SGK2_MOUSE
ID SGK2_MOUSE Reviewed; 367 AA.
AC Q9QZS5; B7ZC31; Q8R0P6;
DT 22-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=Serine/threonine-protein kinase Sgk2;
DE EC=2.7.11.1;
DE AltName: Full=Serum/glucocorticoid-regulated kinase 2;
GN Name=Sgk2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=10548550; DOI=10.1042/bj3440189;
RA Kobayashi T., Deak M., Morrice N., Cohen P.;
RT "Characterization of the structure and regulation of two novel isoforms of
RT serum- and glucocorticoid-induced protein kinase.";
RL Biochem. J. 344:189-197(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Kidney;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Kidney;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP FUNCTION IN THE REGULATION OF GRIA1/GLUR1.
RX PubMed=15774536; DOI=10.1113/jphysiol.2004.079582;
RA Strutz-Seebohm N., Seebohm G., Mack A.F., Wagner H.J., Just L.,
RA Skutella T., Lang U.E., Henke G., Striegel M., Hollmann M., Rouach N.,
RA Nicoll R.A., McCormick J.A., Wang J., Pearce D., Lang F.;
RT "Regulation of GluR1 abundance in murine hippocampal neurones by serum- and
RT glucocorticoid-inducible kinase 3.";
RL J. Physiol. (Lond.) 565:381-390(2005).
RN [6]
RP FUNCTION IN THE REGULATION OF GRIK2/GLUR6.
RX PubMed=15774535; DOI=10.1113/jphysiol.2004.079624;
RA Strutz-Seebohm N., Seebohm G., Shumilina E., Mack A.F., Wagner H.J.,
RA Lampert A., Grahammer F., Henke G., Just L., Skutella T., Hollmann M.,
RA Lang F.;
RT "Glucocorticoid adrenal steroids and glucocorticoid-inducible kinase
RT isoforms in the regulation of GluR6 expression.";
RL J. Physiol. (Lond.) 565:391-401(2005).
RN [7]
RP FUNCTION IN THE REGULATION OF SLC9A3/NHE3, AND SUBCELLULAR LOCATION.
RX PubMed=21865597; DOI=10.1091/mbc.e11-04-0328;
RA He P., Lee S.J., Lin S., Seidler U., Lang F., Fejes-Toth G.,
RA Naray-Fejes-Toth A., Yun C.C.;
RT "Serum- and glucocorticoid-induced kinase 3 in recycling endosomes mediates
RT acute activation of Na+/H+ exchanger NHE3 by glucocorticoids.";
RL Mol. Biol. Cell 22:3812-3825(2011).
CC -!- FUNCTION: Serine/threonine-protein kinase which is involved in the
CC regulation of a wide variety of ion channels, membrane transporters,
CC cell growth, survival and proliferation. Up-regulates Na(+) channels:
CC SCNN1A/ENAC, K(+) channels: KCNA3/Kv1.3, KCNE1 and KCNQ1, amino acid
CC transporter: SLC6A19, glutamate transporter: SLC1A6/EAAT4, glutamate
CC receptors: GRIA1/GLUR1 and GRIK2/GLUR6, Na(+)/H(+) exchanger:
CC SLC9A3/NHE3, and the Na(+)/K(+) ATPase. {ECO:0000269|PubMed:15774535,
CC ECO:0000269|PubMed:15774536, ECO:0000269|PubMed:21865597}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1;
CC -!- ACTIVITY REGULATION: Two specific sites, one in the kinase domain (Thr-
CC 193) and the other in the C-terminal regulatory region (Ser-356), need
CC to be phosphorylated for its full activation.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9QZS5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9QZS5-2; Sequence=VSP_004933;
CC -!- PTM: Activated by phosphorylation on Ser-356 by an unknown kinase (may
CC be mTORC2 but not confirmed), transforming it into a substrate for
CC PDPK1 which then phosphorylates it on Thr-193. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC protein kinase family. {ECO:0000305}.
CC -!- CAUTION: Not regulated by serum or glucocorticoids. {ECO:0000305}.
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DR EMBL; AF169033; AAF12756.1; -; mRNA.
DR EMBL; AK050009; BAC34031.1; -; mRNA.
DR EMBL; AL591584; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC026549; AAH26549.1; -; mRNA.
DR CCDS; CCDS17004.1; -. [Q9QZS5-1]
DR CCDS; CCDS71184.1; -. [Q9QZS5-2]
DR RefSeq; NP_001278081.1; NM_001291152.1.
