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P22736

- NR4A1_HUMAN

UniProt

P22736 - NR4A1_HUMAN

Protein

Nuclear receptor subfamily 4 group A member 1

Gene

NR4A1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 163 (01 Oct 2014)
      Sequence version 1 (01 Aug 1991)
      Previous versions | rss
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    Functioni

    Orphan nuclear receptor. May act concomitantly with NURR1 in regulating the expression of delayed-early genes during liver regeneration. Binds the NGFI-B response element (NBRE) 5'-AAAAGGTCA-3' By similarity. May inhibit NF-kappa-B transactivation of IL2. Participates in energy homeostasis by sequestrating the kinase STK11 in the nucleus, thereby attenuating cytoplasmic AMPK activation.By similarity2 Publications

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    DNA bindingi264 – 33976Nuclear receptorPROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri267 – 28721NR C4-typePROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri303 – 32725NR C4-typePROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. DNA binding Source: BHF-UCL
    2. ligand-activated sequence-specific DNA binding RNA polymerase II transcription factor activity Source: ProtInc
    3. protein binding Source: IntAct
    4. RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription Source: Ensembl
    5. sequence-specific DNA binding Source: Ensembl
    6. steroid hormone receptor activity Source: InterPro
    7. zinc ion binding Source: InterPro

    GO - Biological processi

    1. cell migration involved in sprouting angiogenesis Source: BHF-UCL
    2. cellular response to fibroblast growth factor stimulus Source: BHF-UCL
    3. cellular response to vascular endothelial growth factor stimulus Source: BHF-UCL
    4. endothelial cell chemotaxis Source: BHF-UCL
    5. epidermal growth factor receptor signaling pathway Source: Reactome
    6. Fc-epsilon receptor signaling pathway Source: Reactome
    7. fibroblast growth factor receptor signaling pathway Source: Reactome
    8. gene expression Source: Reactome
    9. innate immune response Source: Reactome
    10. intracellular receptor signaling pathway Source: GOC
    11. negative regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: Ensembl
    12. neurotrophin TRK receptor signaling pathway Source: Reactome
    13. phosphatidylinositol-mediated signaling Source: Reactome
    14. positive regulation of apoptotic process Source: Ensembl
    15. positive regulation of endothelial cell proliferation Source: BHF-UCL
    16. signal transduction Source: ProtInc
    17. skeletal muscle cell differentiation Source: Ensembl
    18. transcription initiation from RNA polymerase II promoter Source: Reactome

    Keywords - Molecular functioni

    Receptor

    Keywords - Biological processi

    Transcription, Transcription regulation

    Keywords - Ligandi

    DNA-binding, Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_12442. AKT phosphorylates targets in the nucleus.
    REACT_147727. Constitutive PI3K/AKT Signaling in Cancer.
    REACT_15525. Nuclear Receptor transcription pathway.
    SignaLinkiP22736.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Nuclear receptor subfamily 4 group A member 1
    Alternative name(s):
    Early response protein NAK1
    Nuclear hormone receptor NUR/77
    Short name:
    Nur77
    Orphan nuclear receptor HMR
    Orphan nuclear receptor TR3
    ST-59
    Testicular receptor 3
    Gene namesi
    Name:NR4A1
    Synonyms:GFRP1, HMR, NAK1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:7980. NR4A1.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell
    2. nucleoplasm Source: Reactome
    3. nucleus Source: BHF-UCL
    4. transcription factor complex Source: Ensembl

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi595 – 5951T → E: Strongly weakens interaction with STK11. 1 Publication

    Organism-specific databases

    PharmGKBiPA31761.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 598598Nuclear receptor subfamily 4 group A member 1PRO_0000053715Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei341 – 3411Phosphoserine; by PKABy similarity
    Modified residuei351 – 3511Phosphoserine2 Publications

    Post-translational modificationi

    Phosphorylated at Ser-351 by RPS6KA1 and RPS6KA3 in response to mitogenic or stress stimuli.2 Publications
    Acetylated by p300/CBP, acetylation increases stability. Deacetylated by HDAC1.1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP22736.
    PaxDbiP22736.
    PRIDEiP22736.

    PTM databases

    PhosphoSiteiP22736.

    Expressioni

    Tissue specificityi

    Fetal muscle and adult liver, brain and thyroid.

    Inductioni

    By growth-stimulating agents.

    Gene expression databases

    ArrayExpressiP22736.
    BgeeiP22736.
    CleanExiHS_NR4A1.
    GenevestigatoriP22736.

