O00141 (SGK1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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

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

Gene names

Name:	SGK1
Synonyms:	SGK

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

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

General annotation (Comments)

Function	Serine/threonine-protein kinase which is involved in the regulation of a wide variety of ion channels, membrane transporters, cellular enzymes, transcription factors, neuronal excitability, cell growth, proliferation, survival, migration and apoptosis. Plays an important role in cellular stress response. Contributes to regulation of renal Na+ retention, renal K+ elimination, salt appetite, gastric acid secretion, intestinal Na+/H+ exchange and nutrient transport, insulin-dependent salt sensitivity of blood pressure, salt sensitivity of peripheral glucose uptake, cardiac repolarization and memory consolidation. Up-regulates Na+ channels: SCNN1A/ENAC, SCN5A and ASIC1/ACCN2, K+ channels: KCNJ1/ROMK1, KCNA1-5, KCNQ1-5 and KCNE1, epithelial Ca2+ channels: TRPV5 and TRPV6, chloride channels: BSND, CLCN2 and CFTR, glutamate transporters: SLC1A3/EAAT1, SLC1A2 /EAAT2, SLC1A1/EAAT3, SLC1A6/EAAT4 and SLC1A7/EAAT5, amino acid transporters: SLC1A5/ASCT2, SLC38A1/SN1 and SLC6A19, creatine transporter: SLC6A8, Na+/dicarboxylate cotransporter: SLC13A2/NADC1, Na+-dependent phosphate cotransporter: SLC34A2/NAPI-2B, glutamate receptor: GRIK2/GLUR6. Up-regulates carriers: SLC9A3/NHE3, SLC12A1/NKCC2, SLC12A3/NCC, SLC5A3/SMIT, SLC2A1/GLUT1, SLC5A1/SGLT1 and SLC15A2/PEPT2. Regulates enzymes: GSK3A/B, PMM2 and Na+/K+ ATPase, and transcription factors: CTNNB1 and nuclear factor NF-kappa-B. Stimulates sodium transport into epithelial cells by enhancing the stability and expression of SCNN1A/ENAC. This is achieved by phosphorylating the NEDD4L ubiquitin E3 ligase, promoting its interaction with 14-3-3 proteins, thereby preventing it from binding to SCNN1A/ENAC and targeting it for degradation. Regulates store-operated Ca(+2) entry (SOCE) by stimulating ORAI1 and STIM1. Regulates KCNJ1/ROMK1 directly via its phosphorylation or indirectly via increased interaction with SLC9A3R2/NHERF2. Phosphorylates MDM2 and activates MDM2-dependent ubiquitination of p53/TP53. Phosphorylates MAPT/TAU and mediates microtubule depolymerization and neurite formation in hippocampal neurons. Phosphorylates SLC2A4/GLUT4 and up-regulates its activity. Phosphorylates APBB1/FE65 and promotes its localization to the nucleus. Phosphorylates MAPK1/ERK2 and activates it by enhancing its interaction with MAP2K1/MEK1 and MAP2K2/MEK2. Phosphorylates FBXW7 and plays an inhibitory role in the NOTCH1 signaling. Phosphorylates FOXO1 resulting in its relocalization from the nucleus to the cytoplasm. Phosphorylates FOXO3, promoting its exit from the nucleus and interference with FOXO3-dependent transcription. Phosphorylates BRAF and MAP3K3/MEKK3 and inhibits their activity. Phosphorylates SLC9A3/NHE3 in response to dexamethasone, resulting in its activation and increased localization at the cell membrane. Phosphorylates CREB1. Necessary for vascular remodeling during angiogenesis. 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. Ref.3 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19 Ref.20 Ref.21 Ref.22 Ref.23 Ref.25 Ref.26 Ref.27 Ref.28 Ref.29 Ref.30 Ref.31 Ref.32 Ref.33 Ref.34 Ref.35 Ref.36 Ref.38 Ref.39 Ref.41 Ref.42 Ref.43 Ref.48 Ref.49 Ref.51 Ref.53 Ref.55
Catalytic activity	ATP + a protein = ADP + a phosphoprotein.
Enzyme regulation	Two specific sites, one in the kinase domain (Thr-256) and the other in the C-terminal regulatory region (Ser-422), need to be phosphorylated for its full activation. Phosphorylation at Ser-397 and Ser-401 are also essential for its activity. Activated by WNK1, WNK2, WNK3 and WNK4.
Subunit structure	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. Ref.13 Ref.17 Ref.20 Ref.36 Ref.39 Ref.48 Ref.52 Ref.60
Subcellular location	Cytoplasm. Nucleus. Endoplasmic reticulum membrane. Cell membrane Ref.3 Ref.40 Ref.55. 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. Ref.3 Ref.40 Ref.55 Isoform 2: Cell membrane Ref.3 Ref.40 Ref.55.
Tissue specificity	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. Ref.3 Ref.10
Induction	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. Ref.3
Domain	Isoform 2 subcellular localization at the cell membrane and resistance to proteasomal degradation is mediated by the sequences within the first 120 amino acids.
Post-translational modification	Regulated by phosphorylation. Activated by phosphorylation on Ser-422 by mTORC2, transforming it into a substrate for PDPK1 which phosphorylates it on Thr-256. Phosphorylation on Ser-397 and Ser-401 are also essential for its activity. Phosphorylation on Ser-78 by MAPK7 is required for growth factor-induced cell cycle progression. 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. Ref.37
Sequence similarities	Belongs to the protein kinase superfamily. AGC Ser/Thr protein kinase family. Contains 1 AGC-kinase C-terminal domain. Contains 1 protein kinase domain.

