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O00141

- SGK1_HUMAN

UniProt

O00141 - SGK1_HUMAN

Protein

Serine/threonine-protein kinase Sgk1

Gene

SGK1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 150 (01 Oct 2014)
      Sequence version 2 (07 Mar 2006)
      Previous versions | rss
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    Functioni

    Serine/threonine-protein kinase which is involved in the regulation of a wide variety of ion channels, membrane transporters, cellular enzymes, transcription factors, neuronal excitability, cell growth, proliferation, survival, migration and apoptosis. Plays an important role in cellular stress response. Contributes to regulation of renal Na+ retention, renal K+ elimination, salt appetite, gastric acid secretion, intestinal Na+/H+ exchange and nutrient transport, insulin-dependent salt sensitivity of blood pressure, salt sensitivity of peripheral glucose uptake, cardiac repolarization and memory consolidation. Up-regulates Na+ channels: SCNN1A/ENAC, SCN5A and ASIC1/ACCN2, K+ channels: KCNJ1/ROMK1, KCNA1-5, KCNQ1-5 and KCNE1, epithelial Ca2+ channels: TRPV5 and TRPV6, chloride channels: BSND, CLCN2 and CFTR, glutamate transporters: SLC1A3/EAAT1, SLC1A2 /EAAT2, SLC1A1/EAAT3, SLC1A6/EAAT4 and SLC1A7/EAAT5, amino acid transporters: SLC1A5/ASCT2, SLC38A1/SN1 and SLC6A19, creatine transporter: SLC6A8, Na+/dicarboxylate cotransporter: SLC13A2/NADC1, Na+-dependent phosphate cotransporter: SLC34A2/NAPI-2B, glutamate receptor: GRIK2/GLUR6. Up-regulates carriers: SLC9A3/NHE3, SLC12A1/NKCC2, SLC12A3/NCC, SLC5A3/SMIT, SLC2A1/GLUT1, SLC5A1/SGLT1 and SLC15A2/PEPT2. Regulates enzymes: GSK3A/B, PMM2 and Na+/K+ ATPase, and transcription factors: CTNNB1 and nuclear factor NF-kappa-B. Stimulates sodium transport into epithelial cells by enhancing the stability and expression of SCNN1A/ENAC. This is achieved by phosphorylating the NEDD4L ubiquitin E3 ligase, promoting its interaction with 14-3-3 proteins, thereby preventing it from binding to SCNN1A/ENAC and targeting it for degradation. Regulates store-operated Ca(+2) entry (SOCE) by stimulating ORAI1 and STIM1. Regulates KCNJ1/ROMK1 directly via its phosphorylation or indirectly via increased interaction with SLC9A3R2/NHERF2. Phosphorylates MDM2 and activates MDM2-dependent ubiquitination of p53/TP53. Phosphorylates MAPT/TAU and mediates microtubule depolymerization and neurite formation in hippocampal neurons. Phosphorylates SLC2A4/GLUT4 and up-regulates its activity. Phosphorylates APBB1/FE65 and promotes its localization to the nucleus. Phosphorylates MAPK1/ERK2 and activates it by enhancing its interaction with MAP2K1/MEK1 and MAP2K2/MEK2. Phosphorylates FBXW7 and plays an inhibitory role in the NOTCH1 signaling. Phosphorylates FOXO1 resulting in its relocalization from the nucleus to the cytoplasm. Phosphorylates FOXO3, promoting its exit from the nucleus and interference with FOXO3-dependent transcription. Phosphorylates BRAF and MAP3K3/MEKK3 and inhibits their activity. Phosphorylates SLC9A3/NHE3 in response to dexamethasone, resulting in its activation and increased localization at the cell membrane. Phosphorylates CREB1. Necessary for vascular remodeling during angiogenesis. Sustained high levels and activity may contribute to conditions such as hypertension and diabetic nephropathy. Isoform 2 exhibited a greater effect on cell plasma membrane expression of SCNN1A/ENAC and Na+ transport than isoform 1.32 Publications

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.

