NR4A1
entrez
3164
canonical
uniprot
P22736
canonical
ensembl
ENSG00000123358
resolver
ensp
ENSP00000243050
resolver
ensp
ENSP00000353427
resolver
ensp
ENSP00000378302
resolver
ensp
ENSP00000440864
resolver
ensp
ENSP00000618162
resolver
enst
ENST00000545748
resolver
genesymbol
NR4A1
resolver
genesymbol_syn
GFRP1
resolver
genesymbol_syn
HMR
resolver
genesymbol_syn
NAK1
resolver
hgnc
HGNC:7980
resolver
uniprot
B4DML7
resolver
uniprot
F5GXF0
resolver
uniprot
Q15627
resolver
uniprot
Q53Y00
resolver
uniprot
Q6IBU8
resolver
uniprot
Q6ZMM6
resolver
uniprot_entry
F5GXF0_HUMAN
resolver
uniprot_entry
NR4A1_HUMAN
resolver
uniprot_entry
Q6ZMM6_HUMAN
resolver
uniprot_sec
B4DML7
resolver
uniprot_sec
Q15627
resolver
uniprot_sec
Q53Y00
resolver
uniprot_sec
Q6IBU8
resolver
activity_regulation
ACTIVITY REGULATION: Its transcription factor activity is activated by binding cytosporone B (Csn-B) via its ligand-binding (NR LBD) domain and stimulates recruitment of coactivators NCOA1 and NCOA2, but not NCOA3, to promoters (PubMed:18690216). Csn-B-binding is also accompanied by its translocation to the mitochondrion (PubMed:18690216). Its transcription factor activity is activated by corticotropin-releasing hormone (CRH) and forskolin (PubMed:9315652). Not activated by binding cytosporone C (Csn-C) (PubMed:18690216). {ECO:0000269|PubMed:18690216, ECO:0000269|PubMed:9315652}.
uniprot
proteins
amino_acid_sequence
MPCIQAQYGTPAPSPGPRDHLASDPLTPEFIKPTMDLASPEAAPAAPTALPSFSTFMDGYTGEFDTFLYQLPGTVQPCSSASSSASSTSSSSATSPASASFKFEDFQVYGCYPGPLSGPVDEALSSSGSDYYGSPCSAPSPSTPSFQPPQLSPWDGSFGHFSPSQTYEGLRAWTEQLPKASGPPQPPAFFSFSPPTGPSPSLAQSPLKLFPSQATHQLGEGESYSMPTAFPGLAPTSPHLEGSGILDTPVTSTKARSGAPGGSEGRCAVCGDNASCQHYGVRTCEGCKGFFKRTVQKNAKYICLANKDCPVDKRRRNRCQFCRFQKCLAVGMVKEVVRTDSLKGRRGRLPSKPKQPPDASPANLLTSLVRAHLDSGPSTAKLDYSKFQELVLPHFGKEDAGDVQQFYDLLSGSLEVIRKWAEKIPGFAELSPADQDLLLESAFLELFILRLAYRSKPGEGKLIFCSGLVLHRLQCARGFGDWIDSILAFSRSLHSLLVDVPAFACLSALVLITDRHGLQEPRRVEELQNRIASCLKEHVAAVAGEPQPASCLSRLLGKLPELRTLCTQGLQRIFYLKLEDLVPPPPIIDKIFMDTLPF
uniprot
proteins
function
FUNCTION: Orphan nuclear receptor. Binds the NGFI-B response element (NBRE) 5'-AAAGGTCA-3' (PubMed:18690216, PubMed:8121493, PubMed:9315652). Binds 9-cis-retinoic acid outside of its ligand-binding (NR LBD) domain (PubMed:18690216). Participates in energy homeostasis by sequestrating the kinase STK11 in the nucleus, thereby attenuating cytoplasmic AMPK activation (PubMed:22983157). Regulates the inflammatory response in macrophages by regulating metabolic adaptations during inflammation, including repressing the transcription of genes involved in the citric acid cycle (TCA) (By similarity). Inhibits NF-kappa-B signaling by binding to low-affinity NF-kappa-B binding sites, such as at the IL2 promoter (PubMed:15466594). May act concomitantly with NR4A2 in regulating the expression of delayed-early genes during liver regeneration (By similarity). Plays a role in the vascular response to injury (By similarity). {ECO:0000250|UniProtKB:P12813, ECO:0000250|UniProtKB:P22829, ECO:0000269|PubMed:15466594, ECO:0000269|PubMed:18690216, ECO:0000269|PubMed:22983157, ECO:0000269|PubMed:8121493, ECO:0000269|PubMed:9315652}.; FUNCTION: In the cytosol, upon its detection of both bacterial lipopolysaccharide (LPS) and NBRE-containing mitochondrial DNA released by GSDMD pores during pyroptosis, it promotes non-canonical NLRP3 inflammasome activation by stimulating association of NLRP3 and NEK7. {ECO:0000250|UniProtKB:P12813}.
