Skip Header

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

COUP transcription factor 1

Gene

NR2F1

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

Functioni

Coup (chicken ovalbumin upstream promoter) transcription factor binds to the ovalbumin promoter and, in conjunction with another protein (S300-II) stimulates initiation of transcription. Binds to both direct repeats and palindromes of the 5'-AGGTCA-3' motif. Represses transcriptional activity of LHCG.2 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi83 – 15876Nuclear receptorPROSITE-ProRule annotationAdd
BLAST
Zinc fingeri86 – 10621NR C4-typePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri122 – 14625NR C4-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. ligand-activated sequence-specific DNA binding RNA polymerase II transcription factor activity Source: ProtInc
  2. retinoic acid-responsive element binding Source: Ensembl
  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. cerebral cortex regionalization Source: Ensembl
  2. gene expression Source: Reactome
  3. intracellular receptor signaling pathway Source: GOC
  4. negative regulation of neuron projection development Source: Ensembl
  5. negative regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  6. neuron migration Source: Ensembl
  7. positive regulation of transcription from RNA polymerase II promoter Source: Ensembl
  8. signal transduction Source: ProtInc
  9. 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.
SignaLinkiP10589.

Names & Taxonomyi

Protein namesi
Recommended name:
COUP transcription factor 1
Short name:
COUP-TF1
Alternative name(s):
COUP transcription factor I
Short name:
COUP-TF I
Nuclear receptor subfamily 2 group F member 1
V-erbA-related protein 3
Short name:
EAR-3
Gene namesi
Name:NR2F1
Synonyms:EAR3, ERBAL3, TFCOUP1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 5

Organism-specific databases

HGNCiHGNC:7975. NR2F1.

Subcellular locationi

Nucleus Curated

GO - Cellular componenti

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

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Involvement in diseasei

Bosch-Boonstra-Schaaf optic atrophy syndrome1 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionAn autosomal dominant disorder characterized by optic atrophy associated with developmental delay and intellectual disability. Most patients also have evidence of cerebral visual impairment.

See also OMIM:615722
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti112 – 1121R → K in BBSOAS; decreases transcriptional activity. 1 Publication
VAR_071319
Natural varianti113 – 1131S → R in BBSOAS; decreases transcriptional activity. 1 Publication
VAR_071320
Natural varianti115 – 1151R → P in BBSOAS; decreases transcriptional activity. 1 Publication
VAR_071321
Natural varianti252 – 2521L → P in BBSOAS; decreases transcriptional activity. 1 Publication
VAR_071322

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi615722. phenotype.
Orphaneti401777. Optic atrophy-intellectual disability syndrome.
PharmGKBiPA31758.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 423423COUP transcription factor 1PRO_0000053602Add
BLAST

Proteomic databases

MaxQBiP10589.
PaxDbiP10589.
PRIDEiP10589.

PTM databases

PhosphoSiteiP10589.

Expressioni

Inductioni

Inhibited by gonadotropin in granulosa cells.1 Publication

Gene expression databases

BgeeiP10589.
CleanExiHS_NR2F1.
ExpressionAtlasiP10589. baseline and differential.
GenevestigatoriP10589.

Organism-specific databases

HPAiCAB019281.

Interactioni

Subunit structurei

Binds DNA as dimer; homodimer and probable heterodimer with NR2F6. Interacts with COPS2.2 Publications

Protein-protein interaction databases

BioGridi112883. 20 interactions.
DIPiDIP-622N.
IntActiP10589. 1 interaction.
MINTiMINT-1514389.
STRINGi9606.ENSP00000325819.

Structurei

Secondary structure

1
423
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni87 – 893Combined sources
Beta strandi95 – 973Combined sources
Helixi104 – 11411Combined sources
Turni115 – 1173Combined sources
Beta strandi132 – 1365Combined sources
Helixi140 – 14910Combined sources
Helixi153 – 1564Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2EBLNMR-A84-159[»]
ProteinModelPortaliP10589.
SMRiP10589. Positions 82-414.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP10589.

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi32 – 365Poly-Gly

Sequence similaritiesi

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

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri86 – 10621NR C4-typePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri122 – 14625NR C4-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiNOG327099.
GeneTreeiENSGT00760000118948.
HOGENOMiHOG000260820.
HOVERGENiHBG005606.
InParanoidiP10589.
KOiK08547.
OMAiGHTYLSS.
OrthoDBiEOG72RMZ5.
PhylomeDBiP10589.
TreeFamiTF352097.

