SGK3

Identifiers

SGK3, CISK, SGK2, SGKL, serum/glucocorticoid regulated kinase family member 3

External IDs

MGI: 2182368 HomoloGene: 56582 GeneCards: SGK3

Gene ontology
Molecular function	• transferase activity • protein kinase activity • nucleotide binding • sodium channel regulator activity • calcium channel regulator activity • kinase activity • protein serine/threonine kinase activity • potassium channel regulator activity • protein binding • phosphatidylinositol binding • chloride channel regulator activity • ATP binding
Cellular component	• recycling endosome • cytosol • endosome • cytoplasmic, membrane-bounded vesicle • early endosome • cytoplasmic vesicle
Biological process	• regulation of apoptotic process • intracellular signal transduction • regulation of cell migration • positive regulation of transporter activity • phosphorylation • cellular sodium ion homeostasis • response to stress • protein phosphorylation • ion transmembrane transport • regulation of cell proliferation • peptidyl-serine phosphorylation • regulation of sequence-specific DNA binding transcription factor activity • regulation of cell growth • positive regulation of sodium ion transport
Sources:Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

Entrez


23678


170755

Ensembl


ENSG00000104205


ENSMUSG00000025915

UniProt


Q96BR1


Q9ERE3

RefSeq (mRNA)


NM_170709 NM_001033578 NM_013257


NM_001037759 NM_133220 NM_177547

RefSeq (protein)


NP_001028750.1 NP_001191102.1 NP_037389.4 NP_733827.2


NP_001032848.1 NP_573483.1 NP_808215.2

Location (UCSC)

Chr 8: 66.71 – 66.86 Mb

Chr 1: 9.8 – 9.9 Mb

PubMed search

^[1]

^[2]

Wikidata

View/Edit Human

View/Edit Mouse

Serine/threonine-protein kinase Sgk3 is an enzyme that in humans is encoded by the SGK3 gene.^[3]^[4]^[5]

Function

This gene is a member of the Ser/Thr protein kinase family and encodes a phosphoprotein with a PX (phox homology) domain. The protein phosphorylates several target proteins and has a role in neutral amino acid transport and activation of potassium and chloride channels. Alternate transcriptional splice variants, encoding different isoforms, have been characterized.^[5]

In melanocytic cells SGK3 gene expression may be regulated by MITF.^[6]

Interactions

SGK3 has been shown to interact with GSK3B.^[7]

References

↑ "Human PubMed Reference:".
↑ "Mouse PubMed Reference:".
↑ Dai F, Yu L, He H, Zhao Y, Yang J, Zhang X, Zhao S (February 2000). "Cloning and mapping of a novel human serum/glucocorticoid regulated kinase-like gene, SGKL, to chromosome 8q12.3-q13.1". Genomics. 62 (1): 95–7. doi:10.1006/geno.1999.5969. PMID 10585774.
↑ Kobayashi T, Deak M, Morrice N, Cohen P (January 2000). "Characterization of the structure and regulation of two novel isoforms of serum- and glucocorticoid-induced protein kinase". Biochem J. 344 Pt 1 (Pt 1): 189–97. doi:10.1042/0264-6021:3440189. PMC 1220630. PMID 10548550.
1 2 "Entrez Gene: SGK3 serum/glucocorticoid regulated kinase family, member 3".
↑ Hoek KS, Schlegel NC, Eichhoff OM, Widmer DS, Praetorius C, Einarsson SO, Valgeirsdottir S, Bergsteinsdottir K, Schepsky A, Dummer R, Steingrimsson E (2008). "Novel MITF targets identified using a two-step DNA microarray strategy". Pigment Cell Melanoma Res. 21 (6): 665–76. doi:10.1111/j.1755-148X.2008.00505.x. PMID 19067971.
↑ Dai F, Yu L, He H, Chen Y, Yu J, Yang Y, Xu Y, Ling W, Zhao S (May 2002). "Human serum and glucocorticoid-inducible kinase-like kinase (SGKL) phosphorylates glycogen syntheses kinase 3 beta (GSK-3beta) at serine-9 through direct interaction". Biochem. Biophys. Res. Commun. 293 (4): 1191–6. doi:10.1016/S0006-291X(02)00349-2. PMID 12054501.

