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O00141 (SGK1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 144. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length431 AA.
Sequence statusComplete.
Protein existenceEvidence 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 processApoptosis
Stress response
   Cellular componentCell membrane
Cytoplasm
Endoplasmic reticulum
Membrane
Mitochondrion
Nucleus
   Coding sequence diversityAlternative promoter usage
Alternative splicing
Polymorphism
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
   PTMDisulfide bond
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processapoptotic process

Inferred from electronic annotation. Source: UniProtKB-KW

cellular response to DNA damage stimulus

Inferred from electronic annotation. Source: Ensembl

ion transmembrane transport

Traceable author statement. Source: Reactome

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 stress

Traceable author statement Ref.1. Source: ProtInc

   Cellular_componentcytosol

Traceable author statement. Source: Reactome

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_functionATP 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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 431431Serine/threonine-protein kinase Sgk1
PRO_0000086642

Regions

Domain98 – 355258Protein kinase
Domain356 – 43176AGC-kinase C-terminal
Nucleotide binding104 – 1129ATP
Region1 – 6060Necessary for localization to the mitochondria
Motif131 – 14111Nuclear localization signal Ref.24
Compositional bias131 – 14111Glu/Lys-rich

Sites

Active site2221Proton acceptor
Binding site1271ATP

Amino acid modifications

Modified residue741Phosphoserine Ref.45 Ref.50
Modified residue781Phosphoserine; by MAPK7 Ref.13
Modified residue2561Phosphothreonine; by PDPK1 Ref.11
Modified residue3691Phosphothreonine; by PKA Ref.14
Modified residue3971Phosphoserine Ref.45 Ref.47 Ref.50 Ref.54
Modified residue4011Phosphoserine Ref.45 Ref.47 Ref.50
Modified residue4221Phosphoserine Ref.11 Ref.44 Ref.52
Disulfide bond193Interchain (with C-258) Ref.60
Disulfide bond258Interchain (with C-193) Ref.60

Natural variations

Alternative sequence1 – 2525MTVKT…VAILI → MVNKDMNGFPVKKCSAFQFF KKRVRRWIKSPMVSVDKHQS PSLKYTGSSMVHIPPGEPDF ESSLCQTCLGEHAFQRGVLP QENESCSWETQSGCEVREPC NHANILTKPDPRTFWTNDDP in isoform 2.
VSP_037784
Alternative sequence1 – 2525MTVKT…VAILI → MGEMQGALARARLESLLRPR HKKRAEAQKRSESFLLSGL in isoform 3.
VSP_037785
Alternative sequence1 – 2525MTVKT…VAILI → MKPSKRFFISPPSST in isoform 4.
VSP_037786
Alternative sequence1 – 2525MTVKT…VAILI → MSSQSSSLSEACSREAYSSH NWALPPASRSNPQPAYPWAT RRMKEEAIKPPLK in isoform 5.
VSP_037787
Natural variant2191V → I. Ref.61
Corresponds to variant rs34133418 [ dbSNP | Ensembl ].
VAR_041071
Natural variant3421A → V. Ref.61
Corresponds to variant rs55932330 [ dbSNP | Ensembl ].
VAR_041072

Experimental info

Mutagenesis1271K → M: Abolishes enzymatic activity. Ref.17 Ref.23 Ref.30
Mutagenesis2561T → A: Low activity. Ref.11
Mutagenesis2561T → D: Low activity. Ref.11
Mutagenesis2561T → E: Low activity. Ref.11
Mutagenesis2981Y → A: Abolishes interaction with NEDD4 and NEDD4L. Ref.17
Mutagenesis4221S → A: Low activity. Ref.11 Ref.17 Ref.23 Ref.30
Mutagenesis4221S → D: 10-fold activation. Ref.11 Ref.17 Ref.23 Ref.30
Sequence conflict621Q → E in CAR58097. Ref.4
Sequence conflict1521K → R in CAR58096. Ref.4
Sequence conflict1961E → G in CAR58095. Ref.4
Sequence conflict2281I → V in BAH12848. Ref.6
Sequence conflict3711P → R in CAR58097. Ref.4
Sequence conflict3811D → E in CAA71138. Ref.1
Sequence conflict3811D → E in CAA04146. Ref.2

Secondary structure

................................................ 431
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified March 7, 2006. Version 2.
Checksum: F3697C63AB1F499D

FASTA43148,942
        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 

« Hide

Isoform 2 (Sgk1.1) (Sgk1_v2) [UniParc].

