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Protein

COUP transcription factor 2

Gene

NR2F2

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

Functioni

Ligand-activated transcription factor. Activated by high concentrations of 9-cis-retinoic acid and all-trans-retinoic acid, but not by dexamethasone, cortisol or progesterone (in vitro). Regulation of the apolipoprotein A-I gene transcription. Binds to DNA site A.3 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi76 – 15176Nuclear receptorPROSITE-ProRule annotationAdd
BLAST
Zinc fingeri79 – 9921NR C4-typePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri115 – 13925NR C4-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  • ligand-activated sequence-specific DNA binding RNA polymerase II transcription factor activity Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB
  • retinoic acid binding Source: UniProtKB
  • sequence-specific DNA binding Source: UniProtKB
  • sequence-specific DNA binding transcription factor activity Source: UniProtKB
  • steroid hormone receptor activity Source: InterPro
  • transcription corepressor activity Source: ProtInc
  • zinc ion binding Source: InterPro

GO - Biological processi

  • anterior/posterior pattern specification Source: Ensembl
  • blood vessel morphogenesis Source: Ensembl
  • fertilization Source: Ensembl
  • forebrain development Source: Ensembl
  • intracellular receptor signaling pathway Source: GOC
  • limb development Source: Ensembl
  • lipid metabolic process Source: ProtInc
  • maternal placenta development Source: Ensembl
  • negative regulation of cyclin-dependent protein serine/threonine kinase activity Source: BHF-UCL
  • negative regulation of endothelial cell migration Source: BHF-UCL
  • negative regulation of endothelial cell proliferation Source: BHF-UCL
  • negative regulation of transcription, DNA-templated Source: BHF-UCL
  • negative regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  • neuron migration Source: Ensembl
  • placenta blood vessel development Source: Ensembl
  • positive regulation of transcription, DNA-templated Source: UniProtKB
  • radial pattern formation Source: Ensembl
  • regulation of transcription from RNA polymerase II promoter Source: ProtInc
  • regulation of transcription involved in lymphatic endothelial cell fate commitment Source: BHF-UCL
  • response to estradiol Source: Ensembl
  • signal transduction Source: ProtInc
  • skeletal muscle tissue development Source: Ensembl
  • transcription, DNA-templated Source: UniProtKB-KW
  • trophoblast giant cell differentiation Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Activator, Receptor

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding, Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_27161. Transcriptional regulation of white adipocyte differentiation.
SignaLinkiP24468.

Names & Taxonomyi

Protein namesi
Recommended name:
COUP transcription factor 2
Short name:
COUP-TF2
Alternative name(s):
Apolipoprotein A-I regulatory protein 1
Short name:
ARP-1
COUP transcription factor II
Short name:
COUP-TF II
Nuclear receptor subfamily 2 group F member 2
Gene namesi
Name:NR2F2
Synonyms:ARP1, TFCOUP2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 15

Organism-specific databases

HGNCiHGNC:7976. NR2F2.

Subcellular locationi

GO - Cellular componenti

  • nucleus Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Involvement in diseasei

Congenital heart defects, multiple types, 4 (CHTD4)1 Publication

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

Disease descriptionA disorder characterized by congenital developmental abnormalities involving structures of the heart. Common defects include transposition of the great arteries, aortic stenosis, atrial septal defect, ventricular septal defect, pulmonic stenosis, and patent ductus arteriosus. Some patients also have cardiac arrhythmias, which may be due to the anatomic defect itself or to surgical interventions.

