NR0B2_HUMAN
ID NR0B2_HUMAN Reviewed; 257 AA.
AC Q15466; F1D8P5; Q5QP36;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 197.
DE RecName: Full=Nuclear receptor subfamily 0 group B member 2;
DE AltName: Full=Orphan nuclear receptor SHP;
DE AltName: Full=Small heterodimer partner;
GN Name=NR0B2; Synonyms=SHP;
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 [GENOMIC DNA], AND TISSUE SPECIFICITY.
RX PubMed=8650544; DOI=10.1126/science.272.5266.1336;
RA Seol W., Choi H.-S., Moore D.D.;
RT "An orphan nuclear hormone receptor that lacks a DNA binding domain and
RT heterodimerizes with other receptors.";
RL Science 272:1336-1339(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9603951; DOI=10.1074/jbc.273.23.14398;
RA Lee H.-K., Lee Y.-K., Park S.-H., Kim Y.-S., Park S.H., Lee J.W.,
RA Kwon H.-B., Soh J., Moore D.D., Choi H.-S.;
RT "Structure and expression of the orphan nuclear receptor SHP gene.";
RL J. Biol. Chem. 273:14398-14402(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS EARLY-ONSET OBESITY TRP-57;
RP GLU-189; SER-195 AND CYS-213, VARIANT HIS-216, CHARACTERIZATION OF VARIANTS
RP EARLY-ONSET OBESITY TRP-57; GLU-189; SER-195 AND CYS-213, AND
RP CHARACTERIZATION OF VARIANT HIS-216.
RX PubMed=11136233; DOI=10.1073/pnas.98.2.575;
RA Nishigori H., Tomura H., Tonooka N., Kanamori M., Yamada S., Sho K.,
RA Inoue I., Kikuchi N., Onigata K., Kojima I., Kohama T., Yamagata K.,
RA Yang Q., Matsuzawa Y., Miki T., Seino S., Kim M.-Y., Choi H.-S., Lee Y.-K.,
RA Moore D.D., Takeda J.;
RT "Mutations in the small heterodimer partner gene are associated with mild
RT obesity in Japanese subjects.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:575-580(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RA Kaighin V.A., Martin A.L., Aronstam R.S.;
RT "Isolation of cDNA coding for multiple human nuclear receptor clones.";
RL Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Pancreas, and Spleen;
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 [8]
RP FUNCTION, HETERODIMERIZATION, INTERACTION WITH ID2 AND NEUROD1, AND
RP SUBCELLULAR LOCATION.
RX PubMed=14752053; DOI=10.1210/me.2003-0311;
RA Kim J.Y., Chu K., Kim H.J., Seong H.A., Park K.C., Sanyal S., Takeda J.,
RA Ha H., Shong M., Tsai M.J., Choi H.S.;
RT "Orphan nuclear receptor small heterodimer partner, a novel corepressor for
RT a basic helix-loop-helix transcription factor BETA2/neuroD.";
RL Mol. Endocrinol. 18:776-790(2004).
RN [9]
RP SUBCELLULAR LOCATION.
RX PubMed=28797635; DOI=10.1016/j.abb.2017.08.004;
RA Marczak M.M., Yan B.;
RT "Circadian rhythmicity: A functional connection between differentiated
RT embryonic chondrocyte-1 (DEC1) and small heterodimer partner (SHP).";
RL Arch. Biochem. Biophys. 631:11-18(2017).
RN [10]
RP INTERACTION WITH DDX3X AND HNF4A.
RX PubMed=28128295; DOI=10.1038/srep41452;
RA Tsai T.Y., Wang W.T., Li H.K., Chen W.J., Tsai Y.H., Chao C.H.,
RA Wu Lee Y.H.;
RT "RNA helicase DDX3 maintains lipid homeostasis through upregulation of the
RT microsomal triglyceride transfer protein by interacting with HNF4 and
RT SHP.";
RL Sci. Rep. 7:41452-41452(2017).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 15-28 IN COMPLEX WITH NR5A2.
