1 (SGK1).";
FASEB J. 25:2012-2021(2011).
[15]
FUNCTION, AND INTERACTION WITH MAPKAP1/SIN1.
PubMed=21757730; DOI=10.1074/jbc.M111.257592;
Lu M., Wang J., Ives H.E., Pearce D.;
"mSIN1 protein mediates SGK1 protein interaction with mTORC2 protein
complex and is required for selective activation of the epithelial
sodium channel.";
J. Biol. Chem. 286:30647-30654(2011).
[16]
FUNCTION IN PHOSPHORYLATION OF FBXW7, AND INTERACTION WITH NOTCH1 AND
FBXW7.
PubMed=21147854; DOI=10.1242/jcs.073924;
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.;
"Serum- and glucocorticoid-inducible kinase 1 (SGK1) controls Notch1
signaling by downregulation of protein stability through Fbw7
ubiquitin ligase.";
J. Cell Sci. 124:100-112(2011).
[17]
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).
-!- 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.
{ECO:0000269|PubMed:12488318, ECO:0000269|PubMed:12684516,
ECO:0000269|PubMed:15774535, ECO:0000269|PubMed:19756449,
ECO:0000269|PubMed:19965929, ECO:0000269|PubMed:20568246,
ECO:0000269|PubMed:21147854, ECO:0000269|PubMed:21385992,
ECO:0000269|PubMed:21757730, 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.
{ECO:0000269|PubMed:20525693}.
-!- SUBUNIT: 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. {ECO:0000250,
ECO:0000269|PubMed:21147854, ECO:0000269|PubMed:21757730}.
-!- INTERACTION:
Q99N57:Raf1; NbExp=2; IntAct=EBI-15591730, EBI-397757;
Q9Z2S7-3:Tsc22d3; NbExp=2; IntAct=EBI-15591730, EBI-15771036;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus
{ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}. Cell
membrane {ECO:0000250}. Mitochondrion {ECO:0000250}. 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). {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q9WVC6-1; Sequence=Displayed;
Name=2;
IsoId=Q9WVC6-2; Sequence=VSP_037788;
Name=3;
IsoId=Q9WVC6-3; Sequence=VSP_037789;
-!- INDUCTION: Up-regulated by tumor suppressor p53 in mammary
epithelial tumor cells.
-!- 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 (By similarity). {ECO:0000250}.
-!- 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 (By similarity). {ECO:0000250}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
protein kinase family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAH70401.1; Type=Erroneous initiation; Evidence={ECO:0000305};
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AF139638; AAD43302.1; -; mRNA.
EMBL; AF205855; AAF19429.1; -; mRNA.
EMBL; AK132234; BAE21048.1; -; mRNA.
EMBL; AK146037; BAE26849.1; -; mRNA.
EMBL; AK146062; BAE26871.1; -; mRNA.
EMBL; AK159131; BAE34843.1; -; mRNA.
EMBL; AK167364; BAE39461.1; -; mRNA.
EMBL; CH466562; EDL03408.1; -; Genomic_DNA.
EMBL; BC005720; AAH05720.1; -; mRNA.
EMBL; BC070401; AAH70401.1; ALT_INIT; mRNA.
CCDS; CCDS23726.1; -. [Q9WVC6-1]
CCDS; CCDS48515.1; -. [Q9WVC6-2]
CCDS; CCDS48517.1; -. [Q9WVC6-3]
RefSeq; NP_001155317.2; NM_001161845.2. [Q9WVC6-2]
RefSeq; NP_001155319.1; NM_001161847.2.
RefSeq; NP_001155320.1; NM_001161848.2.
RefSeq; NP_001155321.1; NM_001161849.2.
RefSeq; NP_001155322.1; NM_001161850.2. [Q9WVC6-3]
RefSeq; NP_035491.1; NM_011361.3. [Q9WVC6-1]
UniGene; Mm.28405; -.
ProteinModelPortal; Q9WVC6; -.
SMR; Q9WVC6; -.
BioGrid; 203197; 5.
DIP; DIP-48845N; -.
IntAct; Q9WVC6; 5.
STRING; 10090.ENSMUSP00000114074; -.
BindingDB; Q9WVC6; -.
iPTMnet; Q9WVC6; -.
PhosphoSitePlus; Q9WVC6; -.
PaxDb; Q9WVC6; -.
PRIDE; Q9WVC6; -.
Ensembl; ENSMUST00000020145; ENSMUSP00000020145; ENSMUSG00000019970. [Q9WVC6-1]
Ensembl; ENSMUST00000092673; ENSMUSP00000090343; ENSMUSG00000019970. [Q9WVC6-3]
Ensembl; ENSMUST00000120509; ENSMUSP00000114074; ENSMUSG00000019970. [Q9WVC6-2]
GeneID; 20393; -.
