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P13056

- NR2C1_HUMAN

UniProt

P13056 - NR2C1_HUMAN

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Protein

Nuclear receptor subfamily 2 group C member 1

Gene

NR2C1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.2 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi110 – 18576Nuclear receptorPROSITE-ProRule annotationAdd
BLAST
Zinc fingeri113 – 13321NR C4-typePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri149 – 17325NR C4-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. DNA binding Source: ProtInc
  2. receptor activity Source: ProtInc
  3. sequence-specific DNA binding Source: InterPro
  4. sequence-specific DNA binding transcription factor activity Source: InterPro
  5. steroid hormone receptor activity Source: ProtInc
  6. zinc ion binding Source: InterPro

GO - Biological processi

  1. gene expression Source: Reactome
  2. negative regulation of transcription from RNA polymerase II promoter Source: Ensembl
  3. positive regulation of retinoic acid receptor signaling pathway Source: Ensembl
  4. transcription initiation from RNA polymerase II promoter Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Activator, Receptor, Repressor

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding, Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_15525. Nuclear Receptor transcription pathway.
SignaLinkiP13056.

Names & Taxonomyi

Protein namesi
Recommended name:
Nuclear receptor subfamily 2 group C member 1
Alternative name(s):
Orphan nuclear receptor TR2
Testicular receptor 2
Gene namesi
Name:NR2C1
Synonyms:TR2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 12

Organism-specific databases

HGNCiHGNC:7971. NR2C1.

Subcellular locationi

Nucleus PROSITE-ProRule annotation. NucleusPML 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

GO - Cellular componenti

  1. nucleoplasm Source: Reactome
  2. PML body Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA31754.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 603603Nuclear receptor subfamily 2 group C member 1PRO_0000053586Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei197 – 1971PhosphoserineBy similarity
Modified residuei215 – 2151Phosphoserine1 Publication
Modified residuei220 – 2201Phosphothreonine1 Publication
Modified residuei222 – 2221Phosphothreonine; by MAPK1By similarity
Cross-linki250 – 250Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity
Modified residuei581 – 5811Phosphoserine; by PKCBy similarity

Post-translational modificationi

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).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).By similarity

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP13056.
PaxDbiP13056.
PRIDEiP13056.

PTM databases

PhosphoSiteiP13056.

Expressioni

Gene expression databases

BgeeiP13056.
CleanExiHS_NR2C1.
ExpressionAtlasiP13056. baseline and differential.
GenevestigatoriP13056.

Interactioni

Subunit structurei

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.By similarity1 Publication

Protein-protein interaction databases

BioGridi113033. 29 interactions.
IntActiP13056. 3 interactions.
MINTiMINT-8247579.
STRINGi9606.ENSP00000333275.

Structurei

3D structure databases

ProteinModelPortaliP13056.
SMRiP13056. Positions 112-220, 356-589.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 178178Required for interaction with KAT2BBy similarityAdd
BLAST
Regioni584 – 60320Required for interaction with NRIP1By similarityAdd
BLAST

Sequence similaritiesi

Contains 1 nuclear receptor DNA-binding domain.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri113 – 13321NR C4-typePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri149 – 17325NR C4-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiNOG297520.
GeneTreeiENSGT00760000118948.
HOGENOMiHOG000013058.
HOVERGENiHBG008596.
InParanoidiP13056.
KOiK08543.
OMAiEKAYMEF.
OrthoDBiEOG7FJH0K.
PhylomeDBiP13056.
TreeFamiTF316650.