RX PubMed=15723037; DOI=10.1038/nsmb910;
RA Ortlund E.A., Lee Y., Solomon I.H., Hager J.M., Safi R., Choi Y., Guan Z.,
RA Tripathy A., Raetz C.R.H., McDonnell D.P., Moore D.D., Redinbo M.R.;
RT "Modulation of human nuclear receptor LRH-1 activity by phospholipids and
RT SHP.";
RL Nat. Struct. Mol. Biol. 12:357-363(2005).
RN [12]
RP VARIANT TRP-57.
RX PubMed=21262773; DOI=10.1128/mcb.01212-10;
RA Kanamaluru D., Xiao Z., Fang S., Choi S.E., Kim D.H., Veenstra T.D.,
RA Kemper J.K.;
RT "Arginine methylation by PRMT5 at a naturally occurring mutation site is
RT critical for liver metabolic regulation by small heterodimer partner.";
RL Mol. Cell. Biol. 31:1540-1550(2011).
CC -!- FUNCTION: Transcriptional regulator that acts as a negative regulator
CC of receptor-dependent signaling pathways (By similarity). Specifically
CC inhibits transactivation of the nuclear receptor with which it
CC interacts (By similarity). Inhibits transcriptional activity of NEUROD1
CC on E-box-containing promoter by interfering with the coactivation
CC function of the p300/CBP-mediated transcription complex for NEUROD1
CC (PubMed:14752053). Essential component of the liver circadian clock
CC which via its interaction with NR1D1 and RORG regulates NPAS2-mediated
CC hepatic lipid metabolism (By similarity). Regulates the circadian
CC expression of cytochrome P450 (CYP) enzymes (By similarity). Represses:
CC NR5A2 and HNF4A to down-regulate CYP2C38, NFLI3 to up-regulate CYP2A5,
CC BHLHE41/HNF1A axis to up-regulate CYP1A2, CYP2E1 and CYP3A11, and NR1D1
CC to up-regulate CYP2B10, CYP4A10 and CYP4A14 (By similarity).
CC {ECO:0000250|UniProtKB:Q62227, ECO:0000269|PubMed:14752053}.
CC -!- SUBUNIT: Interacts (via N-terminus) with NEUROD1 (via N-terminus and C-
CC terminus) (PubMed:14752053). Interacts with ID2 (PubMed:14752053).
CC Interacts with RORG, NFIL3, NR1D1 and BHLHE41 (By similarity).
CC Heterodimer; efficient DNA binding requires dimerization with another
CC bHLH protein (PubMed:14752053). Interacts with RARA, RXRA, THRB, NR5A1,
CC NR5A2, NR1I3, PPARA, PPARG and EID1 (By similarity). Interacts with
CC HNF4A; the resulting heterodimer is transcriptionnally inactive
CC (PubMed:28128295). Interacts with DDX3X; this interaction disrupts the
CC interaction between HNF4 and NR0B2/SHP that forms inactive heterodimers
CC and enhances the formation of active HNF4 homodimers (PubMed:28128295).
CC {ECO:0000250|UniProtKB:P97947, ECO:0000250|UniProtKB:Q62227,
CC ECO:0000269|PubMed:14752053, ECO:0000269|PubMed:28128295}.