See also OMIM:615779
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti75 – 751Q → QQ in CHTD4; the mutation results in reduced transcription activation of the EGR1 promoter; does not affect transcription activation of the APOB FT promoter. 1 Publication
VAR_071766
Natural varianti170 – 1701D → V in CHTD4. 1 Publication
VAR_071767
Natural varianti205 – 2051N → I in CHTD4; the mutation results in increased transcription activation of the EGR1 promoter; transcription activation of the APOB promoter is decreased. 1 Publication
VAR_071768
Natural varianti251 – 2511E → D in CHTD4. 1 Publication
VAR_071769
Natural varianti341 – 3411S → Y in CHTD4; the mutation results in reduced transcriptional activity. 1 Publication
VAR_071770
Natural varianti412 – 4121A → S in CHTD4. 1 Publication
VAR_071771

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi228 – 2281R → E: Reduces transcription activation by 40%; when associated with R-398. 1 Publication
Mutagenesisi249 – 2491W → A: Reduces transcription activation by 50%; when associated with A-250. 1 Publication
Mutagenesisi250 – 2501S → A: Reduces transcription activation by 50%; when associated with A-249. 1 Publication
Mutagenesisi250 – 2501S → W: Reduces transcription activation by 50%. 1 Publication
Mutagenesisi253 – 2542FV → AA: Reduces transcription activation by 50%. 1 Publication
Mutagenesisi269 – 2702LL → AA: Reduces transcription activation by 50%.
Mutagenesisi364 – 3652LL → AA: Reduces transcription activation by 80%. 1 Publication
Mutagenesisi398 – 3981D → R: Reduces transcription activation by 40%; when associated with E-228. 1 Publication

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi615779. phenotype.
Orphaneti1329. Complete atrioventricular canal.
1330. Partial atrioventricular canal.
PharmGKBiPA31759.

Polymorphism and mutation databases

BioMutaiNR2F2.
DMDMi114203.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 414414COUP transcription factor 2PRO_0000053606Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei51 – 511Phosphothreonine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP24468.
PaxDbiP24468.
PRIDEiP24468.

PTM databases

PhosphoSiteiP24468.

Expressioni

Tissue specificityi

Ubiquitous.

Gene expression databases

BgeeiP24468.
CleanExiHS_NR2F2.
ExpressionAtlasiP24468. baseline and differential.
GenevisibleiP24468. HS.

Interactioni

Subunit structurei

Interacts with SQSTM1 (By similarity). Binds DNA as a dimer; homodimer or heterodimer with NR2F6. Interacts with NCOA1, NCOA2, NCOA3 and PPARGC1A. Interacts with ZFPM2 (By similarity).By similarity

Protein-protein interaction databases

BioGridi112884. 44 interactions.
DIPiDIP-29713N.
IntActiP24468. 10 interactions.
MINTiMINT-1183332.
STRINGi9606.ENSP00000377721.

Structurei

Secondary structure

1
414
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi175 – 18713Combined sources
Helixi212 – 22918Combined sources
Beta strandi230 – 2323Combined sources
Helixi233 – 2353Combined sources
Helixi238 – 26023Combined sources
Helixi290 – 30415Combined sources
Helixi309 – 32012Combined sources
Helixi331 – 35222Combined sources
Helixi359 – 3646Combined sources
Helixi367 – 3726Combined sources
Helixi375 – 3828Combined sources
Helixi384 – 3874Combined sources
Helixi392 – 3943Combined sources
Helixi396 – 4005Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3CJWX-ray1.48A175-414[»]
ProteinModelPortaliP24468.
SMRiP24468. Positions 75-407.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP24468.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni117 – 414298Interaction with ZFPM2By similarityAdd
BLAST
Regioni183 – 414232Ligand-bindingBy similarityAdd
BLAST
Regioni337 – 41478Important for dimerizationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi71 – 755Poly-Gln