    Organism-specific databases

    HPAiHPA051230.

    Interactioni

    Subunit structurei

    Binds DNA as a monomer By similarity. Interacts with GADD45GIP1. Interacts with STK11.By similarity2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Q9WMX22EBI-721550,EBI-9028517From a different organism.
    ANKIB1Q9P2G12EBI-721550,EBI-2687890
    BCL2P104157EBI-721550,EBI-77694
    CUTAO608882EBI-721550,EBI-1051556
    GKP321893EBI-721550,EBI-3926629
    MATR3P432432EBI-721550,EBI-352602
    PLXND1Q9Y4D72EBI-721550,EBI-310731
    STAT3P407633EBI-721550,EBI-518675
    TP53P046376EBI-721550,EBI-366083
    TUBB4AP043502EBI-721550,EBI-355007
    VASPP505522EBI-721550,EBI-748201

    Protein-protein interaction databases

    BioGridi109407. 84 interactions.
    DIPiDIP-40392N.
    IntActiP22736. 82 interactions.
    MINTiMINT-2859679.
    STRINGi9606.ENSP00000243050.

    Structurei

    Secondary structure

    1
    598
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi363 – 37412
    Helixi379 – 3813
    Helixi400 – 41213
    Helixi414 – 4229
    Helixi427 – 4293
    Helixi432 – 45423
    Helixi457 – 4593
    Beta strandi461 – 4633
    Beta strandi467 – 4715
    Helixi472 – 4798
    Helixi482 – 49514
    Helixi500 – 51112
    Helixi521 – 54323
    Helixi550 – 5567
    Helixi558 – 57922
    Helixi586 – 59510

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2QW4X-ray2.80A/B/C/D347-598[»]
    3V3EX-ray2.06A/B351-598[»]
    3V3QX-ray2.22A/B351-598[»]
    4JGVX-ray3.01A/B351-598[»]
    4KZIX-ray2.41A/B351-598[»]
    4KZJX-ray2.12A/B351-598[»]
    4KZMX-ray2.30A/B351-598[»]
    ProteinModelPortaliP22736.
    SMRiP22736. Positions 265-598.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP22736.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni409 – 45951Ligand-bindingSequence AnalysisAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi82 – 9211Poly-SerAdd
    BLAST
    Compositional biasi583 – 5864Poly-Pro

    Sequence similaritiesi

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

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri267 – 28721NR C4-typePROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri303 – 32725NR C4-typePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Zinc-finger

    Phylogenomic databases

    eggNOGiNOG245120.
    HOGENOMiHOG000230925.
    HOVERGENiHBG052663.
    InParanoidiP22736.
    KOiK04465.
    OMAiFISIEAQ.
    PhylomeDBiP22736.
    TreeFamiTF315430.

    Family and domain databases

    Gene3Di1.10.565.10. 1 hit.
    3.30.50.10. 1 hit.
    InterProiIPR003071. Nuc_orp_HMR_rcpt.
    IPR003070. Nuc_orph_rcpt.
    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]
    PRINTSiPR01285. HMRNUCRECPTR.
    PR01284. NUCLEARECPTR.
    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. Align

    Isoform 1 (identifier: P22736-1) [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

    MPCIQAQYGT PAPSPGPRDH LASDPLTPEF IKPTMDLASP EAAPAAPTAL    50
    PSFSTFMDGY TGEFDTFLYQ LPGTVQPCSS ASSSASSTSS SSATSPASAS 100
    FKFEDFQVYG CYPGPLSGPV DEALSSSGSD YYGSPCSAPS PSTPSFQPPQ 150
    LSPWDGSFGH FSPSQTYEGL RAWTEQLPKA SGPPQPPAFF SFSPPTGPSP 200
    SLAQSPLKLF PSQATHQLGE GESYSMPTAF PGLAPTSPHL EGSGILDTPV 250
    TSTKARSGAP GGSEGRCAVC GDNASCQHYG VRTCEGCKGF FKRTVQKNAK 300
    YICLANKDCP VDKRRRNRCQ FCRFQKCLAV GMVKEVVRTD SLKGRRGRLP 350
    SKPKQPPDAS PANLLTSLVR AHLDSGPSTA KLDYSKFQEL VLPHFGKEDA 400
    GDVQQFYDLL SGSLEVIRKW AEKIPGFAEL SPADQDLLLE SAFLELFILR 450
    LAYRSKPGEG KLIFCSGLVL HRLQCARGFG DWIDSILAFS RSLHSLLVDV 500
    PAFACLSALV LITDRHGLQE PRRVEELQNR IASCLKEHVA AVAGEPQPAS 550
    CLSRLLGKLP ELRTLCTQGL QRIFYLKLED LVPPPPIIDK IFMDTLPF 598
    Length:598
    Mass (Da):64,463
    Last modified:August 1, 1991 - v1
    Checksum:i41DAAEA7C25FDA22
    GO
    Isoform 2 (identifier: P22736-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-1: M → MWLAKACWSIQSEM

    Note: No experimental confirmation available.

