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P49116 (NR2C2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 138. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length596 AA.
Sequence statusComplete.
Protein existenceEvidence 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 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. 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 processDifferentiation
Spermatogenesis
Transcription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
   DomainZinc-finger
   LigandDNA-binding
Metal-binding
Zinc
   Molecular functionActivator
Receptor
Repressor
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcell differentiation

Inferred from electronic annotation. Source: UniProtKB-KW

cerebellum development

Inferred from electronic annotation. Source: Ensembl

gene expression

Traceable author statement. Source: Reactome

meiotic cell cycle

Inferred from electronic annotation. Source: Ensembl

nervous system development

Traceable author statement PubMed 9006963. Source: ProtInc

positive regulation of behavior

Inferred from electronic annotation. Source: Ensembl

positive regulation of embryonic development

Inferred from electronic annotation. Source: Ensembl

positive regulation of transcription from RNA polymerase II promoter

Inferred from direct assay Ref.10. Source: UniProtKB

regulation of transcription, DNA-templated

Traceable author statement PubMed 9006963. Source: ProtInc

spermatogenesis

Inferred from electronic annotation. Source: UniProtKB-KW

transcription initiation from RNA polymerase II promoter

Traceable author statement. Source: Reactome

   Cellular_componentnucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay. Source: HPA

   Molecular_functionprotein binding

Inferred from physical interaction PubMed 16887930PubMed 22486638. Source: UniProtKB

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 596596Nuclear receptor subfamily 2 group C member 2
PRO_0000053588

Regions

DNA binding114 – 18976Nuclear receptor Ref.3 Ref.7 Ref.8 Ref.9
Zinc finger117 – 13721NR C4-type
Zinc finger153 – 17725NR C4-type
Region388 – 554167Ligand-binding By similarity

Amino acid modifications

Modified residue191Phosphoserine; by MAPK Ref.15 Ref.16
Modified residue461Phosphoserine Ref.15 Ref.16
Modified residue551Phosphoserine; by MAPK By similarity
Modified residue681Phosphoserine; by MAPK Ref.16
Modified residue981Phosphoserine Ref.16
Modified residue2191Phosphoserine Ref.14 Ref.16
Modified residue2311N6-acetyllysine By similarity

Natural variations

Alternative sequence241Q → QGSEPASGPLSVFTSLNKEK in isoform 2.
VSP_039522

Experimental info

Sequence conflict1081V → A in BAH02299. Ref.3
Sequence conflict1561N → S in AAA21474. Ref.2
Sequence conflict3261S → F in BAH02299. Ref.3
Sequence conflict4001W → R in AAA21474. Ref.2
Sequence conflict4091A → G in AAA21474. Ref.2
Sequence conflict484 – 4852KL → NW in AAA21474. Ref.2
Sequence conflict5941A → V in AAA21474. Ref.2
Sequence conflict5941A → V in BAH02299. Ref.3

Secondary structure

.............................. 596
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified February 1, 1996. Version 1.
Checksum: 5180BDC3F3C8BD79

FASTA59665,414
        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 

« Hide

Isoform 2 [UniParc].

Checksum: 5D557E04602C1BAB
Show »

FASTA61567,345

References

« Hide '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. expand/collapse author list , 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. expand/collapse author list , 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. expand/collapse author list , 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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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.
CCDSCCDS2621.1. [P49116-2]
PIRA57031.
I59309.
RefSeqNP_001278623.1. NM_001291694.1.
NP_003289.2. NM_003298.4. [P49116-2]
UniGeneHs.555973.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3P0UX-ray3.00A/B348-596[»]
ProteinModelPortalP49116.
SMRP49116. Positions 115-582.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid113034. 32 interactions.
DIPDIP-5999N.
IntActP49116. 4 interactions.
MINTMINT-7004540.
STRING9606.ENSP00000320447.

Chemistry

BindingDBP49116.
ChEMBLCHEMBL5716.
GuidetoPHARMACOLOGY614.

PTM databases

PhosphoSiteP49116.

Polymorphism databases

DMDM1351190.

Proteomic databases

MaxQBP49116.
PaxDbP49116.
PRIDEP49116.

Protocols and materials databases

DNASU7182.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000323373; ENSP00000320447; ENSG00000177463. [P49116-2]
ENST00000393102; ENSP00000376814; ENSG00000177463. [P49116-1]
ENST00000406272; ENSP00000384463; ENSG00000177463. [P49116-1]
ENST00000425241; ENSP00000388387; ENSG00000177463. [P49116-1]
GeneID7182.
KEGGhsa:7182.
UCSCuc003bzj.4. human. [P49116-1]

Organism-specific databases

CTD7182.
GeneCardsGC03P014989.
HGNCHGNC:7972. NR2C2.
HPAHPA006313.
MIM601426. gene.
neXtProtNX_P49116.
PharmGKBPA31755.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG297520.
HOGENOMHOG000013058.
HOVERGENHBG008596.
KOK08544.
OMAYVQKTYP.
OrthoDBEOG7FJH0K.
PhylomeDBP49116.
TreeFamTF316650.

Enzyme and pathway databases

ReactomeREACT_71. Gene Expression.
SignaLinkP49116.

Gene expression databases

ArrayExpressP49116.
BgeeP49116.
CleanExHS_NR2C2.
GenevestigatorP49116.

Family and domain databases

Gene3D1.10.565.10. 3 hits.
3.30.50.10. 1 hit.
InterProIPR008946. 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]
PfamPF00104. Hormone_recep. 1 hit.
PF00105. zf-C4. 1 hit.
[Graphical view]
PRINTSPR00398. STRDHORMONER.
PR00047. STROIDFINGER.
SMARTSM00430. HOLI. 1 hit.
SM00399. ZnF_C4. 1 hit.
[Graphical view]
SUPFAMSSF48508. SSF48508. 2 hits.
PROSITEPS00031. NUCLEAR_REC_DBD_1. 1 hit.
PS51030. NUCLEAR_REC_DBD_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSNR2C2. human.
EvolutionaryTraceP49116.
GeneWikiTesticular_receptor_4.
GenomeRNAi7182.
NextBio28158.
PROP49116.
SOURCESearch...

Entry information

Entry nameNR2C2_HUMAN
AccessionPrimary (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: July 9, 2014
This is version 138 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 3

Human chromosome 3: entries, gene names and cross-references to MIM