    Enzyme regulationi

    Two specific sites, one in the kinase domain (Thr-256) and the other in the C-terminal regulatory region (Ser-422), need to be phosphorylated for its full activation. Phosphorylation at Ser-397 and Ser-401 are also essential for its activity. Activated by WNK1, WNK2, WNK3 and WNK4.

    Sites

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

    Regions

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

    GO - Molecular functioni

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

    GO - Biological processi

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

    Keywords - Molecular functioni

    Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Biological processi

    Apoptosis, Stress response

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BRENDAi2.7.11.1. 2681.
    ReactomeiREACT_160189. Stimuli-sensing channels.
    SignaLinkiO00141.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Serine/threonine-protein kinase Sgk1 (EC:2.7.11.1)
    Alternative name(s):
    Serum/glucocorticoid-regulated kinase 1
    Gene namesi
    Name:SGK1
    Synonyms:SGK
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 6

    Organism-specific databases

    HGNCiHGNC:10810. SGK1.

    Subcellular locationi

    Cytoplasm. Nucleus. Endoplasmic reticulum membrane. Cell membrane. Mitochondrion
    Note: The subcellular localization is controlled by the cell cycle, as well as by exposure to specific hormones and environmental stress stimuli. In proliferating cells, it shuttles between the nucleus and cytoplasm in synchrony with the cell cycle, and in serum/growth factor-stimulated cells it resides in the nucleus. In contrast, after exposure to environmental stress or treatment with glucocorticoids, it is detected in the cytoplasm and with certain stress conditions is associated with the mitochondria. In osmoregulation through the epithelial sodium channel, it can be localized to the cytoplasmic surface of the cell membrane. Nuclear, upon phosphorylation.

    GO - Cellular componenti

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

    Keywords - Cellular componenti

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

    Pathology & Biotechi

    Mutagenesis

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

    Organism-specific databases

    PharmGKBiPA162403013.

    PTM / Processingi

    Molecule processing

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

    Amino acid modifications

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

    Post-translational modificationi

    Regulated by phosphorylation. Activated by phosphorylation on Ser-422 by mTORC2, transforming it into a substrate for PDPK1 which phosphorylates it on Thr-256. Phosphorylation on Ser-397 and Ser-401 are also essential for its activity. Phosphorylation on Ser-78 by MAPK7 is required for growth factor-induced cell cycle progression.9 Publications
    Ubiquitinated by NEDD4L; which promotes proteasomal degradation. Ubiquitinated by SYVN1 at the endoplasmic reticulum; which promotes rapid proteasomal degradation and maintains a high turnover rate in resting cells. Isoform 2 shows enhanced stability.1 Publication

    Keywords - PTMi

    Disulfide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiO00141.
    PaxDbiO00141.
    PRIDEiO00141.

    PTM databases

    PhosphoSiteiO00141.

    Expressioni

    Tissue specificityi

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

    Inductioni

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

    Gene expression databases

    ArrayExpressiO00141.
    BgeeiO00141.
    CleanExiHS_SGK1.
    GenevestigatoriO00141.

    Organism-specific databases

    HPAiCAB022085.
    CAB025148.
    HPA051251.

    Interactioni

    Subunit structurei

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

    Protein-protein interaction databases

    BioGridi112344. 46 interactions.
    DIPiDIP-42464N.
    IntActiO00141. 10 interactions.
    MINTiMINT-1338693.

    Structurei

    Secondary structure

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

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2R5TX-ray1.90A60-431[»]
    3HDMX-ray2.60A60-431[»]
    3HDNX-ray3.10A60-431[»]
    ProteinModelPortaliO00141.
    SMRiO00141. Positions 36-427.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO00141.