    Show »
    Length:611
    Mass (Da):65,998
    Checksum:i21F3BC282AE6BE8D
    GO
    Isoform 3 (identifier: P22736-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         293-325: RTVQKNAKYICLANKDCPVDKRRRNRCQFCRFQ → VPRSPRWGLLLEMERGWPHPIGTCGLPLGSPPS
         326-598: Missing.

    Show »
    Length:325
    Mass (Da):33,754
    Checksum:iBCF2490A32A09175
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti253 – 2531T → I(PubMed:1651101)Curated
    Sequence conflicti262 – 2621G → P in AAA36763. (PubMed:2626032)Curated
    Sequence conflicti360 – 3601S → F in CAG32985. 1 PublicationCurated
    Sequence conflicti370 – 3701R → L in AAA36763. (PubMed:2626032)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti26 – 261L → V.
    Corresponds to variant rs1882118 [ dbSNP | Ensembl ].
    VAR_061534

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 11M → MWLAKACWSIQSEM in isoform 2. 1 PublicationVSP_043086
    Alternative sequencei293 – 32533RTVQK…FCRFQ → VPRSPRWGLLLEMERGWPHP IGTCGLPLGSPPS in isoform 3. 2 PublicationsVSP_047769Add
    BLAST
    Alternative sequencei326 – 598273Missing in isoform 3. 2 PublicationsVSP_047770Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D49728 mRNA. Translation: BAA08565.1.
    L13740 mRNA. Translation: AAA36763.1.
    D85245 mRNA. Translation: BAA12746.1.
    AK297526 mRNA. Translation: BAG59929.1.
    HQ692855 mRNA. Translation: ADZ17366.1.
    AB307717 mRNA. Translation: BAH02308.1.
    BT007144 mRNA. Translation: AAP35808.1.
    AK314437 mRNA. Translation: BAG37048.1.
    CR456704 mRNA. Translation: CAG32985.1.
    AC025259 Genomic DNA. No translation available.
    CH471111 Genomic DNA. Translation: EAW58222.1.
    CH471111 Genomic DNA. Translation: EAW58224.1.
    CH471111 Genomic DNA. Translation: EAW58225.1.
    BC016147 mRNA. Translation: AAH16147.1.
    CCDSiCCDS55828.1. [P22736-2]
    CCDS8818.1. [P22736-1]
    PIRiA37251.
    RefSeqiNP_001189162.1. NM_001202233.1. [P22736-2]
    NP_002126.2. NM_002135.4. [P22736-1]
    NP_775180.1. NM_173157.2. [P22736-1]
    XP_005268881.1. XM_005268824.2. [P22736-1]
    XP_006719426.1. XM_006719363.1. [P22736-1]
    XP_006719427.1. XM_006719364.1. [P22736-1]
    UniGeneiHs.524430.
    Hs.670088.

    Genome annotation databases

    EnsembliENST00000243050; ENSP00000243050; ENSG00000123358. [P22736-1]
    ENST00000360284; ENSP00000353427; ENSG00000123358. [P22736-2]
    ENST00000394824; ENSP00000378301; ENSG00000123358. [P22736-1]
    ENST00000394825; ENSP00000378302; ENSG00000123358. [P22736-1]
    ENST00000548232; ENSP00000449587; ENSG00000123358. [P22736-3]
    ENST00000550082; ENSP00000449539; ENSG00000123358. [P22736-2]
    GeneIDi3164.
    KEGGihsa:3164.
    UCSCiuc001rzr.2. human.
    uc001rzs.3. human. [P22736-1]
    uc010sno.2. human. [P22736-2]