CC -!- INTERACTION:
CC Q15466; P54252: ATXN3; NbExp=3; IntAct=EBI-3910729, EBI-946046;
CC Q15466; Q96AQ7: CIDEC; NbExp=3; IntAct=EBI-3910729, EBI-14151404;
CC Q15466; P50570-2: DNM2; NbExp=3; IntAct=EBI-3910729, EBI-10968534;
CC Q15466; P62508-3: ESRRG; NbExp=3; IntAct=EBI-3910729, EBI-12001340;
CC Q15466; Q9Y4H4: GPSM3; NbExp=3; IntAct=EBI-3910729, EBI-347538;
CC Q15466; Q13547: HDAC1; NbExp=2; IntAct=EBI-3910729, EBI-301834;
CC Q15466; O15379: HDAC3; NbExp=2; IntAct=EBI-3910729, EBI-607682;
CC Q15466; Q00987: MDM2; NbExp=4; IntAct=EBI-3910729, EBI-389668;
CC Q15466; O00482-1: NR5A2; NbExp=2; IntAct=EBI-3910729, EBI-15960777;
CC Q15466; Q96EB6: SIRT1; NbExp=6; IntAct=EBI-3910729, EBI-1802965;
CC Q15466; P04637: TP53; NbExp=3; IntAct=EBI-3910729, EBI-366083;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14752053,
CC ECO:0000269|PubMed:28797635}. Cytoplasm {ECO:0000269|PubMed:14752053}.
CC Note=Colocalizes with NEUROD1 in the nucleus.
CC -!- TISSUE SPECIFICITY: Liver. Low levels of expression were detected in
CC heart and pancreas. {ECO:0000269|PubMed:8650544}.
CC -!- PTM: Arginine methylation by PRMT5 enhances repression activity of
CC metabolic genes in liver in response to bile acid signaling, by
CC increasing interaction with cofactors. {ECO:0000250|UniProtKB:Q62227}.
CC -!- DISEASE: Obesity (OBESITY) [MIM:601665]: A condition characterized by
CC an increase of body weight beyond the limitation of skeletal and
CC physical requirements, as the result of excessive accumulation of body
CC fat. {ECO:0000269|PubMed:11136233}. Note=Disease susceptibility is
CC associated with variants affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR0
CC subfamily. {ECO:0000305}.
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DR EMBL; L76571; AAC41998.1; -; Genomic_DNA.
DR EMBL; AB058644; BAB68530.1; -; Genomic_DNA.
DR EMBL; HQ692833; ADZ17344.1; -; mRNA.
DR EMBL; AL356390; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471059; EAX07781.1; -; Genomic_DNA.
DR EMBL; BC030207; AAH30207.1; -; mRNA.
DR CCDS; CCDS291.1; -.
DR RefSeq; NP_068804.1; NM_021969.2.
DR PDB; 1YUC; X-ray; 1.90 A; C/D=15-28.
DR PDB; 2Q3Y; X-ray; 2.40 A; B=18-27.
DR PDB; 2Z4J; X-ray; 2.60 A; B=115-124.
DR PDB; 4DOR; X-ray; 1.90 A; C/D=15-28.
DR PDB; 4ONI; X-ray; 1.80 A; C/D=12-30.
DR PDB; 5UFS; X-ray; 2.12 A; C/D=18-27.
DR PDB; 6W9M; X-ray; 1.59 A; B=17-27.
DR PDBsum; 1YUC; -.
DR PDBsum; 2Q3Y; -.
DR PDBsum; 2Z4J; -.
DR PDBsum; 4DOR; -.
DR PDBsum; 4ONI; -.
DR PDBsum; 5UFS; -.
DR PDBsum; 6W9M; -.
DR AlphaFoldDB; Q15466; -.
DR SMR; Q15466; -.
DR BioGRID; 114012; 71.
DR CORUM; Q15466; -.
DR DIP; DIP-46313N; -.
DR IntAct; Q15466; 30.
DR MINT; Q15466; -.
DR STRING; 9606.ENSP00000254227; -.
DR ChEMBL; CHEMBL5603; -.
DR GuidetoPHARMACOLOGY; 636; -.
DR GlyGen; Q15466; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q15466; -.
DR PhosphoSitePlus; Q15466; -.
DR BioMuta; NR0B2; -.
DR DMDM; 9978744; -.
DR jPOST; Q15466; -.
DR MassIVE; Q15466; -.
DR PaxDb; Q15466; -.
DR PeptideAtlas; Q15466; -.
