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 24-JAN-2024, entry version 204. 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 transcriptionally 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 PDB; 7YXC; X-ray; 2.25 A; R=17-27. DR PDB; 7YXD; X-ray; 2.30 A; C/F/J/N=17-28. DR PDB; 7YXN; X-ray; 2.46 A; R/S=17-27. DR PDB; 7YXO; X-ray; 2.99 A; B/D/F=17-27. DR PDB; 7YXP; X-ray; 3.36 A; B=16-28. DR PDB; 7YXR; X-ray; 2.50 A; R/S=17-28. DR PDBsum; 1YUC; -. DR PDBsum; 2Q3Y; -. DR PDBsum; 2Z4J; -. DR PDBsum; 4DOR; -. DR PDBsum; 4ONI; -. DR PDBsum; 5UFS; -. DR PDBsum; 6W9M; -. DR PDBsum; 7YXC; -. DR PDBsum; 7YXD; -. DR PDBsum; 7YXN; -. DR PDBsum; 7YXO; -. DR PDBsum; 7YXP; -. DR PDBsum; 7YXR; -. DR AlphaFoldDB; Q15466; -. DR SMR; Q15466; -. DR BioGRID; 114012; 72. 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; 9606-ENSP00000254227; -. DR PeptideAtlas; Q15466; -. DR Antibodypedia; 16231; 484 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 AGR; HGNC:7961; -. 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; 5393882at2759; -. 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; 25 hits in 1168 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 60 other cell types or tissues. 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: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:0045892; P:negative regulation of DNA-templated transcription; ISS: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:0007219; P:Notch signaling pathway; IEA:Ensembl. DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; IDA:MGI. 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: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 CDD; cd07349; NR_LBD_SHP; 1. DR Gene3D; 1.10.565.10; Retinoid X Receptor; 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; NUCLEAR RECEPTOR SUBFAMILY 0 GROUP B; 1. DR PANTHER; PTHR24081:SF0; NUCLEAR RECEPTOR SUBFAMILY 0 GROUP B MEMBER 2; 1. DR Pfam; PF00104; Hormone_recep; 1. DR PRINTS; PR00398; STRDHORMONER. DR SMART; SM00430; HOLI; 1. DR SUPFAM; SSF48508; Nuclear receptor ligand-binding domain; 1. DR PROSITE; PS51843; NR_LBD; 1. DR Genevisible; Q15466; HS. 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 //