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O00482

- NR5A2_HUMAN

UniProt

O00482 - NR5A2_HUMAN

Protein

Nuclear receptor subfamily 5 group A member 2

Gene

NR5A2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 147 (01 Oct 2014)
      Sequence version 2 (30 May 2000)
      Previous versions | rss
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    Functioni

    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.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei516 – 5161Lipid headgroup
    Binding sitei520 – 5201Lipid headgroup

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    DNA bindingi83 – 15472Nuclear receptorPROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri86 – 10621NR C4-typePROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri122 – 14625NR C4-typePROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. DNA binding Source: UniProtKB
    2. ligand-activated sequence-specific DNA binding RNA polymerase II transcription factor activity Source: UniProtKB
    3. phospholipid binding Source: UniProtKB
    4. protein binding Source: UniProtKB
    5. RNA polymerase II distal enhancer sequence-specific DNA binding transcription factor activity Source: ProtInc
    6. sequence-specific DNA binding Source: UniProtKB
    7. sequence-specific DNA binding transcription factor activity Source: UniProtKB
    8. steroid hormone receptor activity Source: InterPro
    9. transcription regulatory region DNA binding Source: BHF-UCL
    10. zinc ion binding Source: InterPro

    GO - Biological processi

    1. bile acid metabolic process Source: Ensembl
    2. cholesterol homeostasis Source: Ensembl
    3. embryo development Source: UniProtKB
    4. endocrine pancreas development Source: Reactome
    5. gene expression Source: Reactome
    6. homeostatic process Source: UniProtKB
    7. intracellular receptor signaling pathway Source: GOC
    8. positive regulation of transcription, DNA-templated Source: BHF-UCL
    9. positive regulation of transcription from RNA polymerase II promoter Source: Ensembl
    10. positive regulation of viral genome replication Source: BHF-UCL
    11. regulation of cell proliferation Source: Ensembl
    12. regulation of transcription, DNA-templated Source: UniProtKB
    13. transcription initiation from RNA polymerase II promoter Source: Reactome

    Keywords - Molecular functioni

    Receptor

    Keywords - Biological processi

    Transcription, Transcription regulation

    Keywords - Ligandi

    DNA-binding, Lipid-binding, Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_13778. Regulation of gene expression in early pancreatic precursor cells.
    REACT_15525. Nuclear Receptor transcription pathway.
    SignaLinkiO00482.

    Names & Taxonomyi

    Protein namesi
    Recommended 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 namesi
    Name:NR5A2
    Synonyms:B1F, CPF, FTF
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:7984. NR5A2.

    Subcellular locationi

    Nucleus Curated

    GO - Cellular componenti

    1. cytoplasm Source: BHF-UCL
    2. nucleoplasm Source: Reactome
    3. nucleus Source: BHF-UCL

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi96 – 961Y → A: Slightly reduced DNA binding. Strongly reduced transactivation; when associated with A-168 and A-172. 1 Publication
    Mutagenesisi168 – 1681F → A: Slightly reduced DNA binding. Strongly reduced transactivation; when associated with A-96 and A-172. 1 Publication
    Mutagenesisi169 – 1702GP → VA: Reduced DNA binding. Loss of transactivation.
    Mutagenesisi172 – 1721Y → A: Slightly reduced DNA binding. Strongly reduced transactivation; when associated with A-96 and A-168. 1 Publication
    Mutagenesisi342 – 3421F → W: Reduced phospholipid binding. Strongly reduced transactivation; when associated with W-416. 1 Publication
    Mutagenesisi416 – 4161I → W: Reduced phospholipid binding. Strongly reduced transactivation; when associated with W-342. 1 Publication

    Organism-specific databases

    PharmGKBiPA31765.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 541541Nuclear receptor subfamily 5 group A member 2PRO_0000053735Add
    BLAST

    Proteomic databases

    PaxDbiO00482.
    PRIDEiO00482.

    PTM databases

    PhosphoSiteiO00482.

    Expressioni

    Tissue specificityi

    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.

    Gene expression databases

    ArrayExpressiO00482.
    BgeeiO00482.
    CleanExiHS_NR5A2.
    GenevestigatoriO00482.

    Organism-specific databases

    HPAiHPA005455.
    HPA017067.

    Interactioni

    Subunit structurei

    Binds DNA as a monomer By similarity. Interacts with GRIP1, NCOA2 and NR0B2.By similarity4 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    EDF1O608692EBI-781320,EBI-781301

    Protein-protein interaction databases

    BioGridi108772. 21 interactions.
    DIPiDIP-37952N.
    IntActiO00482. 2 interactions.
    MINTiMINT-2997724.
    STRINGi9606.ENSP00000356331.