Ontologies

Keywords
Biological process	Apoptosis Stress response
Cellular component	Cell membrane Cytoplasm Endoplasmic reticulum Membrane Mitochondrion Nucleus
Coding sequence diversity	Alternative promoter usage Alternative splicing Polymorphism
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Disulfide bond Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	apoptotic process Inferred from electronic annotation. Source: UniProtKB-KW long-term memory Traceable author statement Ref.59. Source: UniProtKB positive regulation of transporter activity Traceable author statement Ref.59. Source: UniProtKB regulation of apoptotic process Traceable author statement Ref.59. Source: UniProtKB regulation of blood pressure Traceable author statement Ref.57. Source: UniProtKB regulation of catalytic activity Traceable author statement Ref.59. Source: UniProtKB regulation of cell growth Traceable author statement Ref.58. Source: UniProtKB regulation of cell migration Traceable author statement Ref.58. Source: UniProtKB regulation of cell proliferation Traceable author statement Ref.59. Source: UniProtKB regulation of gastric acid secretion Traceable author statement Ref.59. Source: UniProtKB regulation of sequence-specific DNA binding transcription factor activity Traceable author statement Ref.59. Source: UniProtKB renal sodium ion absorption Traceable author statement Ref.57. Source: UniProtKB response to DNA damage stimulus Inferred from electronic annotation. Source: Compara response to stress Traceable author statement Ref.1. Source: ProtInc
Cellular_component	endoplasmic reticulum membrane Inferred from electronic annotation. Source: UniProtKB-SubCell mitochondrion Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW calcium channel regulator activity Traceable author statement Ref.59. Source: UniProtKB chloride channel regulator activity Traceable author statement Ref.59. Source: UniProtKB potassium channel regulator activity Traceable author statement Ref.59. Source: UniProtKB protein serine/threonine kinase activity Traceable author statement Ref.1. Source: ProtInc sodium channel regulator activity Traceable author statement Ref.59. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 5 isoforms produced by alternative promoter usage and alternative splicing. [Align] [Select]

Isoform 1 (identifier: O00141-1)

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

Isoform 2 (identifier: O00141-2)

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.

Isoform 3 (identifier: O00141-3)

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.

Isoform 4 (identifier: O00141-4)

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

Note: Produced by alternative splicing of isoform 1.

