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Q9ERE3

- SGK3_MOUSE

UniProt

Q9ERE3 - SGK3_MOUSE

Protein

Serine/threonine-protein kinase Sgk3

Gene

Sgk3

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 127 (01 Oct 2014)
      Sequence version 1 (01 Mar 2001)
      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, cell growth, proliferation, survival and migration. Up-regulates Na+ channels: SCNN1A/ENAC and SCN5A, K+ channels: KCNA3/KV1.3, KCNE1, KCNQ1 and KCNH2/HERG, epithelial Ca2+ channels: TRPV5 and TRPV6, chloride channel: BSND, creatine transporter: SLC6A8, Na+/dicarboxylate cotransporter: SLC13A2/NADC1, Na+-dependent phosphate cotransporter: SLC34A2/NAPI-2B, amino acid transporters: SLC1A5/ASCT2 and SLC6A19, glutamate transporters: SLC1A3/EAAT1, SLC1A6/EAAT4 and SLC1A7/EAAT5, glutamate receptors: GRIA1/GLUR1 and GRIK2/GLUR6, Na+/H+ exchanger: SLC9A3/NHE3, and the Na+/K+ ATPase. Plays a role in the regulation of renal tubular phosphate transport and bone density. Phosphorylates NEDD4L and GSK3B. Positively regulates ER transcription activity through phosphorylation of FLII. Negatively regulates the function of ITCH/AIP4 via its phosphorylation and thereby prevents CXCR4 from being efficiently sorted to lysosomes.5 Publications

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.

    Enzyme regulationi

    Two specific sites, one in the kinase domain (Thr-320) and the other in the C-terminal regulatory region (Ser-486), need to be phosphorylated for its full activation.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei191 – 1911ATPPROSITE-ProRule annotation
    Active sitei286 – 2861Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi168 – 1769ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. phosphatidylinositol binding Source: InterPro
    3. protein serine/threonine kinase activity Source: MGI

    GO - Biological processi

    1. negative regulation of extrinsic apoptotic signaling pathway in absence of ligand Source: MGI

    Keywords - Molecular functioni

    Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_196640. Stimuli-sensing channels.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Serine/threonine-protein kinase Sgk3 (EC:2.7.11.1)
    Alternative name(s):
    Cytokine-independent survival kinase
    Serum/glucocorticoid-regulated kinase 3
    Serum/glucocorticoid-regulated kinase-like
    Gene namesi
    Name:Sgk3
    Synonyms:Cisk, Sgkl
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 1

    Organism-specific databases

    MGIiMGI:2182368. Sgk3.

    Subcellular locationi

    Cytoplasmic vesicle 1 Publication. Early endosome 1 Publication. Recycling endosome By similarity
    Note: Endosomal localization is a prerequisite for complete kinase activity. It is essential for its colocalization with the kinase responsible for phosphorylating Ser-486 thus allowing PDPK1 phosphorylation of Thr-320 resulting in complete activation of SGK3. Colocalizes with SLC9A3/NHE3 in the recycling endosomes By similarity. Localized in vesicle-like structures and in the early endosome.By similarity

    GO - Cellular componenti

    1. cytoplasmic membrane-bounded vesicle Source: MGI
    2. early endosome Source: UniProtKB-SubCell
    3. recycling endosome Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasmic vesicle, Endosome

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi90 – 901R → A: Diminishes binding to phosphoinositides. 1 Publication
    Mutagenesisi191 – 1911K → A: No activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 496496Serine/threonine-protein kinase Sgk3PRO_0000086650Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei126 – 1261Phosphoserine1 Publication
    Modified residuei129 – 1291Phosphoserine1 Publication
    Modified residuei320 – 3201Phosphothreonine; by PDPK1By similarity
    Modified residuei486 – 4861PhosphoserineBy similarity

    Post-translational modificationi

    Activated by phosphorylation on Ser-486 by an unknown kinase (may be mTORC2 but not confirmed), transforming it into a substrate for PDPK1 which then phosphorylates it on Thr-320.By similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiQ9ERE3.
    PRIDEiQ9ERE3.

