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Q9HBY8

- SGK2_HUMAN

UniProt

Q9HBY8 - SGK2_HUMAN

Protein

Serine/threonine-protein kinase Sgk2

Gene

SGK2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 129 (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, survival and proliferation. Up-regulates Na+ channels: SCNN1A/ENAC, K+ channels: KCNA3/Kv1.3, KCNE1 and KCNQ1, amino acid transporter: SLC6A19, glutamate transporter: SLC1A6/EAAT4, glutamate receptors: GRIA1/GLUR1 and GRIK2/GLUR6, Na+/H+ exchanger: SLC9A3/NHE3, and the Na+/K+ ATPase.7 Publications

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.

    Enzyme regulationi

    Two specific sites, one in the kinase domain (Thr-253) and the other in the C-terminal regulatory region (Ser-416), need to be phosphorylated for its full activation.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei124 – 1241ATPPROSITE-ProRule annotation
    Active sitei219 – 2191Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi101 – 1099ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. potassium channel regulator activity Source: UniProtKB
    3. protein serine/threonine kinase activity Source: ProtInc
    4. sodium channel regulator activity Source: UniProtKB

    GO - Biological processi

    1. intracellular signal transduction Source: ProtInc
    2. ion transmembrane transport Source: Reactome
    3. positive regulation of transporter activity Source: UniProtKB
    4. protein phosphorylation Source: UniProtKB
    5. regulation of cell growth Source: UniProtKB
    6. regulation of cell proliferation Source: UniProtKB
    7. response to oxidative stress Source: ProtInc
    8. transmembrane transport Source: Reactome

    Keywords - Molecular functioni

    Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_160189. Stimuli-sensing channels.
    SignaLinkiQ9HBY8.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Serine/threonine-protein kinase Sgk2 (EC:2.7.11.1)
    Alternative name(s):
    Serum/glucocorticoid-regulated kinase 2
    Gene namesi
    Name:SGK2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 20

    Organism-specific databases

    HGNCiHGNC:13900. SGK2.

    Subcellular locationi

    Cytoplasm 1 Publication. Nucleus 1 Publication

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. nucleus Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi416 – 4161S → D: Increased activation. 1 Publication

    Organism-specific databases

    PharmGKBiPA37824.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 427427Serine/threonine-protein kinase Sgk2PRO_0000086646Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei253 – 2531Phosphothreonine; by PDPK11 Publication
    Modified residuei416 – 4161PhosphoserineSequence Analysis

    Post-translational modificationi

    Activated by phosphorylation on Ser-416 by an unknown kinase (may be mTORC2 but not confirmed), transforming it into a substrate for PDPK1 which then phosphorylates it on Thr-253.1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ9HBY8.
    PaxDbiQ9HBY8.
    PRIDEiQ9HBY8.

    PTM databases

    PhosphoSiteiQ9HBY8.

    Expressioni

    Tissue specificityi

    Highly expressed in liver, kidney and pancreas, and at lower levels in brain.1 Publication

    Gene expression databases

    ArrayExpressiQ9HBY8.
    BgeeiQ9HBY8.
    CleanExiHS_SGK2.
    GenevestigatoriQ9HBY8.

    Organism-specific databases

    HPAiHPA011387.

    Interactioni

    Protein-protein interaction databases

    BioGridi115416. 7 interactions.
    IntActiQ9HBY8. 2 interactions.
    STRINGi9606.ENSP00000340608.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9HBY8.
    SMRiQ9HBY8. Positions 80-418.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini95 – 352258Protein kinasePROSITE-ProRule annotationAdd
    BLAST
    Domaini353 – 42775AGC-kinase C-terminalAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi128 – 13811Nuclear localization signalBy similarityAdd
    BLAST

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0515.
    HOGENOMiHOG000233033.
    HOVERGENiHBG108317.
    InParanoidiQ9HBY8.
    KOiK13303.
    OMAiCQGHVVL.
    OrthoDBiEOG7Q5HCW.
    PhylomeDBiQ9HBY8.
    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 (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 2 (identifier: Q9HBY8-1) [UniParc]FASTAAdd to Basket

