P13056 (NR2C1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Nuclear receptor subfamily 2 group C member 1

Alternative name(s):
Orphan nuclear receptor TR2
Testicular receptor 2

Gene names

Name:	NR2C1
Synonyms:	TR2

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	603 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Orphan nuclear receptor. Binds the IR7 element in the promoter of its own gene in an autoregulatory negative feedback mechanism. Primarily repressor of a broad range of genes. Binds to hormone response elements (HREs) consisting of two 5'-AGGTCA-3' half site direct repeat consensus sequences. Together with NR2C2, forms the core of the DRED (direct repeat erythroid-definitive) complex that represses embryonic and fetal globin transcription. Also activator of OCT4 gene expression. May be involved in stem cell proliferation and differentiation. Mediator of retinoic acid-regulated preadipocyte proliferation. Ref.7 Ref.8
Subunit structure	Homodimer By similarity. Heterodimer; binds DNA as a heterodimer with NR2C2 required for chromatin remodeling and for binding to promoter regions such as globin DR1 repeats By similarity. Interacts with NRIP1 (via its LXXLL motifs); the interaction provides corepressor activity. Interacts with HDAC3 (via the DNA-binding domain). Interacts with HDAC4 (via the DNA-binding domain). Interacts with PIAS1; the interaction is required for sumoylation of NR2C1. Interacts with UBE2I; the interaction is required for sumoylation of NR2C1. Interacts with KAT2B; the interaction acts as a corepressor of gene expression By similarity. Interacts with ESR1; the interaction prevents homodimerization of ESR1 and suppresses its transcriptional activity and cell growth. Ref.7
Subcellular location	Nucleus By similarity. Nucleus › PML body By similarity. Note: Recruited by HDAC3, after all-trans retinoic acid stimulated MAPK1-mediated Thr-223 phosphorylation, to PML bodies for subsequent sumoylation By similarity.
Post-translational modification	Sumoylation requires both PIAS1 and UBE2I. Sumoylation appears to dissociate NR2C1 from the PML nuclear bodies. Enhances the interaction with NRIP1 but inhibits interaction with KAT2B. In proliferating cells, stimulation by all-trans retinoic acid, activation of MAPK1-mediated phosphorylation and recruitment to PML bodies with subsequent sumoylation, suppresses OCT4 expression By similarity. Phosphorylated on several serine and threonine residues. Phosphorylation on Thr-222, stimulated by all-trans retinoic acid (atRA) mediates PML location and sumoylation in proliferating cells which then modulates its association with effector molecules, KAT2B and NRIP1. Phosphorylation on Ser-581 by PKC is important for protein stability and function as activator of RARB By similarity.
Sequence similarities	Belongs to the nuclear hormone receptor family. NR2 subfamily. Contains 1 nuclear receptor DNA-binding domain.

Ontologies

Keywords
Biological process	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	Isopeptide bond Phosphoprotein Ubl conjugation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	negative regulation of transcription from RNA polymerase II promoter Inferred from electronic annotation. Source: Compara positive regulation of retinoic acid receptor signaling pathway Inferred from electronic annotation. Source: Compara transcription initiation from RNA polymerase II promoter Traceable author statement. Source: Reactome
Cellular_component	PML body Inferred from electronic annotation. Source: UniProtKB-SubCell nucleoplasm Traceable author statement. Source: Reactome
Molecular_function	DNA binding Traceable author statement Ref.1. Source: ProtInc sequence-specific DNA binding Inferred from electronic annotation. Source: InterPro sequence-specific DNA binding transcription factor activity Inferred from electronic annotation. Source: InterPro steroid hormone receptor activity Traceable author statement Ref.2. Source: ProtInc zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P13056-1)

Also known as: TR2-11;

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: P13056-2)

Also known as: TR2-9;

The sequence of this isoform differs from the canonical sequence as follows:
     465-467: DKM → AEG
     468-603: Missing.

Isoform 3 (identifier: P13056-3)

Also known as: TR2-7;