    Family & Domainsi

    Domains and Repeats

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

    Region

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

    Motif

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

    Compositional bias

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

    Domaini

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

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0515.
    HOVERGENiHBG108317.
    KOiK13302.
    OMAiQFYAVKV.
    OrthoDBiEOG7Q5HCW.
    PhylomeDBiO00141.
    TreeFamiTF320906.

    Family and domain databases

    InterProiIPR000961. AGC-kinase_C.
    IPR011009. Kinase-like_dom.
    IPR017892. Pkinase_C.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR002290. Ser/Thr_dual-sp_kinase_dom.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view]
    PfamiPF00069. Pkinase. 1 hit.
    PF00433. Pkinase_C. 1 hit.
    [Graphical view]
    SMARTiSM00133. S_TK_X. 1 hit.
    SM00220. S_TKc. 1 hit.
    [Graphical view]
    SUPFAMiSSF56112. SSF56112. 1 hit.
    PROSITEiPS51285. AGC_KINASE_CTER. 1 hit.
    PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view]

    Sequences (5)i

    Sequence statusi: Complete.

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

    Isoform 1 (identifier: O00141-1) [UniParc]FASTAAdd to Basket

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

    « Hide

    MTVKTEAAKG TLTYSRMRGM VAILIAFMKQ RRMGLNDFIQ KIANNSYACK    50
    HPEVQSILKI SQPQEPELMN ANPSPPPSPS QQINLGPSSN PHAKPSDFHF 100
    LKVIGKGSFG KVLLARHKAE EVFYAVKVLQ KKAILKKKEE KHIMSERNVL 150
    LKNVKHPFLV GLHFSFQTAD KLYFVLDYIN GGELFYHLQR ERCFLEPRAR 200
    FYAAEIASAL GYLHSLNIVY RDLKPENILL DSQGHIVLTD FGLCKENIEH 250
    NSTTSTFCGT PEYLAPEVLH KQPYDRTVDW WCLGAVLYEM LYGLPPFYSR 300
    NTAEMYDNIL NKPLQLKPNI TNSARHLLEG LLQKDRTKRL GAKDDFMEIK 350
    SHVFFSLINW DDLINKKITP PFNPNVSGPN DLRHFDPEFT EEPVPNSIGK 400
    SPDSVLVTAS VKEAAEAFLG FSYAPPTDSF L 431
    Length:431
    Mass (Da):48,942
    Last modified:March 7, 2006 - v2
    Checksum:iF3697C63AB1F499D
    GO
    Isoform 2 (identifier: O00141-2) [UniParc]FASTAAdd to Basket

    Also known as: Sgk1.1, Sgk1_v2

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

    Note: Produced by alternative promoter usage.

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

    Also known as: Sgk1.2

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

    Note: Produced by alternative promoter usage.

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

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

    Note: Produced by alternative splicing of isoform 1.

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

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

    Note: Produced by alternative promoter usage.

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

    Experimental Info

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

    Natural variant

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

    Alternative sequence

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

    Sequence databases

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

    Genome annotation databases

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

    Keywords - Coding sequence diversityi

    Alternative promoter usage, Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

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

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2R5T X-ray 1.90 A 60-431 [» ]
    3HDM X-ray 2.60 A 60-431 [» ]
    3HDN X-ray 3.10 A 60-431 [» ]
    ProteinModelPortali O00141.
    SMRi O00141. Positions 36-427.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112344. 46 interactions.
    DIPi DIP-42464N.
    IntActi O00141. 10 interactions.
    MINTi MINT-1338693.

    Chemistry

    BindingDBi O00141.
    ChEMBLi CHEMBL2343.
    GuidetoPHARMACOLOGYi 1534.

    PTM databases

    PhosphoSitei O00141.

    Proteomic databases

    MaxQBi O00141.
    PaxDbi O00141.
    PRIDEi O00141.

    Protocols and materials databases

    DNASUi 6446.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

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

    Organism-specific databases

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

    Phylogenomic databases

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

    Enzyme and pathway databases

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

    Miscellaneous databases

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

    Gene expression databases

    ArrayExpressi O00141.
    Bgeei O00141.
    CleanExi HS_SGK1.
    Genevestigatori O00141.

