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Serine/threonine-protein kinase Sgk2 (EC 2.7.11.1) (Serum/glucocorticoid-regulated kinase 2)

 SGK2_HUMAN              Reviewed;         427 AA.
Q9HBY8; Q52PK5; Q5H8Y6; Q5H8Z1; Q5TZR3; Q9UKG6;
22-FEB-2003, integrated into UniProtKB/Swiss-Prot.
01-MAR-2001, sequence version 1.
18-JUL-2018, entry version 159.
RecName: Full=Serine/threonine-protein kinase Sgk2;
EC=2.7.11.1;
AltName: Full=Serum/glucocorticoid-regulated kinase 2;
Name=SGK2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), TISSUE SPECIFICITY,
PHOSPHORYLATION AT THR-253, AND MUTAGENESIS OF SER-416.
PubMed=10548550; DOI=10.1042/bj3440189;
Kobayashi T., Deak M., Morrice N., Cohen P.;
"Characterization of the structure and regulation of two novel
isoforms of serum- and glucocorticoid-induced protein kinase.";
Biochem. J. 344:189-197(1999).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
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.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=11780052; DOI=10.1038/414865a;
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.;
"The DNA sequence and comparative analysis of human chromosome 20.";
Nature 414:865-871(2001).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain, and Colon;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
FUNCTION IN THE REGULATION OF NA(+)/K(+) ATPASE.
PubMed=12590200; DOI=10.1159/000068699;
Henke G., Setiawan I., Boehmer C., Lang F.;
"Activation of Na+/K+-ATPase by the serum and glucocorticoid-dependent
kinase isoforms.";
Kidney Blood Press. Res. 25:370-374(2002).
[7]
FUNCTION.
PubMed=12397388; DOI=10.1007/s00424-002-0873-2;
Gamper N., Fillon S., Feng Y., Friedrich B., Lang P.A., Henke G.,
Huber S.M., Kobayashi T., Cohen P., Lang F.;
"K(+) channel activation by all three isoforms of serum- and
glucocorticoid-dependent protein kinase SGK.";
Pflugers Arch. 445:60-66(2002).
[8]
FUNCTION IN THE REGULATION OF KCNE1 AND KCNQ1.
PubMed=12634932; DOI=10.1007/s00424-002-0982-y;
Embark H.M., Boehmer C., Vallon V., Luft F., Lang F.;
"Regulation of KCNE1-dependent K(+) current by the serum and
glucocorticoid-inducible kinase (SGK) isoforms.";
Pflugers Arch. 445:601-606(2003).
[9]
FUNCTION IN THE REGULATION OF SCNN1A/ENAC.
PubMed=12632189; DOI=10.1007/s00424-002-0993-8;
Friedrich B., Feng Y., Cohen P., Risler T., Vandewalle A., Broeer S.,
Wang J., Pearce D., Lang F.;
"The serine/threonine kinases SGK2 and SGK3 are potent stimulators of
the epithelial Na+ channel alpha,beta,gamma-ENaC.";
Pflugers Arch. 445:693-696(2003).
[10]
FUNCTION IN THE REGULATION OF KCNA3/KV1.3.
PubMed=15040001; DOI=10.1002/jcp.10430;
Henke G., Maier G., Wallisch S., Boehmer C., Lang F.;
"Regulation of the voltage gated K+ channel Kv1.3 by the ubiquitin
ligase Nedd4-2 and the serum and glucocorticoid inducible kinase
SGK1.";
J. Cell. Physiol. 199:194-199(2004).
[11]
FUNCTION IN THE REGULATION OF SLC6A19.
PubMed=20511718; DOI=10.1159/000315092;
Boehmer C., Sopjani M., Klaus F., Lindner R., Laufer J., Jeyaraj S.,
Lang F., Palmada M.;
"The serum and glucocorticoid inducible kinases SGK1-3 stimulate the
neutral amino acid transporter SLC6A19.";
Cell. Physiol. Biochem. 25:723-732(2010).
[12]
FUNCTION IN THE REGULATION OF SLC9A3/NHE3, AND SUBCELLULAR LOCATION.
PubMed=21865597; DOI=10.1091/mbc.E11-04-0328;
He P., Lee S.J., Lin S., Seidler U., Lang F., Fejes-Toth G.,
Naray-Fejes-Toth A., Yun C.C.;
"Serum- and glucocorticoid-induced kinase 3 in recycling endosomes
mediates acute activation of Na+/H+ exchanger NHE3 by
glucocorticoids.";
Mol. Biol. Cell 22:3812-3825(2011).
[13]
REVIEW.
PubMed=16460280; DOI=10.1146/annurev.physiol.68.040104.131654;
Loffing J., Flores S.Y., Staub O.;
"Sgk kinases and their role in epithelial transport.";
Annu. Rev. Physiol. 68:461-490(2006).
[14]
REVIEW ON FUNCTION.
PubMed=20919962; DOI=10.3109/08977194.2010.518616;
Bruhn M.A., Pearson R.B., Hannan R.D., Sheppard K.E.;
"Second AKT: the rise of SGK in cancer signalling.";
Growth Factors 28:394-408(2010).