uniprot
proteins
mass_dalton
64463
uniprot
proteins
mutagenesis
MUTAGEN 1..50; /note="Missing: No impact on the interaction with RXRA."; /evidence="ECO:0000269|PubMed:17761950"; MUTAGEN 299..361; /note="Missing: Loss of interaction with RXRA."; /evidence="ECO:0000269|PubMed:17761950"; MUTAGEN 453; /note="Y->A: Abolishes binding to activity regulator Cytosporone B."; /evidence="ECO:0000269|PubMed:18690216"; MUTAGEN 595; /note="T->E: Strongly weakens interaction with STK11."; /evidence="ECO:0000269|PubMed:22983157
uniprot
proteins
post_translational_modification
PTM: Phosphorylated at Ser-351 by RPS6KA1 and RPS6KA3 in response to mitogenic or stress stimuli. {ECO:0000269|PubMed:17360704}.; PTM: Acetylated by p300/CBP, acetylation increases stability. Deacetylated by HDAC1. {ECO:0000269|PubMed:20438716}.
uniprot
proteins
protein_family
NR4 subfamily
uniprot
proteins
protein_family
Nuclear hormone receptor family
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15459248
uniprot
proteins
pubmed
15466594
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15509776
uniprot
proteins
pubmed
1651101
uniprot
proteins
pubmed
16541075
uniprot
proteins
pubmed
17360704
uniprot
proteins
pubmed
17761950
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
18690216
uniprot
proteins
pubmed
18691976
uniprot
proteins
pubmed
20438716
uniprot
proteins
pubmed
22427340
uniprot
proteins
pubmed
2283997
uniprot
proteins
pubmed
22983157
uniprot
proteins
pubmed
2626032
uniprot
proteins
pubmed
37001519
uniprot
proteins
pubmed
8121493
uniprot
proteins
pubmed
9315652
uniprot
proteins
sequence_length
598
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15509776, ECO:0000269|PubMed:17761950, ECO:0000269|PubMed:18690216, ECO:0000269|PubMed:20438716, ECO:0000269|PubMed:22427340, ECO:0000269|PubMed:22983157, ECO:0000269|PubMed:8121493}. Cytoplasm, cytosol {ECO:0000269|PubMed:15509776, ECO:0000269|PubMed:20438716, ECO:0000269|PubMed:22427340}. Mitochondrion {ECO:0000269|PubMed:17761950, ECO:0000269|PubMed:18690216}. Note=Nuclear export to the cytosol is XPO1-mediated and positively regulated by IFI27 (PubMed:22427340). Translocation to the mitochondrion upon interaction with RXRA and upon the presence of 9-cis retinoic acid (PubMed:17761950). {ECO:0000269|PubMed:17761950, ECO:0000269|PubMed:22427340}.
uniprot
proteins