    Family and domain databases

    InterProi IPR000961. AGC-kinase_C.
    IPR011009. Kinase-like_dom.
    IPR017892. Pkinase_C.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR002290. Ser/Thr_dual-sp_kinase_dom.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view ]
    Pfami PF00069. Pkinase. 1 hit.
    PF00433. Pkinase_C. 1 hit.
    [Graphical view ]
    SMARTi SM00133. S_TK_X. 1 hit.
    SM00220. S_TKc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56112. SSF56112. 1 hit.
    PROSITEi PS51285. AGC_KINASE_CTER. 1 hit.
    PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and characterization of a putative human serine/threonine protein kinase transcriptionally modified during anisotonic and isotonic alterations of cell volume."
      Waldegger S., Barth P., Raber G., Lang F.
      Proc. Natl. Acad. Sci. U.S.A. 94:4440-4445(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. "Genomic organization and chromosomal localization of the human SGK protein kinase gene."
      Waldegger S., Erdel M., Nagl U.O., Barth P., Raber G., Steuer S., Utermann G., Paulmichl M., Lang F.
      Genomics 51:299-302(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING (ISOFORM 1).
    3. "An evolutionarily conserved N-terminal Sgk1 variant with enhanced stability and improved function."
      Raikwar N.S., Snyder P.M., Thomas C.P.
      Am. J. Physiol. 295:F1440-F1448(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, ALTERNATIVE PROMOTER USAGE, INDUCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
      Tissue: Brain.
    4. "Transcriptional variants of serum/glucocorticoid regulated kinase 1 show differential localisation and regulation."
      Hall B.A., Blakeley S., Daniels N.A., Jamieson D., Brickley D., Reynolds N.J., Conzen S.D., Jackson T.R.
      Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3; 4 AND 5), ALTERNATIVE PROMOTER USAGE.
      Tissue: Glioblastoma, Hippocampus and Skin.
    5. "A catalogue of genes in the human dermal papilla cells as identified by expressed sequence tags."
      Kim M.K., Kim Y.H., Seo J.M., Lee H.M., Chung H.J., Sohn M.Y., Hwang S.Y., Im S.U., Jung E.J., Lee J.H., Kim J.C.
      Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Hair follicle dermal papilla.
    6. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
      Tissue: Brain.
    7. "The DNA sequence and analysis of human chromosome 6."
      Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
      , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
      Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    9. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Cervix.
    10. "Characterization of the structure and regulation of two novel isoforms of serum- and glucocorticoid-induced protein kinase."
      Kobayashi T., Deak M., Morrice N., Cohen P.
      Biochem. J. 344:189-197(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.
    11. "Activation of serum- and glucocorticoid-regulated protein kinase by agonists that activate phosphatidylinositide 3-kinase is mediated by 3-phosphoinositide-dependent protein kinase-1 (PDK1) and PDK2."
      Kobayashi T., Cohen P.
      Biochem. J. 339:319-328(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT THR-256 AND SER-422, MUTAGENESIS OF THR-256 AND SER-422.
      Tissue: Brain.
    12. Cited for: CHARACTERIZATION.
    13. "BMK1 mediates growth factor-induced cell proliferation through direct cellular activation of serum and glucocorticoid-inducible kinase."
      Hayashi M., Tapping R.I., Chao T.H., Lo J.F., King C.C., Yang Y., Lee J.D.
      J. Biol. Chem. 276:8631-8634(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-78 BY MAPK7, INTERACTION WITH MAPK7.