Sequence similaritiesi

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

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri79 – 9921NR C4-typePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri115 – 13925NR C4-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiNOG327099.
GeneTreeiENSGT00760000118948.
HOGENOMiHOG000260820.
HOVERGENiHBG005606.
InParanoidiP24468.
KOiK08548.
OMAiGPPNNTQ.
OrthoDBiEOG72RMZ5.
PhylomeDBiP24468.
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]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P24468-1) [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
MAMVVSTWRD PQDEVPGSQG SQASQAPPVP GPPPGAPHTP QTPGQGGPAS
60 70 80 90 100
TPAQTAAGGQ GGPGGPGSDK QQQQQHIECV VCGDKSSGKH YGQFTCEGCK
110 120 130 140 150
SFFKRSVRRN LSYTCRANRN CPIDQHHRNQ CQYCRLKKCL KVGMRREAVQ
160 170 180 190 200
RGRMPPTQPT HGQFALTNGD PLNCHSYLSG YISLLLRAEP YPTSRFGSQC
210 220 230 240 250
MQPNNIMGIE NICELAARML FSAVEWARNI PFFPDLQITD QVALLRLTWS
260 270 280 290 300
ELFVLNAAQC SMPLHVAPLL AAAGLHASPM SADRVVAFMD HIRIFQEQVE
310 320 330 340 350
KLKALHVDSA EYSCLKAIVL FTSDACGLSD VAHVESLQEK SQCALEEYVR
360 370 380 390 400
SQYPNQPTRF GKLLLRLPSL RTVSSSVIEQ LFFVRLVGKT PIETLIRDML
410
LSGSSFNWPY MAIQ
Length:414
Mass (Da):45,571
Last modified:March 1, 1992 - v1
Checksum:iC24CB2E8C8A27E8C
GO
Isoform 2 (identifier: P24468-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-147: MAMVVSTWRD...KCLKVGMRRE → MQAVWDLEQGKYGF

Show »
Length:281
Mass (Da):31,484
Checksum:i038DD27B80868BB5
GO
Isoform 3 (identifier: P24468-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-153: Missing.

Show »
Length:261
Mass (Da):29,163
Checksum:i5526AD057E2A639E
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti75 – 751Q → QQ in CHTD4; the mutation results in reduced transcription activation of the EGR1 promoter; does not affect transcription activation of the APOB FT promoter. 1 Publication
VAR_071766
Natural varianti170 – 1701D → V in CHTD4. 1 Publication
VAR_071767
Natural varianti205 – 2051N → I in CHTD4; the mutation results in increased transcription activation of the EGR1 promoter; transcription activation of the APOB promoter is decreased. 1 Publication
VAR_071768
Natural varianti251 – 2511E → D in CHTD4. 1 Publication
VAR_071769
Natural varianti341 – 3411S → Y in CHTD4; the mutation results in reduced transcriptional activity. 1 Publication
VAR_071770
Natural varianti412 – 4121A → S in CHTD4. 1 Publication
VAR_071771

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 153153Missing in isoform 3. 2 PublicationsVSP_043897Add
BLAST
Alternative sequencei1 – 147147MAMVV…GMRRE → MQAVWDLEQGKYGF in isoform 2. 4 PublicationsVSP_042630Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M64497 mRNA. Translation: AAA86429.1.
U60477 Genomic DNA. Translation: AAB09475.1.
AB307711 mRNA. Translation: BAH02302.1.
FM208183 mRNA. Translation: CAR63888.1.
AK298824 mRNA. Translation: BAG60954.1.
AK301595 mRNA. Translation: BAG63083.1.
AK316086 mRNA. Translation: BAH14457.1.
HQ692849 mRNA. Translation: ADZ17360.1.
HQ692850 mRNA. Translation: ADZ17361.1.
AC016251 Genomic DNA. No translation available.
CH471101 Genomic DNA. Translation: EAX02195.1.
CH471101 Genomic DNA. Translation: EAX02196.1.
CH471101 Genomic DNA. Translation: EAX02197.1.
BC014664 mRNA. Translation: AAH14664.1.
BC042897 mRNA. Translation: AAH42897.1.
BC106083 mRNA. Translation: AAI06084.1.
M62760 mRNA. Translation: AAA21479.1.
CCDSiCCDS10375.1. [P24468-1]
CCDS45358.1. [P24468-2]
CCDS45359.1. [P24468-3]
PIRiA37133.
RefSeqiNP_001138627.1. NM_001145155.1. [P24468-2]
NP_001138628.1. NM_001145156.1. [P24468-3]
NP_001138629.1. NM_001145157.1. [P24468-3]
NP_066285.1. NM_021005.3. [P24468-1]
UniGeneiHs.347991.