DR PRIDE; Q15466; -.
DR Antibodypedia; 16231; 433 antibodies from 35 providers.
DR DNASU; 8431; -.
DR Ensembl; ENST00000254227.4; ENSP00000254227.3; ENSG00000131910.5.
DR GeneID; 8431; -.
DR KEGG; hsa:8431; -.
DR MANE-Select; ENST00000254227.4; ENSP00000254227.3; NM_021969.3; NP_068804.1.
DR UCSC; uc001bnf.4; human.
DR CTD; 8431; -.
DR DisGeNET; 8431; -.
DR GeneCards; NR0B2; -.
DR HGNC; HGNC:7961; NR0B2.
DR HPA; ENSG00000131910; Tissue enhanced (intestine, liver).
DR MalaCards; NR0B2; -.
DR MIM; 601665; phenotype.
DR MIM; 604630; gene.
DR neXtProt; NX_Q15466; -.
DR OpenTargets; ENSG00000131910; -.
DR PharmGKB; PA31747; -.
DR VEuPathDB; HostDB:ENSG00000131910; -.
DR eggNOG; KOG3575; Eukaryota.
DR GeneTree; ENSGT00390000015719; -.
DR HOGENOM; CLU_093194_0_0_1; -.
DR InParanoid; Q15466; -.
DR OMA; FFRPIVG; -.
DR OrthoDB; 1474731at2759; -.
DR PhylomeDB; Q15466; -.
DR TreeFam; TF332386; -.
DR PathwayCommons; Q15466; -.
DR Reactome; R-HSA-383280; Nuclear Receptor transcription pathway.
DR SignaLink; Q15466; -.
DR SIGNOR; Q15466; -.
DR BioGRID-ORCS; 8431; 22 hits in 1088 CRISPR screens.
DR ChiTaRS; NR0B2; human.
DR EvolutionaryTrace; Q15466; -.
DR GeneWiki; Small_heterodimer_partner; -.
DR GenomeRNAi; 8431; -.
DR Pharos; Q15466; Tchem.
DR PRO; PR:Q15466; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q15466; protein.
DR Bgee; ENSG00000131910; Expressed in right lobe of liver and 59 other tissues.
DR Genevisible; Q15466; HS.
DR GO; GO:0000785; C:chromatin; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; IEA:Ensembl.
DR GO; GO:0046965; F:nuclear retinoid X receptor binding; IEA:Ensembl.
DR GO; GO:0046966; F:nuclear thyroid hormone receptor binding; IEA:Ensembl.
DR GO; GO:0042975; F:peroxisome proliferator activated receptor binding; IEA:Ensembl.
DR GO; GO:0019904; F:protein domain specific binding; IPI:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB.
DR GO; GO:0044877; F:protein-containing complex binding; IEA:Ensembl.
DR GO; GO:0003714; F:transcription corepressor activity; IDA:GO_Central.
DR GO; GO:0140416; F:transcription regulator inhibitor activity; IDA:MGI.
DR GO; GO:0031100; P:animal organ regeneration; IEA:Ensembl.
DR GO; GO:0015721; P:bile acid and bile salt transport; IEA:Ensembl.
DR GO; GO:0008203; P:cholesterol metabolic process; TAS:ProtInc.
DR GO; GO:0032922; P:circadian regulation of gene expression; ISS:UniProtKB.
DR GO; GO:0007623; P:circadian rhythm; IDA:UniProtKB.
DR GO; GO:0043433; P:negative regulation of DNA-binding transcription factor activity; IDA:UniProtKB.
DR GO; GO:0010629; P:negative regulation of gene expression; IMP:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0007219; P:Notch signaling pathway; IEA:Ensembl.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:UniProtKB.
DR GO; GO:0032024; P:positive regulation of insulin secretion; IEA:Ensembl.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:MGI.
DR GO; GO:0045471; P:response to ethanol; IEA:Ensembl.
