Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q96BR1 (SGK3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 132. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:SGK3
Synonyms:CISK, SGKL
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length496 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Serine/threonine-protein kinase which is involved in the regulation of a wide variety of ion channels, membrane transporters, 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. Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.18 Ref.19 Ref.20 Ref.21 Ref.22 Ref.23 Ref.24 Ref.26 Ref.27 Ref.28 Ref.29

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Enzyme regulation

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.

Subunit structure

Interacts with GSK3B and FLII. Interacts with PDPK1 in a phosphorylation-dependent manner. Ref.7 Ref.17 Ref.24 Ref.27

Subcellular location

Cytoplasmic vesicle By similarity. Early endosome. Recycling endosome. 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. Localized in vesicle-like structures and in the early endosome. Colocalizes with SLC9A3/NHE3 in the recycling endosomes. Ref.24 Ref.29

Tissue specificity

Expressed in most tissues with highest levels in pancreas, kidney liver, heart and brain and lower levels in lung, placenta and skeletal muscle. Expression is higher in ER-positive breast tumors than ER-negative breast tumors. Ref.30

Induction

Induced by estrogen/ER in breast cancer cells. Ref.30

Post-translational modification

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.

Sequence similarities

Belongs to the protein kinase superfamily. AGC Ser/Thr protein kinase family.

Contains 1 AGC-kinase C-terminal domain.

Contains 1 protein kinase domain.

Contains 1 PX (phox homology) domain.

Sequence caution

The sequence AAF12758.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
   Cellular componentCytoplasmic vesicle
Endosome
   Coding sequence diversityAlternative splicing
Polymorphism
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Serine/threonine-protein kinase
Transferase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_procession transmembrane transport

Traceable author statement. Source: Reactome

protein phosphorylation

Traceable author statement Ref.1. Source: ProtInc

regulation of cell growth

Traceable author statement Ref.32. Source: UniProtKB

regulation of cell migration

Traceable author statement Ref.32. Source: UniProtKB

regulation of cell proliferation

Traceable author statement Ref.32. Source: UniProtKB

regulation of sequence-specific DNA binding transcription factor activity

Traceable author statement Ref.32. Source: UniProtKB

response to stress

Traceable author statement Ref.1. Source: ProtInc

transmembrane transport

Traceable author statement. Source: Reactome

   Cellular_componentcytoplasmic membrane-bounded vesicle

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytosol

Traceable author statement. Source: Reactome

early endosome

Inferred from electronic annotation. Source: UniProtKB-SubCell

recycling endosome

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

calcium channel regulator activity

Traceable author statement Ref.31. Source: UniProtKB

chloride channel regulator activity

Traceable author statement Ref.31. Source: UniProtKB

phosphatidylinositol binding

Inferred from electronic annotation. Source: InterPro

potassium channel regulator activity

Traceable author statement Ref.31. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.24. Source: IntAct

protein kinase activity

Traceable author statement Ref.1Ref.2. Source: ProtInc

protein serine/threonine kinase activity

Traceable author statement Ref.1. Source: ProtInc

sodium channel regulator activity

Traceable author statement Ref.31. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

ITCHQ96J025EBI-2801236,EBI-1564678

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q96BR1-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q96BR1-2)

The sequence of this isoform differs from the canonical sequence as follows:
     327-358: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 496496Serine/threonine-protein kinase Sgk3
PRO_0000086649

Regions

Domain12 – 124113PX
Domain162 – 419258Protein kinase
Domain420 – 49677AGC-kinase C-terminal
Nucleotide binding168 – 1769ATP By similarity
Motif195 – 20511Nuclear localization signal By similarity

Sites

Active site2861Proton acceptor By similarity
Binding site1911ATP By similarity

Amino acid modifications

Modified residue1261Phosphoserine By similarity
Modified residue1291Phosphoserine By similarity
Modified residue3201Phosphothreonine; by PDPK1 Ref.1 Ref.25
Modified residue4861Phosphoserine Ref.24 Ref.25

Natural variations

Alternative sequence327 – 35832Missing in isoform 2.
VSP_041903
Natural variant921A → V in a breast cancer sample; somatic mutation. Ref.33
VAR_035636
Natural variant3551L → P. Ref.34
VAR_041076

Experimental info

Mutagenesis901R → A: Partially localized to the membrane. Ref.25
Mutagenesis1911K → M: Abolishes activity. Ref.25
Mutagenesis4861S → D: Increased activation. Ref.1
Sequence conflict541F → V in AAF27051. Ref.2
Sequence conflict1271D → G in AAF27051. Ref.2
Sequence conflict1871F → V in AAF27051. Ref.2
Sequence conflict2941L → V in AAF27051. Ref.2
Sequence conflict3871T → R in AAF27051. Ref.2

