ID NR2C2_HUMAN Reviewed; 596 AA. AC P49116; A8K3H5; B6ZGT8; P55092; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 27-MAR-2024, entry version 210. DE RecName: Full=Nuclear receptor subfamily 2 group C member 2; DE AltName: Full=Orphan nuclear receptor TAK1; DE AltName: Full=Orphan nuclear receptor TR4; DE AltName: Full=Testicular receptor 4; GN Name=NR2C2; Synonyms=TAK1, TR4; 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 1). RC TISSUE=Testis; RX PubMed=7708055; DOI=10.1210/mend.8.12.7708055; RA Hirose T., Fujimoto W., Yamaai T., Kim K.H., Matsuura H., Jetten A.M.; RT "TAK1: molecular cloning and characterization of a new member of the RT nuclear receptor superfamily."; RL Mol. Endocrinol. 8:1667-1680(1994). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). RC TISSUE=Prostate, and Testis; RX PubMed=8016112; DOI=10.1073/pnas.91.13.6040; RA Chang C., da Silva S.L., Ideta R., Lee Y., Yeh S., Burbach J.P.; RT "Human and rat TR4 orphan receptors specify a subclass of the steroid RT receptor superfamily."; RL Proc. Natl. Acad. Sci. U.S.A. 91:6040-6044(1994). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND DNA-BINDING SPECIFICITY. RX PubMed=18619963; DOI=10.1016/j.febslet.2008.07.003; RA Kobayashi T., Kodani Y., Nozawa A., Endo Y., Sawasaki T.; RT "DNA-binding profiling of human hormone nuclear receptors via fluorescence RT correlation spectroscopy in a cell-free system."; RL FEBS Lett. 582:2737-2744(2008). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). 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 [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16641997; DOI=10.1038/nature04728; RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.; RT "The DNA sequence, annotation and analysis of human chromosome 3."; RL Nature 440:1194-1198(2006). RN [6] 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 [7] RP DNA-BINDING, AND FUNCTION. RX PubMed=7779113; DOI=10.1006/bbrc.1995.1781; RA Hirose T., Apfel R., Pfahl M., Jetten A.M.; RT "The orphan receptor TAK1 acts as a repressor of RAR-, RXR- and T3R- RT mediated signaling pathways."; RL Biochem. Biophys. Res. Commun. 211:83-91(1995). RN [8] RP DNA-BINDING, INTERACTION WITH NRIP1, AND FUNCTION. RX PubMed=9556573; DOI=10.1074/jbc.273.18.10948; RA Yan Z.H., Karam W.G., Staudinger J.L., Medvedev A., Ghanayem B.I., RA Jetten A.M.; RT "Regulation of peroxisome proliferator-activated receptor alpha-induced RT transactivation by the nuclear orphan receptor TAK1/TR4."; RL J. Biol. Chem. 273:10948-10957(1998). RN [9] RP DNA-BINDING, AND FUNCTION. RX PubMed=10347174; DOI=10.1074/jbc.274.23.16198; RA Lee Y.F., Young W.J., Lin W.J., Shyr C.R., Chang C.; RT "Differential regulation of direct repeat 3 vitamin D3 and direct repeat 4 RT thyroid hormone signaling pathways by the human TR4 orphan receptor."; RL J. Biol. Chem. 274:16198-16205(1999). RN [10] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=10644740; DOI=10.1074/jbc.275.4.2763; RA Zhang Y., Dufau M.L.; RT "Nuclear orphan receptors regulate transcription of the gene for the human RT luteinizing hormone receptor."; RL J. Biol. Chem. 275:2763-2770(2000). RN [11] RP INTERACTION WITH NR2C2AP. RX PubMed=12486131; DOI=10.1074/jbc.m207116200; RA Yang Y., Wang X., Dong T., Kim E., Lin W.