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O00482 (NR5A2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 145. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Nuclear receptor subfamily 5 group A member 2
Alternative name(s):
Alpha-1-fetoprotein transcription factor
B1-binding factor
Short name=hB1F
CYP7A promoter-binding factor
Hepatocytic transcription factor
Liver receptor homolog 1
Short name=LRH-1
Gene names
Name:NR5A2
Synonyms:B1F, CPF, FTF
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length541 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Binds to the sequence element 5'-AACGACCGACCTTGAG-3' of the enhancer II of hepatitis B virus genes, a critical cis-element of their expression and regulation. May be responsible for the liver-specific activity of enhancer II, probably in combination with other hepatocyte transcription factors. Key regulator of cholesterol 7-alpha-hydroxylase gene (CYP7A) expression in liver. May also contribute to the regulation of pancreas-specific genes and play important roles in embryonic development.

Subunit structure

Binds DNA as a monomer By similarity. Interacts with GRIP1, NCOA2 and NR0B2.

Subcellular location

Nucleus Probable.

Tissue specificity

Abundantly expressed in pancreas, less in liver, very low levels in heart and lung. Expressed in the Hep-G2 cell line. Isoform 1 and isoform 2 seem to be present in fetal and adult liver and Hep-G2 cells.

Sequence similarities

Belongs to the nuclear hormone receptor family. NR5 subfamily.

Contains 1 nuclear receptor DNA-binding domain.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
   DomainZinc-finger
   LigandDNA-binding
Lipid-binding
Metal-binding
Zinc
   Molecular functionReceptor
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processbile acid metabolic process

Inferred from electronic annotation. Source: Ensembl

cholesterol homeostasis

Inferred from electronic annotation. Source: Ensembl

embryo development

Traceable author statement Ref.11. Source: UniProtKB

endocrine pancreas development

Traceable author statement. Source: Reactome

gene expression

Traceable author statement. Source: Reactome

homeostatic process

Non-traceable author statement Ref.11. Source: UniProtKB

intracellular receptor signaling pathway

Traceable author statement PubMed 16271724. Source: GOC

positive regulation of transcription from RNA polymerase II promoter

Inferred from electronic annotation. Source: Ensembl

positive regulation of transcription, DNA-templated

Inferred from direct assay PubMed 15143342. Source: BHF-UCL

positive regulation of viral genome replication

Inferred from direct assay PubMed 19264593. Source: BHF-UCL

regulation of cell proliferation

Inferred from electronic annotation. Source: Ensembl

regulation of transcription, DNA-templated

Inferred from direct assay Ref.12. Source: UniProtKB

transcription initiation from RNA polymerase II promoter

Traceable author statement. Source: Reactome

   Cellular_componentcytoplasm

Inferred from direct assay PubMed 15205472. Source: BHF-UCL

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay PubMed 15143342PubMed 15205472. Source: BHF-UCL

   Molecular_functionDNA binding

Inferred from direct assay Ref.11. Source: UniProtKB

RNA polymerase II distal enhancer sequence-specific DNA binding transcription factor activity

Traceable author statement Ref.1. Source: ProtInc

ligand-activated sequence-specific DNA binding RNA polymerase II transcription factor activity

Traceable author statement PubMed 16271724. Source: UniProtKB

phospholipid binding

Inferred from direct assay Ref.12. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 12040021PubMed 14701856PubMed 17664281. Source: UniProtKB

sequence-specific DNA binding

Inferred from direct assay Ref.11. Source: UniProtKB

sequence-specific DNA binding transcription factor activity

Inferred from direct assay Ref.12Ref.11. Source: UniProtKB

steroid hormone receptor activity

Inferred from electronic annotation. Source: InterPro

transcription regulatory region DNA binding

Inferred from direct assay PubMed 15205472. Source: BHF-UCL

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

EDF1O608692EBI-781320,EBI-781301

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 2 (identifier: O00482-1)

Also known as: B1F2;

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.
Isoform 1 (identifier: O00482-2)

The sequence of this isoform differs from the canonical sequence as follows:
     22-67: Missing.
Isoform 3 (identifier: O00482-3)