    14. "Activation of serum- and glucocorticoid-induced protein kinase (Sgk) by cyclic AMP and insulin."
      Perrotti N., He R.A., Phillips S.A., Haft C.R., Taylor S.I.
      J. Biol. Chem. 276:9406-9412(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT THR-369 BY PKA.
    15. "Serum- and glucocorticoid-inducible kinase SGK phosphorylates and negatively regulates B-Raf."
      Zhang B.H., Tang E.D., Zhu T., Greenberg M.E., Vojtek A.B., Guan K.L.
      J. Biol. Chem. 276:31620-31626(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF BRAF.
    16. "Protein kinase SGK mediates survival signals by phosphorylating the forkhead transcription factor FKHRL1 (FOXO3a)."
      Brunet A., Park J., Tran H., Hu L.S., Hemmings B.A., Greenberg M.E.
      Mol. Cell. Biol. 21:952-965(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    17. "Serum and glucocorticoid-regulated kinase modulates Nedd4-2-mediated inhibition of the epithelial Na+ channel."
      Snyder P.M., Olson D.R., Thomas B.C.
      J. Biol. Chem. 277:5-8(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NEDD4 AND NEDD4L, MUTAGENESIS OF LYS-127; TYR-298 AND SER-422, FUNCTION.
    18. "Activation of Na+/K+-ATPase by the serum and glucocorticoid-dependent kinase isoforms."
      Henke G., Setiawan I., Boehmer C., Lang F.
      Kidney Blood Press. Res. 25:370-374(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN REGULATION OF NA(+)/K(+) ATPASE.
    19. "K(+) channel activation by all three isoforms of serum- and glucocorticoid-dependent protein kinase SGK."
      Gamper N., Fillon S., Feng Y., Friedrich B., Lang P.A., Henke G., Huber S.M., Kobayashi T., Cohen P., Lang F.
      Pflugers Arch. 445:60-66(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    20. "Molecular requirements for the regulation of the renal outer medullary K(+) channel ROMK1 by the serum- and glucocorticoid-inducible kinase SGK1."
      Palmada M., Embark H.M., Yun C., Bohmer C., Lang F.
      Biochem. Biophys. Res. Commun. 311:629-634(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH SLC9A3R2/NHERF2 AND KCNJ1/ROMK1.
    21. "Serum and glucocorticoid inducible kinases in the regulation of the cardiac sodium channel SCN5A."
      Boehmer C., Wilhelm V., Palmada M., Wallisch S., Henke G., Brinkmeier H., Cohen P., Pieske B., Lang F.
      Cardiovasc. Res. 57:1079-1084(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN REGULATION OF SCN5A.
    22. "Inhibition of mitogen-activated kinase kinase kinase 3 activity through phosphorylation by the serum- and glucocorticoid-induced kinase 1."
      Chun J., Kwon T., Kim D.J., Park I., Chung G., Lee E.J., Hong S.K., Chang S.I., Kim H.Y., Kang S.S.
      J. Biochem. 133:103-108(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF MAP3K3/MEKK3.
    23. "Regulation of the glutamate transporter EAAT1 by the ubiquitin ligase Nedd4-2 and the serum and glucocorticoid-inducible kinase isoforms SGK1/3 and protein kinase B."
      Boehmer C., Henke G., Schniepp R., Palmada M., Rothstein J.D., Broeer S., Lang F.
      J. Neurochem. 86:1181-1188(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN REGULATION OF KCNA3/KV1.3, MUTAGENESIS OF LYS-127 AND SER-422.
    24. "Importin-alpha mediates the regulated nuclear targeting of serum- and glucocorticoid-inducible protein kinase (Sgk) by recognition of a nuclear localization signal in the kinase central domain."
      Maiyar A.C., Leong M.L., Firestone G.L.
      Mol. Biol. Cell 14:1221-1239(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEAR LOCALIZATION SIGNAL.
    25. "Regulation of KCNE1-dependent K(+) current by the serum and glucocorticoid-inducible kinase (SGK) isoforms."
      Embark H.M., Boehmer C., Vallon V., Luft F., Lang F.
      Pflugers Arch. 445:601-606(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN REGULATION OF KCNE1 AND KCNQ1.
    26. "Regulation of intestinal phosphate cotransporter NaPi IIb by ubiquitin ligase Nedd4-2 and by serum- and glucocorticoid-dependent kinase 1."
      Palmada M., Dieter M., Speil A., Boehmer C., Mack A.F., Wagner H.J., Klingel K., Kandolf R., Murer H., Biber J., Closs E.I., Lang F.
      Am. J. Physiol. 287:G143-G150(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN REGULATION OF SLC34A2/NAPI-2B, FUNCTION IN PHOSPHORYLATION OF NEDD4L.
    27. "Stimulation of renal Na+ dicarboxylate cotransporter 1 by Na+/H+ exchanger regulating factor 2, serum and glucocorticoid inducible kinase isoforms, and protein kinase B."
      Boehmer C., Embark H.M., Bauer A., Palmada M., Yun C.H., Weinman E.J., Endou H., Cohen P., Lahme S., Bichler K.H., Lang F.
      Biochem. Biophys. Res. Commun. 313:998-1003(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN REGULATION OF SLC13A2/NADC1.
    28. "Regulation of the epithelial Ca2+ channel TRPV5 by the NHE regulating factor NHERF2 and the serum and glucocorticoid inducible kinase isoforms SGK1 and SGK3 expressed in Xenopus oocytes."
      Embark H.M., Setiawan I., Poppendieck S., van de Graaf S.F., Boehmer C., Palmada M., Wieder T., Gerstberger R., Cohen P., Yun C.C., Bindels R.J., Lang F.
      Cell. Physiol. Biochem. 14:203-212(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN REGULATION OF TRPV5.
    29. "A novel pathway of epithelial sodium channel activation involves a serum- and glucocorticoid-inducible kinase consensus motif in the C terminus of the channel's alpha-subunit."
      Diakov A., Korbmacher C.
      J. Biol. Chem. 279:38134-38142(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    30. "Regulation of the voltage gated K+ channel Kv1.3 by the ubiquitin ligase Nedd4-2 and the serum and glucocorticoid inducible kinase SGK1."
      Henke G., Maier G., Wallisch S., Boehmer C., Lang F.
      J. Cell. Physiol. 199:194-199(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF LYS-127 AND SER-422.
    31. "Regulation of CLC-Ka/barttin by the ubiquitin ligase Nedd4-2 and the serum- and glucocorticoid-dependent kinases."
      Embark H.M., Boehmer C., Palmada M., Rajamanickam J., Wyatt A.W., Wallisch S., Capasso G., Waldegger P., Seyberth H.W., Waldegger S., Lang F.
      Kidney Int. 66:1918-1925(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN REGULATION OF BSND.
    32. "Activation of NHE3 by dexamethasone requires phosphorylation of NHE3 at Ser663 by SGK1."
      Wang D., Sun H., Lang F., Yun C.C.
      Am. J. Physiol. 289:C802-C810(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF SLC9A3/NHE3.
    33. "The serine/threonine kinases SGK1, 3 and PKB stimulate the amino acid transporter ASCT2."
      Palmada M., Speil A., Jeyaraj S., Boehmer C., Lang F.
      Biochem. Biophys. Res. Commun. 331:272-277(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN REGULATION OF SLC1A5/ASCT2.
    34. "Regulation of the excitatory amino acid transporter EAAT5 by the serum and glucocorticoid dependent kinases SGK1 and SGK3."
      Boehmer C., Rajamanickam J., Schniepp R., Kohler K., Wulff P., Kuhl D., Palmada M., Lang F.
      Biochem. Biophys. Res. Commun. 329:738-742(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN REGULATION OF SLC1A7/EAAT5.
    35. "Stimulation of the creatine transporter SLC6A8 by the protein kinases SGK1 and SGK3."
      Shojaiefard M., Christie D.L., Lang F.
      Biochem. Biophys. Res. Commun. 334:742-746(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN REGULATION OF SLC6A8.
    36. "Serum/glucocorticoid-inducible kinase can phosphorylate the cyclic AMP response element binding protein, CREB."
      David S., Kalb R.G.