-J., Chang C.; RT "Identification of a novel testicular orphan receptor-4 (TR4)-associated RT protein as repressor for the selective suppression of TR4-mediated RT transactivation."; RL J. Biol. Chem. 278:7709-7717(2003). RN [12] RP INTERACTION WITH JAZF1, SUBCELLULAR LOCATION, AND MUTAGENESIS OF ILE-576. RX PubMed=15302918; DOI=10.1093/nar/gkh741; RA Nakajima T., Fujino S., Nakanishi G., Kim Y.S., Jetten A.M.; RT "TIP27: a novel repressor of the nuclear orphan receptor TAK1/TR4."; RL Nucleic Acids Res. 32:4194-4204(2004). RN [13] RP HETERODIMERIZATION, AND FUNCTION. RX PubMed=17974920; DOI=10.1101/gad.1593307; RA Tanabe O., Shen Y., Liu Q., Campbell A.D., Kuroha T., Yamamoto M., RA Engel J.D.; RT "The TR2 and TR4 orphan nuclear receptors repress Gata1 transcription."; RL Genes Dev. 21:2832-2844(2007). RN [14] RP INDUCTION. RX PubMed=18388194; DOI=10.1210/en.2008-0121; RA Li G., Lee Y.F., Liu S., Cai Y., Xie S., Liu N.C., Bao B.Y., Chen Z., RA Chang C.; RT "Oxidative stress stimulates testicular orphan receptor 4 through forkhead RT transcription factor forkhead box O3a."; RL Endocrinology 149:3490-3499(2008). RN [15] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-219, AND IDENTIFICATION BY RP 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 [16] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19 AND SER-46, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [17] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19; SER-46; SER-68; SER-98 RP AND SER-219, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP 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 [18] RP INTERACTION WITH NLRP10. RX PubMed=22672233; DOI=10.1111/j.1462-5822.2012.01822.x; RA Lautz K., Damm A., Menning M., Wenger J., Adam A.C., Zigrino P., RA Kremmer E., Kufer T.A.; RT "NLRP10 enhances Shigella-induced pro-inflammatory responses."; RL Cell. Microbiol. 14:1568-1583(2012). RN [19] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19; SER-46; SER-68; SER-98 RP AND SER-219, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP 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 [20] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-192, AND IDENTIFICATION BY MASS RP 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 that can act as a repressor or CC activator of transcription. An important repressor of nuclear receptor CC signaling pathways such as retinoic acid receptor, retinoid X, vitamin CC D3 receptor, thyroid hormone receptor and estrogen receptor pathways. CC May regulate gene expression during the late phase of spermatogenesis. CC Together with NR2C1, forms the core of the DRED (direct repeat CC erythroid-definitive) complex that represses embryonic and fetal globin CC transcription including that of GATA1. Binds to hormone response CC elements (HREs) consisting of two 5'-AGGTCA-3' half site direct repeat CC consensus sequences. Plays a fundamental role in early embryonic CC development and embryonic stem cells. Required for normal CC spermatogenesis and cerebellum development. Appears to be important for CC neurodevelopmentally regulated behavior (By similarity). Activates CC transcriptional activity of LHCG. Antagonist of PPARA-mediated CC transactivation. {ECO:0000250, ECO:0000269|PubMed:10347174, CC ECO:0000269|PubMed:10644740, ECO:0000269|PubMed:17974920, CC ECO:0000269|PubMed:7779113, ECO:0000269|PubMed:9556573}. CC -!- SUBUNIT: Homodimer; can bind DNA as homodimer (By similarity). CC Heterodimer; binds DNA as a heterodimer with NR2C1 required for CC chromatin remodeling and for binding to promoter regions such as globin CC DR1 repeats. Interacts with PCAF; the interaction preferentially occurs CC on the non-phosphorylated form and induces NR2C2-mediated CC transactivation activity and does not require the ligand-binding domain CC (By similarity). Interacts (MAPK-mediated phosphorylated form) with CC NRIP1; the interaction promotes repression of NR2C2-mediated activity CC (PubMed:9556573). Interacts with NR2C2AP; the interaction represses CC selective NR2C2-mediated transcriptional activity (PubMed:12486131). CC Interacts with NLRP10 (PubMed:22672233). Interacts (via ligand-binding CC region) with transcriptional corepressor JAZF1; the interaction CC promotes NR2C2-mediated transcriptional repression (PubMed:15302918). CC {ECO:0000250|UniProtKB:P49117, ECO:0000269|PubMed:12486131, CC ECO:0000269|PubMed:15302918, ECO:0000269|PubMed:22672233, CC ECO:0000269|PubMed:9556573}. CC -!