    PTM databases

    PhosphoSiteiQ9ERE3.

    Expressioni

    Tissue specificityi

    Widely expressed, predominantly in the heart, spleen and 7-day embryo.

    Gene expression databases

    ArrayExpressiQ9ERE3.
    BgeeiQ9ERE3.
    CleanExiMM_SGK3.
    GenevestigatoriQ9ERE3.

    Interactioni

    Subunit structurei

    Interacts with GSK3B and FLII. Interacts with PDPK1 in a phosphorylation-dependent manner.By similarity

    Structurei

    Secondary structure

    1
    496
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi15 – 2612
    Beta strandi29 – 4012
    Beta strandi43 – 508
    Helixi51 – 6414
    Helixi66 – 683
    Helixi84 – 10118
    Helixi105 – 1084
    Helixi111 – 1166
    Turni117 – 1204
    Helixi122 – 1243

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1XTEX-ray1.60A7-160[»]
    1XTNX-ray2.20A/B7-126[»]
    ProteinModelPortaliQ9ERE3.
    SMRiQ9ERE3. Positions 10-490.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9ERE3.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini12 – 124113PXPROSITE-ProRule annotationAdd
    BLAST
    Domaini162 – 419258Protein kinasePROSITE-ProRule annotationAdd
    BLAST
    Domaini420 – 49677AGC-kinase C-terminalAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi195 – 20511Nuclear localization signalBy similarityAdd
    BLAST

    Sequence similaritiesi

    Contains 1 AGC-kinase C-terminal domain.Curated
    Contains 1 protein kinase domain.PROSITE-ProRule annotation
    Contains 1 PX (phox homology) domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0515.
    GeneTreeiENSGT00740000115309.
    HOGENOMiHOG000233033.
    HOVERGENiHBG108317.
    InParanoidiQ9ERE3.
    KOiK13304.
    OMAiHPELYNH.
    OrthoDBiEOG7Q5HCW.
    PhylomeDBiQ9ERE3.
    TreeFamiTF320906.

    Family and domain databases

    Gene3Di3.30.1520.10. 1 hit.
    InterProiIPR000961. AGC-kinase_C.
    IPR011009. Kinase-like_dom.
    IPR001683. Phox.
    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.
    PF00787. PX. 1 hit.
    [Graphical view]
    SMARTiSM00312. PX. 1 hit.
    SM00133. S_TK_X. 1 hit.
    SM00220. S_TKc. 1 hit.
    [Graphical view]
    SUPFAMiSSF56112. SSF56112. 1 hit.
    SSF64268. SSF64268. 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.
    PS50195. PX. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q9ERE3-1 [UniParc]FASTAAdd to Basket