KEGG; mmu:20393; -.
UCSC; uc007eov.2; mouse. [Q9WVC6-2]
UCSC; uc007eow.2; mouse. [Q9WVC6-3]
UCSC; uc007eox.2; mouse. [Q9WVC6-1]
CTD; 6446; -.
MGI; MGI:1340062; Sgk1.
eggNOG; KOG0598; Eukaryota.
eggNOG; ENOG410XNPH; LUCA.
GeneTree; ENSGT00890000139324; -.
HOGENOM; HOG000233033; -.
HOVERGEN; HBG108317; -.
InParanoid; Q9WVC6; -.
KO; K13302; -.
OMA; EVKEPCN; -.
OrthoDB; EOG091G06FF; -.
PhylomeDB; Q9WVC6; -.
TreeFam; TF320906; -.
BRENDA; 2.7.11.1; 3474.
Reactome; R-MMU-2672351; Stimuli-sensing channels.
Reactome; R-MMU-6804757; Regulation of TP53 Degradation.
PRO; PR:Q9WVC6; -.
Proteomes; UP000000589; Chromosome 10.
Bgee; ENSMUSG00000019970; -.
CleanEx; MM_SGK1; -.
ExpressionAtlas; Q9WVC6; baseline and differential.
Genevisible; Q9WVC6; MM.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
GO; GO:0016607; C:nuclear speck; ISO:MGI.
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:0004672; F:protein kinase activity; IDA:MGI.
GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
GO; GO:0004712; F:protein serine/threonine/tyrosine kinase activity; ISO:MGI.
GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
GO; GO:0006974; P:cellular response to DNA damage stimulus; IDA:MGI.
GO; GO:0032869; P:cellular response to insulin stimulus; ISO:MGI.
GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
GO; GO:0048812; P:neuron projection morphogenesis; IBA:GO_Central.
GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
GO; GO:0010765; P:positive regulation of sodium ion transport; ISO:MGI.
GO; GO:0006468; P:protein phosphorylation; IDA:MGI.
GO; GO:0032880; P:regulation of protein localization; ISO:MGI.
InterPro; IPR000961; AGC-kinase_C.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR017892; Pkinase_C.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; 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;
Alternative splicing; Apoptosis; ATP-binding; Cell membrane;
Complete proteome; Cytoplasm; Disulfide bond; Endoplasmic reticulum;
Kinase; Membrane; Mitochondrion; Nucleotide-binding; Nucleus;
Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
Stress response; Transferase; Ubl conjugation.
CHAIN 1 431 Serine/threonine-protein kinase Sgk1.
/FTId=PRO_0000086643.
DOMAIN 98 355 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
DOMAIN 356 431 AGC-kinase C-terminal.
NP_BIND 104 112 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
REGION 1 60 Necessary for localization to the
mitochondria. {ECO:0000250}.
MOTIF 131 141 Nuclear localization signal.
{ECO:0000250}.
COMPBIAS 131 141 Glu/Lys-rich.
ACT_SITE 222 222 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 127 127 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 74 74 Phosphoserine.
{ECO:0000250|UniProtKB:O00141}.
MOD_RES 78 78 Phosphoserine; by MAPK7.
{ECO:0000250|UniProtKB:O00141}.
MOD_RES 256 256 Phosphothreonine; by PDPK1.
{ECO:0000250|UniProtKB:O00141}.
MOD_RES 369 369 Phosphothreonine; by PKA.
{ECO:0000250|UniProtKB:O00141}.
MOD_RES 397 397 Phosphoserine.
{ECO:0000250|UniProtKB:O00141}.
MOD_RES 401 401 Phosphoserine.
{ECO:0000250|UniProtKB:O00141}.
MOD_RES 422 422 Phosphoserine.
{ECO:0000250|UniProtKB:O00141}.
DISULFID 193 193 Interchain (with C-258). {ECO:0000250}.
DISULFID 258 258 Interchain (with C-193). {ECO:0000250}.
VAR_SEQ 1 25 MTVKAEAARSTLTYSRMRGMVAILI -> MVNKDMNGFPVK
KCSAFQFFKKRVRRWIKSPMVSVDKHQSPNLKYTGPAGVHL
PPGESDFEAMCQSCLGDHAFQRGMLPPEESCSWEIQPGCEV
KEQCNHANILTKPDPRTFWTNDDA (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_037788.