      FEBS Lett. 579:1534-1538(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF CREB1, INTERACTION WITH CREB1.
    37. "Nedd4-2 phosphorylation induces serum and glucocorticoid-regulated kinase (SGK) ubiquitination and degradation."
      Zhou R., Snyder P.M.
      J. Biol. Chem. 280:4518-4523(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: UBIQUITINATION.
    38. "SGK1 kinase upregulates GLUT1 activity and plasma membrane expression."
      Palmada M., Boehmer C., Akel A., Rajamanickam J., Jeyaraj S., Keller K., Lang F.
      Diabetes 55:421-427(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN REGULATION OF SLC2A1/GLUT1.
    39. "Serum- and glucocorticoid-inducible kinase 1 (SGK1) increases neurite formation through microtubule depolymerization by SGK1 and by SGK1 phosphorylation of tau."
      Yang Y.C., Lin C.H., Lee E.H.
      Mol. Cell. Biol. 26:8357-8370(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF MAPT/TAU, INTERACTION WITH MAPT/TAU.
    40. "Subcellular location of serum- and glucocorticoid-induced kinase-1 in renal and mammary epithelial cells."
      Cordas E., Naray-Fejes-Toth A., Fejes-Toth G.
      Am. J. Physiol. 292:C1971-C1981(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    41. "Role of SGK1 kinase in regulating glucose transport via glucose transporter GLUT4."
      Jeyaraj S., Boehmer C., Lang F., Palmada M.
      Biochem. Biophys. Res. Commun. 356:629-635(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF SLC2A4/GLUT4.
    42. "Regulation of the epithelial calcium channel TRPV6 by the serum and glucocorticoid-inducible kinase isoforms SGK1 and SGK3."
      Boehmer C., Palmada M., Kenngott C., Lindner R., Klaus F., Laufer J., Lang F.
      FEBS Lett. 581:5586-5590(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN REGULATION OF TRPV6.
    43. "Regulation Fe65 localization to the nucleus by SGK1 phosphorylation of its Ser566 residue."
      Lee E.J., Chun J., Hyun S., Ahn H.R., Jeong J.M., Hong S.K., Hong J.T., Chang I.K., Jeon H.Y., Han Y.S., Auh C.K., Park J.I., Kang S.S.
      BMB Rep. 41:41-47(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF APBB1/FE65.
    44. "mTOR complex 2 (mTORC2) controls hydrophobic motif phosphorylation and activation of serum- and glucocorticoid-induced protein kinase 1 (SGK1)."
      Garcia-Martinez J.M., Alessi D.R.
      Biochem. J. 416:375-385(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-422 BY MTORC2.
    45. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
      Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
      Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-74; SER-397 AND SER-401, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    46. "A brain-specific SGK1 splice isoform regulates expression of ASIC1 in neurons."
      Arteaga M.F., Coric T., Straub C., Canessa C.M.
      Proc. Natl. Acad. Sci. U.S.A. 105:4459-4464(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: ALTERNATIVE PROMOTER USAGE (ISOFORMS 2 AND 3).
    47. "Regulation of a third conserved phosphorylation site in SGK1."
      Chen W., Chen Y., Xu B.E., Juang Y.C., Stippec S., Zhao Y., Cobb M.H.
      J. Biol. Chem. 284:3453-3460(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-397 AND SER-401.
    48. "Protein kinase SGK1 enhances MEK/ERK complex formation through the phosphorylation of ERK2: implication for the positive regulatory role of SGK1 on the ERK function during liver regeneration."
      Won M., Park K.A., Byun H.S., Kim Y.R., Choi B.L., Hong J.H., Park J., Seok J.H., Lee Y.H., Cho C.H., Song I.S., Kim Y.K., Shen H.M., Hur G.M.
      J. Hepatol. 51:67-76(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF MAPK1/ERK2, INTERACTION WITH MAPK3/ERK1; MAPK1/ERK2; MAP2K1/MEK1 AND MAP2K2/MEK2.