    « Hide

    MQRDCIMDYK ESCPSVSIPS SDEHREKKKR FTVYKVLVSV GRSEWFVFRR    50
    YAEFDKLYNS LKKQFPAMAL KIPAKRIFGD NFDPDFIKQR RAGLNEFIQN 100
    LVRYPELYNH PDVRAFLQMD SPRHQSDPSE DEDERSTSKP HSTSRNINLG 150
    PTGNPHAKPT DFDFLKVIGK GSFGKVLLAK RKLDGKFYAV KVLQKKIVLN 200
    RKEQKHIMAE RNVLLKNVKH PFLVGLHYSF QTTEKLYFVL DFVNGGELFF 250
    HLQRERSFPE PRARFYAAEI ASALGYLHSI KIVYRDLKPE NILLDSMGHV 300
    VLTDFGLCKE GIAISDTTTT FCGTPEYLAP EVIRKQPYDN TVDWWCLGAV 350
    LYEMLYGLPP FYCRDVAEMY DNILHKPLNL RPGVSLTAWS ILEELLEKNR 400
    QNRLGAKEDF LEIQNHPFFE SLSWTDLVQK KIPPPFNPNV AGPDDIRNFD 450
    AVFTEETVPY SVCVSSDYSI VNASVLEADD AFVGFSYAPP SEDLFL 496
    Length:496
    Mass (Da):57,145
    Last modified:March 1, 2001 - v1
    Checksum:i4B7D2804A5948BAD
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti114 – 1141R → G in BAC27349. (PubMed:16141072)Curated
    Sequence conflicti204 – 2041Q → P in BAC27349. (PubMed:16141072)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF312007 mRNA. Translation: AAG34115.1.
    AK030314 mRNA. Translation: BAC26895.1.
    AK031133 mRNA. Translation: BAC27269.1.
    AK031328 mRNA. Translation: BAC27349.1.
    AK146561 mRNA. Translation: BAE27261.1.
    AK151181 mRNA. Translation: BAE30182.1.
    AK171120 mRNA. Translation: BAE42262.1.
    AK171186 mRNA. Translation: BAE42298.1.
    AK171959 mRNA. Translation: BAE42748.1.
    AK172323 mRNA. Translation: BAE42945.1.
    CCDSiCCDS14816.1.
    RefSeqiNP_001032848.1. NM_001037759.1.
    NP_573483.1. NM_133220.2.
    NP_808215.2. NM_177547.3.
    UniGeneiMm.336410.

    Genome annotation databases

    EnsembliENSMUST00000097826; ENSMUSP00000095437; ENSMUSG00000025915.
    ENSMUST00000166384; ENSMUSP00000130078; ENSMUSG00000025915.
    ENSMUST00000168907; ENSMUSP00000126861; ENSMUSG00000025915.
    ENSMUST00000171265; ENSMUSP00000127462; ENSMUSG00000025915.
    GeneIDi170755.
    KEGGimmu:170755.
    UCSCiuc007agu.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF312007 mRNA. Translation: AAG34115.1 .
    AK030314 mRNA. Translation: BAC26895.1 .
    AK031133 mRNA. Translation: BAC27269.1 .
    AK031328 mRNA. Translation: BAC27349.1 .
    AK146561 mRNA. Translation: BAE27261.1 .
    AK151181 mRNA. Translation: BAE30182.1 .
    AK171120 mRNA. Translation: BAE42262.1 .
    AK171186 mRNA. Translation: BAE42298.1 .
    AK171959 mRNA. Translation: BAE42748.1 .
    AK172323 mRNA. Translation: BAE42945.1 .
    CCDSi CCDS14816.1.
    RefSeqi NP_001032848.1. NM_001037759.1.
    NP_573483.1. NM_133220.2.
    NP_808215.2. NM_177547.3.
    UniGenei Mm.336410.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1XTE X-ray 1.60 A 7-160 [» ]
    1XTN X-ray 2.20 A/B 7-126 [» ]
    ProteinModelPortali Q9ERE3.
    SMRi Q9ERE3. Positions 10-490.
    ModBasei Search...
    MobiDBi Search...

    PTM databases

    PhosphoSitei Q9ERE3.

    Proteomic databases

    PaxDbi Q9ERE3.
    PRIDEi Q9ERE3.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000097826 ; ENSMUSP00000095437 ; ENSMUSG00000025915 .
    ENSMUST00000166384 ; ENSMUSP00000130078 ; ENSMUSG00000025915 .
    ENSMUST00000168907 ; ENSMUSP00000126861 ; ENSMUSG00000025915 .
    ENSMUST00000171265 ; ENSMUSP00000127462 ; ENSMUSG00000025915 .
    GeneIDi 170755.
    KEGGi mmu:170755.
    UCSCi uc007agu.1. mouse.

    Organism-specific databases

    CTDi 23678.
    MGIi MGI:2182368. Sgk3.

    Phylogenomic databases

    eggNOGi COG0515.
    GeneTreei ENSGT00740000115309.
    HOGENOMi HOG000233033.
    HOVERGENi HBG108317.
    InParanoidi Q9ERE3.
    KOi K13304.
    OMAi HPELYNH.
    OrthoDBi EOG7Q5HCW.
    PhylomeDBi Q9ERE3.
    TreeFami TF320906.