Isoform 5 (identifier: O00141-5)

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

Note: Produced by alternative promoter usage.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 431

431

Serine/threonine-protein kinase Sgk1

PRO_0000086642

Regions

Domain

98 – 355

258

Protein kinase

Domain

356 – 431

76

AGC-kinase C-terminal

Nucleotide binding

104 – 112

9

ATP

Region

1 – 60

60

Necessary for localization to the mitochondria

Motif

131 – 141

11

Nuclear localization signal Ref.24

Compositional bias

131 – 141

11

Glu/Lys-rich

Sites

Active site

222

1

Proton acceptor

Binding site

127

1

ATP

Amino acid modifications

Modified residue

74

1

Phosphoserine Ref.45 Ref.50

Modified residue

78

1

Phosphoserine; by MAPK7 Ref.13

Modified residue

256

1

Phosphothreonine; by PDPK1 Ref.11

Modified residue

369

1

Phosphothreonine; by PKA Ref.14

Modified residue

397

1

Phosphoserine Ref.45 Ref.47 Ref.50 Ref.54

Modified residue

401

1

Phosphoserine Ref.45 Ref.47 Ref.50

Modified residue

422

1

Phosphoserine Ref.11 Ref.44 Ref.52

Disulfide bond

193

Interchain (with C-258) Ref.60

Disulfide bond

258

Interchain (with C-193) Ref.60

Natural variations

Alternative sequence

1 – 25

25

MTVKT…VAILI → MVNKDMNGFPVKKCSAFQFF KKRVRRWIKSPMVSVDKHQS PSLKYTGSSMVHIPPGEPDF ESSLCQTCLGEHAFQRGVLP QENESCSWETQSGCEVREPC NHANILTKPDPRTFWTNDDP in isoform 2.

VSP_037784

Alternative sequence

1 – 25

25

MTVKT…VAILI → MGEMQGALARARLESLLRPR HKKRAEAQKRSESFLLSGL in isoform 3.

VSP_037785

Alternative sequence

1 – 25

25

MTVKT…VAILI → MKPSKRFFISPPSST in isoform 4.

VSP_037786

Alternative sequence

1 – 25

25

MTVKT…VAILI → MSSQSSSLSEACSREAYSSH NWALPPASRSNPQPAYPWAT RRMKEEAIKPPLK in isoform 5.

VSP_037787

Natural variant

219

1

V → I. Ref.61
Corresponds to variant rs34133418 [ dbSNP | Ensembl ].

VAR_041071

Natural variant

342

1

A → V. Ref.61
Corresponds to variant rs55932330 [ dbSNP | Ensembl ].

VAR_041072

Experimental info

Mutagenesis

127

1

K → M: Abolishes enzymatic activity. Ref.17 Ref.23 Ref.30

Mutagenesis

256

1

T → A: Low activity. Ref.11

Mutagenesis

256

1

T → D: Low activity. Ref.11

Mutagenesis

256

1

T → E: Low activity. Ref.11

Mutagenesis

298

1

Y → A: Abolishes interaction with NEDD4 and NEDD4L. Ref.17

Mutagenesis

422

1

S → A: Low activity. Ref.11 Ref.17 Ref.23 Ref.30

Mutagenesis

422

1

S → D: 10-fold activation. Ref.11 Ref.17 Ref.23 Ref.30

Sequence conflict

62

1

Q → E in CAR58097. Ref.4

Sequence conflict

152

1

K → R in CAR58096. Ref.4

Sequence conflict

196

1

E → G in CAR58095. Ref.4

Sequence conflict

228

1

I → V in BAH12848. Ref.6

Sequence conflict

371

1

P → R in CAR58097. Ref.4

Sequence conflict

381

1

D → E in CAA71138. Ref.1

Sequence conflict

381

1

D → E in CAA04146. Ref.2

Secondary structure

1

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431

Helix Strand Turn

Details...