Family and domain databases

Gene3Di1.10.565.10. 1 hit.
3.30.50.10. 1 hit.
InterProiIPR003068. COUP_TF.
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]
PfamiPF00104. Hormone_recep. 1 hit.
PF00105. zf-C4. 1 hit.
[Graphical view]
PRINTSiPR01282. COUPTNFACTOR.
PR00398. STRDHORMONER.
PR00047. STROIDFINGER.
SMARTiSM00430. HOLI. 1 hit.
SM00399. ZnF_C4. 1 hit.
[Graphical view]
SUPFAMiSSF48508. SSF48508. 1 hit.
PROSITEiPS00031. NUCLEAR_REC_DBD_1. 1 hit.
PS51030. NUCLEAR_REC_DBD_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P10589-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAMVVSSWRD PQDDVAGGNP GGPNPAAQAA RGGGGGAGEQ QQQAGSGAPH
60 70 80 90 100
TPQTPGQPGA PATPGTAGDK GQGPPGSGQS QQHIECVVCG DKSSGKHYGQ
110 120 130 140 150
FTCEGCKSFF KRSVRRNLTY TCRANRNCPI DQHHRNQCQY CRLKKCLKVG
160 170 180 190 200
MRREAVQRGR MPPTQPNPGQ YALTNGDPLN GHCYLSGYIS LLLRAEPYPT
210 220 230 240 250
SRYGSQCMQP NNIMGIENIC ELAARLLFSA VEWARNIPFF PDLQITDQVS
260 270 280 290 300
LLRLTWSELF VLNAAQCSMP LHVAPLLAAA GLHASPMSAD RVVAFMDHIR
310 320 330 340 350
IFQEQVEKLK ALHVDSAEYS CLKAIVLFTS DACGLSDAAH IESLQEKSQC
360 370 380 390 400
ALEEYVRSQY PNQPSRFGKL LLRLPSLRTV SSSVIEQLFF VRLVGKTPIE
410 420
TLIRDMLLSG SSFNWPYMSI QCS
Length:423
Mass (Da):46,156
Last modified:July 1, 1989 - v1
Checksum:i6EE634BE96242731
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti112 – 1121R → K in BBSOAS; decreases transcriptional activity. 1 Publication
VAR_071319
Natural varianti113 – 1131S → R in BBSOAS; decreases transcriptional activity. 1 Publication
VAR_071320
Natural varianti115 – 1151R → P in BBSOAS; decreases transcriptional activity. 1 Publication
VAR_071321
Natural varianti252 – 2521L → P in BBSOAS; decreases transcriptional activity. 1 Publication
VAR_071322

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X16155 mRNA. Translation: CAA34277.1.
X12795 Genomic DNA. Translation: CAA31283.1.
BC004154 mRNA. Translation: AAH04154.1.
BC017493 mRNA. Translation: AAH17493.1.
CCDSiCCDS4068.1.
PIRiS02710.
RefSeqiNP_005645.1. NM_005654.5.
UniGeneiHs.519445.

Genome annotation databases

EnsembliENST00000327111; ENSP00000325819; ENSG00000175745.
GeneIDi7025.
KEGGihsa:7025.
UCSCiuc003kkj.3. human.

Polymorphism databases

DMDMi116959.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X16155 mRNA. Translation: CAA34277.1.
X12795 Genomic DNA. Translation: CAA31283.1.
BC004154 mRNA. Translation: AAH04154.1.
BC017493 mRNA. Translation: AAH17493.1.
CCDSiCCDS4068.1.
PIRiS02710.
RefSeqiNP_005645.1. NM_005654.5.
UniGeneiHs.519445.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2EBLNMR-A84-159[»]
ProteinModelPortaliP10589.
SMRiP10589. Positions 82-414.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112883. 20 interactions.
DIPiDIP-622N.
IntActiP10589. 1 interaction.
MINTiMINT-1514389.
STRINGi9606.ENSP00000325819.

Chemistry

BindingDBiP10589.
ChEMBLiCHEMBL1961789.

PTM databases

PhosphoSiteiP10589.

Polymorphism databases

DMDMi116959.

