P49116 (NR2C2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Nuclear receptor subfamily 2 group C member 2

Alternative name(s):
Orphan nuclear receptor TAK1
Orphan nuclear receptor TR4
Testicular receptor 4

Gene names

Name:	NR2C2
Synonyms:	TAK1, TR4

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	596 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Orphan nuclear receptor that can act as a repressor or activator of transcription. An important repressor of nuclear recptor 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. Ref.7 Ref.8 Ref.9 Ref.10 Ref.12
Subunit structure	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. Interacts (MAPK-mediated phosphorylated form) with NRIP1; the interaction promotes repression of NR2C2-mediated activity By similarity. Interacts with NR2C2AP; the interaction represses selective NR2C2-mediated transcriptional activity. Interacts with NLRP10. Ref.8 Ref.11 Ref.12 Ref.17
Subcellular location	Nucleus Ref.10.
Developmental stage	Transiently repressed during the meiotic phase of spermatogenesis.
Induction	Induced by oxidative stress via FOXO3 activation. Ref.13
Post-translational modification	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.
Sequence similarities	Belongs to the nuclear hormone receptor family. NR2 subfamily. Contains 1 nuclear receptor DNA-binding domain.

Ontologies

Keywords
Biological process	Differentiation Spermatogenesis Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing
Domain	Zinc-finger
Ligand	DNA-binding Metal-binding Zinc
Molecular function	Activator Receptor Repressor
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cell differentiation Inferred from electronic annotation. Source: UniProtKB-KW cerebellum development Inferred from electronic annotation. Source: Compara meiotic cell cycle Inferred from electronic annotation. Source: Compara nervous system development Traceable author statement PubMed 9006963. Source: ProtInc positive regulation of behavior Inferred from electronic annotation. Source: Compara positive regulation of embryonic development Inferred from electronic annotation. Source: Compara positive regulation of transcription from RNA polymerase II promoter Inferred from direct assay Ref.10. Source: UniProtKB spermatogenesis Inferred from electronic annotation. Source: UniProtKB-KW transcription initiation from RNA polymerase II promoter Traceable author statement. Source: Reactome
Cellular_component	nucleoplasm Traceable author statement. Source: Reactome
Molecular_function	protein heterodimerization activity Inferred from direct assay Ref.12. Source: UniProtKB receptor activity Traceable author statement PubMed 9006963. Source: ProtInc sequence-specific DNA binding Inferred from direct assay Ref.10. Source: UniProtKB sequence-specific DNA binding transcription factor activity Inferred from direct assay Ref.10. Source: UniProtKB steroid hormone receptor activity Inferred from electronic annotation. Source: InterPro transcription coactivator activity Traceable author statement PubMed 9006963. Source: ProtInc zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P49116-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: P49116-2)

The sequence of this isoform differs from the canonical sequence as follows:
     24-24: Q → QGSEPASGPLSVFTSLNKEK

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 596

596

Nuclear receptor subfamily 2 group C member 2

PRO_0000053588

Regions

DNA binding

114 – 189

76

Nuclear receptor Ref.3 Ref.7 Ref.8 Ref.9

Zinc finger

117 – 137

21

NR C4-type

Zinc finger

153 – 177

25

NR C4-type

Region

388 – 554

167

Ligand-binding By similarity

Amino acid modifications

Modified residue

19

1

Phosphoserine; by MAPK Ref.15 Ref.16

Modified residue

46

1

Phosphoserine Ref.15 Ref.16

Modified residue

55

1

Phosphoserine; by MAPK By similarity

Modified residue

68

1

Phosphoserine; by MAPK Ref.16

Modified residue

98

1

Phosphoserine Ref.16

Modified residue

219

1

Phosphoserine Ref.14 Ref.16

Natural variations

Alternative sequence

24

1

Q → QGSEPASGPLSVFTSLNKEK in isoform 2.