[15]
VARIANTS [LARGE SCALE ANALYSIS] THR-12; LYS-259 AND TYR-349.
PubMed=17344846; DOI=10.1038/nature05610;
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.;
"Patterns of somatic mutation in human cancer genomes.";
Nature 446:153-158(2007).
-!- FUNCTION: 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. {ECO:0000269|PubMed:12397388, ECO:0000269|PubMed:12590200,
ECO:0000269|PubMed:12632189, ECO:0000269|PubMed:12634932,
ECO:0000269|PubMed:15040001, ECO:0000269|PubMed:20511718,
ECO:0000269|PubMed:21865597}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
-!- ENZYME REGULATION: 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.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21865597}.
Nucleus {ECO:0000269|PubMed:21865597}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=2; Synonyms=beta;
IsoId=Q9HBY8-1; Sequence=Displayed;
Name=1; Synonyms=alpha;
IsoId=Q9HBY8-2; Sequence=VSP_004932;
Name=3;
IsoId=Q9HBY8-3; Sequence=VSP_026682;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Highly expressed in liver, kidney and
pancreas, and at lower levels in brain.
{ECO:0000269|PubMed:10548550}.
-!- PTM: 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.
{ECO:0000269|PubMed:10548550}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
protein kinase family. {ECO:0000305}.
-!- CAUTION: Not regulated by serum or glucocorticoids. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AF169034; AAF12757.2; -; mRNA.
EMBL; AF186470; AAG17012.1; -; mRNA.
EMBL; AY987010; AAX88805.1; -; mRNA.
EMBL; BT020098; AAV38901.1; -; mRNA.
EMBL; Z98752; CAC18509.1; -; Genomic_DNA.
EMBL; Z98752; CAI42312.1; -; Genomic_DNA.
EMBL; Z98752; CAI42315.1; -; Genomic_DNA.
EMBL; BC014037; AAH14037.3; -; mRNA.
EMBL; BC065511; AAH65511.1; -; mRNA.
CCDS; CCDS13320.1; -. [Q9HBY8-1]
CCDS; CCDS13321.1; -. [Q9HBY8-2]
RefSeq; NP_001186193.1; NM_001199264.1. [Q9HBY8-2]
RefSeq; NP_057360.2; NM_016276.3. [Q9HBY8-1]
RefSeq; NP_733794.1; NM_170693.2. [Q9HBY8-2]
UniGene; Hs.300863; -.
UniGene; Hs.740147; -.
ProteinModelPortal; Q9HBY8; -.
SMR; Q9HBY8; -.
BioGrid; 115416; 23.
IntAct; Q9HBY8; 14.
STRING; 9606.ENSP00000340608; -.
BindingDB; Q9HBY8; -.
ChEMBL; CHEMBL5794; -.
GuidetoPHARMACOLOGY; 1535; -.
iPTMnet; Q9HBY8; -.
PhosphoSitePlus; Q9HBY8; -.
BioMuta; SGK2; -.
DMDM; 28558166; -.
MaxQB; Q9HBY8; -.
PaxDb; Q9HBY8; -.
PeptideAtlas; Q9HBY8; -.
PRIDE; Q9HBY8; -.
ProteomicsDB; 81612; -.
ProteomicsDB; 81613; -. [Q9HBY8-2]
ProteomicsDB; 81614; -. [Q9HBY8-3]
DNASU; 10110; -.
Ensembl; ENST00000341458; ENSP00000340608; ENSG00000101049. [Q9HBY8-1]
Ensembl; ENST00000373092; ENSP00000362184; ENSG00000101049. [Q9HBY8-2]
Ensembl; ENST00000373100; ENSP00000362192; ENSG00000101049. [Q9HBY8-2]
Ensembl; ENST00000423407; ENSP00000392795; ENSG00000101049. [Q9HBY8-2]
Ensembl; ENST00000426287; ENSP00000412214; ENSG00000101049. [Q9HBY8-3]
GeneID; 10110; -.
KEGG; hsa:10110; -.
UCSC; uc002xkr.4; human. [Q9HBY8-1]
CTD; 10110; -.
DisGeNET; 10110; -.
EuPathDB; HostDB:ENSG00000101049.14; -.
GeneCards; SGK2; -.
H-InvDB; HIX0080189; -.
HGNC; HGNC:13900; SGK2.
HPA; HPA008859; -.
HPA; HPA011387; -.
MIM; 607589; gene.
neXtProt; NX_Q9HBY8; -.
OpenTargets; ENSG00000101049; -.
PharmGKB; PA37824; -.
eggNOG; KOG0598; Eukaryota.
eggNOG; ENOG410XNPH; LUCA.
GeneTree; ENSGT00920000148938; -.
HOGENOM; HOG000233033; -.
HOVERGEN; HBG108317; -.
InParanoid; Q9HBY8; -.
KO; K13303; -.
OrthoDB; EOG091G06FF; -.
PhylomeDB; Q9HBY8; -.
TreeFam; TF320906; -.
Reactome; R-HSA-2672351; Stimuli-sensing channels.
SignaLink; Q9HBY8; -.
