SGK2_HUMAN
ID SGK2_HUMAN Reviewed; 367 AA.
AC Q9HBY8; Q52PK5; Q5H8Y6; Q5H8Z1; Q5TZR3; Q9UKG6;
DT 22-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2021, sequence version 2.
DT 03-AUG-2022, entry version 182.
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 Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), TISSUE SPECIFICITY,
RP PHOSPHORYLATION AT THR-193, AND MUTAGENESIS OF SER-356.
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 [MRNA] (ISOFORM 3).
RA Li H., Nong W., Zhou G., Ke R., Shen C., Zhong G., Zheng Z., Liang M.,
RA Xiao W., Lin L., Yang S.;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain, and Colon;
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 [6]
RP FUNCTION IN THE REGULATION OF NA(+)/K(+) ATPASE.
RX PubMed=12590200; DOI=10.1159/000068699;
RA Henke G., Setiawan I., Boehmer C., Lang F.;
RT "Activation of Na+/K+-ATPase by the serum and glucocorticoid-dependent
RT kinase isoforms.";
RL Kidney Blood Press. Res. 25:370-374(2002).
RN [7]
RP FUNCTION.
RX PubMed=12397388; DOI=10.1007/s00424-002-0873-2;
RA Gamper N., Fillon S., Feng Y., Friedrich B., Lang P.A., Henke G.,
RA Huber S.M., Kobayashi T., Cohen P., Lang F.;
RT "K(+) channel activation by all three isoforms of serum- and
RT glucocorticoid-dependent protein kinase SGK.";
RL Pflugers Arch. 445:60-66(2002).
RN [8]
RP FUNCTION IN THE REGULATION OF KCNE1 AND KCNQ1.
RX PubMed=12634932; DOI=10.1007/s00424-002-0982-y;
RA Embark H.M., Boehmer C., Vallon V., Luft F., Lang F.;
RT "Regulation of KCNE1-dependent K(+) current by the serum and
RT glucocorticoid-inducible kinase (SGK) isoforms.";
RL Pflugers Arch. 445:601-606(2003).
RN [9]
RP FUNCTION IN THE REGULATION OF SCNN1A/ENAC.
RX PubMed=12632189; DOI=10.1007/s00424-002-0993-8;
RA Friedrich B., Feng Y., Cohen P., Risler T., Vandewalle A., Broeer S.,
RA Wang J., Pearce D., Lang F.;
RT "The serine/threonine kinases SGK2 and SGK3 are potent stimulators of the
RT epithelial Na+ channel alpha,beta,gamma-ENaC.";
RL Pflugers Arch. 445:693-696(2003).
RN [10]
RP FUNCTION IN THE REGULATION OF KCNA3/KV1.3.
RX PubMed=15040001; DOI=10.1002/jcp.10430;
RA Henke G., Maier G., Wallisch S., Boehmer C., Lang F.;
RT "Regulation of the voltage gated K+ channel Kv1.3 by the ubiquitin ligase
RT Nedd4-2 and the serum and glucocorticoid inducible kinase SGK1.";
RL J. Cell. Physiol. 199:194-199(2004).
RN [11]
RP FUNCTION IN THE REGULATION OF SLC6A19.
RX PubMed=20511718; DOI=10.1159/000315092;
RA Boehmer C., Sopjani M., Klaus F., Lindner R., Laufer J., Jeyaraj S.,
RA Lang F., Palmada M.;
RT "The serum and glucocorticoid inducible kinases SGK1-3 stimulate the
RT neutral amino acid transporter SLC6A19.";
RL Cell. Physiol. Biochem. 25:723-732(2010).
RN [12]
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).
RN [13]
RP REVIEW.
RX PubMed=16460280; DOI=10.1146/annurev.physiol.68.040104.131654;
RA Loffing J., Flores S.Y., Staub O.;
RT "Sgk kinases and their role in epithelial transport.";
RL Annu. Rev. Physiol. 68:461-490(2006).
RN [14]
RP REVIEW ON FUNCTION.
RX PubMed=20919962; DOI=10.3109/08977194.2010.518616;
RA Bruhn M.A., Pearson R.B., Hannan R.D., Sheppard K.E.;
RT "Second AKT: the rise of SGK in cancer signalling.";
RL Growth Factors 28:394-408(2010).