    Polymorphism databases

    DMDMi127819.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D49728 mRNA. Translation: BAA08565.1 .
    L13740 mRNA. Translation: AAA36763.1 .
    D85245 mRNA. Translation: BAA12746.1 .
    AK297526 mRNA. Translation: BAG59929.1 .
    HQ692855 mRNA. Translation: ADZ17366.1 .
    AB307717 mRNA. Translation: BAH02308.1 .
    BT007144 mRNA. Translation: AAP35808.1 .
    AK314437 mRNA. Translation: BAG37048.1 .
    CR456704 mRNA. Translation: CAG32985.1 .
    AC025259 Genomic DNA. No translation available.
    CH471111 Genomic DNA. Translation: EAW58222.1 .
    CH471111 Genomic DNA. Translation: EAW58224.1 .
    CH471111 Genomic DNA. Translation: EAW58225.1 .
    BC016147 mRNA. Translation: AAH16147.1 .
    CCDSi CCDS55828.1. [P22736-2 ]
    CCDS8818.1. [P22736-1 ]
    PIRi A37251.
    RefSeqi NP_001189162.1. NM_001202233.1. [P22736-2 ]
    NP_002126.2. NM_002135.4. [P22736-1 ]
    NP_775180.1. NM_173157.2. [P22736-1 ]
    XP_005268881.1. XM_005268824.2. [P22736-1 ]
    XP_006719426.1. XM_006719363.1. [P22736-1 ]
    XP_006719427.1. XM_006719364.1. [P22736-1 ]
    UniGenei Hs.524430.
    Hs.670088.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2QW4 X-ray 2.80 A/B/C/D 347-598 [» ]
    3V3E X-ray 2.06 A/B 351-598 [» ]
    3V3Q X-ray 2.22 A/B 351-598 [» ]
    4JGV X-ray 3.01 A/B 351-598 [» ]
    4KZI X-ray 2.41 A/B 351-598 [» ]
    4KZJ X-ray 2.12 A/B 351-598 [» ]
    4KZM X-ray 2.30 A/B 351-598 [» ]
    ProteinModelPortali P22736.
    SMRi P22736. Positions 265-598.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109407. 84 interactions.
    DIPi DIP-40392N.
    IntActi P22736. 82 interactions.
    MINTi MINT-2859679.
    STRINGi 9606.ENSP00000243050.

    Chemistry

    BindingDBi P22736.
    ChEMBLi CHEMBL1293229.

    PTM databases

    PhosphoSitei P22736.

    Polymorphism databases

    DMDMi 127819.

    Proteomic databases

    MaxQBi P22736.
    PaxDbi P22736.
    PRIDEi P22736.

    Protocols and materials databases

    DNASUi 3164.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000243050 ; ENSP00000243050 ; ENSG00000123358 . [P22736-1 ]
    ENST00000360284 ; ENSP00000353427 ; ENSG00000123358 . [P22736-2 ]
    ENST00000394824 ; ENSP00000378301 ; ENSG00000123358 . [P22736-1 ]
    ENST00000394825 ; ENSP00000378302 ; ENSG00000123358 . [P22736-1 ]
    ENST00000548232 ; ENSP00000449587 ; ENSG00000123358 . [P22736-3 ]
    ENST00000550082 ; ENSP00000449539 ; ENSG00000123358 . [P22736-2 ]
    GeneIDi 3164.
    KEGGi hsa:3164.
    UCSCi uc001rzr.2. human.
    uc001rzs.3. human. [P22736-1 ]
    uc010sno.2. human. [P22736-2 ]

    Organism-specific databases

    CTDi 3164.
    GeneCardsi GC12P052416.
    H-InvDB HIX0171621.
    HGNCi HGNC:7980. NR4A1.
    HPAi HPA051230.
    MIMi 139139. gene.
    neXtProti NX_P22736.
    PharmGKBi PA31761.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG245120.
    HOGENOMi HOG000230925.
    HOVERGENi HBG052663.
    InParanoidi P22736.
    KOi K04465.
    OMAi FISIEAQ.
    PhylomeDBi P22736.
    TreeFami TF315430.

    Enzyme and pathway databases

    Reactomei REACT_12442. AKT phosphorylates targets in the nucleus.
    REACT_147727. Constitutive PI3K/AKT Signaling in Cancer.
    REACT_15525. Nuclear Receptor transcription pathway.
    SignaLinki P22736.

    Miscellaneous databases

    ChiTaRSi NR4A1. human.
    EvolutionaryTracei P22736.
    GeneWikii Nerve_Growth_factor_IB.
    GenomeRNAii 3164.
    NextBioi 12546.
    PROi P22736.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P22736.
    Bgeei P22736.
    CleanExi HS_NR4A1.
    Genevestigatori P22736.