    Structurei

    Secondary structure

    1
    541
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni87 – 893
    Beta strandi92 – 976
    Beta strandi100 – 1034
    Helixi104 – 11512
    Turni132 – 1376
    Helixi139 – 14810
    Helixi153 – 1553
    Helixi169 – 1779
    Helixi303 – 3108
    Helixi315 – 32814
    Helixi335 – 3373
    Helixi341 – 36222
    Helixi366 – 3683
    Helixi371 – 39727
    Beta strandi402 – 4043
    Beta strandi410 – 4123
    Helixi413 – 4175
    Helixi422 – 44019
    Helixi445 – 45612
    Helixi467 – 48822
    Beta strandi490 – 4923
    Helixi495 – 5006
    Helixi502 – 52221
    Helixi531 – 5366

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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[»]
    ProteinModelPortaliO00482.
    SMRiO00482. Positions 84-540.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO00482.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni342 – 39049Ligand-bindingAdd
    BLAST
    Regioni419 – 4246Lipid binding

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi155 – 18430FTZ-F1 boxAdd
    BLAST

    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

    eggNOGiNOG240365.
    HOGENOMiHOG000063718.
    HOVERGENiHBG106677.
    InParanoidiO00482.
    KOiK08027.
    OMAiNTFGLMC.
    OrthoDBiEOG7BS4B9.
    PhylomeDBiO00482.
    TreeFamiTF350737.

    Family and domain databases

    Gene3Di1.10.565.10. 1 hit.
    3.30.50.10. 1 hit.
    InterProiIPR008946. 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]
    PfamiPF00104. Hormone_recep. 1 hit.
    PF00105. zf-C4. 1 hit.
    [Graphical view]
    PIRSFiPIRSF002530. Nuc_orph_FTZ-F1. 1 hit.
    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 (4)i

    Sequence statusi: Complete.

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform 2 (identifier: O00482-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MSSNSDTGDL QESLKHGLTP IGAGLPDRHG SPIPARGRLV MLPKVETEAL    50
    GLARSHGEQG QMPENMQVSQ FKMVNYSYDE DLEELCPVCG DKVSGYHYGL 100
    LTCESCKGFF KRTVQNNKRY TCIENQNCQI DKTQRKRCPY CRFQKCLSVG 150
    MKLEAVRADR MRGGRNKFGP MYKRDRALKQ QKKALIRANG LKLEAMSQVI 200
    QAMPSDLTIS SAIQNIHSAS KGLPLNHAAL PPTDYDRSPF VTSPISMTMP 250
    PHGSLQGYQT YGHFPSRAIK SEYPDPYTSS PESIMGYSYM DSYQTSSPAS 300
    IPHLILELLK CEPDEPQVQA KIMAYLQQEQ ANRSKHEKLS TFGLMCKMAD 350
    QTLFSIVEWA RSSIFFRELK VDDQMKLLQN CWSELLILDH IYRQVVHGKE 400
    GSIFLVTGQQ VDYSIIASQA GATLNNLMSH AQELVAKLRS LQFDQREFVC 450
    LKFLVLFSLD VKNLENFQLV EGVQEQVNAA LLDYTMCNYP QQTEKFGQLL 500
    LRLPEIRAIS MQAEEYLYYK HLNGDVPYNN LLIEMLHAKR A 541
    Length:541
    Mass (Da):61,331
    Last modified:May 30, 2000 - v2
    Checksum:i7B07170C075490FE
    GO
    Isoform 1 (identifier: O00482-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         22-67: Missing.

    Show »
    Length:495
    Mass (Da):56,459
    Checksum:iE73E60DCE9880855
    GO
    Isoform 3 (identifier: O00482-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         199-370: Missing.

    Note: Does not induce CYP7A promoter activity.

    Show »
    Length:369
    Mass (Da):42,102
    Checksum:i1357C2AAEFB4E46B
    GO
    Isoform 4 (identifier: O00482-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-72: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:469
    Mass (Da):53,657
    Checksum:i49F21C2F09CF0AB4
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti250 – 2512PP → L in AAD03155. (PubMed:9858833)Curated
    Sequence conflicti353 – 3531L → V in AAD03155. (PubMed:9858833)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 7272Missing in isoform 4. 1 PublicationVSP_054548Add
    BLAST
    Alternative sequencei22 – 6746Missing in isoform 1. 3 PublicationsVSP_003716Add
    BLAST
    Alternative sequencei199 – 370172Missing in isoform 3. 1 PublicationVSP_003717Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS1400.1. [O00482-2]
    CCDS1401.1. [O00482-1]
    CCDS60383.1. [O00482-4]
    RefSeqiNP_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]
    UniGeneiHs.33446.