The sequence of this isoform differs from the canonical sequence as follows:
     199-370: Missing.
Note: Does not induce CYP7A promoter activity.
Isoform 4 (identifier: O00482-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-72: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 541541Nuclear receptor subfamily 5 group A member 2
PRO_0000053735

Regions

DNA binding83 – 15472Nuclear receptor
Zinc finger86 – 10621NR C4-type
Zinc finger122 – 14625NR C4-type
Region342 – 39049Ligand-binding
Region419 – 4246Lipid binding
Motif155 – 18430FTZ-F1 box

Sites

Binding site5161Lipid headgroup
Binding site5201Lipid headgroup

Natural variations

Alternative sequence1 – 7272Missing in isoform 4.
VSP_054548
Alternative sequence22 – 6746Missing in isoform 1.
VSP_003716
Alternative sequence199 – 370172Missing in isoform 3.
VSP_003717

Experimental info

Mutagenesis961Y → A: Slightly reduced DNA binding. Strongly reduced transactivation; when associated with A-168 and A-172. Ref.11
Mutagenesis1681F → A: Slightly reduced DNA binding. Strongly reduced transactivation; when associated with A-96 and A-172. Ref.11
Mutagenesis169 – 1702GP → VA: Reduced DNA binding. Loss of transactivation.
Mutagenesis1721Y → A: Slightly reduced DNA binding. Strongly reduced transactivation; when associated with A-96 and A-168. Ref.11
Mutagenesis3421F → W: Reduced phospholipid binding. Strongly reduced transactivation; when associated with W-416. Ref.12
Mutagenesis4161I → W: Reduced phospholipid binding. Strongly reduced transactivation; when associated with W-342. Ref.12
Sequence conflict250 – 2512PP → L in AAD03155. Ref.9
Sequence conflict3531L → V in AAD03155. Ref.9

Secondary structure

............................................... 541
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 2 (B1F2) [UniParc].

Last modified May 30, 2000. Version 2.
Checksum: 7B07170C075490FE

FASTA54161,331
        10         20         30         40         50         60 
MSSNSDTGDL QESLKHGLTP IGAGLPDRHG SPIPARGRLV MLPKVETEAL GLARSHGEQG 

        70         80         90        100        110        120 
QMPENMQVSQ FKMVNYSYDE DLEELCPVCG DKVSGYHYGL LTCESCKGFF KRTVQNNKRY 

       130        140        150        160        170        180 
TCIENQNCQI DKTQRKRCPY CRFQKCLSVG MKLEAVRADR MRGGRNKFGP MYKRDRALKQ 

       190        200        210        220        230        240 
QKKALIRANG LKLEAMSQVI QAMPSDLTIS SAIQNIHSAS KGLPLNHAAL PPTDYDRSPF 

       250        260        270        280        290        300 
VTSPISMTMP PHGSLQGYQT YGHFPSRAIK SEYPDPYTSS PESIMGYSYM DSYQTSSPAS 

       310        320        330        340        350        360 
IPHLILELLK CEPDEPQVQA KIMAYLQQEQ ANRSKHEKLS TFGLMCKMAD QTLFSIVEWA 

       370        380        390        400        410        420 
RSSIFFRELK VDDQMKLLQN CWSELLILDH IYRQVVHGKE GSIFLVTGQQ VDYSIIASQA 

       430        440        450        460        470        480 
GATLNNLMSH AQELVAKLRS LQFDQREFVC LKFLVLFSLD VKNLENFQLV EGVQEQVNAA 

       490        500        510        520        530        540 
LLDYTMCNYP QQTEKFGQLL LRLPEIRAIS MQAEEYLYYK HLNGDVPYNN LLIEMLHAKR 


A 

« Hide

Isoform 1 [UniParc].

Checksum: E73E60DCE9880855
Show »

FASTA49556,459
Isoform 3 [UniParc].

Checksum: 1357C2AAEFB4E46B
Show »

FASTA36942,102
Isoform 4 [UniParc].