    Enzyme and pathway databases

    Reactomei REACT_196640. Stimuli-sensing channels.

    Miscellaneous databases

    EvolutionaryTracei Q9ERE3.
    NextBioi 370338.
    PROi Q9ERE3.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9ERE3.
    Bgeei Q9ERE3.
    CleanExi MM_SGK3.
    Genevestigatori Q9ERE3.

    Family and domain databases

    Gene3Di 3.30.1520.10. 1 hit.
    InterProi IPR000961. AGC-kinase_C.
    IPR011009. Kinase-like_dom.
    IPR001683. Phox.
    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.
    PF00787. PX. 1 hit.
    [Graphical view ]
    SMARTi SM00312. PX. 1 hit.
    SM00133. S_TK_X. 1 hit.
    SM00220. S_TKc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56112. SSF56112. 1 hit.
    SSF64268. SSF64268. 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.
    PS50195. PX. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Identification of CISK, a new member of the SGK kinase family that promotes IL-3-dependent survival."
      Liu D., Yang X., Songyang Z.
      Curr. Biol. 10:1233-1236(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], MUTAGENESIS OF LYS-191.
    2. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J and NOD.
      Tissue: Amnion, Bone marrow, Forelimb and Spleen.
    3. "Regulation of cytokine-independent survival kinase (CISK) by the Phox homology domain and phosphoinositides."
      Xu J., Liu D., Gill G., Songyang Z.
      J. Cell Biol. 154:699-705(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION, MUTAGENESIS OF ARG-90.
    4. "Regulation of GluR1 abundance in murine hippocampal neurones by serum- and glucocorticoid-inducible kinase 3."
      Strutz-Seebohm N., Seebohm G., Mack A.F., Wagner H.J., Just L., Skutella T., Lang U.E., Henke G., Striegel M., Hollmann M., Rouach N., Nicoll R.A., McCormick J.A., Wang J., Pearce D., Lang F.
      J. Physiol. (Lond.) 565:381-390(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN THE REGULATION OF GRIA1/GLUR1.
    5. "Glucocorticoid adrenal steroids and glucocorticoid-inducible kinase isoforms in the regulation of GluR6 expression."
      Strutz-Seebohm N., Seebohm G., Shumilina E., Mack A.F., Wagner H.J., Lampert A., Grahammer F., Henke G., Just L., Skutella T., Hollmann M., Lang F.
      J. Physiol. (Lond.) 565:391-401(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN THE REGULATION OF GRIK2/GLUR6.
    6. "The phagosomal proteome in interferon-gamma-activated macrophages."
      Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
      Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-126 AND SER-129, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    7. "Regulation of gastric acid secretion by the serum and glucocorticoid inducible kinase isoform SGK3."
      Pasham V., Rotte A., Bhandaru M., Eichenmueller M., Froehlich H., Mack A.F., Bobbala D., Yang W., Pearce D., Lang F.
      J. Gastroenterol. 46:305-317(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    8. "Decreased bone density and increased phosphaturia in gene-targeted mice lacking functional serum- and glucocorticoid-inducible kinase 3."
      Bhandaru M., Kempe D.S., Rotte A., Capuano P., Pathare G., Sopjani M., Alesutan I., Tyan L., Huang D.Y., Siraskar B., Judenhofer M.S., Stange G., Pichler B.J., Biber J., Quintanilla-Martinez L., Wagner C.A., Pearce D., Foeller M., Lang F.
      Kidney Int. 80:61-67(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    9. "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 THE REGULATION OF SLC9A3/NHE3, SUBCELLULAR LOCATION.

    Entry informationi

    Entry nameiSGK3_MOUSE
    AccessioniPrimary (citable) accession number: Q9ERE3
    Secondary accession number(s): Q3UAY2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 22, 2003
    Last sequence update: March 1, 2001
    Last modified: October 1, 2014
    This is version 127 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3