Genome annotation databases

EnsembliENST00000394166; ENSP00000377721; ENSG00000185551.
ENST00000394171; ENSP00000377726; ENSG00000185551. [P24468-3]
ENST00000421109; ENSP00000401674; ENSG00000185551. [P24468-2]
ENST00000453270; ENSP00000389853; ENSG00000185551. [P24468-3]
GeneIDi7026.
KEGGihsa:7026.
UCSCiuc002btp.3. human. [P24468-2]
uc010uri.2. human. [P24468-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M64497 mRNA. Translation: AAA86429.1.
U60477 Genomic DNA. Translation: AAB09475.1.
AB307711 mRNA. Translation: BAH02302.1.
FM208183 mRNA. Translation: CAR63888.1.
AK298824 mRNA. Translation: BAG60954.1.
AK301595 mRNA. Translation: BAG63083.1.
AK316086 mRNA. Translation: BAH14457.1.
HQ692849 mRNA. Translation: ADZ17360.1.
HQ692850 mRNA. Translation: ADZ17361.1.
AC016251 Genomic DNA. No translation available.
CH471101 Genomic DNA. Translation: EAX02195.1.
CH471101 Genomic DNA. Translation: EAX02196.1.
CH471101 Genomic DNA. Translation: EAX02197.1.
BC014664 mRNA. Translation: AAH14664.1.
BC042897 mRNA. Translation: AAH42897.1.
BC106083 mRNA. Translation: AAI06084.1.
M62760 mRNA. Translation: AAA21479.1.
CCDSiCCDS10375.1. [P24468-1]
CCDS45358.1. [P24468-2]
CCDS45359.1. [P24468-3]
PIRiA37133.
RefSeqiNP_001138627.1. NM_001145155.1. [P24468-2]
NP_001138628.1. NM_001145156.1. [P24468-3]
NP_001138629.1. NM_001145157.1. [P24468-3]
NP_066285.1. NM_021005.3. [P24468-1]
UniGeneiHs.347991.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3CJWX-ray1.48A175-414[»]
ProteinModelPortaliP24468.
SMRiP24468. Positions 75-407.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112884. 44 interactions.
DIPiDIP-29713N.
IntActiP24468. 10 interactions.
MINTiMINT-1183332.
STRINGi9606.ENSP00000377721.

Chemistry

BindingDBiP24468.
ChEMBLiCHEMBL1961790.

PTM databases

PhosphoSiteiP24468.

Polymorphism and mutation databases

BioMutaiNR2F2.
DMDMi114203.

Proteomic databases

MaxQBiP24468.
PaxDbiP24468.
PRIDEiP24468.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000394166; ENSP00000377721; ENSG00000185551.
ENST00000394171; ENSP00000377726; ENSG00000185551. [P24468-3]
ENST00000421109; ENSP00000401674; ENSG00000185551. [P24468-2]
ENST00000453270; ENSP00000389853; ENSG00000185551. [P24468-3]
GeneIDi7026.
KEGGihsa:7026.
UCSCiuc002btp.3. human. [P24468-2]
uc010uri.2. human. [P24468-1]

Organism-specific databases

CTDi7026.
GeneCardsiGC15P096869.
HGNCiHGNC:7976. NR2F2.
MIMi107773. gene.
615779. phenotype.
neXtProtiNX_P24468.
Orphaneti1329. Complete atrioventricular canal.
1330. Partial atrioventricular canal.
PharmGKBiPA31759.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG327099.
GeneTreeiENSGT00760000118948.
HOGENOMiHOG000260820.
HOVERGENiHBG005606.
InParanoidiP24468.
KOiK08548.
OMAiGPPNNTQ.
OrthoDBiEOG72RMZ5.
PhylomeDBiP24468.
TreeFamiTF352097.