Checksum: 49F21C2F09CF0AB4
Show »

FASTA46953,657

References

« Hide 'large scale' references
[1]"Cloning and characterization of a novel human hepatocyte transcription factor, hB1F, which binds and activates enhancer II of hepatitis B virus."
Li M., Xie Y.-H., Kong Y.-Y., Wu X., Zhu L., Wang Y.
J. Biol. Chem. 273:29022-29031(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), ALTERNATIVE SPLICING.
Tissue: Liver.
[2]Li M., Xie Y.-H., Wang Y.
Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
Tissue: Hepatoma.
[3]"CPF: an orphan nuclear receptor that regulates liver-specific expression of the human cholesterol 7alpha-hydroxylase gene."
Nitta M., Ku S., Brown C., Okamoto A.Y., Shan B.
Proc. Natl. Acad. Sci. U.S.A. 96:6660-6665(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3).
Tissue: Liver.
[4]"Characterization of the genomic structure and tissue-specific promoter of the human nuclear receptor NR5A2 (hB1F) gene."
Zhang C.K., Lin W., Cai Y.N., Xu P.L., Dong H., Li M., Kong Y.Y., Fu G., Xie Y.H., Huang G.M., Wang Y.
Gene 273:239-249(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING.
[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. expand/collapse author list , 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 4).
Tissue: Trachea.
[6]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]"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 1).
[9]"Assignment of the fetoprotein transcription factor gene (FTF) to human chromosome band 1q32.11 by in situ hybridization."
Galarneau L., Drouin R., Belanger L.
Cytogenet. Cell Genet. 82:269-270(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 41-541.
[10]"Structural analyses reveal phosphatidyl inositols as ligands for the NR5 orphan receptors SF-1 and LRH-1."
Krylova I.N., Sablin E.P., Moore J., Xu R.X., Waitt G.M., MacKay J.A., Juzumiene D., Bynum J.M., Madauss K., Montana V., Lebedeva L., Suzawa M., Williams J.D., Williams S.P., Guy R.K., Thornton J.W., Fletterick R.J., Willson T.M., Ingraham H.A.
Cell 120:343-355(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 300-541 IN COMPLEX WITH NCOA2 AND PHOSPHOLIPIDS.
[11]"Crystal structure of the human LRH-1 DBD-DNA complex reveals Ftz-F1 domain positioning is required for receptor activity."
Solomon I.H., Hager J.M., Safi R., McDonnell D.P., Redinbo M.R., Ortlund E.A.
J. Mol. Biol. 354:1091-1102(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 79-187 IN COMPLEX WITH DNA, MUTAGENESIS OF TYR-96; PHE-168; 169-GLY-PRO-170 AND TYR-172.
[12]"Modulation of human nuclear receptor LRH-1 activity by phospholipids and SHP."
Ortlund E.A., Lee Y., Solomon I.H., Hager J.M., Safi R., Choi Y., Guan Z., Tripathy A., Raetz C.R.H., McDonnell D.P., Moore D.D., Redinbo M.R.
Nat. Struct. Mol. Biol. 12:357-363(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 290-541 IN COMPLEX WITH NR0B2 AND PHOSPHOLIPID, MUTAGENESIS OF PHE-342 AND ILE-416.
[13]"The crystal structures of human steroidogenic factor-1 and liver receptor homologue-1."
Wang W., Zhang C., Marimuthu A., Krupka H.I., Tabrizizad M., Shelloe R., Mehra U., Eng K., Nguyen H., Settachatgul C., Powell B., Milburn M.V., West B.L.
Proc. Natl. Acad. Sci. U.S.A. 102:7505-7510(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 297-541 IN COMPLEX WITH NCOA2 AND PHOSPHOLIPID.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U80251 mRNA. Translation: AAC78727.1.
AF146343 mRNA. Translation: AAD37378.1.
AF124247 mRNA. Translation: AAD26565.1.
AF190464 Genomic DNA. Translation: AAG17124.1.
AF190464 Genomic DNA. Translation: AAG17125.1.
AK304365 mRNA. Translation: BAG65205.1.
AK316513 mRNA. Translation: BAH14884.1.
AC096633 Genomic DNA. No translation available.
CH471067 Genomic DNA. Translation: EAW91306.1.
BC118571 mRNA. Translation: AAI18572.1.
BC118652 mRNA. Translation: AAI18653.1.
U93553 mRNA. Translation: AAD03155.1.
CCDSCCDS1400.1. [O00482-2]
CCDS1401.1. [O00482-1]
RefSeqNP_001263393.1. NM_001276464.1. [O00482-4]
NP_003813.1. NM_003822.4. [O00482-2]
NP_995582.1. NM_205860.2. [O00482-1]
XP_005245119.1. XM_005245062.1. [O00482-4]
UniGeneHs.33446.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1YOKX-ray2.50A300-541[»]
1YUCX-ray1.90A/B290-541[»]
1ZDUX-ray2.50A297-541[»]
2A66X-ray2.20A79-187[»]
3PLZX-ray1.75A/B300-541[»]
3TX7X-ray2.76B191-541[»]
4DORX-ray1.90A/B290-541[»]
4DOSX-ray2.00A299-538[»]
4IS8X-ray2.78A/B300-538[»]
ProteinModelPortalO00482.
SMRO00482. Positions 84-540.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108772. 21 interactions.
DIPDIP-37952N.
IntActO00482. 2 interactions.
MINTMINT-2997724.
STRING9606.ENSP00000356331.

