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O00141

- SGK1_HUMAN

UniProt

O00141 - SGK1_HUMAN

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Protein

Serine/threonine-protein kinase Sgk1

Gene

SGK1

Organism
Homo sapiens (Human)
Status
Reviewed - 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. Sustained high levels and activity may contribute to conditions such as hypertension and diabetic nephropathy. Isoform 2 exhibited a greater effect on cell plasma membrane expression of SCNN1A/ENAC and Na+ transport than isoform 1.32 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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei127 – 1271ATP
Active sitei222 – 2221Proton acceptor

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi104 – 1129ATP

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. calcium channel regulator activity Source: UniProtKB
  3. chloride channel regulator activity Source: UniProtKB
  4. potassium channel regulator activity Source: UniProtKB
  5. protein serine/threonine/tyrosine kinase activity Source: MGI
  6. protein serine/threonine kinase activity Source: ProtInc
  7. sodium channel regulator activity Source: UniProtKB

GO - Biological processi

  1. apoptotic process Source: UniProtKB-KW
  2. cellular response to DNA damage stimulus Source: Ensembl
  3. ion transmembrane transport Source: Reactome
  4. long-term memory Source: UniProtKB
  5. positive regulation of transporter activity Source: UniProtKB
  6. protein phosphorylation Source: ProtInc
  7. regulation of apoptotic process Source: UniProtKB
  8. regulation of blood pressure Source: UniProtKB
  9. regulation of catalytic activity Source: UniProtKB
  10. regulation of cell growth Source: UniProtKB
  11. regulation of cell migration Source: UniProtKB
  12. regulation of cell proliferation Source: UniProtKB
  13. regulation of gastric acid secretion Source: UniProtKB
  14. regulation of sequence-specific DNA binding transcription factor activity Source: UniProtKB
  15. renal sodium ion absorption Source: UniProtKB
  16. response to stress Source: ProtInc
  17. sodium ion transport Source: ProtInc
  18. transmembrane transport Source: Reactome
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. 2681.
ReactomeiREACT_160189. Stimuli-sensing channels.
SignaLinkiO00141.

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
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 6

Organism-specific databases

HGNCiHGNC:10810. SGK1.

Subcellular locationi

Cytoplasm. Nucleus. Endoplasmic reticulum membrane. Cell membrane. Mitochondrion
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.

GO - Cellular componenti

  1. cytoplasm Source: HPA
  2. cytosol Source: Reactome
  3. endoplasmic reticulum Source: UniProtKB-KW
  4. mitochondrion Source: UniProtKB-KW
  5. nucleus Source: HPA
  6. plasma membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

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

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi127 – 1271K → M: Abolishes enzymatic activity. 3 Publications
Mutagenesisi256 – 2561T → A: Low activity. 1 Publication
Mutagenesisi256 – 2561T → D: Low activity. 1 Publication
Mutagenesisi256 – 2561T → E: Low activity. 1 Publication
Mutagenesisi298 – 2981Y → A: Abolishes interaction with NEDD4 and NEDD4L. 1 Publication
Mutagenesisi422 – 4221S → A: Low activity. 4 Publications
Mutagenesisi422 – 4221S → D: 10-fold activation. 4 Publications

Organism-specific databases

PharmGKBiPA162403013.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 431431Serine/threonine-protein kinase Sgk1PRO_0000086642Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei74 – 741Phosphoserine2 Publications
Modified residuei78 – 781Phosphoserine; by MAPK71 Publication
Disulfide bondi193 – 193Interchain (with C-258)1 Publication
Modified residuei256 – 2561Phosphothreonine; by PDPK11 Publication
Disulfide bondi258 – 258Interchain (with C-193)1 Publication
Modified residuei369 – 3691Phosphothreonine; by PKA1 Publication
Modified residuei397 – 3971Phosphoserine4 Publications
Modified residuei401 – 4011Phosphoserine3 Publications
Modified residuei422 – 4221Phosphoserine3 Publications

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.9 Publications
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. Isoform 2 shows enhanced stability.1 Publication

Keywords - PTMi

Disulfide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiO00141.
PaxDbiO00141.
PRIDEiO00141.

PTM databases

PhosphoSiteiO00141.

Expressioni

Tissue specificityi

Expressed in most tissues with highest levels in the pancreas, followed by placenta, kidney and lung. Isoform 2 is strongly expressed in brain and pancreas, weaker in heart, placenta, lung, liver and skeletal muscle.2 Publications

Inductioni

Induced by a very large spectrum of stimuli distinct from glucocorticoids and serum. These include aldosterone, cell shrinkage, cell swelling, TGF-beta, ischemic injury of the brain, neuronal excitotoxicity memory consolidation, chronic viral hepatitis, DNA-damaging agents, vitamin D3 psychophysiological stress, iron, glucose, EDN1, CSF2, fibroblast growth factor, platelet-derived growth factor, phorbolesters, follicle-stimulating hormone, sorbitol, heat shock, oxidative stress, UV irradiation, and p53/TP53. Many of these stimuli are highly cell-specific, as is the case, for example for aldosterone, which has been found to stimulate its expression only in cells derived from aldosterone-responsive epithelia. Isoform 2 is not induced by glucocorticoids but by excessive extracellular glucose and by TGFB1, in cultured cells.1 Publication

Gene expression databases

BgeeiO00141.
CleanExiHS_SGK1.
ExpressionAtlasiO00141. baseline and differential.
GenevestigatoriO00141.

Organism-specific databases

HPAiCAB022085.
CAB025148.
HPA051251.

Interactioni

Subunit structurei

Homodimer; disulfide-linked. Forms a trimeric complex with FBXW7 and NOTCH1. Interacts with MAPK3/ERK1, MAPK1/ERK2, MAP2K1/MEK1, MAP2K2/MEK2, NEDD4, NEDD4L, MAPT/TAU, MAPK7, CREB1, SLC9A3R2/NHERF2 and KCNJ1/ROMK1. Associates with the mammalian target of rapamycin complex 2 (mTORC2) via an interaction with MAPKAP1/SIN1.8 Publications

Protein-protein interaction databases

BioGridi112344. 51 interactions.
DIPiDIP-42464N.
IntActiO00141. 10 interactions.
MINTiMINT-1338693.

Structurei

Secondary structure

1
431
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi95 – 973Combined sources
Beta strandi98 – 1058Combined sources
Beta strandi111 – 1177Combined sources
Turni118 – 1203Combined sources
Beta strandi123 – 1308Combined sources
Helixi131 – 1333Combined sources
Beta strandi162 – 1676Combined sources
Beta strandi169 – 1779Combined sources
Helixi184 – 1918Combined sources
Helixi196 – 21520Combined sources
Helixi225 – 2273Combined sources
Beta strandi228 – 2303Combined sources
Beta strandi232 – 2343Combined sources
Beta strandi236 – 2383Combined sources
Helixi245 – 2473Combined sources
Beta strandi256 – 2583Combined sources
Helixi266 – 2694Combined sources
Helixi277 – 29216Combined sources
Helixi302 – 31110Combined sources
Beta strandi318 – 3203Combined sources
Helixi322 – 33110Combined sources
Helixi336 – 3383Combined sources
Turni340 – 3456Combined sources
Helixi346 – 3505Combined sources
Helixi353 – 3553Combined sources
Helixi360 – 3645Combined sources

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2R5TX-ray1.90A60-431[»]
3HDMX-ray2.60A60-431[»]
3HDNX-ray3.10A60-431[»]
ProteinModelPortaliO00141.
SMRiO00141. Positions 2-427.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO00141.

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 mitochondriaAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi131 – 14111Nuclear localization signal1 PublicationAdd
BLAST

Compositional bias

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

Domaini

Isoform 2 subcellular localization at the cell membrane and resistance to proteasomal degradation is mediated by the sequences within the first 120 amino acids.

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00760000118793.
HOVERGENiHBG108317.
InParanoidiO00141.
KOiK13302.
OMAiQFYAVKV.
OrthoDBiEOG7Q5HCW.
PhylomeDBiO00141.
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.
IPR002290. Ser/Thr_dual-sp_kinase.
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 (5)i

Sequence statusi: Complete.

This entry describes 5 isoformsi produced by alternative promoter usage and alternative splicing. Align

Isoform 1 (identifier: O00141-1) [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
MTVKTEAAKG TLTYSRMRGM VAILIAFMKQ RRMGLNDFIQ KIANNSYACK
60 70 80 90 100
HPEVQSILKI SQPQEPELMN 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
NSTTSTFCGT PEYLAPEVLH KQPYDRTVDW WCLGAVLYEM LYGLPPFYSR
310 320 330 340 350
NTAEMYDNIL NKPLQLKPNI TNSARHLLEG LLQKDRTKRL GAKDDFMEIK
360 370 380 390 400
SHVFFSLINW DDLINKKITP PFNPNVSGPN DLRHFDPEFT EEPVPNSIGK
410 420 430
SPDSVLVTAS VKEAAEAFLG FSYAPPTDSF L
Length:431
Mass (Da):48,942
Last modified:March 7, 2006 - v2
Checksum:iF3697C63AB1F499D
GO
Isoform 2 (identifier: O00141-2) [UniParc]FASTAAdd to Basket

Also known as: Sgk1.1, Sgk1_v2

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

Note: Produced by alternative promoter usage.

Show »
Length:526
Mass (Da):59,904
Checksum:i8CE1E9DFB949D5A5
GO
Isoform 3 (identifier: O00141-3) [UniParc]FASTAAdd to Basket

Also known as: Sgk1.2

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

Note: Produced by alternative promoter usage.

Show »
Length:445
Mass (Da):50,623
Checksum:iDC7076E1F43BCBAB
GO
Isoform 4 (identifier: O00141-4) [UniParc]FASTAAdd to Basket

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

Note: Produced by alternative splicing of isoform 1.

Show »
Length:421
Mass (Da):47,910
Checksum:i6BDCD1FA7D9AFD0E
GO
Isoform 5 (identifier: O00141-5) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-25: MTVKTEAAKGTLTYSRMRGMVAILI → MSSQSSSLSE...KEEAIKPPLK

Note: Produced by alternative promoter usage.

Show »
Length:459
Mass (Da):52,119
Checksum:i1B108E7CF17935E5
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti62 – 621Q → E in CAR58097. 1 PublicationCurated
Sequence conflicti152 – 1521K → R in CAR58096. 1 PublicationCurated
Sequence conflicti196 – 1961E → G in CAR58095. 1 PublicationCurated
Sequence conflicti228 – 2281I → V in BAH12848. (PubMed:14702039)Curated
Sequence conflicti371 – 3711P → R in CAR58097. 1 PublicationCurated
Sequence conflicti381 – 3811D → E in CAA71138. (PubMed:9114008)Curated
Sequence conflicti381 – 3811D → E in CAA04146. (PubMed:9722955)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti219 – 2191V → I.1 Publication
Corresponds to variant rs34133418 [ dbSNP | Ensembl ].
VAR_041071
Natural varianti342 – 3421A → V.1 Publication
Corresponds to variant rs55932330 [ dbSNP | Ensembl ].
VAR_041072

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 2525MTVKT…VAILI → MVNKDMNGFPVKKCSAFQFF KKRVRRWIKSPMVSVDKHQS PSLKYTGSSMVHIPPGEPDF ESSLCQTCLGEHAFQRGVLP QENESCSWETQSGCEVREPC NHANILTKPDPRTFWTNDDP in isoform 2. 3 PublicationsVSP_037784Add
BLAST
Alternative sequencei1 – 2525MTVKT…VAILI → MGEMQGALARARLESLLRPR HKKRAEAQKRSESFLLSGL in isoform 3. 2 PublicationsVSP_037785Add
BLAST
Alternative sequencei1 – 2525MTVKT…VAILI → MKPSKRFFISPPSST in isoform 4. 1 PublicationVSP_037786Add
BLAST
Alternative sequencei1 – 2525MTVKT…VAILI → MSSQSSSLSEACSREAYSSH NWALPPASRSNPQPAYPWAT RRMKEEAIKPPLK in isoform 5. 1 PublicationVSP_037787Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Y10032 mRNA. Translation: CAA71138.1.
AJ000512 Genomic DNA. Translation: CAA04146.1.
EU518415 mRNA. Translation: ACD35864.1.
FM205707 mRNA. Translation: CAR58095.1.
FM205708 mRNA. Translation: CAR58096.1.
FM205709 mRNA. Translation: CAR58097.1.
FM205710 mRNA. Translation: CAR58098.1.
AF153609 mRNA. Translation: AAD41091.1.
AK055077 mRNA. Translation: BAG51463.1.
AK298688 mRNA. Translation: BAH12848.1.
AL355881, AL135839, Z84486 Genomic DNA. Translation: CAH72579.1.
AL135839 Genomic DNA. Translation: CAI19718.1.
AL135839 Genomic DNA. Translation: CAI19719.1.
AL135839 Genomic DNA. Translation: CAI19720.1.
AL135839, AL355881, Z84486 Genomic DNA. Translation: CAI19721.1.
Z84486, AL135839, AL355881 Genomic DNA. Translation: CAI21678.1.
CH471051 Genomic DNA. Translation: EAW47991.1.
CH471051 Genomic DNA. Translation: EAW47992.1.
CH471051 Genomic DNA. Translation: EAW47993.1.
BC001263 mRNA. Translation: AAH01263.1.
CCDSiCCDS47476.1. [O00141-2]
CCDS47477.1. [O00141-5]
CCDS47478.1. [O00141-3]
CCDS5170.1. [O00141-1]
RefSeqiNP_001137148.1. NM_001143676.1. [O00141-2]
NP_001137149.1. NM_001143677.1. [O00141-5]
NP_001137150.1. NM_001143678.1. [O00141-3]
NP_001278924.1. NM_001291995.1.
NP_005618.2. NM_005627.3. [O00141-1]
UniGeneiHs.510078.

Genome annotation databases

EnsembliENST00000237305; ENSP00000237305; ENSG00000118515. [O00141-1]
ENST00000367857; ENSP00000356831; ENSG00000118515. [O00141-4]
ENST00000367858; ENSP00000356832; ENSG00000118515. [O00141-2]
ENST00000413996; ENSP00000396242; ENSG00000118515. [O00141-3]
ENST00000528577; ENSP00000434450; ENSG00000118515. [O00141-5]
GeneIDi6446.
KEGGihsa:6446.
UCSCiuc003qen.4. human. [O00141-1]
uc003qeo.4. human. [O00141-2]
uc011ect.2. human. [O00141-4]
uc011ecv.2. human. [O00141-3]
uc011ecw.2. human. [O00141-5]

Keywords - Coding sequence diversityi

Alternative promoter usage, Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Y10032 mRNA. Translation: CAA71138.1 .
AJ000512 Genomic DNA. Translation: CAA04146.1 .
EU518415 mRNA. Translation: ACD35864.1 .
FM205707 mRNA. Translation: CAR58095.1 .
FM205708 mRNA. Translation: CAR58096.1 .
FM205709 mRNA. Translation: CAR58097.1 .
FM205710 mRNA. Translation: CAR58098.1 .
AF153609 mRNA. Translation: AAD41091.1 .
AK055077 mRNA. Translation: BAG51463.1 .
AK298688 mRNA. Translation: BAH12848.1 .
AL355881 , AL135839 , Z84486 Genomic DNA. Translation: CAH72579.1 .
AL135839 Genomic DNA. Translation: CAI19718.1 .
AL135839 Genomic DNA. Translation: CAI19719.1 .
AL135839 Genomic DNA. Translation: CAI19720.1 .
AL135839 , AL355881 , Z84486 Genomic DNA. Translation: CAI19721.1 .
Z84486 , AL135839 , AL355881 Genomic DNA. Translation: CAI21678.1 .
CH471051 Genomic DNA. Translation: EAW47991.1 .
CH471051 Genomic DNA. Translation: EAW47992.1 .
CH471051 Genomic DNA. Translation: EAW47993.1 .
BC001263 mRNA. Translation: AAH01263.1 .
CCDSi CCDS47476.1. [O00141-2 ]
CCDS47477.1. [O00141-5 ]
CCDS47478.1. [O00141-3 ]
CCDS5170.1. [O00141-1 ]
RefSeqi NP_001137148.1. NM_001143676.1. [O00141-2 ]
NP_001137149.1. NM_001143677.1. [O00141-5 ]
NP_001137150.1. NM_001143678.1. [O00141-3 ]
NP_001278924.1. NM_001291995.1.
NP_005618.2. NM_005627.3. [O00141-1 ]
UniGenei Hs.510078.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2R5T X-ray 1.90 A 60-431 [» ]
3HDM X-ray 2.60 A 60-431 [» ]
3HDN X-ray 3.10 A 60-431 [» ]
ProteinModelPortali O00141.
SMRi O00141. Positions 2-427.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 112344. 51 interactions.
DIPi DIP-42464N.
IntActi O00141. 10 interactions.
MINTi MINT-1338693.

Chemistry

BindingDBi O00141.
ChEMBLi CHEMBL2343.
GuidetoPHARMACOLOGYi 1534.

PTM databases

PhosphoSitei O00141.

Proteomic databases

MaxQBi O00141.
PaxDbi O00141.
PRIDEi O00141.

Protocols and materials databases

DNASUi 6446.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000237305 ; ENSP00000237305 ; ENSG00000118515 . [O00141-1 ]
ENST00000367857 ; ENSP00000356831 ; ENSG00000118515 . [O00141-4 ]
ENST00000367858 ; ENSP00000356832 ; ENSG00000118515 . [O00141-2 ]
ENST00000413996 ; ENSP00000396242 ; ENSG00000118515 . [O00141-3 ]
ENST00000528577 ; ENSP00000434450 ; ENSG00000118515 . [O00141-5 ]
GeneIDi 6446.
KEGGi hsa:6446.
UCSCi uc003qen.4. human. [O00141-1 ]
uc003qeo.4. human. [O00141-2 ]
uc011ect.2. human. [O00141-4 ]
uc011ecv.2. human. [O00141-3 ]
uc011ecw.2. human. [O00141-5 ]

Organism-specific databases

CTDi 6446.
GeneCardsi GC06M134490.
HGNCi HGNC:10810. SGK1.
HPAi CAB022085.
CAB025148.
HPA051251.
MIMi 602958. gene.
neXtProti NX_O00141.
PharmGKBi PA162403013.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0515.
GeneTreei ENSGT00760000118793.
HOVERGENi HBG108317.
InParanoidi O00141.
KOi K13302.
OMAi QFYAVKV.
OrthoDBi EOG7Q5HCW.
PhylomeDBi O00141.
TreeFami TF320906.

Enzyme and pathway databases

BRENDAi 2.7.11.1. 2681.
Reactomei REACT_160189. Stimuli-sensing channels.
SignaLinki O00141.

Miscellaneous databases

ChiTaRSi SGK1. human.
EvolutionaryTracei O00141.
GeneWikii SGK.
GenomeRNAii 6446.
NextBioi 25053.
PROi O00141.
SOURCEi Search...

Gene expression databases

Bgeei O00141.
CleanExi HS_SGK1.
ExpressionAtlasi O00141. baseline and differential.
Genevestigatori O00141.

Family and domain databases

InterProi IPR000961. AGC-kinase_C.
IPR011009. Kinase-like_dom.
IPR017892. Pkinase_C.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view ]
Pfami PF00069. Pkinase. 1 hit.
PF00433. Pkinase_C. 1 hit.
[Graphical view ]
SMARTi SM00133. S_TK_X. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view ]
SUPFAMi SSF56112. SSF56112. 1 hit.
PROSITEi 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 ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and characterization of a putative human serine/threonine protein kinase transcriptionally modified during anisotonic and isotonic alterations of cell volume."
    Waldegger S., Barth P., Raber G., Lang F.
    Proc. Natl. Acad. Sci. U.S.A. 94:4440-4445(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. "Genomic organization and chromosomal localization of the human SGK protein kinase gene."
    Waldegger S., Erdel M., Nagl U.O., Barth P., Raber G., Steuer S., Utermann G., Paulmichl M., Lang F.
    Genomics 51:299-302(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING (ISOFORM 1).
  3. "An evolutionarily conserved N-terminal Sgk1 variant with enhanced stability and improved function."
    Raikwar N.S., Snyder P.M., Thomas C.P.
    Am. J. Physiol. 295:F1440-F1448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, ALTERNATIVE PROMOTER USAGE, INDUCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    Tissue: Brain.
  4. "Transcriptional variants of serum/glucocorticoid regulated kinase 1 show differential localisation and regulation."
    Hall B.A., Blakeley S., Daniels N.A., Jamieson D., Brickley D., Reynolds N.J., Conzen S.D., Jackson T.R.
    Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3; 4 AND 5), ALTERNATIVE PROMOTER USAGE.
    Tissue: Glioblastoma, Hippocampus and Skin.
  5. "A catalogue of genes in the human dermal papilla cells as identified by expressed sequence tags."
    Kim M.K., Kim Y.H., Seo J.M., Lee H.M., Chung H.J., Sohn M.Y., Hwang S.Y., Im S.U., Jung E.J., Lee J.H., Kim J.C.
    Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Hair follicle dermal papilla.
  6. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
    Tissue: Brain.
  7. "The DNA sequence and analysis of human chromosome 6."
    Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
    , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
    Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  9. "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] (ISOFORM 1).
    Tissue: Cervix.
  10. "Characterization of the structure and regulation of two novel isoforms of serum- and glucocorticoid-induced protein kinase."
    Kobayashi T., Deak M., Morrice N., Cohen P.
    Biochem. J. 344:189-197(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  11. "Activation of serum- and glucocorticoid-regulated protein kinase by agonists that activate phosphatidylinositide 3-kinase is mediated by 3-phosphoinositide-dependent protein kinase-1 (PDK1) and PDK2."
    Kobayashi T., Cohen P.
    Biochem. J. 339:319-328(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT THR-256 AND SER-422, MUTAGENESIS OF THR-256 AND SER-422.
    Tissue: Brain.
  12. Cited for: CHARACTERIZATION.
  13. "BMK1 mediates growth factor-induced cell proliferation through direct cellular activation of serum and glucocorticoid-inducible kinase."
    Hayashi M., Tapping R.I., Chao T.H., Lo J.F., King C.C., Yang Y., Lee J.D.
    J. Biol. Chem. 276:8631-8634(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-78 BY MAPK7, INTERACTION WITH MAPK7.
  14. "Activation of serum- and glucocorticoid-induced protein kinase (Sgk) by cyclic AMP and insulin."
    Perrotti N., He R.A., Phillips S.A., Haft C.R., Taylor S.I.
    J. Biol. Chem. 276:9406-9412(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT THR-369 BY PKA.
  15. "Serum- and glucocorticoid-inducible kinase SGK phosphorylates and negatively regulates B-Raf."
    Zhang B.H., Tang E.D., Zhu T., Greenberg M.E., Vojtek A.B., Guan K.L.
    J. Biol. Chem. 276:31620-31626(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF BRAF.
  16. "Protein kinase SGK mediates survival signals by phosphorylating the forkhead transcription factor FKHRL1 (FOXO3a)."
    Brunet A., Park J., Tran H., Hu L.S., Hemmings B.A., Greenberg M.E.
    Mol. Cell. Biol. 21:952-965(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  17. "Serum and glucocorticoid-regulated kinase modulates Nedd4-2-mediated inhibition of the epithelial Na+ channel."
    Snyder P.M., Olson D.R., Thomas B.C.
    J. Biol. Chem. 277:5-8(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NEDD4 AND NEDD4L, MUTAGENESIS OF LYS-127; TYR-298 AND SER-422, FUNCTION.
  18. "Activation of Na+/K+-ATPase by the serum and glucocorticoid-dependent kinase isoforms."
    Henke G., Setiawan I., Boehmer C., Lang F.
    Kidney Blood Press. Res. 25:370-374(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN REGULATION OF NA(+)/K(+) ATPASE.
  19. "K(+) channel activation by all three isoforms of serum- and glucocorticoid-dependent protein kinase SGK."
    Gamper N., Fillon S., Feng Y., Friedrich B., Lang P.A., Henke G., Huber S.M., Kobayashi T., Cohen P., Lang F.
    Pflugers Arch. 445:60-66(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  20. "Molecular requirements for the regulation of the renal outer medullary K(+) channel ROMK1 by the serum- and glucocorticoid-inducible kinase SGK1."
    Palmada M., Embark H.M., Yun C., Bohmer C., Lang F.
    Biochem. Biophys. Res. Commun. 311:629-634(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH SLC9A3R2/NHERF2 AND KCNJ1/ROMK1.
  21. "Serum and glucocorticoid inducible kinases in the regulation of the cardiac sodium channel SCN5A."
    Boehmer C., Wilhelm V., Palmada M., Wallisch S., Henke G., Brinkmeier H., Cohen P., Pieske B., Lang F.
    Cardiovasc. Res. 57:1079-1084(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN REGULATION OF SCN5A.
  22. "Inhibition of mitogen-activated kinase kinase kinase 3 activity through phosphorylation by the serum- and glucocorticoid-induced kinase 1."
    Chun J., Kwon T., Kim D.J., Park I., Chung G., Lee E.J., Hong S.K., Chang S.I., Kim H.Y., Kang S.S.
    J. Biochem. 133:103-108(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF MAP3K3/MEKK3.
  23. "Regulation of the glutamate transporter EAAT1 by the ubiquitin ligase Nedd4-2 and the serum and glucocorticoid-inducible kinase isoforms SGK1/3 and protein kinase B."
    Boehmer C., Henke G., Schniepp R., Palmada M., Rothstein J.D., Broeer S., Lang F.
    J. Neurochem. 86:1181-1188(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN REGULATION OF KCNA3/KV1.3, MUTAGENESIS OF LYS-127 AND SER-422.
  24. "Importin-alpha mediates the regulated nuclear targeting of serum- and glucocorticoid-inducible protein kinase (Sgk) by recognition of a nuclear localization signal in the kinase central domain."
    Maiyar A.C., Leong M.L., Firestone G.L.
    Mol. Biol. Cell 14:1221-1239(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEAR LOCALIZATION SIGNAL.
  25. "Regulation of KCNE1-dependent K(+) current by the serum and glucocorticoid-inducible kinase (SGK) isoforms."
    Embark H.M., Boehmer C., Vallon V., Luft F., Lang F.
    Pflugers Arch. 445:601-606(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN REGULATION OF KCNE1 AND KCNQ1.
  26. "Regulation of intestinal phosphate cotransporter NaPi IIb by ubiquitin ligase Nedd4-2 and by serum- and glucocorticoid-dependent kinase 1."
    Palmada M., Dieter M., Speil A., Boehmer C., Mack A.F., Wagner H.J., Klingel K., Kandolf R., Murer H., Biber J., Closs E.I., Lang F.
    Am. J. Physiol. 287:G143-G150(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN REGULATION OF SLC34A2/NAPI-2B, FUNCTION IN PHOSPHORYLATION OF NEDD4L.
  27. "Stimulation of renal Na+ dicarboxylate cotransporter 1 by Na+/H+ exchanger regulating factor 2, serum and glucocorticoid inducible kinase isoforms, and protein kinase B."
    Boehmer C., Embark H.M., Bauer A., Palmada M., Yun C.H., Weinman E.J., Endou H., Cohen P., Lahme S., Bichler K.H., Lang F.
    Biochem. Biophys. Res. Commun. 313:998-1003(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN REGULATION OF SLC13A2/NADC1.
  28. "Regulation of the epithelial Ca2+ channel TRPV5 by the NHE regulating factor NHERF2 and the serum and glucocorticoid inducible kinase isoforms SGK1 and SGK3 expressed in Xenopus oocytes."
    Embark H.M., Setiawan I., Poppendieck S., van de Graaf S.F., Boehmer C., Palmada M., Wieder T., Gerstberger R., Cohen P., Yun C.C., Bindels R.J., Lang F.
    Cell. Physiol. Biochem. 14:203-212(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN REGULATION OF TRPV5.
  29. "A novel pathway of epithelial sodium channel activation involves a serum- and glucocorticoid-inducible kinase consensus motif in the C terminus of the channel's alpha-subunit."
    Diakov A., Korbmacher C.
    J. Biol. Chem. 279:38134-38142(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  30. "Regulation of the voltage gated K+ channel Kv1.3 by the ubiquitin ligase Nedd4-2 and the serum and glucocorticoid inducible kinase SGK1."
    Henke G., Maier G., Wallisch S., Boehmer C., Lang F.
    J. Cell. Physiol. 199:194-199(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF LYS-127 AND SER-422.
  31. "Regulation of CLC-Ka/barttin by the ubiquitin ligase Nedd4-2 and the serum- and glucocorticoid-dependent kinases."
    Embark H.M., Boehmer C., Palmada M., Rajamanickam J., Wyatt A.W., Wallisch S., Capasso G., Waldegger P., Seyberth H.W., Waldegger S., Lang F.
    Kidney Int. 66:1918-1925(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN REGULATION OF BSND.
  32. "Activation of NHE3 by dexamethasone requires phosphorylation of NHE3 at Ser663 by SGK1."
    Wang D., Sun H., Lang F., Yun C.C.
    Am. J. Physiol. 289:C802-C810(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF SLC9A3/NHE3.
  33. "The serine/threonine kinases SGK1, 3 and PKB stimulate the amino acid transporter ASCT2."
    Palmada M., Speil A., Jeyaraj S., Boehmer C., Lang F.
    Biochem. Biophys. Res. Commun. 331:272-277(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN REGULATION OF SLC1A5/ASCT2.
  34. "Regulation of the excitatory amino acid transporter EAAT5 by the serum and glucocorticoid dependent kinases SGK1 and SGK3."
    Boehmer C., Rajamanickam J., Schniepp R., Kohler K., Wulff P., Kuhl D., Palmada M., Lang F.
    Biochem. Biophys. Res. Commun. 329:738-742(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN REGULATION OF SLC1A7/EAAT5.
  35. "Stimulation of the creatine transporter SLC6A8 by the protein kinases SGK1 and SGK3."
    Shojaiefard M., Christie D.L., Lang F.
    Biochem. Biophys. Res. Commun. 334:742-746(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN REGULATION OF SLC6A8.
  36. "Serum/glucocorticoid-inducible kinase can phosphorylate the cyclic AMP response element binding protein, CREB."
    David S., Kalb R.G.
    FEBS Lett. 579:1534-1538(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF CREB1, INTERACTION WITH CREB1.
  37. "Nedd4-2 phosphorylation induces serum and glucocorticoid-regulated kinase (SGK) ubiquitination and degradation."
    Zhou R., Snyder P.M.
    J. Biol. Chem. 280:4518-4523(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION.
  38. "SGK1 kinase upregulates GLUT1 activity and plasma membrane expression."
    Palmada M., Boehmer C., Akel A., Rajamanickam J., Jeyaraj S., Keller K., Lang F.
    Diabetes 55:421-427(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN REGULATION OF SLC2A1/GLUT1.
  39. "Serum- and glucocorticoid-inducible kinase 1 (SGK1) increases neurite formation through microtubule depolymerization by SGK1 and by SGK1 phosphorylation of tau."
    Yang Y.C., Lin C.H., Lee E.H.
    Mol. Cell. Biol. 26:8357-8370(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF MAPT/TAU, INTERACTION WITH MAPT/TAU.
  40. "Subcellular location of serum- and glucocorticoid-induced kinase-1 in renal and mammary epithelial cells."
    Cordas E., Naray-Fejes-Toth A., Fejes-Toth G.
    Am. J. Physiol. 292:C1971-C1981(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  41. "Role of SGK1 kinase in regulating glucose transport via glucose transporter GLUT4."
    Jeyaraj S., Boehmer C., Lang F., Palmada M.
    Biochem. Biophys. Res. Commun. 356:629-635(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF SLC2A4/GLUT4.
  42. "Regulation of the epithelial calcium channel TRPV6 by the serum and glucocorticoid-inducible kinase isoforms SGK1 and SGK3."
    Boehmer C., Palmada M., Kenngott C., Lindner R., Klaus F., Laufer J., Lang F.
    FEBS Lett. 581:5586-5590(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN REGULATION OF TRPV6.
  43. "Regulation Fe65 localization to the nucleus by SGK1 phosphorylation of its Ser566 residue."
    Lee E.J., Chun J., Hyun S., Ahn H.R., Jeong J.M., Hong S.K., Hong J.T., Chang I.K., Jeon H.Y., Han Y.S., Auh C.K., Park J.I., Kang S.S.
    BMB Rep. 41:41-47(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF APBB1/FE65.
  44. "mTOR complex 2 (mTORC2) controls hydrophobic motif phosphorylation and activation of serum- and glucocorticoid-induced protein kinase 1 (SGK1)."
    Garcia-Martinez J.M., Alessi D.R.
    Biochem. J. 416:375-385(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-422 BY MTORC2.
  45. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-74; SER-397 AND SER-401, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  46. "A brain-specific SGK1 splice isoform regulates expression of ASIC1 in neurons."
    Arteaga M.F., Coric T., Straub C., Canessa C.M.
    Proc. Natl. Acad. Sci. U.S.A. 105:4459-4464(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: ALTERNATIVE PROMOTER USAGE (ISOFORMS 2 AND 3).
  47. "Regulation of a third conserved phosphorylation site in SGK1."
    Chen W., Chen Y., Xu B.E., Juang Y.C., Stippec S., Zhao Y., Cobb M.H.
    J. Biol. Chem. 284:3453-3460(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-397 AND SER-401.
  48. "Protein kinase SGK1 enhances MEK/ERK complex formation through the phosphorylation of ERK2: implication for the positive regulatory role of SGK1 on the ERK function during liver regeneration."
    Won M., Park K.A., Byun H.S., Kim Y.R., Choi B.L., Hong J.H., Park J., Seok J.H., Lee Y.H., Cho C.H., Song I.S., Kim Y.K., Shen H.M., Hur G.M.
    J. Hepatol. 51:67-76(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF MAPK1/ERK2, INTERACTION WITH MAPK3/ERK1; MAPK1/ERK2; MAP2K1/MEK1 AND MAP2K2/MEK2.
  49. "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.
  50. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-74; SER-397 AND SER-401, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  51. "The serum and glucocorticoid inducible kinases SGK1-3 stimulate the neutral amino acid transporter SLC6A19."
    Boehmer C., Sopjani M., Klaus F., Lindner R., Laufer J., Jeyaraj S., Lang F., Palmada M.
    Cell. Physiol. Biochem. 25:723-732(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN REGULATION OF SLC6A19.
  52. Cited for: PHOSPHORYLATION AT SER-422 BY MTORC2, INTERACTION WITH MTORC2.
  53. "Interaction of serum- and glucocorticoid regulated kinase 1 (SGK1) with the WW-domains of Nedd4-2 is required for epithelial sodium channel regulation."
    Wiemuth D., Lott J.S., Ly K., Ke Y., Teesdale-Spittle P., Snyder P.M., McDonald F.J.
    PLoS ONE 5:E12163-E12163(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  54. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-397, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  55. "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.
  56. "Stimulus-dependent regulation of serum and glucocorticoid inducible protein kinase (SGK) transcription, subcellular localization and enzymatic activity."
    Firestone G.L., Giampaolo J.R., O'Keeffe B.A.
    Cell. Physiol. Biochem. 13:1-12(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  57. "Sgk kinases and their role in epithelial transport."
    Loffing J., Flores S.Y., Staub O.
    Annu. Rev. Physiol. 68:461-490(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  58. Cited for: REVIEW ON FUNCTION.
  59. "Significance of SGK1 in the regulation of neuronal function."
    Lang F., Strutz-Seebohm N., Seebohm G., Lang U.E.
    J. Physiol. (Lond.) 588:3349-3354(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON FUNCTION.
  60. "Crystal structure of the kinase domain of serum and glucocorticoid-regulated kinase 1 in complex with AMP PNP."
    Zhao B., Lehr R., Smallwood A.M., Ho T.F., Maley K., Randall T., Head M.S., Koretke K.K., Schnackenberg C.G.
    Protein Sci. 16:2761-2769(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 60-431, SUBUNIT, DISULFIDE BOND.
  61. "Patterns of somatic mutation in human cancer genomes."
    Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.
    , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
    Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS [LARGE SCALE ANALYSIS] ILE-219 AND VAL-342.

Entry informationi

Entry nameiSGK1_HUMAN
AccessioniPrimary (citable) accession number: O00141
Secondary accession number(s): B7UUP7
, B7UUP8, B7UUP9, B7Z5B2, E1P583, Q5TCN2, Q5TCN3, Q5TCN4, Q5VY65, Q9UN56
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: March 7, 2006
Last modified: October 29, 2014
This is version 151 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 6
    Human chromosome 6: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3