Lang F, Cohen P (2002). "Regulation and physiological roles of serum- and glucocorticoid-induced protein kinase isoforms". Sci. STKE. 2001 (108): RE17. doi:10.1126/stke.2001.108.re17. PMID 11707620.
Ali A, Hoeflich KP, Woodgett JR (2002). "Glycogen synthase kinase-3: properties, functions, and regulation". Chem. Rev. 101 (8): 2527–40. doi:10.1021/cr000110o. PMID 11749387.
Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
Fang X, Yu SX, Lu Y, Bast RC, Woodgett JR, Mills GB (2000). "Phosphorylation and inactivation of glycogen synthase kinase 3 by protein kinase A". Proc. Natl. Acad. Sci. U.S.A. 97 (22): 11960–5. doi:10.1073/pnas.220413597. PMC 17277. PMID 11035810.
Xu J, Liu D, Gill G, Songyang Z (2001). "Regulation of cytokine-independent survival kinase (CISK) by the Phox homology domain and phosphoinositides". J. Cell Biol. 154 (4): 699–705. doi:10.1083/jcb.200105089. PMC 2196448. PMID 11514587.
Yun CC, Chen Y, Lang F (2002). "Glucocorticoid activation of Na(+)/H(+) exchanger isoform 3 revisited. The roles of SGK1 and NHERF2". J. Biol. Chem. 277 (10): 7676–83. doi:10.1074/jbc.M107768200. PMID 11751930.
Fang X, Yu S, Tanyi JL, Lu Y, Woodgett JR, Mills GB (2002). "Convergence of Multiple Signaling Cascades at Glycogen Synthase Kinase 3: Edg Receptor-Mediated Phosphorylation and Inactivation by Lysophosphatidic Acid through a Protein Kinase C-Dependent Intracellular Pathway". Mol. Cell. Biol. 22 (7): 2099–110. doi:10.1128/MCB.22.7.2099-2110.2002. PMC 133668. PMID 11884598.
Dai F, Yu L, He H, Chen Y, Yu J, Yang Y, Xu Y, Ling W, Zhao S (2002). "Human serum and glucocorticoid-inducible kinase-like kinase (SGKL) phosphorylates glycogen syntheses kinase 3 beta (GSK-3beta) at serine-9 through direct interaction". Biochem. Biophys. Res. Commun. 293 (4): 1191–6. doi:10.1016/S0006-291X(02)00349-2. PMID 12054501.
Brickley DR, Mikosz CA, Hagan CR, Conzen SD (2003). "Ubiquitin modification of serum and glucocorticoid-induced protein kinase-1 (SGK-1)". J. Biol. Chem. 277 (45): 43064–70. doi:10.1074/jbc.M207604200. PMID 12218062.
Gamper N, Fillon S, Feng Y, Friedrich B, Lang PA, Henke G, Huber SM, Kobayashi T, Cohen P, Lang F (2003). "K+ channel activation by all three isoforms of serum- and glucocorticoid-dependent protein kinase SGK". Pflugers Arch. 445 (1): 60–6. doi:10.1007/s00424-002-0873-2. PMID 12397388.
Henke G, Setiawan I, Böhmer C, Lang F (2003). "Activation of Na+/K+-ATPase by the serum and glucocorticoid-dependent kinase isoforms". Kidney Blood Press. Res. 25 (6): 370–4. doi:10.1159/000068699. PMID 12590200.
Friedrich B, Feng Y, Cohen P, Risler T, Vandewalle A, Bröer S, Wang J, Pearce D, Lang F (2003). "The serine/threonine kinases SGK2 and SGK3 are potent stimulators of the epithelial Na+ channel alpha,beta,gamma-ENaC". Pflugers Arch. 445 (6): 693–6. doi:10.1007/s00424-002-0993-8. PMID 12632189.
Embark HM, Böhmer C, Vallon V, Luft F, Lang F (2003). "Regulation of KCNE1-dependent K(+) current by the serum and glucocorticoid-inducible kinase (SGK) isoforms". Pflugers Arch. 445 (5): 601–6. doi:10.1007/s00424-002-0982-y. PMID 12634932.
Nilsen T, Slagsvold T, Skjerpen CS, Brech A, Stenmark H, Olsnes S (2004). "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". J. Biol. Chem. 279 (6): 4794–801. doi:10.1074/jbc.M309653200. PMID 14604990.

PDB gallery

1xte: crystal structure of CISK-PX domain

1xtn: crystal structure of CISK-PX domain with sulfates

Kinases: Serine/threonine-specific protein kinases (EC 2.7.11-12)

Serine/threonine-specific protein kinases (EC 2.7.11.1-EC 2.7.11.20)

Non-specific serine/threonine protein kinases (EC 2.7.11.1)	LATS1 LATS2 MAST1 MAST2 STK38 STK38L CIT ROCK1 SGK SGK2 SGK3 Protein kinase B AKT1 AKT2 AKT3 Ataxia telangiectasia mutated Mammalian target of rapamycin EIF-2 kinases PKR HRI EIF2AK3 EIF2AK4 Wee1 WEE1

Pyruvate dehydrogenase kinase (EC 2.7.11.2)	PDK1 PDK2 PDK3

Dephospho-(reductase kinase) kinase (EC 2.7.11.3)	AMP-activated protein kinase α PRKAA1 PRKAA2 β PRKAB1 PRKAB2 γ PRKAG1 PRKAG2 PRKAG3

3-methyl-2-oxobutanoate dehydrogenase (acetyl-transferring) kinase (EC 2.7.11.4)	BCKDK BCKDHA BCKDHB

(isocitrate dehydrogenase (NADP+)) kinase (EC 2.7.11.5)	IDH2 IDH3A IDH3B IDH3G

(tyrosine 3-monooxygenase) kinase (EC 2.7.11.6)	STK4

Myosin-heavy-chain kinase (EC 2.7.11.7)	Aurora kinase Aurora A kinase Aurora B kinase