Chemistry

BindingDBO00482.
ChEMBLCHEMBL3544.

PTM databases

PhosphoSiteO00482.

Proteomic databases

PaxDbO00482.
PRIDEO00482.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000236914; ENSP00000236914; ENSG00000116833. [O00482-2]
ENST00000367362; ENSP00000356331; ENSG00000116833. [O00482-1]
ENST00000544748; ENSP00000439116; ENSG00000116833.
GeneID2494.
KEGGhsa:2494.
UCSCuc001gvb.4. human. [O00482-1]

Organism-specific databases

CTD2494.
GeneCardsGC01P199996.
HGNCHGNC:7984. NR5A2.
HPAHPA005455.
HPA017067.
MIM604453. gene.
neXtProtNX_O00482.
PharmGKBPA31765.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG240365.
HOGENOMHOG000063718.
HOVERGENHBG106677.
InParanoidO00482.
KOK08027.
OMANTFGLMC.
OrthoDBEOG7BS4B9.
PhylomeDBO00482.
TreeFamTF350737.

Enzyme and pathway databases

ReactomeREACT_111045. Developmental Biology.
REACT_71. Gene Expression.
SignaLinkO00482.

Gene expression databases

ArrayExpressO00482.
BgeeO00482.
CleanExHS_NR5A2.
GenevestigatorO00482.

Family and domain databases

Gene3D1.10.565.10. 1 hit.
3.30.50.10. 1 hit.
InterProIPR008946. Nucl_hormone_rcpt_ligand-bd.
IPR000536. Nucl_hrmn_rcpt_lig-bd_core.
IPR016355. Steroidogenic_factor_1.
IPR001723. Str_hrmn_rcpt.
IPR001628. Znf_hrmn_rcpt.
IPR013088. Znf_NHR/GATA.
[Graphical view]
PfamPF00104. Hormone_recep. 1 hit.
PF00105. zf-C4. 1 hit.
[Graphical view]
PIRSFPIRSF002530. Nuc_orph_FTZ-F1. 1 hit.
PRINTSPR00398. STRDHORMONER.
PR00047. STROIDFINGER.
SMARTSM00430. HOLI. 1 hit.
SM00399. ZnF_C4. 1 hit.
[Graphical view]
SUPFAMSSF48508. SSF48508. 2 hits.
PROSITEPS00031. NUCLEAR_REC_DBD_1. 1 hit.
PS51030. NUCLEAR_REC_DBD_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceO00482.
GeneWikiLiver_receptor_homolog-1.
GenomeRNAi2494.
NextBio35477332.
PROO00482.
SOURCESearch...

Entry information

Entry nameNR5A2_HUMAN
AccessionPrimary (citable) accession number: O00482
Secondary accession number(s): B4E2P3, O95642, Q147U3
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: May 30, 2000
Last modified: July 9, 2014
This is version 145 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM