Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P49116

- NR2C2_HUMAN

UniProt

P49116 - NR2C2_HUMAN

(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)

Protein

Nuclear receptor subfamily 2 group C member 2

Gene

NR2C2

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

Functioni

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.By similarity5 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi114 – 18976Nuclear receptorPROSITE-ProRule annotationAdd
BLAST
Zinc fingeri117 – 13721NR C4-typePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri153 – 17725NR C4-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

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

GO - Biological processi

  1. cell differentiation Source: UniProtKB-KW
  2. gene expression Source: Reactome
  3. nervous system development Source: ProtInc
  4. positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  5. regulation of transcription, DNA-templated Source: ProtInc
  6. spermatogenesis Source: UniProtKB-KW
  7. transcription initiation from RNA polymerase II promoter Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Activator, Receptor, Repressor

Keywords - Biological processi

Differentiation, Spermatogenesis, Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding, Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_15525. Nuclear Receptor transcription pathway.
SignaLinkiP49116.

Names & Taxonomyi

Protein namesi
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 namesi
Name:NR2C2
Synonyms:TAK1, TR4
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 3

Organism-specific databases

HGNCiHGNC:7972. NR2C2.

Subcellular locationi

Nucleus 1 PublicationPROSITE-ProRule annotation

GO - Cellular componenti

  1. nucleoplasm Source: Reactome
  2. nucleus Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA31755.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 596596Nuclear receptor subfamily 2 group C member 2PRO_0000053588Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei19 – 191Phosphoserine; by MAPK2 Publications
Modified residuei46 – 461Phosphoserine2 Publications
Modified residuei55 – 551Phosphoserine; by MAPKBy similarity
Modified residuei68 – 681Phosphoserine; by MAPK1 Publication
Modified residuei98 – 981Phosphoserine1 Publication
Modified residuei219 – 2191Phosphoserine2 Publications
Modified residuei231 – 2311N6-acetyllysineBy similarity

Post-translational modificationi

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).By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP49116.
PaxDbiP49116.
PRIDEiP49116.

PTM databases

PhosphoSiteiP49116.

Expressioni

Developmental stagei

Transiently repressed during the meiotic phase of spermatogenesis.

Inductioni

Induced by oxidative stress via FOXO3 activation.1 Publication

Gene expression databases

BgeeiP49116.
CleanExiHS_NR2C2.
ExpressionAtlasiP49116. baseline and differential.
GenevestigatoriP49116.

Organism-specific databases

HPAiHPA006313.

Interactioni

Subunit structurei

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.By similarity3 Publications

Protein-protein interaction databases

BioGridi113034. 32 interactions.
DIPiDIP-5999N.
IntActiP49116. 4 interactions.
MINTiMINT-7004540.
STRINGi9606.ENSP00000320447.

Structurei

Secondary structure

1
596
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi354 – 3574Combined sources
Helixi386 – 40217Combined sources
Turni405 – 4073Combined sources
Helixi408 – 4103Combined sources
Helixi412 – 4209Combined sources
Helixi423 – 43311Combined sources
Turni434 – 4363Combined sources
Helixi468 – 48417Combined sources
Helixi489 – 50012Combined sources
Helixi512 – 53221Combined sources
Turni533 – 5353Combined sources
Helixi539 – 5446Combined sources
Helixi547 – 5515Combined sources
Helixi555 – 5628Combined sources
Helixi567 – 5704Combined sources
Helixi572 – 5798Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3P0UX-ray3.00A/B348-596[»]
ProteinModelPortaliP49116.
SMRiP49116. Positions 117-225, 348-582.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP49116.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni388 – 554167Ligand-bindingBy similarityAdd
BLAST

Sequence similaritiesi

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

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri117 – 13721NR C4-typePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri153 – 17725NR C4-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiNOG297520.
GeneTreeiENSGT00760000118948.
HOGENOMiHOG000013058.
HOVERGENiHBG008596.
InParanoidiP49116.
KOiK08544.
OMAiYVQKTYP.
OrthoDBiEOG7FJH0K.
PhylomeDBiP49116.
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. 2 hits.
PROSITEiPS00031. NUCLEAR_REC_DBD_1. 1 hit.
PS51030. NUCLEAR_REC_DBD_2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P49116-1) [UniParc]FASTAAdd to Basket

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
MTSPSPRIQI ISTDSAVASP QRIQIVTDQQ TGQKIQIVTA VDASGSPKQQ
60 70 80 90 100
FILTSPDGAG TGKVILASPE TSSAKQLIFT TSDNLVPGRI QIVTDSASVE
110 120 130 140 150
RLLGKTDVQR PQVVEYCVVC GDKASGRHYG AVSCEGCKGF FKRSVRKNLT
160 170 180 190 200
YSCRSNQDCI INKHHRNRCQ FCRLKKCLEM GMKMESVQSE RKPFDVQREK
210 220 230 240 250
PSNCAASTEK IYIRKDLRSP LIATPTFVAD KDGARQTGLL DPGMLVNIQQ
260 270 280 290 300
PLIREDGTVL LATDSKAETS QGALGTLANV VTSLANLSES LNNGDTSEIQ
310 320 330 340 350
PEDQSASEIT RAFDTLAKAL NTTDSSSSPS LADGIDTSGG GSIHVISRDQ
360 370 380 390 400
STPIIEVEGP LLSDTHVTFK LTMPSPMPEY LNVHYICESA SRLLFLSMHW
410 420 430 440 450
ARSIPAFQAL GQDCNTSLVR ACWNELFTLG LAQCAQVMSL STILAAIVNH
460 470 480 490 500
LQNSIQEDKL SGDRIKQVME HIWKLQEFCN SMAKLDIDGY EYAYLKAIVL
510 520 530 540 550
FSPDHPGLTS TSQIEKFQEK AQMELQDYVQ KTYSEDTYRL ARILVRLPAL
560 570 580 590
RLMSSNITEE LFFTGLIGNV SIDSIIPYIL KMETAEYNGQ ITGASL
Length:596
Mass (Da):65,414
Last modified:February 1, 1996 - v1
Checksum:i5180BDC3F3C8BD79
GO
Isoform 2 (identifier: P49116-2) [UniParc]FASTAAdd to Basket

