NR2C1_HUMAN
ID NR2C1_HUMAN Reviewed; 603 AA.
AC P13056; A8K5K4; Q15625; Q15626;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 14-APR-2009, sequence version 2.
DT 03-AUG-2022, entry version 206.
DE RecName: Full=Nuclear receptor subfamily 2 group C member 1;
DE AltName: Full=Orphan nuclear receptor TR2;
DE AltName: Full=Testicular receptor 2;
GN Name=NR2C1; Synonyms=TR2;
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] (ISOFORM 3).
RC TISSUE=Testis;
RX PubMed=3421977; DOI=10.1016/s0006-291x(88)80591-6;
RA Chang C., Kokontis J.;
RT "Identification of a new member of the steroid receptor super-family by
RT cloning and sequence analysis.";
RL Biochem. Biophys. Res. Commun. 155:971-977(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RX PubMed=2597158; DOI=10.1016/s0006-291x(89)80028-2;
RA Chang C., Kokontis J., Acakpo-Satchivi L., Liao S., Takeda H., Chang Y.;
RT "Molecular cloning of new human TR2 receptors: a class of steroid receptor
RT with multiple ligand-binding domains.";
RL Biochem. Biophys. Res. Commun. 165:735-741(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Tongue;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=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 [7]
RP FUNCTION, AND INTERACTION WITH ESR1.
RX PubMed=12093804; DOI=10.1074/jbc.m203531200;
RA Hu Y.C., Shyr C.R., Che W., Mu X.M., Kim E., Chang C.;
RT "Suppression of estrogen receptor-mediated transcription and cell growth by
RT interaction with TR2 orphan receptor.";
RL J. Biol. Chem. 277:33571-33579(2002).
RN [8]
RP FUNCTION.
RX PubMed=17010934; DOI=10.1016/j.bbrc.2006.09.061;
RA Lin Y.L., Wang Y.H., Lee H.J.;
RT "Transcriptional regulation of the human TR2 orphan receptor gene by
RT nuclear factor 1-A.";
RL Biochem. Biophys. Res. Commun. 350:430-436(2006).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-215 AND THR-220, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-215, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [12]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-250 AND LYS-588, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
CC -!- FUNCTION: Orphan nuclear receptor. Binds the IR7 element in the
CC promoter of its own gene in an autoregulatory negative feedback
CC mechanism. Primarily repressor of a broad range of genes. Binds to
CC hormone response elements (HREs) consisting of two 5'-AGGTCA-3' half
CC site direct repeat consensus sequences. Together with NR2C2, forms the
CC core of the DRED (direct repeat erythroid-definitive) complex that
CC represses embryonic and fetal globin transcription. Also activator of
CC OCT4 gene expression. May be involved in stem cell proliferation and
CC differentiation. Mediator of retinoic acid-regulated preadipocyte
CC proliferation. {ECO:0000269|PubMed:12093804,
CC ECO:0000269|PubMed:17010934}.
CC -!- SUBUNIT: Homodimer (By similarity). Heterodimer; binds DNA as a
CC heterodimer with NR2C2 required for chromatin remodeling and for
CC binding to promoter regions such as globin DR1 repeats (By similarity).
CC Interacts with NRIP1 (via its LXXLL motifs); the interaction provides
CC corepressor activity. Interacts with HDAC3 (via the DNA-binding
CC domain). Interacts with HDAC4 (via the DNA-binding domain). Interacts
CC with PIAS1; the interaction is required for sumoylation of NR2C1.
CC Interacts with UBE2I; the interaction is required for sumoylation of
CC NR2C1. Interacts with KAT2B; the interaction acts as a corepressor of
CC gene expression (By similarity). Interacts with ESR1; the interaction
CC prevents homodimerization of ESR1 and suppresses its transcriptional
CC activity and cell growth. {ECO:0000250, ECO:0000269|PubMed:12093804}.
CC -!- INTERACTION:
CC P13056-2; P10276: RARA; NbExp=3; IntAct=EBI-18764867, EBI-413374;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00407}.
CC Nucleus, PML body {ECO:0000250}. Note=Recruited by HDAC3, after all-
CC trans retinoic acid stimulated MAPK1-mediated Thr-223 phosphorylation,
CC to PML bodies for subsequent sumoylation. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=TR2-11;
CC IsoId=P13056-1; Sequence=Displayed;
CC Name=2; Synonyms=TR2-9;
CC IsoId=P13056-2; Sequence=VSP_036855, VSP_036857;
CC Name=3; Synonyms=TR2-7;
CC IsoId=P13056-3; Sequence=VSP_036856, VSP_036858;
CC -!- PTM: Sumoylation requires both PIAS1 and UBE2I. Sumoylation appears to
CC dissociate NR2C1 from the PML nuclear bodies. Enhances the interaction
CC with NRIP1 but inhibits interaction with KAT2B. In proliferating cells,
CC stimulation by all-trans retinoic acid, activation of MAPK1-mediated
CC phosphorylation and recruitment to PML bodies with subsequent
CC sumoylation, suppresses OCT4 expression (By similarity). {ECO:0000250}.