SIGNOR; Q9HBY8; -.
ChiTaRS; SGK2; human.
GeneWiki; SGK2; -.
GenomeRNAi; 10110; -.
PRO; PR:Q9HBY8; -.
Proteomes; UP000005640; Chromosome 20.
Bgee; ENSG00000101049; -.
CleanEx; HS_SGK2; -.
ExpressionAtlas; Q9HBY8; baseline and differential.
Genevisible; Q9HBY8; HS.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005622; C:intracellular; IBA:GO_Central.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0005246; F:calcium channel regulator activity; IBA:GO_Central.
GO; GO:0017081; F:chloride channel regulator activity; IBA:GO_Central.
GO; GO:0015459; F:potassium channel regulator activity; IDA:UniProtKB.
GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
GO; GO:0017080; F:sodium channel regulator activity; TAS:UniProtKB.
GO; GO:0035556; P:intracellular signal transduction; TAS:ProtInc.
GO; GO:0034220; P:ion transmembrane transport; TAS:Reactome.
GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
GO; GO:0032411; P:positive regulation of transporter activity; TAS:UniProtKB.
GO; GO:0006468; P:protein phosphorylation; TAS:ProtInc.
GO; GO:0042981; P:regulation of apoptotic process; IBA:GO_Central.
GO; GO:0001558; P:regulation of cell growth; TAS:UniProtKB.
GO; GO:0042127; P:regulation of cell proliferation; TAS:UniProtKB.
GO; GO:0006979; P:response to oxidative stress; TAS:ProtInc.
InterPro; IPR000961; AGC-kinase_C.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR017892; Pkinase_C.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR008271; Ser/Thr_kinase_AS.
Pfam; PF00069; Pkinase; 1.
Pfam; PF00433; Pkinase_C; 1.
SMART; SM00133; S_TK_X; 1.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS51285; AGC_KINASE_CTER; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
1: Evidence at protein level;
Alternative splicing; ATP-binding; Complete proteome; Cytoplasm;
Kinase; Nucleotide-binding; Nucleus; Phosphoprotein; Polymorphism;
Reference proteome; Serine/threonine-protein kinase; Transferase.
CHAIN 1 427 Serine/threonine-protein kinase Sgk2.
/FTId=PRO_0000086646.
DOMAIN 95 352 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
DOMAIN 353 427 AGC-kinase C-terminal.
NP_BIND 101 109 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOTIF 128 138 Nuclear localization signal.
{ECO:0000250}.
ACT_SITE 219 219 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 124 124 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 70 70 Phosphoserine.
{ECO:0000250|UniProtKB:Q8R4U9}.
MOD_RES 253 253 Phosphothreonine; by PDPK1.
{ECO:0000269|PubMed:10548550}.
MOD_RES 416 416 Phosphoserine. {ECO:0000255}.
VAR_SEQ 1 60 Missing (in isoform 1).
{ECO:0000303|PubMed:10548550,
ECO:0000303|PubMed:15489334,
ECO:0000303|Ref.3}.
/FTId=VSP_004932.
VAR_SEQ 19 52 Missing (in isoform 3).
{ECO:0000303|Ref.2}.
/FTId=VSP_026682.
VARIANT 12 12 S -> T (in dbSNP:rs33969356).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041073.
VARIANT 259 259 E -> K (in a lung adenocarcinoma sample;
somatic mutation).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041074.
VARIANT 349 349 H -> Y (in dbSNP:rs35793869).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041075.
MUTAGEN 416 416 S->D: Increased activation.
{ECO:0000269|PubMed:10548550}.
CONFLICT 137 137 Missing (in Ref. 4; CAI42315).
{ECO:0000305}.
CONFLICT 168 168 K -> E (in Ref. 2; AAX88805).
{ECO:0000305}.
CONFLICT 208 208 G -> D (in Ref. 3; AAV38901).
{ECO:0000305}.
CONFLICT 337 337 L -> P (in Ref. 2; AAX88805).
{ECO:0000305}.
SEQUENCE 427 AA; 47604 MW; D8F0FA6DF54B1370 CRC64;
MQGLLTSGRK PSGGGRCTGR GGWRGQWCLK PWMGGADPPT PTLSCLLLPV PPELPDHCYR
MNSSPAGTPS PQPSRANGNI NLGPSANPNA QPTDFDFLKV IGKGNYGKVL LAKRKSDGAF
YAVKVLQKKS ILKKKEQSHI MAERSVLLKN VRHPFLVGLR YSFQTPEKLY FVLDYVNGGE
LFFHLQRERR FLEPRARFYA AEVASAIGYL HSLNIIYRDL KPENILLDCQ GHVVLTDFGL
CKEGVEPEDT TSTFCGTPEY LAPEVLRKEP YDRAVDWWCL GAVLYEMLHG LPPFYSQDVS
QMYENILHQP LQIPGGRTVA ACDLLQSLLH KDQRQRLGSK ADFLEIKNHV FFSPINWDDL
YHKRLTPPFN PNVTGPADLK HFDPEFTQEA VSKSIGCTPD TVASSSGASS AFLGFSYAPE
DDDILDC


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