Helix

95 – 97

3

Beta strand

98 – 105

8

Beta strand

111 – 117

7

Turn

118 – 120

3

Beta strand

123 – 130

8

Helix

131 – 133

3

Beta strand

162 – 167

6

Beta strand

169 – 177

9

Helix

184 – 191

8

Helix

196 – 215

20

Helix

225 – 227

3

Beta strand

228 – 230

3

Beta strand

232 – 234

3

Beta strand

236 – 238

3

Helix

245 – 247

3

Beta strand

256 – 258

3

Helix

266 – 269

4

Helix

277 – 292

16

Helix

302 – 311

10

Beta strand

318 – 320

3

Helix

322 – 331

10

Helix

336 – 338

3

Turn

340 – 345

6

Helix

346 – 350

5

Helix

353 – 355

3

Helix

360 – 364

5

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified March 7, 2006. Version 2. Checksum: F3697C63AB1F499D	FASTA	431	48,942
	10 20 30 40 50 60 MTVKTEAAKG TLTYSRMRGM VAILIAFMKQ RRMGLNDFIQ KIANNSYACK HPEVQSILKI 70 80 90 100 110 120 SQPQEPELMN ANPSPPPSPS QQINLGPSSN PHAKPSDFHF LKVIGKGSFG KVLLARHKAE 130 140 150 160 170 180 EVFYAVKVLQ KKAILKKKEE KHIMSERNVL LKNVKHPFLV GLHFSFQTAD KLYFVLDYIN 190 200 210 220 230 240 GGELFYHLQR ERCFLEPRAR FYAAEIASAL GYLHSLNIVY RDLKPENILL DSQGHIVLTD 250 260 270 280 290 300 FGLCKENIEH NSTTSTFCGT PEYLAPEVLH KQPYDRTVDW WCLGAVLYEM LYGLPPFYSR 310 320 330 340 350 360 NTAEMYDNIL NKPLQLKPNI TNSARHLLEG LLQKDRTKRL GAKDDFMEIK SHVFFSLINW 370 380 390 400 410 420 DDLINKKITP PFNPNVSGPN DLRHFDPEFT EEPVPNSIGK SPDSVLVTAS VKEAAEAFLG 430 FSYAPPTDSF L
	Isoform 2 (Sgk1.1) (Sgk1_v2) [UniParc]. Checksum: 8CE1E9DFB949D5A5	FASTA	526	59,904
	10 20 30 40 50 60 MVNKDMNGFP VKKCSAFQFF KKRVRRWIKS PMVSVDKHQS PSLKYTGSSM VHIPPGEPDF 70 80 90 100 110 120 ESSLCQTCLG EHAFQRGVLP QENESCSWET QSGCEVREPC NHANILTKPD PRTFWTNDDP 130 140 150 160 170 180 AFMKQRRMGL NDFIQKIANN SYACKHPEVQ SILKISQPQE PELMNANPSP PPSPSQQINL 190 200 210 220 230 240 GPSSNPHAKP SDFHFLKVIG KGSFGKVLLA RHKAEEVFYA VKVLQKKAIL KKKEEKHIMS 250 260 270 280 290 300 ERNVLLKNVK HPFLVGLHFS FQTADKLYFV LDYINGGELF YHLQRERCFL EPRARFYAAE 310 320 330 340 350 360 IASALGYLHS LNIVYRDLKP ENILLDSQGH IVLTDFGLCK ENIEHNSTTS TFCGTPEYLA 370 380 390 400 410 420 PEVLHKQPYD RTVDWWCLGA VLYEMLYGLP PFYSRNTAEM YDNILNKPLQ LKPNITNSAR 430 440 450 460 470 480 HLLEGLLQKD RTKRLGAKDD FMEIKSHVFF SLINWDDLIN KKITPPFNPN VSGPNDLRHF 490 500 510 520 DPEFTEEPVP NSIGKSPDSV LVTASVKEAA EAFLGFSYAP PTDSFL