VSP_039522

Experimental info

Sequence conflict

108

1

V → A in BAH02299. Ref.3

Sequence conflict

156

1

N → S in AAA21474. Ref.2

Sequence conflict

326

1

S → F in BAH02299. Ref.3

Sequence conflict

400

1

W → R in AAA21474. Ref.2

Sequence conflict

409

1

A → G in AAA21474. Ref.2

Sequence conflict

484 – 485

2

KL → NW in AAA21474. Ref.2

Sequence conflict

594

1

A → V in AAA21474. Ref.2

Sequence conflict

594

1

A → V in BAH02299. Ref.3

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

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.

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.

.

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596

Helix Strand Turn

Details...

Beta strand

354 – 357

4

Helix

386 – 402

17

Turn

405 – 407

3

Helix

408 – 410

3

Helix

412 – 420

9

Helix

423 – 433

11

Turn

434 – 436

3

Helix

468 – 484

17

Helix

489 – 500

12

Helix

512 – 532

21

Turn

533 – 535

3

Helix

539 – 544

6

Helix

547 – 551

5

Helix

555 – 562

8

Helix

567 – 570

4

Helix

572 – 579

8

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified February 1, 1996. Version 1. Checksum: 5180BDC3F3C8BD79	FASTA	596	65,414
	10 20 30 40 50 60 MTSPSPRIQI ISTDSAVASP QRIQIVTDQQ TGQKIQIVTA VDASGSPKQQ FILTSPDGAG 70 80 90 100 110 120 TGKVILASPE TSSAKQLIFT TSDNLVPGRI QIVTDSASVE RLLGKTDVQR PQVVEYCVVC 130 140 150 160 170 180 GDKASGRHYG AVSCEGCKGF FKRSVRKNLT YSCRSNQDCI INKHHRNRCQ FCRLKKCLEM 190 200 210 220 230 240 GMKMESVQSE RKPFDVQREK PSNCAASTEK IYIRKDLRSP LIATPTFVAD KDGARQTGLL 250 260 270 280 290 300 DPGMLVNIQQ PLIREDGTVL LATDSKAETS QGALGTLANV VTSLANLSES LNNGDTSEIQ 310 320 330 340 350 360 PEDQSASEIT RAFDTLAKAL NTTDSSSSPS LADGIDTSGG GSIHVISRDQ STPIIEVEGP 370 380 390 400 410 420 LLSDTHVTFK LTMPSPMPEY LNVHYICESA SRLLFLSMHW ARSIPAFQAL GQDCNTSLVR 430 440 450 460 470 480 ACWNELFTLG LAQCAQVMSL STILAAIVNH LQNSIQEDKL SGDRIKQVME HIWKLQEFCN 490 500 510 520 530 540 SMAKLDIDGY EYAYLKAIVL FSPDHPGLTS TSQIEKFQEK AQMELQDYVQ KTYSEDTYRL 550 560 570 580 590 ARILVRLPAL RLMSSNITEE LFFTGLIGNV SIDSIIPYIL KMETAEYNGQ ITGASL
	Isoform 2 [UniParc]. Checksum: 5D557E04602C1BAB	FASTA	615	67,345
	10 20 30 40 50 60 MTSPSPRIQI ISTDSAVASP QRIQGSEPAS GPLSVFTSLN KEKIVTDQQT GQKIQIVTAV 70 80 90 100 110 120 DASGSPKQQF ILTSPDGAGT GKVILASPET SSAKQLIFTT SDNLVPGRIQ IVTDSASVER 130 140 150 160 170 180 LLGKTDVQRP QVVEYCVVCG DKASGRHYGA VSCEGCKGFF KRSVRKNLTY SCRSNQDCII 190 200 210 220 230 240 NKHHRNRCQF CRLKKCLEMG MKMESVQSER KPFDVQREKP SNCAASTEKI YIRKDLRSPL 250 260 270 280 290 300 IATPTFVADK DGARQTGLLD PGMLVNIQQP LIREDGTVLL ATDSKAETSQ GALGTLANVV 310 320 330 340 350 360 TSLANLSESL NNGDTSEIQP EDQSASEITR AFDTLAKALN TTDSSSSPSL ADGIDTSGGG 370 380 390 400 410 420 SIHVISRDQS TPIIEVEGPL LSDTHVTFKL TMPSPMPEYL NVHYICESAS RLLFLSMHWA 430 440 450 460 470 480 RSIPAFQALG QDCNTSLVRA CWNELFTLGL AQCAQVMSLS TILAAIVNHL QNSIQEDKLS 490 500 510 520 530 540 GDRIKQVMEH IWKLQEFCNS MAKLDIDGYE YAYLKAIVLF SPDHPGLTST SQIEKFQEKA 550 560 570 580 590 600 QMELQDYVQK TYSEDTYRLA RILVRLPALR LMSSNITEEL FFTGLIGNVS IDSIIPYILK 610 METAEYNGQI TGASL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"TAK1: molecular cloning and characterization of a new member of the nuclear receptor superfamily." Hirose T., Fujimoto W., Yamaai T., Kim K.H., Matsuura H., Jetten A.M. Mol. Endocrinol. 8:1667-1680(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Testis.
[2]	"Human and rat TR4 orphan receptors specify a subclass of the steroid receptor superfamily." Chang C., da Silva S.L., Ideta R., Lee Y., Yeh S., Burbach J.P. Proc. Natl. Acad. Sci. U.S.A. 91:6040-6044(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). Tissue: Prostate and Testis.