DR RefSeq; NP_001278083.1; NM_001291154.1. [Q9QZS5-2]
DR RefSeq; NP_038759.1; NM_013731.3. [Q9QZS5-1]
DR RefSeq; XP_006499721.1; XM_006499658.3. [Q9QZS5-1]
DR RefSeq; XP_011237882.1; XM_011239580.2. [Q9QZS5-2]
DR AlphaFoldDB; Q9QZS5; -.
DR SMR; Q9QZS5; -.
DR STRING; 10090.ENSMUSP00000018012; -.
DR iPTMnet; Q9QZS5; -.
DR PhosphoSitePlus; Q9QZS5; -.
DR jPOST; Q9QZS5; -.
DR MaxQB; Q9QZS5; -.
DR PaxDb; Q9QZS5; -.
DR PRIDE; Q9QZS5; -.
DR ProteomicsDB; 261012; -. [Q9QZS5-1]
DR ProteomicsDB; 261013; -. [Q9QZS5-2]
DR Antibodypedia; 1638; 324 antibodies from 32 providers.
DR DNASU; 27219; -.
DR Ensembl; ENSMUST00000018012; ENSMUSP00000018012; ENSMUSG00000017868. [Q9QZS5-1]
DR Ensembl; ENSMUST00000117123; ENSMUSP00000112468; ENSMUSG00000017868. [Q9QZS5-2]
DR GeneID; 27219; -.
DR KEGG; mmu:27219; -.
DR UCSC; uc008nsf.2; mouse. [Q9QZS5-2]
DR UCSC; uc008nsg.3; mouse. [Q9QZS5-1]
DR CTD; 10110; -.
DR MGI; MGI:1351318; Sgk2.
DR VEuPathDB; HostDB:ENSMUSG00000017868; -.
DR eggNOG; KOG0598; Eukaryota.
DR GeneTree; ENSGT00940000153776; -.
DR HOGENOM; CLU_000288_63_5_1; -.
DR InParanoid; Q9QZS5; -.
DR OMA; PRANGNI; -.
DR OrthoDB; 614710at2759; -.
DR PhylomeDB; Q9QZS5; -.
DR TreeFam; TF320906; -.
DR Reactome; R-MMU-2672351; Stimuli-sensing channels.
DR BioGRID-ORCS; 27219; 2 hits in 74 CRISPR screens.
DR ChiTaRS; Sgk2; mouse.
DR PRO; PR:Q9QZS5; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q9QZS5; protein.
DR Bgee; ENSMUSG00000017868; Expressed in right kidney and 71 other tissues.
DR Genevisible; Q9QZS5; MM.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0015459; F:potassium channel regulator activity; ISS:UniProtKB.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR InterPro; IPR000961; AGC-kinase_C.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR017892; Pkinase_C.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00433; Pkinase_C; 1.
DR SMART; SM00133; S_TK_X; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Cytoplasm; Kinase; Nucleotide-binding;
KW Nucleus; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..367
FT /note="Serine/threonine-protein kinase Sgk2"
FT /id="PRO_0000086647"
FT DOMAIN 35..292
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 293..367
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00618"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 68..78
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250"
FT ACT_SITE 159
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 41..49
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 64
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 10
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8R4U9"
FT MOD_RES 193
FT /note="Phosphothreonine; by PDPK1"
FT /evidence="ECO:0000250|UniProtKB:Q9HBY8"
FT MOD_RES 334
FT /note="Phosphoserine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00618"
FT MOD_RES 356
FT /note="Phosphoserine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00618"
FT MOD_RES 357
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00618"
FT VAR_SEQ 171..199
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_004933"
FT CONFLICT 77
FT /note="Missing (in Ref. 4; AAH26549)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 367 AA; 41359 MW; 668C04B1A1E9E33A CRC64;
MASSPVGVPS PQPSRANGNI NLGPSANPNA RPTDFDFLKV IGKGNYGKVL LAKRKSDGAF
YAVKVLQKKS ILKNKEQNHI MAERNVLLKN VRHPFLVGLR YSFQTPEKLY FVLDYVNGGE
LFFHLQRERR FLEPRARFYT AEVASAIGYL HSLNIIYRDL KPENILLDCQ GHVVLTDFGL
CKECVEPEET TSTFCGTPEY LAPEVLRKEP YDRAVDWWCL GAVLYEMLHG LPPFFNTDVA
QMYENILHQP LQIPGGRTVA ACDLLQGLLH KDQRQRLGSK EDFLDIKNHM FFSPINWDDL
YHKRLTPPFN PNVEGPADLK HFDPEFTQEA VSKSIGCTPD TVASSSGASS AFLGFSYAQD
DDDILDS