Sequences

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

Last modified December 1, 2001. Version 1.
Checksum: 76A6CCEB69006CF1

FASTA49657,108
        10         20         30         40         50         60 
MQRDHTMDYK ESCPSVSIPS SDEHREKKKR FTVYKVLVSV GRSEWFVFRR YAEFDKLYNT 

        70         80         90        100        110        120 
LKKQFPAMAL KIPAKRIFGD NFDPDFIKQR RAGLNEFIQN LVRYPELYNH PDVRAFLQMD 

       130        140        150        160        170        180 
SPKHQSDPSE DEDERSSQKL HSTSQNINLG PSGNPHAKPT DFDFLKVIGK GSFGKVLLAK 

       190        200        210        220        230        240 
RKLDGKFYAV KVLQKKIVLN RKEQKHIMAE RNVLLKNVKH PFLVGLHYSF QTTEKLYFVL 

       250        260        270        280        290        300 
DFVNGGELFF HLQRERSFPE HRARFYAAEI ASALGYLHSI KIVYRDLKPE NILLDSVGHV 

       310        320        330        340        350        360 
VLTDFGLCKE GIAISDTTTT FCGTPEYLAP EVIRKQPYDN TVDWWCLGAV LYEMLYGLPP 

       370        380        390        400        410        420 
FYCRDVAEMY DNILHKPLSL RPGVSLTAWS ILEELLEKDR QNRLGAKEDF LEIQNHPFFE 

       430        440        450        460        470        480 
SLSWADLVQK KIPPPFNPNV AGPDDIRNFD TAFTEETVPY SVCVSSDYSI VNASVLEADD 

       490 
AFVGFSYAPP SEDLFL 

« Hide

Isoform 2 [UniParc].

Checksum: D5028F96C651C465
Show »

FASTA46453,306

References

« Hide 'large scale' references
[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] (ISOFORM 1), PHOSPHORYLATION AT THR-320, MUTAGENESIS OF SER-486.
[2]"Cloning and mapping of a novel human Serum/Glucocorticoid regulated kinase-like gene, SGKL, to chromosome 8q12.3-q13.1."
Dai F., Yu L., He H., Zhao Y., Yang J., Zhang X., Zhao S.
Genomics 62:95-97(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[3]Zhao Y.
Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION.
[4]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
Tissue: Brain and Mammary gland.
[5]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"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: Mammary gland.
[7]"Human serum and glucocorticoid-inducible kinase-like kinase (SGKL) phosphorylates glycogen syntheses kinase 3 beta (GSK-3beta) at serine-9 through direct interaction."
Dai F., Yu L., He H., Chen Y., Yu J., Yang Y., Xu Y., Ling W., Zhao S.
Biochem. Biophys. Res. Commun. 293:1191-1196(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN PHOSPHORYLATION OF GSK3B, INTERACTION WITH GSK3B.
[8]"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.
[9]"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.
[10]"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.
[11]"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 SLC1A3/EAAT1.
[12]"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.
[13]"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 REGULATION OF SCNN1A/ENAC.
[14]"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.
[15]"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.
[16]"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.
[17]"Peroxisomal targeting as a tool for assaying protein-protein interactions in the living cell: cytokine-independent survival kinase (CISK) binds PDK-1 in vivo in a phosphorylation-dependent manner."
Nilsen T., Slagsvold T., Skjerpen C.S., Brech A., Stenmark H., Olsnes S.
J. Biol. Chem. 279:4794-4801(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PDPK1, PHOSPHORYLATION BY PDPK1.
[18]"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 REGULATION OF KCNA3/KV1.3.
[19]"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.
[20]"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.
[21]"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.
[22]"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.
[23]"Upregulation of HERG channels by the serum and glucocorticoid inducible kinase isoform SGK3."
Maier G., Palmada M., Rajamanickam J., Shumilina E., Boehmer C., Lang F.
Cell. Physiol. Biochem. 18:177-186(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN REGULATION OF KCNH2/HERG.
[24]"CISK attenuates degradation of the chemokine receptor CXCR4 via the ubiquitin ligase AIP4."
Slagsvold T., Marchese A., Brech A., Stenmark H.
EMBO J. 25:3738-3749(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH ITHC/AIP4, PHOSPHORYLATION AT SER-486.
[25]"Role of the Phox homology domain and phosphorylation in activation of serum and glucocorticoid-regulated kinase-3."
Tessier M., Woodgett J.R.
J. Biol. Chem. 281:23978-23989(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT THR-320 AND SER-486, MUTAGENESIS OF ARG-90 AND LYS-191.
[26]"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.
[27]"Identification of Flightless-I as a substrate of the cytokine-independent survival kinase CISK."
Xu J., Liao L., Qin J., Xu J., Liu D., Songyang Z.
J. Biol. Chem. 284:14377-14385(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN PHOSPHORYLATION OF FLII, INTERACTION WITH FLII.
[28]"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.
[29]"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.
[30]"SGK3 is an estrogen-inducible kinase promoting estrogen-mediated survival of breast cancer cells."
Wang Y., Zhou D., Phung S., Masri S., Smith D., Chen S.
Mol. Endocrinol. 25:72-82(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION, TISSUE SPECIFICITY.
[31]"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.
[32]"Second AKT: the rise of SGK in cancer signalling."
Bruhn M.A., Pearson R.B., Hannan R.D., Sheppard K.E.
Growth Factors 28:394-408(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON FUNCTION.
[33]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] VAL-92.
[34]"Patterns of somatic mutation in human cancer genomes."
Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G. expand/collapse author list , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] PRO-355.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF169035 mRNA. Translation: AAF12758.1. Different initiation.
AF085233 mRNA. Translation: AAF27051.2.
AK074666 mRNA. Translation: BAG51984.1.
AK291428 mRNA. Translation: BAF84117.1.
AC011031 Genomic DNA. No translation available.
AC090154 Genomic DNA. No translation available.
CH471068 Genomic DNA. Translation: EAW86919.1.
BC015326 mRNA. Translation: AAH15326.1.
CCDSCCDS6195.1. [Q96BR1-1]
CCDS6196.1. [Q96BR1-2]
RefSeqNP_001028750.1. NM_001033578.2. [Q96BR1-1]
NP_001191102.1. NM_001204173.1. [Q96BR1-1]
NP_037389.4. NM_013257.4. [Q96BR1-1]
NP_733827.2. NM_170709.2. [Q96BR1-2]
UniGeneHs.613417.
Hs.733251.

