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Nuclear receptor subfamily 2 group C member 2 (Orphan nuclear receptor TAK1) (Orphan nuclear receptor TR4) (Testicular receptor 4)

 NR2C2_HUMAN             Reviewed;         596 AA.
P49116; A8K3H5; B6ZGT8; P55092;
01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
01-FEB-1996, sequence version 1.
05-DEC-2018, entry version 180.
RecName: Full=Nuclear receptor subfamily 2 group C member 2;
AltName: Full=Orphan nuclear receptor TAK1;
AltName: Full=Orphan nuclear receptor TR4;
AltName: Full=Testicular receptor 4;
Name=NR2C2; Synonyms=TAK1, TR4;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Testis;
PubMed=7708055; DOI=10.1210/mend.8.12.7708055;
Hirose T., Fujimoto W., Yamaai T., Kim K.H., Matsuura H., Jetten A.M.;
"TAK1: molecular cloning and characterization of a new member of the
nuclear receptor superfamily.";
Mol. Endocrinol. 8:1667-1680(1994).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
TISSUE=Prostate, and Testis;
PubMed=8016112; DOI=10.1073/pnas.91.13.6040;
Chang C., da Silva S.L., Ideta R., Lee Y., Yeh S., Burbach J.P.;
"Human and rat TR4 orphan receptors specify a subclass of the steroid
receptor superfamily.";
Proc. Natl. Acad. Sci. U.S.A. 91:6040-6044(1994).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND DNA-BINDING SPECIFICITY.
PubMed=18619963; DOI=10.1016/j.febslet.2008.07.003;
Kobayashi T., Kodani Y., Nozawa A., Endo Y., Sawasaki T.;
"DNA-binding profiling of human hormone nuclear receptors via
fluorescence correlation spectroscopy in a cell-free system.";
FEBS Lett. 582:2737-2744(2008).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16641997; DOI=10.1038/nature04728;
Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R.,
Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R.,
Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V.,
Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.,
Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B.,
Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S.,
Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q.,
Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C.,
Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G.,
Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B.,
Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R.,
Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J.,
Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A.,
Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J.,
Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H.,
Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G.,
Gibbs R.A.;
"The DNA sequence, annotation and analysis of human chromosome 3.";
Nature 440:1194-1198(2006).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[7]
DNA-BINDING, AND FUNCTION.
PubMed=7779113; DOI=10.1006/bbrc.1995.1781;
Hirose T., Apfel R., Pfahl M., Jetten A.M.;
"The orphan receptor TAK1 acts as a repressor of RAR-, RXR- and T3R-
mediated signaling pathways.";
Biochem. Biophys. Res. Commun. 211:83-91(1995).
[8]
DNA-BINDING, INTERACTION WITH NRIP1, AND FUNCTION.
PubMed=9556573; DOI=10.1074/jbc.273.18.10948;
Yan Z.H., Karam W.G., Staudinger J.L., Medvedev A., Ghanayem B.I.,
Jetten A.M.;
"Regulation of peroxisome proliferator-activated receptor alpha-
induced transactivation by the nuclear orphan receptor TAK1/TR4.";
J. Biol. Chem. 273:10948-10957(1998).
[9]
DNA-BINDING, AND FUNCTION.
PubMed=10347174; DOI=10.1074/jbc.274.23.16198;
Lee Y.F., Young W.J., Lin W.J., Shyr C.R., Chang C.;
"Differential regulation of direct repeat 3 vitamin D3 and direct
repeat 4 thyroid hormone signaling pathways by the human TR4 orphan
receptor.";
J. Biol. Chem. 274:16198-16205(1999).
[10]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=10644740; DOI=10.1074/jbc.275.4.2763;
Zhang Y., Dufau M.L.;
"Nuclear orphan receptors regulate transcription of the gene for the
human luteinizing hormone receptor.";
J. Biol. Chem. 275:2763-2770(2000).
[11]
INTERACTION WITH NR2C2AP.
PubMed=12486131; DOI=10.1074/jbc.M207116200;
Yang Y., Wang X., Dong T., Kim E., Lin W.-J., Chang C.;
"Identification of a novel testicular orphan receptor-4 (TR4)-
associated protein as repressor for the selective suppression of TR4-
mediated transactivation.";
J. Biol. Chem. 278:7709-7717(2003).
[12]
INTERACTION WITH JAZF1, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
ILE-576.
PubMed=15302918; DOI=10.1093/nar/gkh741;
Nakajima T., Fujino S., Nakanishi G., Kim Y.S., Jetten A.M.;
"TIP27: a novel repressor of the nuclear orphan receptor TAK1/TR4.";
Nucleic Acids Res. 32:4194-4204(2004).
[13]
HETERODIMERIZATION, AND FUNCTION.
PubMed=17974920; DOI=10.1101/gad.1593307;
Tanabe O., Shen Y., Liu Q., Campbell A.D., Kuroha T., Yamamoto M.,
Engel J.D.;
"The TR2 and TR4 orphan nuclear receptors repress Gata1
transcription.";
Genes Dev. 21:2832-2844(2007).
[14]
INDUCTION.
PubMed=18388194; DOI=10.1210/en.2008-0121;
Li G., Lee Y.F., Liu S., Cai Y., Xie S., Liu N.C., Bao B.Y., Chen Z.,
Chang C.;
"Oxidative stress stimulates testicular orphan receptor 4 through
forkhead transcription factor forkhead box O3a.";
Endocrinology 149:3490-3499(2008).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-219, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19 AND SER-46, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19; SER-46; SER-68;
SER-98 AND SER-219, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[18]
INTERACTION WITH NLRP10.
PubMed=22672233; DOI=10.1111/j.1462-5822.2012.01822.x;
Lautz K., Damm A., Menning M., Wenger J., Adam A.C., Zigrino P.,
Kremmer E., Kufer T.A.;
"NLRP10 enhances Shigella-induced pro-inflammatory responses.";
Cell. Microbiol. 14:1568-1583(2012).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19; SER-46; SER-68;
SER-98 AND SER-219, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[20]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-192, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
-!- FUNCTION: Orphan nuclear receptor that can act as a repressor or
activator of transcription. An important repressor of nuclear
receptor signaling pathways such as retinoic acid receptor,
retinoid X, vitamin D3 receptor, thyroid hormone receptor and
estrogen receptor pathways. May regulate gene expression during
the late phase of spermatogenesis. Together with NR2C1, forms the
core of the DRED (direct repeat erythroid-definitive) complex that
represses embryonic and fetal globin transcription including that
of GATA1. Binds to hormone response elements (HREs) consisting of
two 5'-AGGTCA-3' half site direct repeat consensus sequences.
Plays a fundamental role in early embryonic development and
embryonic stem cells. Required for normal spermatogenesis and
cerebellum development. Appears to be important for
neurodevelopmentally regulated behavior (By similarity). Activates
transcriptional activity of LHCG. Antagonist of PPARA-mediated
transactivation. {ECO:0000250, ECO:0000269|PubMed:10347174,
ECO:0000269|PubMed:10644740, ECO:0000269|PubMed:17974920,
ECO:0000269|PubMed:7779113, ECO:0000269|PubMed:9556573}.
-!- SUBUNIT: Homodimer; can bind DNA as homodimer (By similarity).
Heterodimer; binds DNA as a heterodimer with NR2C1 required for
chromatin remodeling and for binding to promoter regions such as
globin DR1 repeats. Interacts with PCAF; the interaction
preferentially occurs on the non-phosphorylated form and induces
NR2C2-mediated transactivation activity and does not require the
ligand-binding domain (By similarity). Interacts (MAPK-mediated
phosphorylated form) with NRIP1; the interaction promotes
repression of NR2C2-mediated activity (PubMed:9556573). Interacts
with NR2C2AP; the interaction represses selective NR2C2-mediated
transcriptional activity (PubMed:12486131). Interacts with NLRP10
(PubMed:22672233). Interacts (via ligand-binding region) with
transcriptional corepressor JAZF1; the interaction promotes NR2C2-
mediated transcriptional repression (PubMed:15302918).
{ECO:0000250|UniProtKB:P49117, ECO:0000269|PubMed:12486131,
ECO:0000269|PubMed:15302918, ECO:0000269|PubMed:22672233,
ECO:0000269|PubMed:9556573}.
-!- INTERACTION:
Q86VZ6:JAZF1; NbExp=6; IntAct=EBI-2652582, EBI-11023753;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-
ProRule:PRU00407, ECO:0000269|PubMed:10644740,
ECO:0000269|PubMed:15302918}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P49116-1; Sequence=Displayed;
Name=2;
IsoId=P49116-2; Sequence=VSP_039522;
-!- DEVELOPMENTAL STAGE: Transiently repressed during the meiotic
phase of spermatogenesis.
-!- INDUCTION: Induced by oxidative stress via FOXO3 activation.
{ECO:0000269|PubMed:18388194}.
-!- PTM: Phosphorylation on Ser-19 and Ser-68 is an important
regulator of NR2C2-mediated transcriptional activity.
Phosphorylation on these residues recruits the corepressor, NRIP1,
leading to transcripional repression, whereas the non-
phosphorylated form preferentially recruits the coactivator, PCAF
(By similarity). {ECO:0000250}.
-!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR2
subfamily. {ECO:0000305}.
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EMBL; U10990; AAC50118.1; -; mRNA.
EMBL; L27586; AAA21474.1; -; mRNA.
EMBL; AB307708; BAH02299.1; -; mRNA.
EMBL; AK290590; BAF83279.1; -; mRNA.
EMBL; AC090937; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC090954; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471055; EAW64215.1; -; Genomic_DNA.
CCDS; CCDS2621.1; -. [P49116-2]
CCDS; CCDS74905.1; -. [P49116-1]
PIR; A57031; A57031.
PIR; I59309; I59309.
RefSeq; NP_001278623.1; NM_001291694.1. [P49116-1]
RefSeq; NP_003289.2; NM_003298.4. [P49116-2]
RefSeq; XP_016862609.1; XM_017007120.1. [P49116-1]
UniGene; Hs.555973; -.
PDB; 3P0U; X-ray; 3.00 A; A/B=348-596.
PDBsum; 3P0U; -.
ProteinModelPortal; P49116; -.
SMR; P49116; -.
BioGrid; 113034; 49.
DIP; DIP-5999N; -.
IntAct; P49116; 22.
MINT; P49116; -.
STRING; 9606.ENSP00000320447; -.
BindingDB; P49116; -.
ChEMBL; CHEMBL5716; -.
GuidetoPHARMACOLOGY; 614; -.
iPTMnet; P49116; -.
PhosphoSitePlus; P49116; -.
BioMuta; NR2C2; -.
DMDM; 1351190; -.
EPD; P49116; -.
MaxQB; P49116; -.
PaxDb; P49116; -.
PeptideAtlas; P49116; -.
PRIDE; P49116; -.
ProteomicsDB; 55962; -.
ProteomicsDB; 55963; -. [P49116-2]
TopDownProteomics; P49116-2; -. [P49116-2]
DNASU; 7182; -.
Ensembl; ENST00000323373; ENSP00000320447; ENSG00000177463. [P49116-2]
Ensembl; ENST00000393102; ENSP00000376814; ENSG00000177463. [P49116-1]
Ensembl; ENST00000406272; ENSP00000384463; ENSG00000177463. [P49116-1]
Ensembl; ENST00000425241; ENSP00000388387; ENSG00000177463. [P49116-1]
Ensembl; ENST00000617312; ENSP00000483059; ENSG00000177463. [P49116-2]
GeneID; 7182; -.
KEGG; hsa:7182; -.
UCSC; uc003bzi.4; human. [P49116-1]
CTD; 7182; -.
DisGeNET; 7182; -.
EuPathDB; HostDB:ENSG00000177463.15; -.
GeneCards; NR2C2; -.
HGNC; HGNC:7972; NR2C2.
HPA; HPA006313; -.
MIM; 601426; gene.
neXtProt; NX_P49116; -.
OpenTargets; ENSG00000177463; -.
PharmGKB; PA31755; -.
eggNOG; KOG3575; Eukaryota.
eggNOG; ENOG410XRZC; LUCA.
GeneTree; ENSGT00940000158393; -.
HOGENOM; HOG000013058; -.
HOVERGEN; HBG008596; -.
InParanoid; P49116; -.
KO; K08544; -.
OMA; REKPTNC; -.
PhylomeDB; P49116; -.
TreeFam; TF316650; -.
Reactome; R-HSA-383280; Nuclear Receptor transcription pathway.
SignaLink; P49116; -.
SIGNOR; P49116; -.
ChiTaRS; NR2C2; human.
EvolutionaryTrace; P49116; -.
GeneWiki; Testicular_receptor_4; -.
GenomeRNAi; 7182; -.
PRO; PR:P49116; -.
Proteomes; UP000005640; Chromosome 3.
Bgee; ENSG00000177463; Expressed in 201 organ(s), highest expression level in left lobe of thyroid gland.
CleanEx; HS_NR2C2; -.
ExpressionAtlas; P49116; baseline and differential.
Genevisible; P49116; HS.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:NTNU_SB.
GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:UniProtKB.
GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
GO; GO:0046982; F:protein heterodimerization activity; IDA:UniProtKB.
GO; GO:0001077; F:proximal promoter DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:NTNU_SB.
GO; GO:0000978; F:RNA polymerase II proximal promoter sequence-specific DNA binding; IDA:NTNU_SB.
GO; GO:0000977; F:RNA polymerase II regulatory region sequence-specific DNA binding; IDA:NTNU_SB.
GO; GO:0043565; F:sequence-specific DNA binding; IDA:UniProtKB.
GO; GO:0038023; F:signaling receptor activity; TAS:ProtInc.
GO; GO:0003707; F:steroid hormone receptor activity; IEA:InterPro.
GO; GO:0003713; F:transcription coactivator activity; TAS:ProtInc.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
GO; GO:0007399; P:nervous system development; TAS:ProtInc.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB.
GO; GO:0006355; P:regulation of transcription, DNA-templated; TAS:ProtInc.
GO; GO:0007283; P:spermatogenesis; IEA:UniProtKB-KW.
GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; TAS:Reactome.
Gene3D; 3.30.50.10; -; 1.
InterPro; IPR035500; NHR_like_dom_sf.
InterPro; IPR000536; Nucl_hrmn_rcpt_lig-bd.
InterPro; IPR001723; Nuclear_hrmn_rcpt.
InterPro; IPR001628; Znf_hrmn_rcpt.
InterPro; IPR013088; Znf_NHR/GATA.
Pfam; PF00104; Hormone_recep; 1.
Pfam; PF00105; zf-C4; 1.
PRINTS; PR00398; STRDHORMONER.
PRINTS; PR00047; STROIDFINGER.
SMART; SM00430; HOLI; 1.
SMART; SM00399; ZnF_C4; 1.
SUPFAM; SSF48508; SSF48508; 1.
PROSITE; PS51843; NR_LBD; 1.
PROSITE; PS00031; NUCLEAR_REC_DBD_1; 1.
PROSITE; PS51030; NUCLEAR_REC_DBD_2; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Activator; Alternative splicing;
Complete proteome; Differentiation; DNA-binding; Isopeptide bond;
Metal-binding; Nucleus; Phosphoprotein; Receptor; Reference proteome;
Repressor; Spermatogenesis; Transcription; Transcription regulation;
Ubl conjugation; Zinc; Zinc-finger.
CHAIN 1 596 Nuclear receptor subfamily 2 group C
member 2.
/FTId=PRO_0000053588.
DOMAIN 341 583 NR LBD. {ECO:0000255|PROSITE-
ProRule:PRU01189}.
DNA_BIND 114 189 Nuclear receptor. {ECO:0000255|PROSITE-
ProRule:PRU00407}.
ZN_FING 117 137 NR C4-type. {ECO:0000255|PROSITE-
ProRule:PRU00407}.
ZN_FING 153 177 NR C4-type. {ECO:0000255|PROSITE-
ProRule:PRU00407}.
MOD_RES 19 19 Phosphoserine; by MAPK.
{ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 46 46 Phosphoserine.
{ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 55 55 Phosphoserine; by MAPK.
{ECO:0000250|UniProtKB:P49117}.
MOD_RES 68 68 Phosphoserine; by MAPK.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 98 98 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 219 219 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 231 231 N6-acetyllysine.
{ECO:0000250|UniProtKB:P49117}.
CROSSLNK 192 192 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
VAR_SEQ 24 24 Q -> QGSEPASGPLSVFTSLNKEK (in isoform 2).
{ECO:0000303|PubMed:8016112}.
/FTId=VSP_039522.
MUTAGEN 576 576 I->N: Reduces interaction with JAZF1.
{ECO:0000269|PubMed:15302918}.
CONFLICT 108 108 V -> A (in Ref. 3; BAH02299).
{ECO:0000305}.
CONFLICT 156 156 N -> S (in Ref. 2; AAA21474).
{ECO:0000305}.
CONFLICT 326 326 S -> F (in Ref. 3; BAH02299).
{ECO:0000305}.
CONFLICT 400 400 W -> R (in Ref. 2; AAA21474).
{ECO:0000305}.
CONFLICT 409 409 A -> G (in Ref. 2; AAA21474).
{ECO:0000305}.
CONFLICT 484 485 KL -> NW (in Ref. 2; AAA21474).
{ECO:0000305}.
CONFLICT 594 594 A -> V (in Ref. 2; AAA21474 and 3;
BAH02299). {ECO:0000305}.
STRAND 354 357 {ECO:0000244|PDB:3P0U}.
HELIX 386 402 {ECO:0000244|PDB:3P0U}.
TURN 405 407 {ECO:0000244|PDB:3P0U}.
HELIX 408 410 {ECO:0000244|PDB:3P0U}.
HELIX 412 420 {ECO:0000244|PDB:3P0U}.
HELIX 423 433 {ECO:0000244|PDB:3P0U}.
TURN 434 436 {ECO:0000244|PDB:3P0U}.
HELIX 468 484 {ECO:0000244|PDB:3P0U}.
HELIX 489 500 {ECO:0000244|PDB:3P0U}.
HELIX 512 532 {ECO:0000244|PDB:3P0U}.
TURN 533 535 {ECO:0000244|PDB:3P0U}.
HELIX 539 544 {ECO:0000244|PDB:3P0U}.
HELIX 547 551 {ECO:0000244|PDB:3P0U}.
HELIX 555 562 {ECO:0000244|PDB:3P0U}.
HELIX 567 570 {ECO:0000244|PDB:3P0U}.
HELIX 572 579 {ECO:0000244|PDB:3P0U}.
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


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