The sequence of this isoform differs from the canonical sequence as follows:
     466-483: KMSTERRKLLMEHIFKLQ → AKVIAALIHFTRRAITDL
     484-603: Missing.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 603	603	Nuclear receptor subfamily 2 group C member 1		PRO_0000053586
Regions
	DNA binding	110 – 185	76	Nuclear receptor
	Zinc finger	113 – 133	21	NR C4-type
	Zinc finger	149 – 173	25	NR C4-type
	Region	1 – 178	178	Required for interaction with KAT2B By similarity
	Region	584 – 603	20	Required for interaction with NRIP1 By similarity
Amino acid modifications
	Modified residue	197	1	Phosphoserine By similarity
	Modified residue	215	1	Phosphoserine Ref.9
	Modified residue	220	1	Phosphothreonine Ref.9
	Modified residue	222	1	Phosphothreonine; by MAPK1 By similarity
	Modified residue	581	1	Phosphoserine; by PKC By similarity
	Cross-link	250		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity
Natural variations
	Alternative sequence	465 – 467	3	DKM → AEG in isoform 2.		VSP_036855
	Alternative sequence	466 – 483	18	KMSTE…IFKLQ → AKVIAALIHFTRRAITDL in isoform 3.		VSP_036856
	Alternative sequence	468 – 603	136	Missing in isoform 2.		VSP_036857
	Alternative sequence	484 – 603	120	Missing in isoform 3.		VSP_036858
Experimental info
	Sequence conflict	291	1	N → K in BAF84008. Ref.3
	Sequence conflict	304	1	D → N in BAF84008. Ref.3
	Sequence conflict	520	1	Q → L in AAA36761. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (TR2-11) [UniParc]. Last modified April 14, 2009. Version 2. Checksum: 37444D2701B9CA60	FASTA	603	67,315
	10 20 30 40 50 60 MATIEEIAHQ IIEQQMGEIV TEQQTGQKIQ IVTALDHNTQ GKQFILTNHD GSTPSKVILA 70 80 90 100 110 120 RQDSTPGKVF LTTPDAAGVN QLFFTTPDLS AQHLQLLTDN SPDQGPNKVF DLCVVCGDKA 130 140 150 160 170 180 SGRHYGAVTC EGCKGFFKRS IRKNLVYSCR GSKDCIINKH HRNRCQYCRL QRCIAFGMKQ 190 200 210 220 230 240 DSVQCERKPI EVSREKSSNC AASTEKIYIR KDLRSPLTAT PTFVTDSEST RSTGLLDSGM 250 260 270 280 290 300 FMNIHPSGVK TESAVLMTSD KAESCQGDLS TLANVVTSLA NLGKTKDLSQ NSNEMSMIES 310 320 330 340 350 360 LSNDDTSLCE FQEMQTNGDV SRAFDTLAKA LNPGESTACQ SSVAGMEGSV HLITGDSSIN 370 380 390 400 410 420 YTEKEGPLLS DSHVAFRLTM PSPMPEYLNV HYIGESASRL LFLSMHWALS IPSFQALGQE 430 440 450 460 470 480 NSISLVKAYW NELFTLGLAQ CWQVMNVATI LATFVNCLHN SLQQDKMSTE RRKLLMEHIF 490 500 510 520 530 540 KLQEFCNSMV KLCIDGYEYA YLKAIVLFSP DHPSLENMEQ IEKFQEKAYV EFQDYITKTY 550 560 570 580 590 600 PDDTYRLSRL LLRLPALRLM NATITEELFF KGLIGNIRID SVIPHILKME PADYNSQIIG HSI
	Isoform 2 (TR2-9) [UniParc]. Checksum: 012EB168180BC63A	FASTA	467	51,193
	10 20 30 40 50 60 MATIEEIAHQ IIEQQMGEIV TEQQTGQKIQ IVTALDHNTQ GKQFILTNHD GSTPSKVILA 70 80 90 100 110 120 RQDSTPGKVF LTTPDAAGVN QLFFTTPDLS AQHLQLLTDN SPDQGPNKVF DLCVVCGDKA 130 140 150 160 170 180 SGRHYGAVTC EGCKGFFKRS IRKNLVYSCR GSKDCIINKH HRNRCQYCRL QRCIAFGMKQ 190 200 210 220 230 240 DSVQCERKPI EVSREKSSNC AASTEKIYIR KDLRSPLTAT PTFVTDSEST RSTGLLDSGM 250 260 270 280 290 300 FMNIHPSGVK TESAVLMTSD KAESCQGDLS TLANVVTSLA NLGKTKDLSQ NSNEMSMIES 310 320 330 340 350 360 LSNDDTSLCE FQEMQTNGDV SRAFDTLAKA LNPGESTACQ SSVAGMEGSV HLITGDSSIN 370 380 390 400 410 420 YTEKEGPLLS DSHVAFRLTM PSPMPEYLNV HYIGESASRL LFLSMHWALS IPSFQALGQE 430 440 450 460 NSISLVKAYW NELFTLGLAQ CWQVMNVATI LATFVNCLHN SLQQAEG
	Isoform 3 (TR2-7) [UniParc]. Checksum: 293E21E317E05814	FASTA	483	53,042
	10 20 30 40 50 60 MATIEEIAHQ IIEQQMGEIV TEQQTGQKIQ IVTALDHNTQ GKQFILTNHD GSTPSKVILA 70 80 90 100 110 120 RQDSTPGKVF LTTPDAAGVN QLFFTTPDLS AQHLQLLTDN SPDQGPNKVF DLCVVCGDKA 130 140 150 160 170 180 SGRHYGAVTC EGCKGFFKRS IRKNLVYSCR GSKDCIINKH HRNRCQYCRL QRCIAFGMKQ 190 200 210 220 230 240 DSVQCERKPI EVSREKSSNC AASTEKIYIR KDLRSPLTAT PTFVTDSEST RSTGLLDSGM 250 260 270 280 290 300 FMNIHPSGVK TESAVLMTSD KAESCQGDLS TLANVVTSLA NLGKTKDLSQ NSNEMSMIES 310 320 330 340 350 360 LSNDDTSLCE FQEMQTNGDV SRAFDTLAKA LNPGESTACQ SSVAGMEGSV HLITGDSSIN 370 380 390 400 410 420 YTEKEGPLLS DSHVAFRLTM PSPMPEYLNV HYIGESASRL LFLSMHWALS IPSFQALGQE 430 440 450 460 470 480 NSISLVKAYW NELFTLGLAQ CWQVMNVATI LATFVNCLHN SLQQDAKVIA ALIHFTRRAI TDL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Identification of a new member of the steroid receptor super-family by cloning and sequence analysis." Chang C., Kokontis J. Biochem. Biophys. Res. Commun. 155:971-977(1988) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3). Tissue: Testis.