RN [15]
RP VARIANTS [LARGE SCALE ANALYSIS] LYS-199 AND TYR-289, AND VARIANT THR-12
RP (ISOFORM 2).
RX PubMed=17344846; DOI=10.1038/nature05610;
RA Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G.,
RA Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S.,
RA Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.,
RA Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K.,
RA Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D.,
RA Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R.,
RA Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A.,
RA Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F.,
RA Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F.,
RA Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G.,
RA Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R.,
RA Futreal P.A., Stratton M.R.;
RT "Patterns of somatic mutation in human cancer genomes.";
RL Nature 446:153-158(2007).
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:12397388,
CC ECO:0000269|PubMed:12590200, ECO:0000269|PubMed:12632189,
CC ECO:0000269|PubMed:12634932, ECO:0000269|PubMed:15040001,
CC ECO:0000269|PubMed:20511718, 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 -!- INTERACTION:
CC Q9HBY8; P08238: HSP90AB1; NbExp=2; IntAct=EBI-3914329, EBI-352572;
CC Q9HBY8-2; Q9BW71: HIRIP3; NbExp=5; IntAct=EBI-12143041, EBI-723624;
CC Q9HBY8-2; O15305: PMM2; NbExp=5; IntAct=EBI-12143041, EBI-10182608;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21865597}. Nucleus
CC {ECO:0000269|PubMed:21865597}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=alpha;
CC IsoId=Q9HBY8-2; Sequence=Displayed;
CC Name=2; Synonyms=beta;
CC IsoId=Q9HBY8-1; Sequence=VSP_060876;
CC Name=3;
CC IsoId=Q9HBY8-3; Sequence=VSP_060877;
CC -!- TISSUE SPECIFICITY: Highly expressed in liver, kidney and pancreas, and
CC at lower levels in brain. {ECO:0000269|PubMed:10548550}.
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.
CC {ECO:0000269|PubMed:10548550}.
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; AF169034; AAF12757.2; -; mRNA.
DR EMBL; AF186470; AAG17012.1; -; mRNA.
DR EMBL; AY987010; AAX88805.1; -; mRNA.
DR EMBL; BT020098; AAV38901.1; -; mRNA.
DR EMBL; Z98752; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC014037; AAH14037.3; -; mRNA.
DR EMBL; BC065511; AAH65511.1; -; mRNA.
DR CCDS; CCDS13320.1; -. [Q9HBY8-2]
DR CCDS; CCDS13321.1; -. [Q9HBY8-2]
DR RefSeq; NP_001186193.1; NM_001199264.1. [Q9HBY8-2]
DR RefSeq; NP_057360.2; NM_016276.3. [Q9HBY8-1]
DR RefSeq; NP_733794.1; NM_170693.2. [Q9HBY8-2]
DR AlphaFoldDB; Q9HBY8; -.
DR SMR; Q9HBY8; -.
DR BioGRID; 115416; 27.
DR IntAct; Q9HBY8; 20.
DR STRING; 9606.ENSP00000340608; -.
DR BindingDB; Q9HBY8; -.
DR ChEMBL; CHEMBL5794; -.
DR GuidetoPHARMACOLOGY; 1535; -.
DR iPTMnet; Q9HBY8; -.
DR PhosphoSitePlus; Q9HBY8; -.
DR BioMuta; SGK2; -.
DR DMDM; 28558166; -.
DR jPOST; Q9HBY8; -.
DR MassIVE; Q9HBY8; -.
DR MaxQB; Q9HBY8; -.
DR PaxDb; Q9HBY8; -.
DR PeptideAtlas; Q9HBY8; -.
DR PRIDE; Q9HBY8; -.
DR ProteomicsDB; 81612; -. [Q9HBY8-1]
DR ProteomicsDB; 81613; -. [Q9HBY8-2]
DR ProteomicsDB; 81614; -. [Q9HBY8-3]
DR Antibodypedia; 1638; 324 antibodies from 32 providers.
DR DNASU; 10110; -.