    Also known as: beta

    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

    MQGLLTSGRK PSGGGRCTGR GGWRGQWCLK PWMGGADPPT PTLSCLLLPV    50
    PPELPDHCYR MNSSPAGTPS PQPSRANGNI NLGPSANPNA QPTDFDFLKV 100
    IGKGNYGKVL LAKRKSDGAF YAVKVLQKKS ILKKKEQSHI MAERSVLLKN 150
    VRHPFLVGLR YSFQTPEKLY FVLDYVNGGE LFFHLQRERR FLEPRARFYA 200
    AEVASAIGYL HSLNIIYRDL KPENILLDCQ GHVVLTDFGL CKEGVEPEDT 250
    TSTFCGTPEY LAPEVLRKEP YDRAVDWWCL GAVLYEMLHG LPPFYSQDVS 300
    QMYENILHQP LQIPGGRTVA ACDLLQSLLH KDQRQRLGSK ADFLEIKNHV 350
    FFSPINWDDL YHKRLTPPFN PNVTGPADLK HFDPEFTQEA VSKSIGCTPD 400
    TVASSSGASS AFLGFSYAPE DDDILDC 427
    Length:427
    Mass (Da):47,604
    Last modified:March 1, 2001 - v1
    Checksum:iD8F0FA6DF54B1370
    GO
    Isoform 1 (identifier: Q9HBY8-2) [UniParc]FASTAAdd to Basket

    Also known as: alpha

    The sequence of this isoform differs from the canonical sequence as follows:
         1-60: Missing.

    Show »
    Length:367
    Mass (Da):41,175
    Checksum:iE53F1ABE253F648B
    GO
    Isoform 3 (identifier: Q9HBY8-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         19-52: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:393
    Mass (Da):43,977
    Checksum:iDB7303AF95D844CE
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti137 – 1371Missing in CAI42315. (PubMed:11780052)Curated
    Sequence conflicti168 – 1681K → E in AAX88805. 1 PublicationCurated
    Sequence conflicti208 – 2081G → D in AAV38901. 1 PublicationCurated
    Sequence conflicti337 – 3371L → P in AAX88805. 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti12 – 121S → T.1 Publication
    Corresponds to variant rs33969356 [ dbSNP | Ensembl ].
    VAR_041073
    Natural varianti259 – 2591E → K in a lung adenocarcinoma sample; somatic mutation. 1 Publication
    VAR_041074
    Natural varianti349 – 3491H → Y.1 Publication
    Corresponds to variant rs35793869 [ dbSNP | Ensembl ].
    VAR_041075

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 6060Missing in isoform 1. 3 PublicationsVSP_004932Add
    BLAST
    Alternative sequencei19 – 5234Missing in isoform 3. 1 PublicationVSP_026682Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF169034 mRNA. Translation: AAF12757.2.
    AF186470 mRNA. Translation: AAG17012.1.
    AY987010 mRNA. Translation: AAX88805.1.
    BT020098 mRNA. Translation: AAV38901.1.
    Z98752 Genomic DNA. Translation: CAC18509.1.
    Z98752 Genomic DNA. Translation: CAI42312.1.
    Z98752 Genomic DNA. Translation: CAI42315.1.
    BC014037 mRNA. Translation: AAH14037.3.
    BC065511 mRNA. Translation: AAH65511.1.
    CCDSiCCDS13320.1. [Q9HBY8-1]
    CCDS13321.1. [Q9HBY8-2]
    RefSeqiNP_001186193.1. NM_001199264.1. [Q9HBY8-2]
    NP_057360.2. NM_016276.3. [Q9HBY8-1]
    NP_733794.1. NM_170693.2. [Q9HBY8-2]
    UniGeneiHs.300863.
    Hs.740147.

    Genome annotation databases

    EnsembliENST00000341458; ENSP00000340608; ENSG00000101049. [Q9HBY8-1]
    ENST00000373092; ENSP00000362184; ENSG00000101049. [Q9HBY8-2]
    ENST00000373100; ENSP00000362192; ENSG00000101049. [Q9HBY8-2]
    ENST00000423407; ENSP00000392795; ENSG00000101049. [Q9HBY8-2]
    ENST00000426287; ENSP00000412214; ENSG00000101049. [Q9HBY8-3]
    GeneIDi10110.
    KEGGihsa:10110.
    UCSCiuc002xkr.3. human. [Q9HBY8-1]

    Polymorphism databases

    DMDMi28558166.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF169034 mRNA. Translation: AAF12757.2 .
    AF186470 mRNA. Translation: AAG17012.1 .
    AY987010 mRNA. Translation: AAX88805.1 .
    BT020098 mRNA. Translation: AAV38901.1 .
    Z98752 Genomic DNA. Translation: CAC18509.1 .
    Z98752 Genomic DNA. Translation: CAI42312.1 .
    Z98752 Genomic DNA. Translation: CAI42315.1 .
    BC014037 mRNA. Translation: AAH14037.3 .
    BC065511 mRNA. Translation: AAH65511.1 .
    CCDSi CCDS13320.1. [Q9HBY8-1 ]
    CCDS13321.1. [Q9HBY8-2 ]
    RefSeqi NP_001186193.1. NM_001199264.1. [Q9HBY8-2 ]
    NP_057360.2. NM_016276.3. [Q9HBY8-1 ]
    NP_733794.1. NM_170693.2. [Q9HBY8-2 ]
    UniGenei Hs.300863.
    Hs.740147.

    3D structure databases

    ProteinModelPortali Q9HBY8.
    SMRi Q9HBY8. Positions 80-418.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115416. 7 interactions.
    IntActi Q9HBY8. 2 interactions.
    STRINGi 9606.ENSP00000340608.

    Chemistry

    ChEMBLi CHEMBL5794.
    GuidetoPHARMACOLOGYi 1535.

    PTM databases

    PhosphoSitei Q9HBY8.

    Polymorphism databases

    DMDMi 28558166.

    Proteomic databases

    MaxQBi Q9HBY8.
    PaxDbi Q9HBY8.
    PRIDEi Q9HBY8.

    Protocols and materials databases

    DNASUi 10110.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000341458 ; ENSP00000340608 ; ENSG00000101049 . [Q9HBY8-1 ]
    ENST00000373092 ; ENSP00000362184 ; ENSG00000101049 . [Q9HBY8-2 ]
    ENST00000373100 ; ENSP00000362192 ; ENSG00000101049 . [Q9HBY8-2 ]
    ENST00000423407 ; ENSP00000392795 ; ENSG00000101049 . [Q9HBY8-2 ]
    ENST00000426287 ; ENSP00000412214 ; ENSG00000101049 . [Q9HBY8-3 ]
    GeneIDi 10110.
    KEGGi hsa:10110.
    UCSCi uc002xkr.3. human. [Q9HBY8-1 ]

    Organism-specific databases

    CTDi 10110.
    GeneCardsi GC20P042187.
    H-InvDB HIX0080189.
    HGNCi HGNC:13900. SGK2.
    HPAi HPA011387.
    MIMi 607589. gene.
    neXtProti NX_Q9HBY8.
    PharmGKBi PA37824.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0515.
    HOGENOMi HOG000233033.
    HOVERGENi HBG108317.
    InParanoidi Q9HBY8.
    KOi K13303.
    OMAi CQGHVVL.
    OrthoDBi EOG7Q5HCW.
    PhylomeDBi Q9HBY8.
    TreeFami TF320906.

    Enzyme and pathway databases

    Reactomei REACT_160189. Stimuli-sensing channels.
    SignaLinki Q9HBY8.

    Miscellaneous databases

    GeneWikii SGK2.
    GenomeRNAii 10110.
    NextBioi 38243.
    PROi Q9HBY8.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9HBY8.
    Bgeei Q9HBY8.
    CleanExi HS_SGK2.
    Genevestigatori Q9HBY8.

    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. "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: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), TISSUE SPECIFICITY, PHOSPHORYLATION AT THR-253, MUTAGENESIS OF SER-416.
    2. Li H., Nong W., Zhou G., Ke R., Shen C., Zhong G., Zheng Z., Liang M., Xiao W., Lin L., Yang S.
      Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
    3. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
      Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
      Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    4. "The DNA sequence and comparative analysis of human chromosome 20."
      Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E.
      , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
      Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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: Brain and Colon.
    6. "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 THE REGULATION OF NA(+)/K(+) ATPASE.
    7. "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.
    8. "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 THE REGULATION OF KCNE1 AND KCNQ1.
    9. "The serine/threonine kinases SGK2 and SGK3 are potent stimulators of the epithelial Na+ channel alpha,beta,gamma-ENaC."
      Friedrich B., Feng Y., Cohen P., Risler T., Vandewalle A., Broeer S., Wang J., Pearce D., Lang F.
      Pflugers Arch. 445:693-696(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN THE REGULATION OF SCNN1A/ENAC.
    10. "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 IN THE REGULATION OF KCNA3/KV1.3.
    11. "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 THE REGULATION OF SLC6A19.
    12. "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.
    13. "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.
    14. Cited for: REVIEW ON FUNCTION.
    15. "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] THR-12; LYS-259 AND TYR-349.

    Entry informationi

    Entry nameiSGK2_HUMAN
    AccessioniPrimary (citable) accession number: Q9HBY8
    Secondary accession number(s): Q52PK5
    , Q5H8Y6, Q5H8Z1, Q5TZR3, Q9UKG6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 22, 2003
    Last sequence update: March 1, 2001
    Last modified: October 1, 2014
    This is version 129 of the entry and version 1 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

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 20
      Human chromosome 20: 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. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3