VAR_SEQ 1 25 MTVKAEAARSTLTYSRMRGMVAILI -> MGEMQGALARAR
LESLLRPRHKKRAEAQKRSESVLLSGL (in isoform
3). {ECO:0000303|PubMed:16141072}.
/FTId=VSP_037789.
CONFLICT 87 87 P -> L (in Ref. 3; BAE26849).
{ECO:0000305}.
CONFLICT 347 347 M -> V (in Ref. 3; BAE26849/BAE26871).
{ECO:0000305}.
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


Related products :

Catalog number Product name Quantity
CSB-EL021189HU Human Serine per threonine-protein kinase Sgk1(SGK1) ELISA kit 96T
H0336 Serine threonine-protein kinase Sgk1 (SGK1), Mouse, ELISA Kit 96T
H0335 Serine threonine-protein kinase Sgk1 (SGK1), Human, ELISA Kit 96T
H0337 Serine threonine-protein kinase Sgk1 (SGK1), Rabbit, ELISA Kit 96T
H0334 Serine threonine-protein kinase Sgk1 (SGK1), Chicken, ELISA Kit 96T
H0333 Serine threonine-protein kinase Sgk1 (SGK1), Bovine, ELISA Kit 96T
H0338 Serine threonine-protein kinase Sgk1 (SGK1), Rat, ELISA Kit 96T
SGK1_RAT ELISA Kit FOR Serine per threonine-protein kinase Sgk1; organism: Rat; gene name: Sgk1 96T
SGK1_MOUSE ELISA Kit FOR Serine per threonine-protein kinase Sgk1; organism: Mouse; gene name: Sgk1 96T
SGK1_HUMAN Human ELISA Kit FOR Serine per threonine-protein kinase Sgk1 96T
EIAAB31334 Bos taurus,Bovine,PKN,PKN1,PRK1,PRKCL1,Protein kinase C-like 1,Protein kinase C-like PKN,Protein kinase PKN-alpha,Protein-kinase C-related kinase 1,Serine_threonine-protein kinase N1,Serine-threonine
EIAAB31332 Mouse,Mus musculus,Pkn,Pkn1,Prk1,Prkcl1,Protein kinase C-like 1,Protein kinase C-like PKN,Protein-kinase C-related kinase 1,Serine_threonine-protein kinase N1,Serine-threonine protein kinase N
EIAAB38131 Oryctolagus cuniculus,Rabbit,Serine_threonine-protein kinase Sgk1,Serum_glucocorticoid-regulated kinase 1,SGK,SGK1
EIAAB38132 Homo sapiens,Human,Serine_threonine-protein kinase Sgk1,Serum_glucocorticoid-regulated kinase 1,SGK,SGK1
EIAAB38130 Rat,Rattus norvegicus,Serine_threonine-protein kinase Sgk1,Serum_glucocorticoid-regulated kinase 1,Sgk,Sgk1
EIAAB38135 Bos taurus,Bovine,Serine_threonine-protein kinase Sgk1,Serum_glucocorticoid-regulated kinase 1,SGK,SGK1
EIAAB38134 Mouse,Mus musculus,Serine_threonine-protein kinase Sgk1,Serum_glucocorticoid-regulated kinase 1,Sgk,Sgk1
EIAAB38133 Chicken,Gallus gallus,Serine_threonine-protein kinase Sgk1,Serum_glucocorticoid-regulated kinase 1,SGK,SGK1
GWB-CEE83D Serine threonine-protein kinase SNF1-like kinase 2 (SNF1LK2) Salt-inducible protein kinase 2 (SIK2) Rabbit anti-Human Polyclonal
GWB-5BE1E2 Serine threonine-protein kinase SNF1-like kinase 2 (SNF1LK2) Salt-inducible protein kinase 2 (SIK2) Mouse anti-Human Monoclonal
15-288-21987A Serine_threonine-protein kinase Sgk1 - EC 2.7.11.1; Serum_glucocorticoid-regulated kinase 1 Polyclonal 0.1 mg
15-288-21987B Serine_threonine-protein kinase Sgk1 - EC 2.7.11.1; Serum_glucocorticoid-regulated kinase 1 Polyclonal 0.1 mg
15-288-21987B Serine_threonine-protein kinase Sgk1 - EC 2.7.11.1; Serum_glucocorticoid-regulated kinase 1 Polyclonal 0.05 mg
15-288-21987A Serine_threonine-protein kinase Sgk1 - EC 2.7.11.1; Serum_glucocorticoid-regulated kinase 1 Polyclonal 0.05 mg
10-288-21987F Serine_threonine-protein kinase Sgk1 - EC 2.7.11.1; Serum_glucocorticoid-regulated kinase 1 0.05 mg


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur