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Protein

Serine/threonine-protein kinase Sgk1

Gene

SGK1

Organism
Homo sapiens (Human)
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. 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)DescriptionActionsGraphical viewLength
Binding sitei127ATP1
Active sitei222Proton acceptor1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi104 – 112ATP9

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • calcium channel regulator activity Source: UniProtKB
  • chloride channel regulator activity Source: UniProtKB
  • potassium channel regulator activity Source: UniProtKB
  • protein serine/threonine/tyrosine kinase activity Source: MGI
  • protein serine/threonine kinase activity Source: Reactome
  • sodium channel regulator activity Source: UniProtKB

GO - Biological processi

  • apoptotic process Source: UniProtKB-KW
  • cellular response to DNA damage stimulus Source: Ensembl
  • cellular sodium ion homeostasis Source: GO_Central
  • intracellular signal transduction Source: GO_Central
  • ion transmembrane transport Source: Reactome
  • long-term memory Source: UniProtKB
  • neuron projection morphogenesis Source: GO_Central
  • peptidyl-serine phosphorylation Source: GO_Central
  • positive regulation of sodium ion transport Source: GO_Central
  • positive regulation of transporter activity Source: UniProtKB
  • protein phosphorylation Source: ProtInc
  • regulation of apoptotic process Source: UniProtKB
  • regulation of blood pressure Source: UniProtKB
  • regulation of catalytic activity Source: UniProtKB
  • regulation of cell growth Source: UniProtKB
  • regulation of cell migration Source: UniProtKB
  • regulation of cell proliferation Source: UniProtKB
  • regulation of gastric acid secretion Source: UniProtKB
  • regulation of sequence-specific DNA binding transcription factor activity Source: UniProtKB
  • renal sodium ion absorption Source: UniProtKB
  • response to stress Source: ProtInc
  • sodium ion transport Source: ProtInc
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

BioCyciZFISH:HS04230-MONOMER.
BRENDAi2.7.11.1. 2681.
ReactomeiR-HSA-2672351. Stimuli-sensing channels.
R-HSA-6804757. Regulation of TP53 Degradation.
SignaLinkiO00141.
SIGNORiO00141.

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
Proteomesi
  • UP000005640 Componenti: 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

Complete GO annotation...

Keywords - Cellular componenti

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

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi127K → M: Abolishes enzymatic activity. 3 Publications1
Mutagenesisi256T → A: Low activity. 1 Publication1
Mutagenesisi256T → D: Low activity. 1 Publication1
Mutagenesisi256T → E: Low activity. 1 Publication1
Mutagenesisi298Y → A: Abolishes interaction with NEDD4 and NEDD4L. 1 Publication1
Mutagenesisi422S → A: Low activity. 4 Publications1
Mutagenesisi422S → D: 10-fold activation. 4 Publications1

Organism-specific databases

DisGeNETi6446.
OpenTargetsiENSG00000118515.
PharmGKBiPA162403013.

Chemistry databases

ChEMBLiCHEMBL2343.
GuidetoPHARMACOLOGYi1534.

Polymorphism and mutation databases

BioMutaiSGK1.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000866421 – 431Serine/threonine-protein kinase Sgk1Add BLAST431

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei74PhosphoserineCombined sources1
Modified residuei78Phosphoserine; by MAPK71 Publication1
Disulfide bondi193Interchain (with C-258)1 Publication
Modified residuei256Phosphothreonine; by PDPK11 Publication1
Disulfide bondi258Interchain (with C-193)1 Publication
Modified residuei369Phosphothreonine; by PKA1 Publication1
Modified residuei397PhosphoserineCombined sources1 Publication1
Modified residuei401PhosphoserineCombined sources1 Publication1
Modified residuei422Phosphoserine3 Publications1

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.6 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.
PeptideAtlasiO00141.
PRIDEiO00141.

PTM databases

iPTMnetiO00141.
PhosphoSitePlusiO00141.

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

BgeeiENSG00000118515.
CleanExiHS_SGK1.
ExpressionAtlasiO00141. baseline and differential.
GenevisibleiO00141. HS.

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. 60 interactors.
DIPiDIP-42464N.
IntActiO00141. 11 interactors.
MINTiMINT-1338693.
STRINGi9606.ENSP00000356832.

Chemistry databases

BindingDBiO00141.

Structurei

Secondary structure

1431
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi95 – 97Combined sources3
Beta strandi98 – 105Combined sources8
Beta strandi111 – 117Combined sources7
Turni118 – 120Combined sources3
Beta strandi123 – 130Combined sources8
Helixi131 – 133Combined sources3
Beta strandi162 – 167Combined sources6
Beta strandi169 – 177Combined sources9
Helixi184 – 191Combined sources8
Helixi196 – 215Combined sources20
Helixi225 – 227Combined sources3
Beta strandi228 – 230Combined sources3
Beta strandi232 – 234Combined sources3
Beta strandi236 – 238Combined sources3
Helixi245 – 247Combined sources3
Beta strandi256 – 258Combined sources3
Helixi266 – 269Combined sources4
Helixi277 – 292Combined sources16
Helixi302 – 311Combined sources10
Beta strandi318 – 320Combined sources3
Helixi322 – 331Combined sources10
Helixi336 – 338Combined sources3
Turni340 – 345Combined sources6
Helixi346 – 350Combined sources5
Helixi353 – 355Combined sources3
Helixi360 – 364Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2R5TX-ray1.90A60-431[»]
3HDMX-ray2.60A60-431[»]
3HDNX-ray3.10A60-431[»]
ProteinModelPortaliO00141.
SMRiO00141.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO00141.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini98 – 355Protein kinasePROSITE-ProRule annotationAdd BLAST258
Domaini356 – 431AGC-kinase C-terminalAdd BLAST76

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 60Necessary for localization to the mitochondriaAdd BLAST60

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi131 – 141Nuclear localization signal1 PublicationAdd BLAST11

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi131 – 141Glu/Lys-richAdd BLAST11

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

eggNOGiKOG0598. Eukaryota.
ENOG410XNPH. LUCA.
GeneTreeiENSGT00860000133668.
HOVERGENiHBG108317.
InParanoidiO00141.
KOiK13302.
OMAiEVKEPCN.
OrthoDBiEOG091G06FF.
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.
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. AlignAdd to basket

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)DescriptionActionsGraphical viewLength
Sequence conflicti62Q → E in CAR58097 (Ref. 4) Curated1
Sequence conflicti152K → R in CAR58096 (Ref. 4) Curated1
Sequence conflicti196E → G in CAR58095 (Ref. 4) Curated1
Sequence conflicti228I → V in BAH12848 (PubMed:14702039).Curated1
Sequence conflicti371P → R in CAR58097 (Ref. 4) Curated1
Sequence conflicti381D → E in CAA71138 (PubMed:9114008).Curated1
Sequence conflicti381D → E in CAA04146 (PubMed:9722955).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_041071219V → I.1 PublicationCorresponds to variant rs34133418dbSNPEnsembl.1
Natural variantiVAR_041072342A → V.1 PublicationCorresponds to variant rs55932330dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0377841 – 25MTVKT…VAILI → MVNKDMNGFPVKKCSAFQFF KKRVRRWIKSPMVSVDKHQS PSLKYTGSSMVHIPPGEPDF ESSLCQTCLGEHAFQRGVLP QENESCSWETQSGCEVREPC NHANILTKPDPRTFWTNDDP in isoform 2. 3 PublicationsAdd BLAST25
Alternative sequenceiVSP_0377851 – 25MTVKT…VAILI → MGEMQGALARARLESLLRPR HKKRAEAQKRSESFLLSGL in isoform 3. 2 PublicationsAdd BLAST25
Alternative sequenceiVSP_0377861 – 25MTVKT…VAILI → MKPSKRFFISPPSST in isoform 4. 1 PublicationAdd BLAST25
Alternative sequenceiVSP_0377871 – 25MTVKT…VAILI → MSSQSSSLSEACSREAYSSH NWALPPASRSNPQPAYPWAT RRMKEEAIKPPLK in isoform 5. 1 PublicationAdd BLAST25

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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]
XP_011534373.1. XM_011536071.1. [O00141-2]
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.5. human. [O00141-1]

Keywords - Coding sequence diversityi

Alternative promoter usage, Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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]
XP_011534373.1. XM_011536071.1. [O00141-2]
UniGeneiHs.510078.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2R5TX-ray1.90A60-431[»]
3HDMX-ray2.60A60-431[»]
3HDNX-ray3.10A60-431[»]
ProteinModelPortaliO00141.
SMRiO00141.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112344. 60 interactors.
DIPiDIP-42464N.
IntActiO00141. 11 interactors.
MINTiMINT-1338693.
STRINGi9606.ENSP00000356832.

Chemistry databases

BindingDBiO00141.
ChEMBLiCHEMBL2343.
GuidetoPHARMACOLOGYi1534.

PTM databases

iPTMnetiO00141.
PhosphoSitePlusiO00141.

Polymorphism and mutation databases

BioMutaiSGK1.

Proteomic databases

MaxQBiO00141.
PaxDbiO00141.
PeptideAtlasiO00141.
PRIDEiO00141.

Protocols and materials databases

DNASUi6446.
Structural Biology KnowledgebaseSearch...

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.5. human. [O00141-1]

Organism-specific databases

CTDi6446.
DisGeNETi6446.
GeneCardsiSGK1.
HGNCiHGNC:10810. SGK1.
HPAiCAB022085.
CAB025148.
HPA051251.
MIMi602958. gene.
neXtProtiNX_O00141.
OpenTargetsiENSG00000118515.
PharmGKBiPA162403013.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0598. Eukaryota.
ENOG410XNPH. LUCA.
GeneTreeiENSGT00860000133668.
HOVERGENiHBG108317.
InParanoidiO00141.
KOiK13302.
OMAiEVKEPCN.
OrthoDBiEOG091G06FF.
PhylomeDBiO00141.
TreeFamiTF320906.

Enzyme and pathway databases

BioCyciZFISH:HS04230-MONOMER.
BRENDAi2.7.11.1. 2681.
ReactomeiR-HSA-2672351. Stimuli-sensing channels.
R-HSA-6804757. Regulation of TP53 Degradation.
SignaLinkiO00141.
SIGNORiO00141.

Miscellaneous databases

ChiTaRSiSGK1. human.
EvolutionaryTraceiO00141.
GeneWikiiSGK.
GenomeRNAii6446.
PROiO00141.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000118515.
CleanExiHS_SGK1.
ExpressionAtlasiO00141. baseline and differential.
GenevisibleiO00141. HS.

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...

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: November 30, 2016
This is version 173 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

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.