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Protein

Serine/threonine-protein kinase Sgk1

Gene

Sgk1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.10 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Enzyme regulationi

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 WNK4.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei127 – 1271ATPPROSITE-ProRule annotation
Active sitei222 – 2221Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi104 – 1129ATPPROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Apoptosis, Stress response

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.11.1. 3474.
ReactomeiR-MMU-2672351. Stimuli-sensing channels.

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/threonine-protein kinase Sgk1 (EC:2.7.11.1)
Alternative name(s):
Serum/glucocorticoid-regulated kinase 1
Gene namesi
Name:Sgk1
Synonyms:Sgk
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 10

Organism-specific databases

MGIiMGI:1340062. Sgk1.

Subcellular locationi

  • 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).By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Endoplasmic reticulum, Membrane, Mitochondrion, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 431431Serine/threonine-protein kinase Sgk1PRO_0000086643Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei74 – 741PhosphoserineBy similarity
Modified residuei78 – 781Phosphoserine; by MAPK7By similarity
Disulfide bondi193 – 193Interchain (with C-258)By similarity
Modified residuei256 – 2561Phosphothreonine; by PDPK1By similarity
Disulfide bondi258 – 258Interchain (with C-193)By similarity
Modified residuei369 – 3691Phosphothreonine; by PKABy similarity
Modified residuei397 – 3971PhosphoserineBy similarity
Modified residuei401 – 4011PhosphoserineBy similarity
Modified residuei422 – 4221PhosphoserineBy similarity

Post-translational modificationi

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).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).By similarity

Keywords - PTMi

Disulfide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ9WVC6.
PaxDbiQ9WVC6.
PRIDEiQ9WVC6.

PTM databases

iPTMnetiQ9WVC6.
PhosphoSiteiQ9WVC6.

Expressioni

Inductioni

Up-regulated by tumor suppressor p53 in mammary epithelial tumor cells.

Gene expression databases

BgeeiQ9WVC6.
CleanExiMM_SGK1.
ExpressionAtlasiQ9WVC6. baseline and differential.
GenevisibleiQ9WVC6. MM.

Interactioni

Subunit structurei

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.By similarity2 Publications

Protein-protein interaction databases

BioGridi203197. 5 interactions.
DIPiDIP-48845N.
STRINGi10090.ENSMUSP00000114074.

Structurei

3D structure databases

ProteinModelPortaliQ9WVC6.
SMRiQ9WVC6. Positions 36-426.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini98 – 355258Protein kinasePROSITE-ProRule annotationAdd
BLAST
Domaini356 – 43176AGC-kinase C-terminalAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 6060Necessary for localization to the mitochondriaBy similarityAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi131 – 14111Nuclear localization signalBy similarityAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi131 – 14111Glu/Lys-richAdd
BLAST

Sequence similaritiesi

Contains 1 AGC-kinase C-terminal domain.Curated
Contains 1 protein kinase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG0598. Eukaryota.
ENOG410XNPH. LUCA.
GeneTreeiENSGT00820000126961.
HOGENOMiHOG000233033.
HOVERGENiHBG108317.
InParanoidiQ9WVC6.
KOiK13302.
OMAiEVKEPCN.
OrthoDBiEOG7Q5HCW.
PhylomeDBiQ9WVC6.
TreeFamiTF320906.

Family and domain databases

InterProiIPR000961. AGC-kinase_C.
IPR011009. Kinase-like_dom.
IPR017892. Pkinase_C.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00069. Pkinase. 1 hit.
PF00433. Pkinase_C. 1 hit.
[Graphical view]
SMARTiSM00133. S_TK_X. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS51285. 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]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9WVC6-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MTVKAEAARS TLTYSRMRGM VAILIAFMKQ RRMGLNDFIQ KIASNTYACK
60 70 80 90 100
HAEVQSILKM SHPQEPELMN ANPSPPPSPS QQINLGPSSN PHAKPSDFHF
110 120 130 140 150
LKVIGKGSFG KVLLARHKAE EVFYAVKVLQ KKAILKKKEE KHIMSERNVL
160 170 180 190 200
LKNVKHPFLV GLHFSFQTAD KLYFVLDYIN GGELFYHLQR ERCFLEPRAR
210 220 230 240 250
FYAAEIASAL GYLHSLNIVY RDLKPENILL DSQGHIVLTD FGLCKENIEH
260 270 280 290 300
NGTTSTFCGT PEYLAPEVLH KQPYDRTVDW WCLGAVLYEM LYGLPPFYSR
310 320 330 340 350
NTAEMYDNIL NKPLQLKPNI TNSARHLLEG LLQKDRTKRL GAKDDFMEIK
360 370 380 390 400
SHIFFSLINW DDLINKKITP PFNPNVSGPS DLRHFDPEFT EEPVPSSIGR
410 420 430
SPDSILVTAS VKEAAEAFLG FSYAPPVDSF L
Length:431
Mass (Da):48,928
Last modified:November 1, 1999 - v1
Checksum:i6DF5B8464A4C2754
GO
Isoform 2 (identifier: Q9WVC6-2) [UniParc]FASTAAdd to basket

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

Show »
Length:524
Mass (Da):59,571
Checksum:i5AB3CBA333DA87D1
GO
Isoform 3 (identifier: Q9WVC6-3) [UniParc]FASTAAdd to basket