    49. "Sgk1 activates MDM2-dependent p53 degradation and affects cell proliferation, survival, and differentiation."
      Amato R., D'Antona L., Porciatti G., Agosti V., Menniti M., Rinaldo C., Costa N., Bellacchio E., Mattarocci S., Fuiano G., Soddu S., Paggi M.G., Lang F., Perrotti N.
      J. Mol. Med. 87:1221-1239(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF MDM2.
    50. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-74; SER-397 AND SER-401, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    51. "The serum and glucocorticoid inducible kinases SGK1-3 stimulate the neutral amino acid transporter SLC6A19."
      Boehmer C., Sopjani M., Klaus F., Lindner R., Laufer J., Jeyaraj S., Lang F., Palmada M.
      Cell. Physiol. Biochem. 25:723-732(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN REGULATION OF SLC6A19.
    52. Cited for: PHOSPHORYLATION AT SER-422 BY MTORC2, INTERACTION WITH MTORC2.
    53. "Interaction of serum- and glucocorticoid regulated kinase 1 (SGK1) with the WW-domains of Nedd4-2 is required for epithelial sodium channel regulation."
      Wiemuth D., Lott J.S., Ly K., Ke Y., Teesdale-Spittle P., Snyder P.M., McDonald F.J.
      PLoS ONE 5:E12163-E12163(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    54. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-397, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    55. "Serum- and glucocorticoid-induced kinase 3 in recycling endosomes mediates acute activation of Na+/H+ exchanger NHE3 by glucocorticoids."
      He P., Lee S.J., Lin S., Seidler U., Lang F., Fejes-Toth G., Naray-Fejes-Toth A., Yun C.C.
      Mol. Biol. Cell 22:3812-3825(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN REGULATION OF SLC9A3/NHE3, SUBCELLULAR LOCATION.
    56. "Stimulus-dependent regulation of serum and glucocorticoid inducible protein kinase (SGK) transcription, subcellular localization and enzymatic activity."
      Firestone G.L., Giampaolo J.R., O'Keeffe B.A.
      Cell. Physiol. Biochem. 13:1-12(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW.
    57. "Sgk kinases and their role in epithelial transport."
      Loffing J., Flores S.Y., Staub O.
      Annu. Rev. Physiol. 68:461-490(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW.
    58. Cited for: REVIEW ON FUNCTION.
    59. "Significance of SGK1 in the regulation of neuronal function."
      Lang F., Strutz-Seebohm N., Seebohm G., Lang U.E.
      J. Physiol. (Lond.) 588:3349-3354(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW ON FUNCTION.
    60. "Crystal structure of the kinase domain of serum and glucocorticoid-regulated kinase 1 in complex with AMP PNP."
      Zhao B., Lehr R., Smallwood A.M., Ho T.F., Maley K., Randall T., Head M.S., Koretke K.K., Schnackenberg C.G.
      Protein Sci. 16:2761-2769(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 60-431, SUBUNIT, DISULFIDE BOND.
    61. "Patterns of somatic mutation in human cancer genomes."
      Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.
      , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
      Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS [LARGE SCALE ANALYSIS] ILE-219 AND VAL-342.

    Entry informationi

    Entry nameiSGK1_HUMAN
    AccessioniPrimary (citable) accession number: O00141
    Secondary accession number(s): B7UUP7
    , B7UUP8, B7UUP9, B7Z5B2, E1P583, Q5TCN2, Q5TCN3, Q5TCN4, Q5VY65, Q9UN56
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 15, 1998
    Last sequence update: March 7, 2006
    Last modified: October 1, 2014
    This is version 150 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

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

    External Data

    Dasty 3