    Family and domain databases

    Gene3Di 1.10.565.10. 1 hit.
    3.30.50.10. 1 hit.
    InterProi IPR003071. Nuc_orp_HMR_rcpt.
    IPR003070. Nuc_orph_rcpt.
    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 PR01285. HMRNUCRECPTR.
    PR01284. NUCLEARECPTR.
    PR00398. STRDHORMONER.
    PR00047. STROIDFINGER.
    SMARTi SM00430. HOLI. 1 hit.
    SM00399. ZnF_C4. 1 hit.
    [Graphical view ]
    SUPFAMi SSF48508. SSF48508. 1 hit.
    PROSITEi PS00031. NUCLEAR_REC_DBD_1. 1 hit.
    PS51030. NUCLEAR_REC_DBD_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "A human early response gene homologous to murine nur77 and rat NGFI-B, and related to the nuclear receptor superfamily."
      Nakai A., Kartha S., Sakurai A., Toback F.G., Degroot L.J.
      Mol. Endocrinol. 4:1438-1443(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Fetal skeletal muscle.
    2. "Isolation and characterization of human TR3 receptor: a member of steroid receptor superfamily."
      Chang C., Kokontis J., Liao S., Chang Y.
      J. Steroid Biochem. 34:391-395(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    3. "Identification of an isoform of human TR3 (NGFI-B, Nur77)."
      Ohkura N., Ito M., Tsukada T., Sasaki K., Yamaguchi K., Miki K.
      Submitted (MAY-1996) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
      Tissue: Skeletal muscle.
    4. "Comprehensive DNA-binding analysis of human hormone nuclear receptors by fluorescence correlation spectroscopy based on cell-free system."
      Kobayashi T., Kodani Y., Sawasaki T., Endo Y.
      Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    5. "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 [MRNA] (ISOFORM 1).
      Tissue: Heart.
    6. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
      Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
      Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    7. "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: Brain and Trachea.
    8. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    9. "The finished DNA sequence of human chromosome 12."
      Scherer S.E., Muzny D.M., 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., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
      Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    10. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    11. "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).
      Tissue: Skin.
    12. "Phorbol ester, forskolin, and serum induction of a human colon nuclear hormone receptor gene related to the NUR 77/NGFI-B genes."
      Bondy G.P.
      Cell Growth Differ. 2:203-208(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 35-398 (ISOFORM 1).
      Tissue: Colon adenocarcinoma.
    13. "Negative cross-talk between the human orphan nuclear receptor Nur77/NAK-1/TR3 and nuclear factor-kappaB."
      Harant H., Lindley I.J.
      Nucleic Acids Res. 32:5280-5290(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    14. "CR6-interacting factor 1 interacts with orphan nuclear receptor Nur77 and inhibits its transactivation."
      Park K.C., Song K.-H., Chung H.K., Kim H., Kim D.W., Song J.H., Hwang E.S., Jung H.S., Park S.-H., Bae I., Lee I.K., Choi H.-S., Shong M.
      Mol. Endocrinol. 19:12-24(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH GADD45GIP1.
    15. "RAS/ERK signaling promotes site-specific ribosomal protein S6 phosphorylation via RSK and stimulates cap-dependent translation."
      Roux P.P., Shahbazian D., Vu H., Holz M.K., Cohen M.S., Taunton J., Sonenberg N., Blenis J.
      J. Biol. Chem. 282:14056-14064(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-351.
    16. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
      Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
      Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    17. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-351, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    18. "Regulation of Nur77 protein turnover through acetylation and deacetylation induced by p300 and HDAC1."
      Kang S.A., Na H., Kang H.J., Kim S.H., Lee M.H., Lee M.O.
      Biochem. Pharmacol. 80:867-873(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION, SUBCELLULAR LOCATION.
    19. Cited for: X-RAY CRYSTALLOGRAPHY (2.06 ANGSTROMS) OF 351-598 ALONE AND IN COMPLEX WITH ANTAGONIST, FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH STK11, MUTAGENESIS OF THR-595.

    Entry informationi

    Entry nameiNR4A1_HUMAN
    AccessioniPrimary (citable) accession number: P22736
    Secondary accession number(s): B4DML7
    , Q15627, Q53Y00, Q6IBU8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1991
    Last sequence update: August 1, 1991
    Last modified: October 1, 2014
    This is version 163 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 12
      Human chromosome 12: 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