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

Show »
Length:445
Mass (Da):50,533
Checksum:i275D16D8FD41AEEC
GO

Sequence cautioni

The sequence AAH70401.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti87 – 871P → L in BAE26849 (PubMed:16141072).Curated
Sequence conflicti347 – 3471M → V in BAE26849 (PubMed:16141072).Curated
Sequence conflicti347 – 3471M → V in BAE26871 (PubMed:16141072).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 2525MTVKA…VAILI → MVNKDMNGFPVKKCSAFQFF KKRVRRWIKSPMVSVDKHQS PNLKYTGPAGVHLPPGESDF EAMCQSCLGDHAFQRGMLPP EESCSWEIQPGCEVKEQCNH ANILTKPDPRTFWTNDDA in isoform 2. 1 PublicationVSP_037788Add
BLAST
Alternative sequencei1 – 2525MTVKA…VAILI → MGEMQGALARARLESLLRPR HKKRAEAQKRSESVLLSGL in isoform 3. 1 PublicationVSP_037789Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS23726.1. [Q9WVC6-1]
CCDS48515.1. [Q9WVC6-2]
CCDS48517.1. [Q9WVC6-3]
RefSeqiNP_001155317.2. NM_001161845.2. [Q9WVC6-2]
NP_001155319.1. NM_001161847.2.
NP_001155320.1. NM_001161848.2.
NP_001155321.1. NM_001161849.2.
NP_001155322.1. NM_001161850.2. [Q9WVC6-3]
NP_035491.1. NM_011361.3. [Q9WVC6-1]
UniGeneiMm.28405.

Genome annotation databases

EnsembliENSMUST00000020145; ENSMUSP00000020145; ENSMUSG00000019970. [Q9WVC6-1]
ENSMUST00000092673; ENSMUSP00000090343; ENSMUSG00000019970. [Q9WVC6-3]
ENSMUST00000120509; ENSMUSP00000114074; ENSMUSG00000019970. [Q9WVC6-2]
GeneIDi20393.
KEGGimmu:20393.
UCSCiuc007eov.2. mouse. [Q9WVC6-2]
uc007eow.2. mouse. [Q9WVC6-3]
uc007eox.2. mouse. [Q9WVC6-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS23726.1. [Q9WVC6-1]
CCDS48515.1. [Q9WVC6-2]
CCDS48517.1. [Q9WVC6-3]
RefSeqiNP_001155317.2. NM_001161845.2. [Q9WVC6-2]
NP_001155319.1. NM_001161847.2.
NP_001155320.1. NM_001161848.2.
NP_001155321.1. NM_001161849.2.
NP_001155322.1. NM_001161850.2. [Q9WVC6-3]
NP_035491.1. NM_011361.3. [Q9WVC6-1]
UniGeneiMm.28405.

3D structure databases

ProteinModelPortaliQ9WVC6.
SMRiQ9WVC6. Positions 36-426.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi203197. 5 interactions.
DIPiDIP-48845N.
STRINGi10090.ENSMUSP00000114074.

PTM databases

iPTMnetiQ9WVC6.
PhosphoSiteiQ9WVC6.

Proteomic databases

MaxQBiQ9WVC6.
PaxDbiQ9WVC6.
PRIDEiQ9WVC6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000020145; ENSMUSP00000020145; ENSMUSG00000019970. [Q9WVC6-1]
ENSMUST00000092673; ENSMUSP00000090343; ENSMUSG00000019970. [Q9WVC6-3]
ENSMUST00000120509; ENSMUSP00000114074; ENSMUSG00000019970. [Q9WVC6-2]
GeneIDi20393.
KEGGimmu:20393.
UCSCiuc007eov.2. mouse. [Q9WVC6-2]
uc007eow.2. mouse. [Q9WVC6-3]
uc007eox.2. mouse. [Q9WVC6-1]

Organism-specific databases

CTDi6446.
MGIiMGI:1340062. Sgk1.

Phylogenomic databases

eggNOGiKOG0598. Eukaryota.
ENOG410XNPH. LUCA.
GeneTreeiENSGT00820000126961.
HOGENOMiHOG000233033.
HOVERGENiHBG108317.
InParanoidiQ9WVC6.
KOiK13302.
OMAiEVKEPCN.
OrthoDBiEOG7Q5HCW.
PhylomeDBiQ9WVC6.
TreeFamiTF320906.

Enzyme and pathway databases

BRENDAi2.7.11.1. 3474.
ReactomeiR-MMU-2672351. Stimuli-sensing channels.

Miscellaneous databases

NextBioi298338.
PROiQ9WVC6.
SOURCEiSearch...

Gene expression databases

BgeeiQ9WVC6.
CleanExiMM_SGK1.
ExpressionAtlasiQ9WVC6. baseline and differential.
GenevisibleiQ9WVC6. MM.

Family and domain databases

InterProiIPR000961. AGC-kinase_C.
IPR011009. Kinase-like_dom.
IPR017892. Pkinase_C.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00069. Pkinase. 1 hit.
PF00433. Pkinase_C. 1 hit.
[Graphical view]
SMARTiSM00133. S_TK_X. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF56112. SSF56112. 1 hit.
PROSITEiPS51285. 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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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/6J 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. 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.

Entry informationi

Entry nameiSGK1_MOUSE
AccessioniPrimary (citable) accession number: Q9WVC6
Secondary accession number(s): Q3TJN4
, Q3UKD0, Q3UKF2, Q3V1V1, Q6NS85
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: November 1, 1999
Last modified: May 11, 2016
This is version 139 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.