Fas-activated serine/threonine kinase (EC 2.7.11.8)	FASTK STK10

Goodpasture-antigen-binding protein kinase (EC 2.7.11.9)	-

IκB kinase (EC 2.7.11.10)	CHUK IKK2 TBK1 IKBKE IKBKG IKBKAP

cAMP-dependent protein kinase (EC 2.7.11.11)	Protein kinase A PRKACG PRKACB PRKACA PRKY

cGMP-dependent protein kinase (EC 2.7.11.12)	Protein kinase G PRKG1

Protein kinase C (EC 2.7.11.13)	Protein kinase C Protein kinase Cζ PKC alpha PRKCB1 PRKCD PRKCE PRKCH PRKCG PRKCI PRKCQ Protein kinase N1 PKN2 PKN3

Rhodopsin kinase (EC 2.7.11.14)	Rhodopsin kinase

Beta adrenergic receptor kinase (EC 2.7.11.15)	Beta adrenergic receptor kinase Beta adrenergic receptor kinase-2

G-protein coupled receptor kinases (EC 2.7.11.16)	GRK4 GRK5 GRK6

Ca2+/calmodulin-dependent (EC 2.7.11.17)	BRSK2 CAMK1 CAMK2A CAMK2B CAMK2D CAMK2G CAMK4 MLCK CASK CHEK1 CHEK2 DAPK1 DAPK2 DAPK3 STK11 MAPKAPK2 MAPKAPK3 MAPKAPK5 MARK1 MARK2 MARK3 MARK4 MELK MKNK1 MKNK2 NUAK1 NUAK2 OBSCN PASK PHKG1 PHKG2 PIM1 PIM2 PKD1 PRKD2 PRKD3 PSKH1 SNF1LK2 KIAA0999 STK40 SNF1LK SNRK SPEG TSSK2 Kalirin TRIB1 TRIB2 TRIB3 TRIO Titin DCLK1

Myosin light-chain kinase (EC 2.7.11.18)	MYLK MYLK2 MYLK3 MYLK4

Phosphorylase kinase (EC 2.7.11.19)	PHKA1 PHKA2 PHKB PHKG1 PHKG2

Elongation factor 2 kinase (EC 2.7.11.20)	EEF2K STK19

Polo kinase (EC 2.7.11.21)	PLK1 PLK2 PLK3 PLK4

Serine/threonine-specific protein kinases (EC 2.7.11.21-EC 2.7.11.30)

Polo kinase (EC 2.7.11.21)	PLK1 PLK2 PLK3 PLK4

Cyclin-dependent kinase (EC 2.7.11.22)	CDK1 CDK2 CDKL2 CDK3 CDK4 CDK5 CDKL5 CDK6 CDK7 CDK8 CDK9 CDK10 CDK12 CDC2L5 PCTK1 PCTK2 PCTK3 PFTK1 CDC2L1

(RNA-polymerase)-subunit kinase (EC 2.7.11.23)	RPS6KA5 RPS6KA4 P70S6 kinase P70-S6 Kinase 1 RPS6KB2 RPS6KA2 RPS6KA3 RPS6KA1 RPS6KC1

Mitogen-activated protein kinase (EC 2.7.11.24)	Extracellular signal-regulated MAPK1 MAPK3 MAPK4 MAPK6 MAPK7 MAPK12 MAPK15 C-Jun N-terminal MAPK8 MAPK9 MAPK10 P38 mitogen-activated protein MAPK11 MAPK13 MAPK14

MAP3K (EC 2.7.11.25)	MAP kinase kinase kinases MAP3K1 MAP3K2 MAP3K3 MAP3K4 MAP3K5 MAP3K6 MAP3K7 MAP3K8 RAFs ARAF BRAF KSR1 KSR2 MLKs MAP3K12 MAP3K13 MAP3K9 MAP3K10 MAP3K11 MAP3K7 ZAK CDC7 MAP3K14

Tau-protein kinase (EC 2.7.11.26)	TPK1 TTK GSK-3

(acetyl-CoA carboxylase) kinase (EC 2.7.11.27)	-

Tropomyosin kinase (EC 2.7.11.28)	-

Low-density-lipoprotein receptor kinase (EC 2.7.11.29)	-

Receptor protein serine/threonine kinase (EC 2.7.11.30)	Bone morphogenetic protein receptors BMPR1 BMPR1A BMPR1B BMPR2 ACVR1 ACVR1B ACVR1C ACVR2A ACVR2B ACVRL1 Anti-Müllerian hormone receptor

Dual-specificity kinases (EC 2.7.12)

MAP2K	MAP2K1 MAP2K2 MAP2K3 MAP2K4 MAP2K5 MAP2K6 MAP2K7

Enzymes

Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Catalytically perfect enzyme Coenzyme Cofactor Enzyme catalysis Enzyme kinetics Lineweaver–Burk plot Michaelis–Menten kinetics

Regulation	Allosteric regulation Cooperativity Enzyme inhibitor

Classification	EC number Enzyme superfamily Enzyme family List of enzymes

Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list)

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SGK3

Function

Interactions

References

Further reading