3D structure databases

ProteinModelPortalQ96BR1.
SMRQ96BR1. Positions 11-490.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid117195. 7 interactions.
IntActQ96BR1. 5 interactions.
MINTMINT-2813751.
STRING9606.ENSP00000262211.

Chemistry

BindingDBQ96BR1.
ChEMBLCHEMBL6186.
GuidetoPHARMACOLOGY1536.

PTM databases

PhosphoSiteQ96BR1.

Polymorphism databases

DMDM28558163.

Proteomic databases

MaxQBQ96BR1.
PaxDbQ96BR1.
PRIDEQ96BR1.

Protocols and materials databases

DNASU23678.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000345714; ENSP00000331816; ENSG00000104205. [Q96BR1-1]
ENST00000396596; ENSP00000379842; ENSG00000104205. [Q96BR1-1]
ENST00000520976; ENSP00000430691; ENSG00000104205. [Q96BR1-2]
ENST00000521198; ENSP00000430463; ENSG00000104205. [Q96BR1-1]
ENST00000522398; ENSP00000430256; ENSG00000104205. [Q96BR1-1]
GeneID100533105.
23678.
KEGGhsa:100533105.
hsa:23678.
UCSCuc003xwp.3. human. [Q96BR1-1]
uc003xwu.3. human. [Q96BR1-2]

Organism-specific databases

CTD100533105.
23678.
GeneCardsGC08P067579.
GC08P067624.
HGNCHGNC:10812. SGK3.
HPAHPA027146.
MIM607591. gene.
neXtProtNX_Q96BR1.
PharmGKBPA35722.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000233033.
HOVERGENHBG108317.
InParanoidQ96BR1.
KOK13304.
OMAHPELYNH.
OrthoDBEOG7Q5HCW.
PhylomeDBQ96BR1.
TreeFamTF320906.

Enzyme and pathway databases

ReactomeREACT_15518. Transmembrane transport of small molecules.
SignaLinkQ96BR1.

Gene expression databases

ArrayExpressQ96BR1.
BgeeQ96BR1.
CleanExHS_SGK2.
HS_SGK3.
GenevestigatorQ96BR1.

Family and domain databases

Gene3D3.30.1520.10. 1 hit.
InterProIPR000961. 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]
PfamPF00069. Pkinase. 1 hit.
PF00433. Pkinase_C. 1 hit.
PF00787. PX. 1 hit.
[Graphical view]
SMARTSM00312. PX. 1 hit.
SM00133. S_TK_X. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 1 hit.
SSF64268. SSF64268. 1 hit.
PROSITEPS51285. AGC_KINASE_CTER. 1 hit.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
PS50195. PX. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiSGK3.
NextBio46545.
PROQ96BR1.
SOURCESearch...

Entry information

Entry nameSGK3_HUMAN
AccessionPrimary (citable) accession number: Q96BR1
Secondary accession number(s): A8K5W3 expand/collapse secondary AC list , B3KQC2, Q9P1Q7, Q9UKG5
Entry history
Integrated into UniProtKB/Swiss-Prot: February 22, 2003
Last sequence update: December 1, 2001
Last modified: July 9, 2014
This is version 132 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 8

Human chromosome 8: entries, gene names and cross-references to MIM