Family and domain databases

Gene3Di1.10.565.10. 3 hits.
3.30.50.10. 1 hit.
InterProiIPR008946. 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]
PfamiPF00104. Hormone_recep. 1 hit.
PF00105. zf-C4. 1 hit.
[Graphical view]
PRINTSiPR00398. STRDHORMONER.
PR00047. STROIDFINGER.
SMARTiSM00430. HOLI. 1 hit.
SM00399. ZnF_C4. 1 hit.
[Graphical view]
SUPFAMiSSF48508. SSF48508. 3 hits.
PROSITEiPS00031. NUCLEAR_REC_DBD_1. 1 hit.
PS51030. NUCLEAR_REC_DBD_2. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P13056-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MATIEEIAHQ IIEQQMGEIV TEQQTGQKIQ IVTALDHNTQ GKQFILTNHD
60 70 80 90 100
GSTPSKVILA RQDSTPGKVF LTTPDAAGVN QLFFTTPDLS AQHLQLLTDN
110 120 130 140 150
SPDQGPNKVF DLCVVCGDKA SGRHYGAVTC EGCKGFFKRS IRKNLVYSCR
160 170 180 190 200
GSKDCIINKH HRNRCQYCRL QRCIAFGMKQ DSVQCERKPI EVSREKSSNC
210 220 230 240 250
AASTEKIYIR KDLRSPLTAT PTFVTDSEST RSTGLLDSGM FMNIHPSGVK
260 270 280 290 300
TESAVLMTSD KAESCQGDLS TLANVVTSLA NLGKTKDLSQ NSNEMSMIES
310 320 330 340 350
LSNDDTSLCE FQEMQTNGDV SRAFDTLAKA LNPGESTACQ SSVAGMEGSV
360 370 380 390 400
HLITGDSSIN YTEKEGPLLS DSHVAFRLTM PSPMPEYLNV HYIGESASRL
410 420 430 440 450
LFLSMHWALS IPSFQALGQE NSISLVKAYW NELFTLGLAQ CWQVMNVATI
460 470 480 490 500
LATFVNCLHN SLQQDKMSTE RRKLLMEHIF KLQEFCNSMV KLCIDGYEYA
510 520 530 540 550
YLKAIVLFSP DHPSLENMEQ IEKFQEKAYV EFQDYITKTY PDDTYRLSRL
560 570 580 590 600
LLRLPALRLM NATITEELFF KGLIGNIRID SVIPHILKME PADYNSQIIG

HSI
Length:603
Mass (Da):67,315
Last modified:April 14, 2009 - v2
Checksum:i37444D2701B9CA60
GO
Isoform 2 (identifier: P13056-2) [UniParc]FASTAAdd to Basket

Also known as: TR2-9

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

Show »
Length:467
Mass (Da):51,193
Checksum:i012EB168180BC63A
GO
Isoform 3 (identifier: P13056-3) [UniParc]FASTAAdd to Basket

Also known as: TR2-7

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

Show »
Length:483
Mass (Da):53,042
Checksum:i293E21E317E05814
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti291 – 2911N → K in BAF84008. (PubMed:14702039)Curated
Sequence conflicti304 – 3041D → N in BAF84008. (PubMed:14702039)Curated
Sequence conflicti520 – 5201Q → L in AAA36761. (PubMed:2597158)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei465 – 4673DKM → AEG in isoform 2. 2 PublicationsVSP_036855
Alternative sequencei466 – 48318KMSTE…IFKLQ → AKVIAALIHFTRRAITDL in isoform 3. 1 PublicationVSP_036856Add
BLAST
Alternative sequencei468 – 603136Missing in isoform 2. 2 PublicationsVSP_036857Add
BLAST
Alternative sequencei484 – 603120Missing in isoform 3. 1 PublicationVSP_036858Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS41821.1. [P13056-2]
CCDS44953.1. [P13056-3]
CCDS9051.1. [P13056-1]
PIRiA31521.
A36738.
B36738.
RefSeqiNP_001027458.1. NM_001032287.2. [P13056-2]
NP_001120834.1. NM_001127362.1. [P13056-3]
NP_003288.2. NM_003297.3. [P13056-1]
UniGeneiHs.108301.
Hs.707524.