Proteomic databases

MaxQBiP10589.
PaxDbiP10589.
PRIDEiP10589.

Protocols and materials databases

DNASUi7025.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000327111; ENSP00000325819; ENSG00000175745.
GeneIDi7025.
KEGGihsa:7025.
UCSCiuc003kkj.3. human.

Organism-specific databases

CTDi7025.
GeneCardsiGC05P092920.
HGNCiHGNC:7975. NR2F1.
HPAiCAB019281.
MIMi132890. gene.
615722. phenotype.
neXtProtiNX_P10589.
Orphaneti401777. Optic atrophy-intellectual disability syndrome.
PharmGKBiPA31758.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG327099.
GeneTreeiENSGT00760000118948.
HOGENOMiHOG000260820.
HOVERGENiHBG005606.
InParanoidiP10589.
KOiK08547.
OMAiGHTYLSS.
OrthoDBiEOG72RMZ5.
PhylomeDBiP10589.
TreeFamiTF352097.

Enzyme and pathway databases

ReactomeiREACT_15525. Nuclear Receptor transcription pathway.
SignaLinkiP10589.

Miscellaneous databases

ChiTaRSiNR2F1. human.
EvolutionaryTraceiP10589.
GeneWikiiCOUP-TFI.
GenomeRNAii7025.
NextBioi27447.
PROiP10589.
SOURCEiSearch...

Gene expression databases

BgeeiP10589.
CleanExiHS_NR2F1.
ExpressionAtlasiP10589. baseline and differential.
GenevestigatoriP10589.

Family and domain databases

Gene3Di1.10.565.10. 1 hit.
3.30.50.10. 1 hit.
InterProiIPR003068. COUP_TF.
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]
PfamiPF00104. Hormone_recep. 1 hit.
PF00105. zf-C4. 1 hit.
[Graphical view]
PRINTSiPR01282. COUPTNFACTOR.
PR00398. STRDHORMONER.
PR00047. STROIDFINGER.
SMARTiSM00430. HOLI. 1 hit.
SM00399. ZnF_C4. 1 hit.
[Graphical view]
SUPFAMiSSF48508. SSF48508. 1 hit.
PROSITEiPS00031. NUCLEAR_REC_DBD_1. 1 hit.
PS51030. NUCLEAR_REC_DBD_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "COUP transcription factor is a member of the steroid receptor superfamily."
    Wang L.-H., Tsai S.Y., Cook R.G., Beattie W.G., Tsai M.-J., O'Malley B.W.
    Nature 340:163-166(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 6-423, PARTIAL PROTEIN SEQUENCE.
  2. "Identification of two novel members of erbA superfamily by molecular cloning: the gene products of the two are highly related to each other."
    Miyajima N., Kadowaki Y., Fukushige S., Shimizu S., Semba K., Yamanashi Y., Matsubara K., Toyoshima K., Yamamoto T.
    Nucleic Acids Res. 16:11057-11074(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Tissue: Lung.
  3. "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].
    Tissue: Lung and Uterus.
  4. "Alien, a highly conserved protein with characteristics of a corepressor for members of the nuclear hormone receptor superfamily."
    Dressel U., Thormeyer D., Altincicek B., Paululat A., Eggert M., Schneider S., Tenbaum S.P., Renkawitz R., Baniahmad A.
    Mol. Cell. Biol. 19:3383-3394(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH COPS2.
  5. "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.
  6. "EAR2 and EAR3/COUP-TFI regulate transcription of the rat LH receptor."
    Zhang Y., Dufau M.L.
    Mol. Endocrinol. 15:1891-1905(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBUNIT, INDUCTION BY GONADOTROPIN.
  7. "Solution structure of the zinc finger, C4-type domain of human COUP transcription factor 1."
    RIKEN structural genomics initiative (RSGI)
    Submitted (FEB-2008) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 84-162.
  8. Cited for: INVOLVEMENT IN BBSOAS, VARIANTS BBSOAS LYS-112; ARG-113; PRO-115 AND PRO-252, CHARACTERIZATION OF VARIANTS BBSOAS LYS-112; ARG-113; PRO-115 AND PRO-252.

Entry informationi

Entry nameiCOT1_HUMAN
AccessioniPrimary (citable) accession number: P10589
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: January 7, 2015
This is version 159 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, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 5
    Human chromosome 5: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.