CC -!- PTM: Phosphorylated on several serine and threonine residues.
CC Phosphorylation on Thr-222, stimulated by all-trans retinoic acid
CC (atRA) mediates PML location and sumoylation in proliferating cells
CC which then modulates its association with effector molecules, KAT2B and
CC NRIP1. Phosphorylation on Ser-581 by PKC is important for protein
CC stability and function as activator of RARB (By similarity).
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR2
CC subfamily. {ECO:0000305}.
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DR EMBL; M21985; AAA36650.1; -; mRNA.
DR EMBL; M29959; AAA36762.1; -; mRNA.
DR EMBL; M29960; AAA36761.1; -; mRNA.
DR EMBL; AK291319; BAF84008.1; -; mRNA.
DR EMBL; AC011598; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471054; EAW97518.1; -; Genomic_DNA.
DR EMBL; BC040141; AAH40141.1; -; mRNA.
DR CCDS; CCDS41821.1; -. [P13056-2]
DR CCDS; CCDS44953.1; -. [P13056-3]
DR CCDS; CCDS9051.1; -. [P13056-1]
DR PIR; A31521; A31521.
DR PIR; A36738; A36738.
DR PIR; B36738; B36738.
DR RefSeq; NP_001027458.1; NM_001032287.2. [P13056-2]
DR RefSeq; NP_001120834.1; NM_001127362.1. [P13056-3]
DR RefSeq; NP_003288.2; NM_003297.3. [P13056-1]
DR AlphaFoldDB; P13056; -.
DR BioGRID; 113033; 75.
DR IntAct; P13056; 41.
DR MINT; P13056; -.
DR STRING; 9606.ENSP00000333275; -.
DR ChEMBL; CHEMBL1961787; -.
DR iPTMnet; P13056; -.
DR PhosphoSitePlus; P13056; -.
DR BioMuta; NR2C1; -.
DR DMDM; 226693548; -.
DR EPD; P13056; -.
DR jPOST; P13056; -.
DR MassIVE; P13056; -.
DR MaxQB; P13056; -.
DR PaxDb; P13056; -.
DR PeptideAtlas; P13056; -.
DR PRIDE; P13056; -.
DR ProteomicsDB; 52893; -. [P13056-1]
DR ProteomicsDB; 52894; -. [P13056-2]
DR ProteomicsDB; 52895; -. [P13056-3]
DR Antibodypedia; 4166; 446 antibodies from 37 providers.
DR DNASU; 7181; -.
DR Ensembl; ENST00000330677.7; ENSP00000328843.7; ENSG00000120798.17. [P13056-3]
DR Ensembl; ENST00000333003.10; ENSP00000333275.4; ENSG00000120798.17. [P13056-1]
DR Ensembl; ENST00000393101.7; ENSP00000376813.3; ENSG00000120798.17. [P13056-2]
DR GeneID; 7181; -.
DR KEGG; hsa:7181; -.
DR MANE-Select; ENST00000333003.10; ENSP00000333275.4; NM_003297.4; NP_003288.2.
DR UCSC; uc001tdm.6; human. [P13056-1]
DR CTD; 7181; -.
DR DisGeNET; 7181; -.
DR GeneCards; NR2C1; -.
DR HGNC; HGNC:7971; NR2C1.
DR HPA; ENSG00000120798; Low tissue specificity.
DR MIM; 601529; gene.
DR neXtProt; NX_P13056; -.
DR OpenTargets; ENSG00000120798; -.
DR PharmGKB; PA31754; -.
DR VEuPathDB; HostDB:ENSG00000120798; -.
DR eggNOG; KOG3575; Eukaryota.
DR GeneTree; ENSGT00940000158165; -.
DR HOGENOM; CLU_007368_16_2_1; -.
DR InParanoid; P13056; -.
DR OMA; RKPIEMS; -.
DR PhylomeDB; P13056; -.
DR TreeFam; TF316650; -.
DR PathwayCommons; P13056; -.
DR Reactome; R-HSA-383280; Nuclear Receptor transcription pathway.
DR Reactome; R-HSA-4090294; SUMOylation of intracellular receptors.
DR SignaLink; P13056; -.
DR BioGRID-ORCS; 7181; 7 hits in 1102 CRISPR screens.
DR ChiTaRS; NR2C1; human.
DR GeneWiki; Testicular_receptor_2; -.
DR GenomeRNAi; 7181; -.
DR Pharos; P13056; Tbio.
DR PRO; PR:P13056; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; P13056; protein.
DR Bgee; ENSG00000120798; Expressed in cerebellar hemisphere and 204 other tissues.
DR ExpressionAtlas; P13056; baseline and differential.
DR Genevisible; P13056; HS.
DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0016605; C:PML body; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; TAS:ProtInc.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IEA:Ensembl.
DR GO; GO:0042826; F:histone deacetylase binding; IEA:Ensembl.
DR GO; GO:0004879; F:nuclear receptor activity; IBA:GO_Central.
DR GO; GO:0003707; F:nuclear steroid receptor activity; TAS:ProtInc.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IDA:ARUK-UCL.
