NR2C2_HUMAN
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 03-AUG-2022, entry version 201.
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}.
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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. [P49116-1]
DR PDB; 3P0U; X-ray; 3.00 A; A/B=348-596.
DR PDBsum; 3P0U; -.
DR AlphaFoldDB; P49116; -.
DR SMR; P49116; -.
DR BioGRID; 113034; 1391.
DR DIP; DIP-5999N; -.
DR IntAct; P49116; 51.
DR MINT; P49116; -.
DR STRING; 9606.ENSP00000483059; -.
DR BindingDB; P49116; -.
DR ChEMBL; CHEMBL5716; -.
DR DrugCentral; P49116; -.
DR GuidetoPHARMACOLOGY; 614; -.
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; P49116; -.
DR PeptideAtlas; P49116; -.
DR PRIDE; P49116; -.
DR ProteomicsDB; 55962; -. [P49116-1]
DR ProteomicsDB; 55963; -. [P49116-2]
DR TopDownProteomics; P49116-2; -. [P49116-2]
DR Antibodypedia; 1697; 497 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 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; DIQPEDQ; -.
DR OrthoDB; 278171at2759; -.
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; 34 hits in 1100 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 179 other tissues.
DR ExpressionAtlas; P49116; baseline and differential.
DR Genevisible; P49116; HS.
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:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; TAS:ProtInc.
DR GO; GO:0007283; P:spermatogenesis; IEA:UniProtKB-KW.
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 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 STRAND 354..357
FT /evidence="ECO:0007829|PDB:3P0U"
FT HELIX 386..402
FT /evidence="ECO:0007829|PDB:3P0U"
FT TURN 405..407
FT /evidence="ECO:0007829|PDB:3P0U"
FT HELIX 408..410
FT /evidence="ECO:0007829|PDB:3P0U"
FT HELIX 412..420
FT /evidence="ECO:0007829|PDB:3P0U"
FT HELIX 423..433
FT /evidence="ECO:0007829|PDB:3P0U"
FT TURN 434..436
FT /evidence="ECO:0007829|PDB:3P0U"
FT HELIX 468..484
FT /evidence="ECO:0007829|PDB:3P0U"
FT HELIX 489..500
FT /evidence="ECO:0007829|PDB:3P0U"
FT HELIX 512..532
FT /evidence="ECO:0007829|PDB:3P0U"
FT TURN 533..535
FT /evidence="ECO:0007829|PDB:3P0U"
FT HELIX 539..544
FT /evidence="ECO:0007829|PDB:3P0U"
FT HELIX 547..551
FT /evidence="ECO:0007829|PDB:3P0U"
FT HELIX 555..562
FT /evidence="ECO:0007829|PDB:3P0U"
FT HELIX 567..570
FT /evidence="ECO:0007829|PDB:3P0U"
FT HELIX 572..579
FT /evidence="ECO:0007829|PDB:3P0U"
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