Enzyme and pathway databases

ReactomeiREACT_27161. Transcriptional regulation of white adipocyte differentiation.
SignaLinkiP24468.

Miscellaneous databases

ChiTaRSiNR2F2. human.
EvolutionaryTraceiP24468.
GeneWikiiCOUP-TFII.
GenomeRNAii7026.
NextBioi27451.
PROiP24468.
SOURCEiSearch...

Gene expression databases

BgeeiP24468.
CleanExiHS_NR2F2.
ExpressionAtlasiP24468. baseline and differential.
GenevisibleiP24468. HS.

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. "Regulation of the apolipoprotein AI gene by ARP-1, a novel member of the steroid receptor superfamily."
    Ladias J.A.A., Karathanasis S.K.
    Science 251:561-565(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBUNIT.
  2. Speckmayer R.W.M., Paulweber B., Sandhofer F.
    Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  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.
  4. "Characterisation of a new, DNA binding domain deficient chicken ovalbumin upstream promoter- transcription factor IIdelta isoform in the human brain."
    Schote A.B., Bechet T., Pirrotte P., Turner J.D., Muller C.P.
    Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    Tissue: Liver.
  5. "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] (ISOFORMS 2 AND 3).
    Tissue: Mammary gland.
  6. "Isolation of cDNA coding for multiple human nuclear receptor clones."
    Kaighin V.A., Martin A.L., Aronstam R.S.
    Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
    Tissue: Kidney.
  7. "Analysis of the DNA sequence and duplication history of human chromosome 15."
    Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K., Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N., Abouelleil A.
    , Arachchi H.M., Baradarani L., Birditt B., Bloom S., Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K., DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.
    Nature 440:671-675(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  9. "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] (ISOFORMS 1 AND 2).
    Tissue: Brain, Kidney and Spleen.
  10. "The COUP-TFs compose a family of functionally related transcription factors."
    Wang L.H., Ing N.H., Tsai S.Y., O'Malley B.W., Tsai M.J.
    Gene Expr. 1:207-216(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-351 (ISOFORM 1).
  11. "The nuclear orphan receptors COUP-TFII and Ear-2 act as silencers of the human oxytocin gene promoter."
    Chu K., Zingg H.H.
    J. Mol. Endocrinol. 19:163-172(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  12. "Heterodimeric interactions between chicken ovalbumin upstream promoter-transcription factor family members ARP1 and ear2."
    Avram D., Ishmael J.E., Nevrivy D.J., Peterson V.J., Lee S.H., Dowell P., Leid M.
    J. Biol. Chem. 274:14331-14336(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT, INTERACTION WITH NR2F6.
  13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-51, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  15. "Identification of COUP-TFII orphan nuclear receptor as a retinoic acid-activated receptor."
    Kruse S.W., Suino-Powell K., Zhou X.E., Kretschman J.E., Reynolds R., Vonrhein C., Xu Y., Wang L., Tsai S.Y., Tsai M.J., Xu H.E.
    PLoS Biol. 6:E227-E227(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.48 ANGSTROMS) OF 175-414, FUNCTION, SUBUNIT, INTERACTION WITH NCOA1; NCOA2; NCOA3 AND PPARGC1A, MUTAGENESIS OF ARG-228; TRP-249; SER-250; 253-PHE-VAL-254; 260-LEU-LEU-270; 364-LEU-LEU-365 AND ASP-398.
  16. Cited for: VARIANTS CHTD4 GLN-75 INS; VAL-170; ILE-205; ASP-251; TYR-341 AND SER-412, CHARACTERIZATION OF VARIANTS CHTD4 GLN-75 INS; ILE-205 AND TYR-341.

Entry informationi

Entry nameiCOT2_HUMAN
AccessioniPrimary (citable) accession number: P24468
Secondary accession number(s): B4DQJ2
, B6ZGU1, Q03754, Q3KQR7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 1, 1992
Last sequence update: March 1, 1992
Last modified: July 22, 2015
This is version 160 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 15
    Human chromosome 15: 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.