	Isoform 3 (Sgk1.2) [UniParc]. Checksum: DC7076E1F43BCBAB	FASTA	445	50,623
	10 20 30 40 50 60 MGEMQGALAR ARLESLLRPR HKKRAEAQKR SESFLLSGLA FMKQRRMGLN DFIQKIANNS 70 80 90 100 110 120 YACKHPEVQS ILKISQPQEP ELMNANPSPP PSPSQQINLG PSSNPHAKPS DFHFLKVIGK 130 140 150 160 170 180 GSFGKVLLAR HKAEEVFYAV KVLQKKAILK KKEEKHIMSE RNVLLKNVKH PFLVGLHFSF 190 200 210 220 230 240 QTADKLYFVL DYINGGELFY HLQRERCFLE PRARFYAAEI ASALGYLHSL NIVYRDLKPE 250 260 270 280 290 300 NILLDSQGHI VLTDFGLCKE NIEHNSTTST FCGTPEYLAP EVLHKQPYDR TVDWWCLGAV 310 320 330 340 350 360 LYEMLYGLPP FYSRNTAEMY DNILNKPLQL KPNITNSARH LLEGLLQKDR TKRLGAKDDF 370 380 390 400 410 420 MEIKSHVFFS LINWDDLINK KITPPFNPNV SGPNDLRHFD PEFTEEPVPN SIGKSPDSVL 430 440 VTASVKEAAE AFLGFSYAPP TDSFL
	Isoform 4 [UniParc]. Checksum: 6BDCD1FA7D9AFD0E	FASTA	421	47,910
	10 20 30 40 50 60 MKPSKRFFIS PPSSTAFMKQ RRMGLNDFIQ KIANNSYACK HPEVQSILKI SQPQEPELMN 70 80 90 100 110 120 ANPSPPPSPS QQINLGPSSN PHAKPSDFHF LKVIGKGSFG KVLLARHKAE EVFYAVKVLQ 130 140 150 160 170 180 KKAILKKKEE KHIMSERNVL LKNVKHPFLV GLHFSFQTAD KLYFVLDYIN GGELFYHLQR 190 200 210 220 230 240 ERCFLEPRAR FYAAEIASAL GYLHSLNIVY RDLKPENILL DSQGHIVLTD FGLCKENIEH 250 260 270 280 290 300 NSTTSTFCGT PEYLAPEVLH KQPYDRTVDW WCLGAVLYEM LYGLPPFYSR NTAEMYDNIL 310 320 330 340 350 360 NKPLQLKPNI TNSARHLLEG LLQKDRTKRL GAKDDFMEIK SHVFFSLINW DDLINKKITP 370 380 390 400 410 420 PFNPNVSGPN DLRHFDPEFT EEPVPNSIGK SPDSVLVTAS VKEAAEAFLG FSYAPPTDSF L
	Isoform 5 [UniParc]. Checksum: 1B108E7CF17935E5	FASTA	459	52,119
	10 20 30 40 50 60 MSSQSSSLSE ACSREAYSSH NWALPPASRS NPQPAYPWAT RRMKEEAIKP PLKAFMKQRR 70 80 90 100 110 120 MGLNDFIQKI ANNSYACKHP EVQSILKISQ PQEPELMNAN PSPPPSPSQQ INLGPSSNPH 130 140 150 160 170 180 AKPSDFHFLK VIGKGSFGKV LLARHKAEEV FYAVKVLQKK AILKKKEEKH IMSERNVLLK 190 200 210 220 230 240 NVKHPFLVGL HFSFQTADKL YFVLDYINGG ELFYHLQRER CFLEPRARFY AAEIASALGY 250 260 270 280 290 300 LHSLNIVYRD LKPENILLDS QGHIVLTDFG LCKENIEHNS TTSTFCGTPE YLAPEVLHKQ 310 320 330 340 350 360 PYDRTVDWWC LGAVLYEMLY GLPPFYSRNT AEMYDNILNK PLQLKPNITN SARHLLEGLL 370 380 390 400 410 420 QKDRTKRLGA KDDFMEIKSH VFFSLINWDD LINKKITPPF NPNVSGPNDL RHFDPEFTEE 430 440 450 PVPNSIGKSP DSVLVTASVK EAAEAFLGFS YAPPTDSFL

