Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P13056

- NR2C1_HUMAN

UniProt

P13056 - NR2C1_HUMAN

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
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 151 (01 Oct 2014)
      Sequence version 2 (14 Apr 2009)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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. protein binding Source: UniProtKB
    3. receptor activity Source: ProtInc
    4. sequence-specific DNA binding Source: InterPro
    5. sequence-specific DNA binding transcription factor activity Source: InterPro
    6. steroid hormone receptor activity Source: ProtInc
    7. 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

    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: UniProtKB-SubCell

    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

    ArrayExpressiP13056.
    BgeeiP13056.
    CleanExiHS_NR2C1.
    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 111-589.
    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.
    HOGENOMiHOG000013058.
    HOVERGENiHBG008596.
    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

    MATIEEIAHQ IIEQQMGEIV TEQQTGQKIQ IVTALDHNTQ GKQFILTNHD    50
    GSTPSKVILA RQDSTPGKVF LTTPDAAGVN QLFFTTPDLS AQHLQLLTDN 100
    SPDQGPNKVF DLCVVCGDKA SGRHYGAVTC EGCKGFFKRS IRKNLVYSCR 150
    GSKDCIINKH HRNRCQYCRL QRCIAFGMKQ DSVQCERKPI EVSREKSSNC 200
    AASTEKIYIR KDLRSPLTAT PTFVTDSEST RSTGLLDSGM FMNIHPSGVK 250
    TESAVLMTSD KAESCQGDLS TLANVVTSLA NLGKTKDLSQ NSNEMSMIES 300
    LSNDDTSLCE FQEMQTNGDV SRAFDTLAKA LNPGESTACQ SSVAGMEGSV 350
    HLITGDSSIN YTEKEGPLLS DSHVAFRLTM PSPMPEYLNV HYIGESASRL 400
    LFLSMHWALS IPSFQALGQE NSISLVKAYW NELFTLGLAQ CWQVMNVATI 450
    LATFVNCLHN SLQQDKMSTE RRKLLMEHIF KLQEFCNSMV KLCIDGYEYA 500
    YLKAIVLFSP DHPSLENMEQ IEKFQEKAYV EFQDYITKTY PDDTYRLSRL 550
    LLRLPALRLM NATITEELFF KGLIGNIRID SVIPHILKME PADYNSQIIG 600
    HSI 603
    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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 111-589.
    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.
    HOGENOMi HOG000013058.
    HOVERGENi HBG008596.
    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

    ArrayExpressi P13056.
    Bgeei P13056.
    CleanExi HS_NR2C1.
    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

    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 1, 2014
    This is version 151 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