[2]	"Molecular cloning of new human TR2 receptors: a class of steroid receptor with multiple ligand-binding domains." Chang C., Kokontis J., Acakpo-Satchivi L., Liao S., Takeda H., Chang Y. Biochem. Biophys. Res. Commun. 165:735-741(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
[3]	"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). Tissue: Tongue.
[4]	"The finished DNA sequence of human chromosome 12." Scherer S.E., Muzny D.M., 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., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A. Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	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].
[6]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Tissue: Colon.
[7]	"Suppression of estrogen receptor-mediated transcription and cell growth by interaction with TR2 orphan receptor." Hu Y.C., Shyr C.R., Che W., Mu X.M., Kim E., Chang C. J. Biol. Chem. 277:33571-33579(2002) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH ESR1.
[8]	"Transcriptional regulation of the human TR2 orphan receptor gene by nuclear factor 1-A." Lin Y.L., Wang Y.H., Lee H.J. Biochem. Biophys. Res. Commun. 350:430-436(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[9]	"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-215 AND THR-220, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[10]	"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M21985 mRNA. Translation: AAA36650.1. M29959 mRNA. Translation: AAA36762.1. M29960 mRNA. Translation: AAA36761.1. AK291319 mRNA. Translation: BAF84008.1. AC011598 Genomic DNA. No translation available. CH471054 Genomic DNA. Translation: EAW97518.1. BC040141 mRNA. Translation: AAH40141.1.
IPI	IPI00019051. IPI00334759. IPI00798023.
PIR	A31521. A36738. B36738.
RefSeq	NP_001027458.1. NM_001032287.2. NP_001120834.1. NM_001127362.1. NP_003288.2. NM_003297.3.
UniGene	Hs.108301. Hs.707524.
3D structure databases
ProteinModelPortal	P13056.
ModBase	Search...
Protein-protein interaction databases
IntAct	P13056. 2 interactions.
MINT	MINT-8247579.
STRING	9606.ENSP00000333275.
PTM databases
PhosphoSite	P13056.
Polymorphism databases
DMDM	226693548.
Proteomic databases
PaxDb	P13056.
PRIDE	P13056.
Protocols and materials databases
DNASU	7181.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000330677; ENSP00000328843; ENSG00000120798. ENST00000333003; ENSP00000333275; ENSG00000120798. ENST00000393101; ENSP00000376813; ENSG00000120798.
GeneID	7181.
KEGG	hsa:7181.
UCSC	uc001tdm.4. human. uc001tdn.4. human. uc001tdo.4. human.
Organism-specific databases
CTD	7181.
GeneCards	GC12M095414.
HGNC	HGNC:7971. NR2C1.
MIM	601529. gene.
neXtProt	NX_P13056.
PharmGKB	PA31754.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG297520.
HOGENOM	HOG000013058.
HOVERGEN	HBG008596.
KO	K08543.
OMA	QNSNEMS.
OrthoDB	EOG476JZT.
PhylomeDB	P13056.
Enzyme and pathway databases
Pathway_Interaction_DB	ar_tf_pathway. Regulation of Androgen receptor activity. hdac_classi_pathway. Signaling events mediated by HDAC Class I.
Reactome	REACT_71. Gene Expression.
SignaLink	P13056.
Gene expression databases
ArrayExpress	P13056.
Bgee	P13056.
CleanEx	HS_NR2C1.
Genevestigator	P13056.
GermOnline	ENSG00000120798. 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
ChEMBL	CHEMBL1961787.
GenomeRNAi	7181.
NextBio	28152.
SOURCE	Search...

Entry information

Entry name

NR2C1_HUMAN

Accession

Primary (citable) accession number: P13056
Secondary accession number(s): A8K5K4, Q15625, Q15626

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1990
Last sequence update:	April 14, 2009
Last modified:	May 29, 2013
This is version 137 of the entry and version 2 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.