DR GO; GO:0038023; F:signaling receptor activity; TAS:ProtInc.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0048856; P:anatomical structure development; IBA:GO_Central.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IPI:UniProtKB.
DR GO; GO:0048386; P:positive regulation of retinoic acid receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR Gene3D; 1.10.565.10; -; 1.
DR Gene3D; 3.30.50.10; -; 1.
DR InterPro; IPR035500; NHR-like_dom_sf.
DR InterPro; IPR000536; Nucl_hrmn_rcpt_lig-bd.
DR InterPro; IPR001723; Nuclear_hrmn_rcpt.
DR InterPro; IPR001628; Znf_hrmn_rcpt.
DR InterPro; IPR013088; Znf_NHR/GATA.
DR Pfam; PF00104; Hormone_recep; 1.
DR Pfam; PF00105; zf-C4; 1.
DR PRINTS; PR00398; STRDHORMONER.
DR PRINTS; PR00047; STROIDFINGER.
DR SMART; SM00430; HOLI; 1.
DR SMART; SM00399; ZnF_C4; 1.
DR SUPFAM; SSF48508; SSF48508; 1.
DR PROSITE; PS51843; NR_LBD; 1.
DR PROSITE; PS00031; NUCLEAR_REC_DBD_1; 1.
DR PROSITE; PS51030; NUCLEAR_REC_DBD_2; 1.
PE 1: Evidence at protein level;
KW Activator; Alternative splicing; DNA-binding; Isopeptide bond;
KW Metal-binding; Nucleus; Phosphoprotein; Receptor; Reference proteome;
KW Repressor; Transcription; Transcription regulation; Ubl conjugation; Zinc;
KW Zinc-finger.
FT CHAIN 1..603
FT /note="Nuclear receptor subfamily 2 group C member 1"
FT /id="PRO_0000053586"
FT DOMAIN 348..590
FT /note="NR LBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01189"
FT DNA_BIND 110..185
FT /note="Nuclear receptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 113..133
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 149..173
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT REGION 1..178
FT /note="Required for interaction with KAT2B"
FT /evidence="ECO:0000250"
FT REGION 584..603
FT /note="Required for interaction with NRIP1"
FT /evidence="ECO:0000250"
FT MOD_RES 197
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q505F1"
FT MOD_RES 215
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 220
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 222
FT /note="Phosphothreonine; by MAPK1"
FT /evidence="ECO:0000250|UniProtKB:Q505F1"
FT MOD_RES 581
FT /note="Phosphoserine; by PKC"
FT /evidence="ECO:0000250|UniProtKB:Q505F1"
FT CROSSLNK 250
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 588
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 465..467
FT /note="DKM -> AEG (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:2597158"
FT /id="VSP_036855"
FT VAR_SEQ 466..483
FT /note="KMSTERRKLLMEHIFKLQ -> AKVIAALIHFTRRAITDL (in isoform
FT 3)"
FT /evidence="ECO:0000303|PubMed:3421977"
FT /id="VSP_036856"
FT VAR_SEQ 468..603
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:2597158"
FT /id="VSP_036857"
FT VAR_SEQ 484..603
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:3421977"
FT /id="VSP_036858"
FT CONFLICT 291
FT /note="N -> K (in Ref. 3; BAF84008)"
FT /evidence="ECO:0000305"
FT CONFLICT 304
FT /note="D -> N (in Ref. 3; BAF84008)"
FT /evidence="ECO:0000305"
FT CONFLICT 520
FT /note="Q -> L (in Ref. 2; AAA36761)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 603 AA; 67315 MW; 37444D2701B9CA60 CRC64;
MATIEEIAHQ IIEQQMGEIV TEQQTGQKIQ IVTALDHNTQ GKQFILTNHD GSTPSKVILA
RQDSTPGKVF LTTPDAAGVN QLFFTTPDLS AQHLQLLTDN SPDQGPNKVF DLCVVCGDKA
SGRHYGAVTC EGCKGFFKRS IRKNLVYSCR GSKDCIINKH HRNRCQYCRL QRCIAFGMKQ
DSVQCERKPI EVSREKSSNC AASTEKIYIR KDLRSPLTAT PTFVTDSEST RSTGLLDSGM
FMNIHPSGVK TESAVLMTSD KAESCQGDLS TLANVVTSLA NLGKTKDLSQ NSNEMSMIES
LSNDDTSLCE FQEMQTNGDV SRAFDTLAKA LNPGESTACQ SSVAGMEGSV HLITGDSSIN
YTEKEGPLLS DSHVAFRLTM PSPMPEYLNV HYIGESASRL LFLSMHWALS IPSFQALGQE
NSISLVKAYW NELFTLGLAQ CWQVMNVATI LATFVNCLHN SLQQDKMSTE RRKLLMEHIF
KLQEFCNSMV KLCIDGYEYA YLKAIVLFSP DHPSLENMEQ IEKFQEKAYV EFQDYITKTY
PDDTYRLSRL LLRLPALRLM NATITEELFF KGLIGNIRID SVIPHILKME PADYNSQIIG
HSI