- INTERACTION: CC P49116; Q86VZ6: JAZF1; NbExp=8; IntAct=EBI-2652582, EBI-11023753; CC P49116-2; Q86WQ0: NR2C2AP; NbExp=5; IntAct=EBI-20709881, EBI-10260040; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00407, CC ECO:0000269|PubMed:10644740, ECO:0000269|PubMed:15302918}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=P49116-1; Sequence=Displayed; CC Name=2; CC IsoId=P49116-2; Sequence=VSP_039522; CC -!- DEVELOPMENTAL STAGE: Transiently repressed during the meiotic phase of CC spermatogenesis. CC -!- INDUCTION: Induced by oxidative stress via FOXO3 activation. CC {ECO:0000269|PubMed:18388194}. CC -!- PTM: Phosphorylation on Ser-19 and Ser-68 is an important regulator of CC NR2C2-mediated transcriptional activity. Phosphorylation on these CC residues recruits the corepressor, NRIP1, leading to transcripional CC repression, whereas the non-phosphorylated form preferentially recruits CC the coactivator, PCAF (By similarity). {ECO:0000250}. CC -!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR2 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; U10990; AAC50118.1; -; mRNA. DR EMBL; L27586; AAA21474.1; -; mRNA. DR EMBL; AB307708; BAH02299.1; -; mRNA. DR EMBL; AK290590; BAF83279.1; -; mRNA. DR EMBL; AC090937; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC090954; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471055; EAW64215.1; -; Genomic_DNA. DR CCDS; CCDS2621.1; -. [P49116-2] DR CCDS; CCDS74905.1; -. [P49116-1] DR PIR; A57031; A57031. DR PIR; I59309; I59309. DR RefSeq; NP_001278623.1; NM_001291694.1. [P49116-1] DR RefSeq; NP_003289.2; NM_003298.4. [P49116-2] DR RefSeq; XP_016862609.1; XM_017007120.1. DR PDB; 3P0U; X-ray; 3.00 A; A/B=348-596. DR PDB; 7XV6; X-ray; 2.30 A; A/B=113-196. DR PDB; 7XV8; X-ray; 3.20 A; A/B=113-189. DR PDB; 7XV9; X-ray; 1.60 A; A/B=113-189. DR PDB; 7XVA; X-ray; 1.86 A; A=341-596. DR PDBsum; 3P0U; -. DR PDBsum; 7XV6; -. DR PDBsum; 7XV8; -. DR PDBsum; 7XV9; -. DR PDBsum; 7XVA; -. DR AlphaFoldDB; P49116; -. DR SMR; P49116; -. DR BioGRID; 113034; 1397. DR DIP; DIP-5999N; -. DR IntAct; P49116; 53. DR MINT; P49116; -. DR STRING; 9606.ENSP00000483059; -. DR BindingDB; P49116; -. DR ChEMBL; CHEMBL5716; -. DR DrugCentral; P49116; -. DR GuidetoPHARMACOLOGY; 614; -. DR GlyGen; P49116; 3 sites, 1 O-linked glycan (3 sites). DR iPTMnet; P49116; -. DR PhosphoSitePlus; P49116; -. DR BioMuta; NR2C2; -. DR DMDM; 1351190; -. DR EPD; P49116; -. DR jPOST; P49116; -. DR MassIVE; P49116; -. DR MaxQB; P49116; -. DR PaxDb; 9606-ENSP00000483059; -. DR PeptideAtlas; P49116; -. DR ProteomicsDB; 55962; -. [P49116-1] DR ProteomicsDB; 55963; -. [P49116-2] DR Pumba; P49116; -. DR TopDownProteomics; P49116-2; -. [P49116-2] DR Antibodypedia; 1697; 578 antibodies from 39 providers. DR DNASU; 7182; -. DR Ensembl; ENST00000323373.10; ENSP00000320447.6; ENSG00000177463.16. [P49116-2] DR Ensembl; ENST00000393102.7; ENSP00000376814.3; ENSG00000177463.16. [P49116-1] DR Ensembl; ENST00000406272.6; ENSP00000384463.2; ENSG00000177463.16. [P49116-1] DR Ensembl; ENST00000425241.6; ENSP00000388387.1; ENSG00000177463.16. [P49116-1] DR Ensembl; ENST00000617312.4; ENSP00000483059.1; ENSG00000177463.16. [P49116-2] DR GeneID; 7182; -. DR KEGG; hsa:7182; -. DR MANE-Select; ENST00000425241.6; ENSP00000388387.1; NM_001291694.2; NP_001278623.1. DR UCSC; uc003bzi.4; human. [P49116-1] DR AGR; HGNC:7972; -. DR CTD; 7182; -. DR DisGeNET; 7182; -. DR GeneCards; NR2C2; -. DR HGNC; HGNC:7972; NR2C2. DR HPA; ENSG00000177463; Low tissue specificity. DR MIM; 601426; gene. DR neXtProt; NX_P49116; -. DR OpenTargets; ENSG00000177463; -. DR PharmGKB; PA31755; -. DR VEuPathDB; HostDB:ENSG00000177463; -. DR eggNOG; KOG3575; Eukaryota. DR GeneTree; ENSGT00940000158393; -. DR HOGENOM; CLU_007368_16_2_1; -. DR InParanoid; P49116; -. DR OMA; SVTEHIC; -. DR OrthoDB; 5400963at2759; -. DR PhylomeDB; P49116; -. DR TreeFam; TF316650; -. DR PathwayCommons; P49116; -. DR Reactome; R-HSA-383280; Nuclear Receptor transcription pathway. DR SignaLink; P49116; -. DR SIGNOR; P49116; -. DR BioGRID-ORCS; 7182; 36 hits in 1180 CRISPR screens. DR ChiTaRS; NR2C2; human. DR EvolutionaryTrace; P49116; -. DR GeneWiki; Testicular_receptor_4; -. DR GenomeRNAi; 7182; -. DR Pharos; P49116; Tchem. DR PRO; PR:P49116; -. DR Proteomes; UP000005640; Chromosome 3. DR RNAct; P49116; Protein. DR Bgee; ENSG00000177463; Expressed in sural nerve and 181 other cell types or tissues. DR ExpressionAtlas; P49116; baseline and differential. DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:NTNU_SB. DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:UniProtKB. DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB. DR GO; GO:0004879; F:nuclear receptor activity; IBA:GO_Central. DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:NTNU_SB. DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IDA:NTNU_SB. DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:UniProtKB. DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IDA:ARUK-UCL. 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:0007399; P:nervous system development; TAS:ProtInc. DR GO; GO:0040019; P:positive regulation of embryonic development; IBA:GO_Central. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB. DR GO; GO:0006355; P:regulation of DNA-templated transcription; TAS:ProtInc. DR GO; GO:0007283; P:spermatogenesis; IEA:UniProtKB-KW. DR CDD; cd06967; NR_DBD_TR2_like; 1. DR CDD; cd06952; NR_LBD_TR2_like; 1. DR Gene3D; 3.30.50.10; Erythroid Transcription Factor GATA-1, subunit A; 1. DR Gene3D; 1.10.565.10; Retinoid X Receptor; 1. DR InterPro; IPR035500; NHR-like_dom_sf. DR InterPro; IPR048245; NR2C1/2-like_DBD. DR InterPro; IPR048246; NR2C1/2-like_LBD. 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 PANTHER; PTHR24083; NUCLEAR HORMONE RECEPTOR; 1. DR PANTHER; PTHR24083:SF48; NUCLEAR RECEPTOR SUBFAMILY 2 GROUP C MEMBER 2; 1. 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; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 1. DR SUPFAM; SSF48508; Nuclear receptor ligand-binding domain; 1. DR PROSITE; PS51843; NR_LBD; 1. DR PROSITE; PS00031; NUCLEAR_REC_DBD_1; 1. DR PROSITE; PS51030; NUCLEAR_REC_DBD_2; 1. DR Genevisible; P49116; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Activator; Alternative splicing; KW Differentiation; DNA-binding; Isopeptide bond; Metal-binding; Nucleus; KW Phosphoprotein; Receptor; Reference proteome; Repressor; Spermatogenesis; KW Transcription; Transcription regulation; Ubl conjugation; Zinc; KW Zinc-finger. FT CHAIN 1..596 FT /note="Nuclear receptor subfamily 2 group C member 2" FT /id="PRO_0000053588" FT DOMAIN 341..583 FT /note="NR LBD" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01189" FT DNA_BIND 114..189 FT /note="Nuclear receptor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407" FT ZN_FING 117..137 FT /note="NR C4-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407" FT ZN_FING 153..177 FT /note="NR C4-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407" FT