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

Show »
Length:615
Mass (Da):67,345
Checksum:i5D557E04602C1BAB
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti108 – 1081V → A in BAH02299. (PubMed:18619963)Curated
Sequence conflicti156 – 1561N → S in AAA21474. (PubMed:8016112)Curated
Sequence conflicti326 – 3261S → F in BAH02299. (PubMed:18619963)Curated
Sequence conflicti400 – 4001W → R in AAA21474. (PubMed:8016112)Curated
Sequence conflicti409 – 4091A → G in AAA21474. (PubMed:8016112)Curated
Sequence conflicti484 – 4852KL → NW in AAA21474. (PubMed:8016112)Curated
Sequence conflicti594 – 5941A → V in AAA21474. (PubMed:8016112)Curated
Sequence conflicti594 – 5941A → V in BAH02299. (PubMed:18619963)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei24 – 241Q → QGSEPASGPLSVFTSLNKEK in isoform 2. 1 PublicationVSP_039522

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS2621.1. [P49116-2]
CCDS74905.1. [P49116-1]
PIRiA57031.
I59309.
RefSeqiNP_001278623.1. NM_001291694.1. [P49116-1]
NP_003289.2. NM_003298.4. [P49116-2]
UniGeneiHs.555973.

Genome annotation databases

EnsembliENST00000323373; ENSP00000320447; ENSG00000177463. [P49116-2]
ENST00000393102; ENSP00000376814; ENSG00000177463. [P49116-1]
ENST00000406272; ENSP00000384463; ENSG00000177463. [P49116-1]
ENST00000425241; ENSP00000388387; ENSG00000177463. [P49116-1]
ENST00000617312; ENSP00000483059; ENSG00000177463. [P49116-2]
GeneIDi7182.
KEGGihsa:7182.
UCSCiuc003bzj.4. human. [P49116-1]

Polymorphism databases

DMDMi1351190.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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 .
CCDSi CCDS2621.1. [P49116-2 ]
CCDS74905.1. [P49116-1 ]
PIRi A57031.
I59309.
RefSeqi NP_001278623.1. NM_001291694.1. [P49116-1 ]
NP_003289.2. NM_003298.4. [P49116-2 ]
UniGenei Hs.555973.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3P0U X-ray 3.00 A/B 348-596 [» ]
ProteinModelPortali P49116.
SMRi P49116. Positions 117-225, 348-582.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 113034. 32 interactions.
DIPi DIP-5999N.
IntActi P49116. 4 interactions.
MINTi MINT-7004540.
STRINGi 9606.ENSP00000320447.

Chemistry

BindingDBi P49116.
ChEMBLi CHEMBL5716.
GuidetoPHARMACOLOGYi 614.

PTM databases

PhosphoSitei P49116.

Polymorphism databases

DMDMi 1351190.

Proteomic databases

MaxQBi P49116.
PaxDbi P49116.
PRIDEi P49116.

Protocols and materials databases

DNASUi 7182.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000323373 ; ENSP00000320447 ; ENSG00000177463 . [P49116-2 ]
ENST00000393102 ; ENSP00000376814 ; ENSG00000177463 . [P49116-1 ]
ENST00000406272 ; ENSP00000384463 ; ENSG00000177463 . [P49116-1 ]
ENST00000425241 ; ENSP00000388387 ; ENSG00000177463 . [P49116-1 ]
ENST00000617312 ; ENSP00000483059 ; ENSG00000177463 . [P49116-2 ]
GeneIDi 7182.
KEGGi hsa:7182.
UCSCi uc003bzj.4. human. [P49116-1 ]

Organism-specific databases

CTDi 7182.
GeneCardsi GC03P014989.
HGNCi HGNC:7972. NR2C2.
HPAi HPA006313.
MIMi 601426. gene.
neXtProti NX_P49116.
PharmGKBi PA31755.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG297520.
GeneTreei ENSGT00760000118948.
HOGENOMi HOG000013058.
HOVERGENi HBG008596.
InParanoidi P49116.
KOi K08544.
OMAi YVQKTYP.
OrthoDBi EOG7FJH0K.
PhylomeDBi P49116.
TreeFami TF316650.

Enzyme and pathway databases

Reactomei REACT_15525. Nuclear Receptor transcription pathway.
SignaLinki P49116.

Miscellaneous databases

ChiTaRSi NR2C2. human.
EvolutionaryTracei P49116.
GeneWikii Testicular_receptor_4.
GenomeRNAii 7182.
NextBioi 28158.
PROi P49116.
SOURCEi Search...

Gene expression databases

Bgeei P49116.
CleanExi HS_NR2C2.
ExpressionAtlasi P49116. baseline and differential.
Genevestigatori P49116.

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. 2 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. "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. 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. 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. Cited for: INTERACTION WITH NLRP10.

Entry informationi

Entry nameiNR2C2_HUMAN
AccessioniPrimary (citable) accession number: P49116
Secondary accession number(s): A8K3H5, B6ZGT8, P55092
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: October 29, 2014
This is version 141 of the entry and version 1 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 3
    Human chromosome 3: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3