Genome annotation databases

EnsembliENST00000330677; ENSP00000328843; ENSG00000120798. [P13056-3]
ENST00000333003; ENSP00000333275; ENSG00000120798. [P13056-1]
ENST00000393101; ENSP00000376813; ENSG00000120798. [P13056-2]
GeneIDi7181.
KEGGihsa:7181.
UCSCiuc001tdm.5. human. [P13056-1]
uc001tdo.4. human. [P13056-3]

Polymorphism databases

DMDMi226693548.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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 .
CCDSi CCDS41821.1. [P13056-2 ]
CCDS44953.1. [P13056-3 ]
CCDS9051.1. [P13056-1 ]
PIRi A31521.
A36738.
B36738.
RefSeqi NP_001027458.1. NM_001032287.2. [P13056-2 ]
NP_001120834.1. NM_001127362.1. [P13056-3 ]
NP_003288.2. NM_003297.3. [P13056-1 ]
UniGenei Hs.108301.
Hs.707524.

3D structure databases

ProteinModelPortali P13056.
SMRi P13056. Positions 112-220, 356-589.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 113033. 29 interactions.
IntActi P13056. 3 interactions.
MINTi MINT-8247579.
STRINGi 9606.ENSP00000333275.

Chemistry

ChEMBLi CHEMBL1961787.

PTM databases

PhosphoSitei P13056.

Polymorphism databases

DMDMi 226693548.

Proteomic databases

MaxQBi P13056.
PaxDbi P13056.
PRIDEi P13056.

Protocols and materials databases

DNASUi 7181.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000330677 ; ENSP00000328843 ; ENSG00000120798 . [P13056-3 ]
ENST00000333003 ; ENSP00000333275 ; ENSG00000120798 . [P13056-1 ]
ENST00000393101 ; ENSP00000376813 ; ENSG00000120798 . [P13056-2 ]
GeneIDi 7181.
KEGGi hsa:7181.
UCSCi uc001tdm.5. human. [P13056-1 ]
uc001tdo.4. human. [P13056-3 ]

Organism-specific databases

CTDi 7181.
GeneCardsi GC12M095414.
HGNCi HGNC:7971. NR2C1.
MIMi 601529. gene.
neXtProti NX_P13056.
PharmGKBi PA31754.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG297520.
GeneTreei ENSGT00760000118948.
HOGENOMi HOG000013058.
HOVERGENi HBG008596.
InParanoidi P13056.
KOi K08543.
OMAi EKAYMEF.
OrthoDBi EOG7FJH0K.
PhylomeDBi P13056.
TreeFami TF316650.

Enzyme and pathway databases

Reactomei REACT_15525. Nuclear Receptor transcription pathway.
SignaLinki P13056.

Miscellaneous databases

GeneWikii Testicular_receptor_2.
GenomeRNAii 7181.
NextBioi 28152.
PROi P13056.
SOURCEi Search...

Gene expression databases

Bgeei P13056.
CleanExi HS_NR2C1.
ExpressionAtlasi P13056. baseline and differential.
Genevestigatori P13056.

Family and domain databases

Gene3Di 1.10.565.10. 3 hits.
3.30.50.10. 1 hit.
InterProi 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 ]
Pfami PF00104. Hormone_recep. 1 hit.
PF00105. zf-C4. 1 hit.
[Graphical view ]
PRINTSi PR00398. STRDHORMONER.
PR00047. STROIDFINGER.
SMARTi SM00430. HOLI. 1 hit.
SM00399. ZnF_C4. 1 hit.
[Graphical view ]
SUPFAMi SSF48508. SSF48508. 3 hits.
PROSITEi PS00031. NUCLEAR_REC_DBD_1. 1 hit.
PS51030. NUCLEAR_REC_DBD_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-215 AND THR-220, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    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.

Entry informationi

Entry nameiNR2C1_HUMAN
AccessioniPrimary (citable) accession number: P13056
Secondary accession number(s): A8K5K4, Q15625, Q15626
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: April 14, 2009
Last modified: October 29, 2014
This is version 152 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3