DR GO; GO:0009749; P:response to glucose; IEA:Ensembl.
DR GO; GO:0014070; P:response to organic cyclic compound; IEA:Ensembl.
DR Gene3D; 1.10.565.10; -; 1.
DR IDEAL; IID00081; -.
DR InterPro; IPR035500; NHR-like_dom_sf.
DR InterPro; IPR033544; NR0B1/2.
DR InterPro; IPR000536; Nucl_hrmn_rcpt_lig-bd.
DR InterPro; IPR001723; Nuclear_hrmn_rcpt.
DR PANTHER; PTHR24081; PTHR24081; 1.
DR Pfam; PF00104; Hormone_recep; 1.
DR PRINTS; PR00398; STRDHORMONER.
DR SMART; SM00430; HOLI; 1.
DR SUPFAM; SSF48508; SSF48508; 1.
DR PROSITE; PS51843; NR_LBD; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Biological rhythms; Cytoplasm; Disease variant; Methylation;
KW Nucleus; Obesity; Receptor; Reference proteome; Repressor; Transcription;
KW Transcription regulation.
FT CHAIN 1..257
FT /note="Nuclear receptor subfamily 0 group B member 2"
FT /id="PRO_0000053752"
FT DOMAIN 16..257
FT /note="NR LBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01189"
FT MOD_RES 57
FT /note="Symmetric dimethylarginine; by PRMT5"
FT /evidence="ECO:0000250|UniProtKB:Q62227"
FT VARIANT 57
FT /note="R -> W (in early-onset obesity; Japanese population;
FT loss of methylation and repressor activity;
FT dbSNP:rs777291973)"
FT /evidence="ECO:0000269|PubMed:11136233,
FT ECO:0000269|PubMed:21262773"
FT /id="VAR_026015"
FT VARIANT 171
FT /note="G -> A (in dbSNP:rs6659176)"
FT /id="VAR_050584"
FT VARIANT 189
FT /note="G -> E (in early-onset obesity; Japanese population;
FT strong decrease of repressor activity; dbSNP:rs202154574)"
FT /evidence="ECO:0000269|PubMed:11136233"
FT /id="VAR_026016"
FT VARIANT 195
FT /note="A -> S (in early-onset obesity; Japanese population;
FT slight decrease of repressor activity; dbSNP:rs74315350)"
FT /evidence="ECO:0000269|PubMed:11136233"
FT /id="VAR_026017"
FT VARIANT 213
FT /note="R -> C (in early-onset obesity; Japanese population;
FT loss of repressor activity; dbSNP:rs199976415)"
FT /evidence="ECO:0000269|PubMed:11136233"
FT /id="VAR_026018"
FT VARIANT 216
FT /note="R -> H (no effect on repressor activity;
FT dbSNP:rs200475847)"
FT /evidence="ECO:0000269|PubMed:11136233"
FT /id="VAR_026019"
FT HELIX 14..16
FT /evidence="ECO:0007829|PDB:4ONI"
FT HELIX 19..25
FT /evidence="ECO:0007829|PDB:6W9M"
FT HELIX 118..122
FT /evidence="ECO:0007829|PDB:2Z4J"
SQ SEQUENCE 257 AA; 28058 MW; 14BEE2B3FF46154A CRC64;
MSTSQPGACP CQGAASRPAI LYALLSSSLK AVPRPRSRCL CRQHRPVQLC APHRTCREAL
DVLAKTVAFL RNLPSFWQLP PQDQRRLLQG CWGPLFLLGL AQDAVTFEVA EAPVPSILKK
ILLEEPSSSG GSGQLPDRPQ PSLAAVQWLQ CCLESFWSLE LSPKEYACLK GTILFNPDVP
GLQAASHIGH LQQEAHWVLC EVLEPWCPAA QGRLTRVLLT ASTLKSIPTS LLGDLFFRPI
IGDVDIAGLL GDMLLLR