DR Ensembl; ENST00000341458.10; ENSP00000340608.5; ENSG00000101049.18. [Q9HBY8-2]
DR Ensembl; ENST00000373100.7; ENSP00000362192.1; ENSG00000101049.18. [Q9HBY8-2]
DR Ensembl; ENST00000423407.7; ENSP00000392795.3; ENSG00000101049.18. [Q9HBY8-2]
DR Ensembl; ENST00000426287.3; ENSP00000412214.2; ENSG00000101049.18. [Q9HBY8-2]
DR GeneID; 10110; -.
DR KEGG; hsa:10110; -.
DR MANE-Select; ENST00000373100.7; ENSP00000362192.1; NM_170693.3; NP_733794.1.
DR UCSC; uc002xkr.4; human. [Q9HBY8-2]
DR CTD; 10110; -.
DR DisGeNET; 10110; -.
DR GeneCards; SGK2; -.
DR HGNC; HGNC:13900; SGK2.
DR HPA; ENSG00000101049; Tissue enhanced (intestine, kidney, liver).
DR MIM; 607589; gene.
DR neXtProt; NX_Q9HBY8; -.
DR OpenTargets; ENSG00000101049; -.
DR VEuPathDB; HostDB:ENSG00000101049; -.
DR eggNOG; KOG0598; Eukaryota.
DR GeneTree; ENSGT00940000153776; -.
DR InParanoid; Q9HBY8; -.
DR OrthoDB; 614710at2759; -.
DR PhylomeDB; Q9HBY8; -.
DR TreeFam; TF320906; -.
DR PathwayCommons; Q9HBY8; -.
DR Reactome; R-HSA-2672351; Stimuli-sensing channels.
DR SignaLink; Q9HBY8; -.
DR SIGNOR; Q9HBY8; -.
DR BioGRID-ORCS; 10110; 11 hits in 1106 CRISPR screens.
DR ChiTaRS; SGK2; human.
DR GeneWiki; SGK2; -.
DR GenomeRNAi; 10110; -.
DR Pharos; Q9HBY8; Tchem.
DR PRO; PR:Q9HBY8; -.
DR Proteomes; UP000005640; Chromosome 20.
DR RNAct; Q9HBY8; protein.
DR Bgee; ENSG00000101049; Expressed in mucosa of transverse colon and 141 other tissues.
DR ExpressionAtlas; Q9HBY8; baseline and differential.
DR Genevisible; Q9HBY8; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0015459; F:potassium channel regulator activity; IDA: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:0017080; F:sodium channel regulator activity; TAS:UniProtKB.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR GO; GO:0032411; P:positive regulation of transporter activity; TAS:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; TAS:ProtInc.
DR GO; GO:0001558; P:regulation of cell growth; TAS:UniProtKB.
DR GO; GO:0042127; P:regulation of cell population proliferation; TAS:UniProtKB.
DR GO; GO:0006979; P:response to oxidative stress; TAS:ProtInc.
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_0000086646"
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..26
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:0000269|PubMed:10548550"
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 1
FT /note="M -> MQGLLTSGRKPSGGGRCTGRGGWRGQWCLKPWMGGADPPTPTLSCLL
FT LPVPPELPDHCYRM (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_060876"
FT VAR_SEQ 1
FT /note="M -> MQGLLTSGRKPSGGGRCTELPDHCYRM (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_060877"
FT VARIANT 199
FT /note="E -> K (in a lung adenocarcinoma sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041074"
FT VARIANT 289
FT /note="H -> Y (in dbSNP:rs35793869)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041075"
FT MUTAGEN 356
FT /note="S->D: Increased activation."
FT /evidence="ECO:0000269|PubMed:10548550"
FT CONFLICT 108
FT /note="K -> E (in Ref. 2; AAX88805)"
FT /evidence="ECO:0000305"
FT CONFLICT 148
FT /note="G -> D (in Ref. 3; AAV38901)"
FT /evidence="ECO:0000305"
FT CONFLICT 277
FT /note="L -> P (in Ref. 2; AAX88805)"
FT /evidence="ECO:0000305"
FT VARIANT Q9HBY8-1:12
FT /note="S -> T (in dbSNP:rs33969356)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_083966"
SQ SEQUENCE 367 AA; 41175 MW; E53F1ABE253F648B CRC64;
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