MOD_RES 19 FT /note="Phosphoserine; by MAPK" FT /evidence="ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163" FT MOD_RES 46 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163" FT MOD_RES 55 FT /note="Phosphoserine; by MAPK" FT /evidence="ECO:0000250|UniProtKB:P49117" FT MOD_RES 68 FT /note="Phosphoserine; by MAPK" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:23186163" FT MOD_RES 98 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:23186163" FT MOD_RES 219 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163" FT MOD_RES 231 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P49117" FT CROSSLNK 192 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT VAR_SEQ 24 FT /note="Q -> QGSEPASGPLSVFTSLNKEK (in isoform 2)" FT /evidence="ECO:0000303|PubMed:8016112" FT /id="VSP_039522" FT MUTAGEN 576 FT /note="I->N: Reduces interaction with JAZF1." FT /evidence="ECO:0000269|PubMed:15302918" FT CONFLICT 108 FT /note="V -> A (in Ref. 3; BAH02299)" FT /evidence="ECO:0000305" FT CONFLICT 156 FT /note="N -> S (in Ref. 2; AAA21474)" FT /evidence="ECO:0000305" FT CONFLICT 326 FT /note="S -> F (in Ref. 3; BAH02299)" FT /evidence="ECO:0000305" FT CONFLICT 400 FT /note="W -> R (in Ref. 2; AAA21474)" FT /evidence="ECO:0000305" FT CONFLICT 409 FT /note="A -> G (in Ref. 2; AAA21474)" FT /evidence="ECO:0000305" FT CONFLICT 484..485 FT /note="KL -> NW (in Ref. 2; AAA21474)" FT /evidence="ECO:0000305" FT CONFLICT 594 FT /note="A -> V (in Ref. 2; AAA21474 and 3; BAH02299)" FT /evidence="ECO:0000305" FT TURN 118..120 FT /evidence="ECO:0007829|PDB:7XV9" FT STRAND 126..128 FT /evidence="ECO:0007829|PDB:7XV9" FT STRAND 131..133 FT /evidence="ECO:0007829|PDB:7XV9" FT HELIX 135..146 FT /evidence="ECO:0007829|PDB:7XV9" FT STRAND 154..157 FT /evidence="ECO:0007829|PDB:7XV9" FT STRAND 163..165 FT /evidence="ECO:0007829|PDB:7XV9" FT HELIX 170..179 FT /evidence="ECO:0007829|PDB:7XV9" FT HELIX 184..186 FT /evidence="ECO:0007829|PDB:7XV9" FT STRAND 354..357 FT /evidence="ECO:0007829|PDB:3P0U" FT HELIX 364..367 FT /evidence="ECO:0007829|PDB:7XVA" FT STRAND 374..376 FT /evidence="ECO:0007829|PDB:7XVA" FT HELIX 383..402 FT /evidence="ECO:0007829|PDB:7XVA" FT HELIX 405..409 FT /evidence="ECO:0007829|PDB:7XVA" FT HELIX 412..433 FT /evidence="ECO:0007829|PDB:7XVA" FT TURN 434..439 FT /evidence="ECO:0007829|PDB:7XVA" FT HELIX 440..448 FT /evidence="ECO:0007829|PDB:7XVA" FT HELIX 466..484 FT /evidence="ECO:0007829|PDB:7XVA" FT HELIX 489..500 FT /evidence="ECO:0007829|PDB:7XVA" FT HELIX 511..532 FT /evidence="ECO:0007829|PDB:7XVA" FT TURN 533..535 FT /evidence="ECO:0007829|PDB:3P0U" FT HELIX 539..544 FT /evidence="ECO:0007829|PDB:7XVA" FT HELIX 547..550 FT /evidence="ECO:0007829|PDB:7XVA" FT HELIX 555..562 FT /evidence="ECO:0007829|PDB:7XVA" FT HELIX 567..570 FT /evidence="ECO:0007829|PDB:3P0U" FT HELIX 572..581 FT /evidence="ECO:0007829|PDB:7XVA" FT HELIX 584..593 FT /evidence="ECO:0007829|PDB:7XVA" SQ SEQUENCE 596 AA; 65414 MW; 5180BDC3F3C8BD79 CRC64; MTSPSPRIQI ISTDSAVASP QRIQIVTDQQ TGQKIQIVTA VDASGSPKQQ FILTSPDGAG TGKVILASPE TSSAKQLIFT TSDNLVPGRI QIVTDSASVE RLLGKTDVQR PQVVEYCVVC GDKASGRHYG AVSCEGCKGF FKRSVRKNLT YSCRSNQDCI INKHHRNRCQ FCRLKKCLEM GMKMESVQSE RKPFDVQREK PSNCAASTEK IYIRKDLRSP LIATPTFVAD KDGARQTGLL DPGMLVNIQQ PLIREDGTVL LATDSKAETS QGALGTLANV VTSLANLSES LNNGDTSEIQ PEDQSASEIT RAFDTLAKAL NTTDSSSSPS LADGIDTSGG GSIHVISRDQ STPIIEVEGP LLSDTHVTFK LTMPSPMPEY LNVHYICESA SRLLFLSMHW ARSIPAFQAL GQDCNTSLVR ACWNELFTLG LAQCAQVMSL STILAAIVNH LQNSIQEDKL SGDRIKQVME HIWKLQEFCN SMAKLDIDGY EYAYLKAIVL FSPDHPGLTS TSQIEKFQEK AQMELQDYVQ KTYSEDTYRL ARILVRLPAL RLMSSNITEE LFFTGLIGNV SIDSIIPYIL KMETAEYNGQ ITGASL //