References

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[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]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases 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]	"Deranged transcriptional regulation of cell-volume-sensitive kinase hSGK in diabetic nephropathy." Lang F., Klingel K., Wagner C.A., Stegen C., Waerntges S., Friedrich B., Lanzendoerfer M., Melzig J., Moschen I., Steuer S., Waldegger S., Sauter M., Paulmichl M., Gerke V., Risler T., Gamba G., Capasso G., Kandolf R. , Hebert S.C., Massry S.G., Broer S. Proc. Natl. Acad. Sci. U.S.A. 97:8157-8162(2000) [PubMed] [Europe PMC] [Abstract] 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, MASS SPECTROMETRY. 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]	"Large-scale proteomics analysis of the human kinome." Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H. Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-74; SER-397 AND SER-401, MASS SPECTROMETRY.
[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]	"mTOR complex-2 activates ENaC by phosphorylating SGK1." Lu M., Wang J., Jones K.T., Ives H.E., Feldman M.E., Yao L.J., Shokat K.M., Ashrafi K., Pearce D. J. Am. Soc. Nephrol. 21:811-818(2010) [PubMed] [Europe PMC] [Abstract] 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, MASS SPECTROMETRY. 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]	"Second AKT: the rise of SGK in cancer signalling." Bruhn M.A., Pearson R.B., Hannan R.D., Sheppard K.E. Growth Factors 28:394-408(2010) [PubMed] [Europe PMC] [Abstract] 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.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

IPI

IPI00297590.
IPI00479349.
IPI00514242.
IPI00645903.
IPI00917765.

RefSeq

NP_001137148.1. NM_001143676.1.
NP_001137149.1. NM_001143677.1.
NP_001137150.1. NM_001143678.1.
NP_005618.2. NM_005627.3.

UniGene

Hs.510078.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

O00141.

ModBase

Search...

Protein-protein interaction databases

IntAct

O00141. 9 interactions.

MINT

MINT-1338693.

PTM databases

PhosphoSite

O00141.

Proteomic databases

PaxDb

O00141.

PRIDE

O00141.

Protocols and materials databases

DNASU

6446.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000237305; ENSP00000237305; ENSG00000118515.
ENST00000367857; ENSP00000356831; ENSG00000118515.
ENST00000367858; ENSP00000356832; ENSG00000118515.
ENST00000413996; ENSP00000396242; ENSG00000118515.
ENST00000528577; ENSP00000434450; ENSG00000118515.

GeneID

6446.

KEGG

hsa:6446.

UCSC

uc003qen.4. human.
uc003qeo.4. human.
uc011ect.2. human.
uc011ecv.2. human.
uc011ecw.2. human.

Organism-specific databases

CTD

6446.

GeneCards

GC06M134490.

HGNC

HGNC:10810. SGK1.

HPA

CAB022085.
CAB025148.

MIM

602958. gene.

neXtProt

NX_O00141.

PharmGKB

PA162403013.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0515.

HOVERGEN

HBG108317.

KO

K13302.

OMA

QFYAVKV.

Enzyme and pathway databases

BRENDA

2.7.11.1. 2681.

Pathway_Interaction_DB

pi3kcipathway. Class I PI3K signaling events.
foxopathway. FoxO family signaling.
insulin_pathway. Insulin Pathway.

Gene expression databases

ArrayExpress

O00141.

Bgee

O00141.

CleanEx

HS_SGK1.

Genevestigator

O00141.

GermOnline

ENSG00000118515. Homo sapiens.

Family and domain databases

InterPro

IPR000961. AGC-kinase_C.
IPR011009. Kinase-like_dom.
IPR017892. Pkinase_C.
IPR000719. Prot_kinase_cat_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]

Pfam

PF00069. Pkinase. 1 hit.
PF00433. Pkinase_C. 1 hit.
[Graphical view]

SMART

SM00133. S_TK_X. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]

SUPFAM

SSF56112. Kinase_like. 1 hit.

PROSITE

PS51285. AGC_KINASE_CTER. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

O00141.

ChEMBL

CHEMBL2343.

ChiTaRS

SGK1. human.

EvolutionaryTrace

O00141.

GenomeRNAi

6446.

NextBio

25053.

SOURCE

Search...

Entry information

Entry name

SGK1_HUMAN

Accession

Primary (citable) accession number: O00141
Secondary accession number(s): B7UUP7 , B7UUP8, B7UUP9, B7Z5B2, E1P583, Q5TCN2, Q5TCN3, Q5TCN4, Q5VY65, Q9UN56

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 15, 1998
Last sequence update:	March 7, 2006
Last modified:	May 1, 2013
This is version 135 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.