Checksum: 8CE1E9DFB949D5A5
Show »

FASTA52659,904
Isoform 3 (Sgk1.2) [UniParc].

Checksum: DC7076E1F43BCBAB
Show »

FASTA44550,623
Isoform 4 [UniParc].

Checksum: 6BDCD1FA7D9AFD0E
Show »

FASTA42147,910
Isoform 5 [UniParc].

Checksum: 1B108E7CF17935E5
Show »

FASTA45952,119

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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. expand/collapse author list , 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. expand/collapse author list , 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, 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]"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, 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]"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, 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]"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. expand/collapse author list , 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.
RefSeqNP_001137148.1. NM_001143676.1.
NP_001137149.1. NM_001143677.1.
NP_001137150.1. NM_001143678.1.
NP_005618.2. NM_005627.3.
UniGeneHs.510078.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2R5TX-ray1.90A60-431[»]
3HDMX-ray2.60A60-431[»]
3HDNX-ray3.10A60-431[»]
ProteinModelPortalO00141.
SMRO00141. Positions 36-425.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112344. 46 interactions.
IntActO00141. 10 interactions.
MINTMINT-1338693.

Chemistry

BindingDBO00141.
ChEMBLCHEMBL2343.
GuidetoPHARMACOLOGY1534.

PTM databases

PhosphoSiteO00141.

Proteomic databases

PaxDbO00141.
PRIDEO00141.

Protocols and materials databases

DNASU6446.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000237305; ENSP00000237305; ENSG00000118515. [O00141-1]
ENST00000367857; ENSP00000356831; ENSG00000118515. [O00141-4]
ENST00000367858; ENSP00000356832; ENSG00000118515. [O00141-2]
ENST00000413996; ENSP00000396242; ENSG00000118515. [O00141-3]
ENST00000528577; ENSP00000434450; ENSG00000118515. [O00141-5]
GeneID6446.
KEGGhsa:6446.
UCSCuc003qen.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

CTD6446.
GeneCardsGC06M134490.
HGNCHGNC:10810. SGK1.
HPACAB022085.
CAB025148.
HPA051251.
MIM602958. gene.
neXtProtNX_O00141.
PharmGKBPA162403013.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0515.
HOVERGENHBG108317.
KOK13302.
OMALKYTGPS.
OrthoDBEOG7Q5HCW.
TreeFamTF320906.

Enzyme and pathway databases

BRENDA2.7.11.1. 2681.
ReactomeREACT_15518. Transmembrane transport of small molecules.
SignaLinkO00141.

Gene expression databases

ArrayExpressO00141.
BgeeO00141.
CleanExHS_SGK1.
GenevestigatorO00141.

Family and domain databases

InterProIPR000961. 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_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamPF00069. Pkinase. 1 hit.
PF00433. Pkinase_C. 1 hit.
[Graphical view]
SMARTSM00133. S_TK_X. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 1 hit.
PROSITEPS51285. 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]
ProtoNetSearch...

Other

ChiTaRSSGK1. human.
EvolutionaryTraceO00141.
GeneWikiSGK.
GenomeRNAi6446.
NextBio25053.
PROO00141.
SOURCESearch...

Entry information

Entry nameSGK1_HUMAN
AccessionPrimary (citable) accession number: O00141
Secondary accession number(s): B7UUP7 expand/collapse secondary AC list , 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: March 19, 2014
This is version 144 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 6

Human chromosome 6: entries, gene names and cross-references to MIM