    Genome annotation databases

    EnsembliENST00000236914; ENSP00000236914; ENSG00000116833. [O00482-2]
    ENST00000367362; ENSP00000356331; ENSG00000116833. [O00482-1]
    ENST00000544748; ENSP00000439116; ENSG00000116833. [O00482-4]
    GeneIDi2494.
    KEGGihsa:2494.
    UCSCiuc001gvb.4. human. [O00482-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS1400.1. [O00482-2 ]
    CCDS1401.1. [O00482-1 ]
    CCDS60383.1. [O00482-4 ]
    RefSeqi NP_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 ]
    UniGenei Hs.33446.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1YOK X-ray 2.50 A 300-541 [» ]
    1YUC X-ray 1.90 A/B 290-541 [» ]
    1ZDU X-ray 2.50 A 297-541 [» ]
    2A66 X-ray 2.20 A 79-187 [» ]
    3PLZ X-ray 1.75 A/B 300-541 [» ]
    3TX7 X-ray 2.76 B 191-541 [» ]
    4DOR X-ray 1.90 A/B 290-541 [» ]
    4DOS X-ray 2.00 A 299-538 [» ]
    4IS8 X-ray 2.78 A/B 300-538 [» ]
    ProteinModelPortali O00482.
    SMRi O00482. Positions 84-540.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108772. 21 interactions.
    DIPi DIP-37952N.
    IntActi O00482. 2 interactions.
    MINTi MINT-2997724.
    STRINGi 9606.ENSP00000356331.

    Chemistry

    BindingDBi O00482.
    ChEMBLi CHEMBL3544.

    PTM databases

    PhosphoSitei O00482.

    Proteomic databases

    PaxDbi O00482.
    PRIDEi O00482.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000236914 ; ENSP00000236914 ; ENSG00000116833 . [O00482-2 ]
    ENST00000367362 ; ENSP00000356331 ; ENSG00000116833 . [O00482-1 ]
    ENST00000544748 ; ENSP00000439116 ; ENSG00000116833 . [O00482-4 ]
    GeneIDi 2494.
    KEGGi hsa:2494.
    UCSCi uc001gvb.4. human. [O00482-1 ]

    Organism-specific databases

    CTDi 2494.
    GeneCardsi GC01P199996.
    HGNCi HGNC:7984. NR5A2.
    HPAi HPA005455.
    HPA017067.
    MIMi 604453. gene.
    neXtProti NX_O00482.
    PharmGKBi PA31765.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG240365.
    HOGENOMi HOG000063718.
    HOVERGENi HBG106677.
    InParanoidi O00482.
    KOi K08027.
    OMAi NTFGLMC.
    OrthoDBi EOG7BS4B9.
    PhylomeDBi O00482.
    TreeFami TF350737.

    Enzyme and pathway databases

    Reactomei REACT_13778. Regulation of gene expression in early pancreatic precursor cells.
    REACT_15525. Nuclear Receptor transcription pathway.
    SignaLinki O00482.

    Miscellaneous databases

    EvolutionaryTracei O00482.
    GeneWikii Liver_receptor_homolog-1.
    GenomeRNAii 2494.
    NextBioi 35477332.
    PROi O00482.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O00482.
    Bgeei O00482.
    CleanExi HS_NR5A2.
    Genevestigatori O00482.

    Family and domain databases

    Gene3Di 1.10.565.10. 1 hit.
    3.30.50.10. 1 hit.
    InterProi IPR008946. 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 ]
    Pfami PF00104. Hormone_recep. 1 hit.
    PF00105. zf-C4. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF002530. Nuc_orph_FTZ-F1. 1 hit.
    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

    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.
      , 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.
      , 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. 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. 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. 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. Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 297-541 IN COMPLEX WITH NCOA2 AND PHOSPHOLIPID.

    Entry informationi

    Entry nameiNR5A2_HUMAN
    AccessioniPrimary (citable) accession number: O00482
    Secondary accession number(s): B4E2P3, O95642, Q147U3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1998
    Last sequence update: May 30, 2000
    Last modified: October 1, 2014
    This is version 147 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: 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