[3]	"DNA-binding profiling of human hormone nuclear receptors via fluorescence correlation spectroscopy in a cell-free system." Kobayashi T., Kodani Y., Nozawa A., Endo Y., Sawasaki T. FEBS Lett. 582:2737-2744(2008) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), DNA-BINDING SPECIFICITY.
[4]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." 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. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[5]	"The DNA sequence, annotation and analysis of human chromosome 3." 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. Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	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 Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	"The orphan receptor TAK1 acts as a repressor of RAR-, RXR- and T3R-mediated signaling pathways." Hirose T., Apfel R., Pfahl M., Jetten A.M. Biochem. Biophys. Res. Commun. 211:83-91(1995) [PubMed] [Europe PMC] [Abstract] Cited for: DNA-BINDING, FUNCTION.
[8]	"Regulation of peroxisome proliferator-activated receptor alpha-induced transactivation by the nuclear orphan receptor TAK1/TR4." Yan Z.H., Karam W.G., Staudinger J.L., Medvedev A., Ghanayem B.I., Jetten A.M. J. Biol. Chem. 273:10948-10957(1998) [PubMed] [Europe PMC] [Abstract] Cited for: DNA-BINDING, INTERACTION WITH NRIP1, FUNCTION.
[9]	"Differential regulation of direct repeat 3 vitamin D3 and direct repeat 4 thyroid hormone signaling pathways by the human TR4 orphan receptor." Lee Y.F., Young W.J., Lin W.J., Shyr C.R., Chang C. J. Biol. Chem. 274:16198-16205(1999) [PubMed] [Europe PMC] [Abstract] Cited for: DNA-BINDING, FUNCTION.
[10]	"Nuclear orphan receptors regulate transcription of the gene for the human luteinizing hormone receptor." Zhang Y., Dufau M.L. J. Biol. Chem. 275:2763-2770(2000) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
[11]	"Identification of a novel testicular orphan receptor-4 (TR4)-associated protein as repressor for the selective suppression of TR4-mediated transactivation." Yang Y., Wang X., Dong T., Kim E., Lin W.-J., Chang C. J. Biol. Chem. 278:7709-7717(2003) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH NR2C2AP.
[12]	"The TR2 and TR4 orphan nuclear receptors repress Gata1 transcription." Tanabe O., Shen Y., Liu Q., Campbell A.D., Kuroha T., Yamamoto M., Engel J.D. Genes Dev. 21:2832-2844(2007) [PubMed] [Europe PMC] [Abstract] Cited for: HETERODIMERIZATION, FUNCTION.
[13]	"Oxidative stress stimulates testicular orphan receptor 4 through forkhead transcription factor forkhead box O3a." Li G., Lee Y.F., Liu S., Cai Y., Xie S., Liu N.C., Bao B.Y., Chen Z., Chang C. Endocrinology 149:3490-3499(2008) [PubMed] [Europe PMC] [Abstract] Cited for: INDUCTION.
[14]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-219, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[15]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19 AND SER-46, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[16]	"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." 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. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19; SER-46; SER-68; SER-98 AND SER-219, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[17]	"NLRP10 enhances Shigella-induced pro-inflammatory responses." Lautz K., Damm A., Menning M., Wenger J., Adam A.C., Zigrino P., Kremmer E., Kufer T.A. Cell. Microbiol. 14:1568-1583(2012) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH NLRP10.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U10990 mRNA. Translation: AAC50118.1.
L27586 mRNA. Translation: AAA21474.1.
AB307708 mRNA. Translation: BAH02299.1.
AK290590 mRNA. Translation: BAF83279.1.
AC090937 Genomic DNA. No translation available.
AC090954 Genomic DNA. No translation available.
CH471055 Genomic DNA. Translation: EAW64215.1.

IPI

IPI00332451.
IPI00749258.

PIR

A57031.
I59309.

RefSeq

NP_003289.2. NM_003298.3.

UniGene

Hs.555973.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3P0U	X-ray	3.00	A/B	348-596	[»]

ProteinModelPortal

P49116.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-5999N.

IntAct

P49116. 2 interactions.

MINT

MINT-7004540.

STRING

9606.ENSP00000320447.

PTM databases

PhosphoSite

P49116.

Polymorphism databases

DMDM

1351190.

Proteomic databases

PaxDb

P49116.

PRIDE

P49116.

Protocols and materials databases

DNASU

7182.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000323373; ENSP00000320447; ENSG00000177463.
ENST00000393102; ENSP00000376814; ENSG00000177463.
ENST00000406272; ENSP00000384463; ENSG00000177463.
ENST00000425241; ENSP00000388387; ENSG00000177463.

GeneID

7182.

KEGG

hsa:7182.

UCSC

uc003bzj.4. human.

Organism-specific databases

CTD

7182.

GeneCards

GC03P014989.

HGNC

HGNC:7972. NR2C2.

HPA

HPA006313.

MIM

601426. gene.

neXtProt

NX_P49116.

PharmGKB

PA31755.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG297520.

HOGENOM

HOG000013058.

HOVERGEN

HBG008596.

KO

K08544.

OMA

KADVQRP.

OrthoDB

EOG4Z36D8.

Enzyme and pathway databases

Pathway_Interaction_DB

ar_tf_pathway. Regulation of Androgen receptor activity.

Reactome

REACT_71. Gene Expression.

SignaLink

P49116.

Gene expression databases

ArrayExpress

P49116.

Bgee

P49116.

CleanEx

HS_NR2C2.

Genevestigator

P49116.

GermOnline

ENSG00000177463. Homo sapiens.

Family and domain databases

Gene3D

1.10.565.10. 3 hits.
3.30.50.10. 1 hit.

InterPro

IPR008946. Nucl_hormone_rcpt_ligand-bd.
IPR000536. Nucl_hrmn_rcpt_lig-bd_core.
IPR001723. Str_hrmn_rcpt.
IPR001628. Znf_hrmn_rcpt.
IPR013088. Znf_NHR/GATA.
[Graphical view]

Pfam

PF00104. Hormone_recep. 1 hit.
PF00105. zf-C4. 1 hit.
[Graphical view]

PRINTS

PR00398. STRDHORMONER.
PR00047. STROIDFINGER.

SMART

SM00430. HOLI. 1 hit.
SM00399. ZnF_C4. 1 hit.
[Graphical view]

SUPFAM

SSF48508. Str_ncl_receptor. 1 hit.

PROSITE

PS00031. NUCLEAR_REC_DBD_1. 1 hit.
PS51030. NUCLEAR_REC_DBD_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

P49116.

ChEMBL

CHEMBL5716.

ChiTaRS

NR2C2. human.

EvolutionaryTrace

P49116.

GenomeRNAi

7182.

NextBio

28158.

SOURCE

Search...

Entry information

Entry name

NR2C2_HUMAN

Accession

Primary (citable) accession number: P49116
Secondary accession number(s): A8K3H5, B6ZGT8, P55092

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1996
Last sequence update:	February 1, 1996
Last modified:	May 29, 2013
This is version 126 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.