RORA
entrez
6095
canonical
uniprot
P35398
canonical
ensembl
ENSG00000069667
resolver
ensp
ENSP00000261523
resolver
ensp
ENSP00000309753
resolver
ensp
ENSP00000335087
resolver
ensp
ENSP00000402971
resolver
enst
ENST00000309157
resolver
enst
ENST00000449337
resolver
genesymbol
RORA
resolver
genesymbol_syn
NR1F1
resolver
genesymbol_syn
RZRA
resolver
hgnc
HGNC:10258
resolver
uniprot
A0A0C4DFP5
resolver
uniprot
A0A0C4DG53
resolver
uniprot
P35397
resolver
uniprot
P35399
resolver
uniprot
P45445
resolver
uniprot
Q495X4
resolver
uniprot
Q96H83
resolver
uniprot_entry
A0A0C4DFP5_HUMAN
resolver
uniprot_entry
A0A0C4DG53_HUMAN
resolver
uniprot_entry
RORA_HUMAN
resolver
uniprot_sec
P35397
resolver
uniprot_sec
P35399
resolver
uniprot_sec
P45445
resolver
uniprot_sec
Q495X4
resolver
uniprot_sec
Q96H83
resolver
amino_acid_sequence
MESAPAAPDPAASEPGSSGADAAAGSRETPLNQESARKSEPPAPVRRQSYSSTSRGISVTKKTHTSQIEIIPCKICGDKSSGIHYGVITCEGCKGFFRRSQQSNATYSCPRQKNCLIDRTSRNRCQHCRLQKCLAVGMSRDAVKFGRMSKKQRDSLYAEVQKHRMQQQQRDHQQQPGEAEPLTPTYNISANGLTELHDDLSNYIDGHTPEGSKADSAVSSFYLDIQPSPDQSGLDINGIKPEPICDYTPASGFFPYCSFTNGETSPTVSMAELEHLAQNISKSHLETCQYLREELQQITWQTFLQEEIENYQNKQREVMWQLCAIKITEAIQYVVEFAKRIDGFMELCQNDQIVLLKAGSLEVVFIRMCRAFDSQNNTVYFDGKYASPDVFKSLGCEDFISFVFEFGKSLCSMHLTEDEIALFSAFVLMSADRSWLQEKVKIEKLQQKIQLALQHVLQKNHREDGILTKLICKVSTLRALCGRHTEKLMAFKAIYPDIVRLHFPPLYKELFTSEFEPAMQIDG
uniprot
proteins
disease_involvement
DISEASE: Intellectual developmental disorder with or without epilepsy or cerebellar ataxia (IDDECA) [MIM:618060]: An autosomal dominant neurodevelopmental disorder that manifests with variable features of mild-to-severe intellectual disability, developmental delay, autism spectrum disorder, cerebellar ataxia and epilepsy. {ECO:0000269|PubMed:29656859}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
function
FUNCTION: Nuclear receptor that binds DNA as a monomer to ROR response elements (RORE) containing a single core motif half-site 5'-AGGTCA-3' preceded by a short A-T-rich sequence. Key regulator of embryonic development, cellular differentiation, immunity, circadian rhythm as well as lipid, steroid, xenobiotics and glucose metabolism. Considered to have intrinsic transcriptional activity, have some natural ligands like oxysterols that act as agonists (25-hydroxycholesterol) or inverse agonists (7-oxygenated sterols), enhancing or repressing the transcriptional activity, respectively. Recruits distinct combinations of cofactors to target genes regulatory regions to modulate their transcriptional expression, depending on the tissue, time and promoter contexts. Regulates genes involved in photoreceptor development including OPN1SW, OPN1SM and ARR3 and skeletal muscle development with MYOD1. Required for proper cerebellum development (PubMed:29656859). Regulates SHH gene expression, among others, to induce granule cells proliferation as well as expression of genes involved in calcium-mediated signal transduction. Regulates the circadian expression of several clock genes, including CLOCK, BMAL1, NPAS2 and CRY1. Competes with NR1D1 for binding to their shared DNA response element on some clock genes such as BMAL1, CRY1 and NR1D1 itself, resulting in NR1D1-mediated repression or RORA-mediated activation of clock genes expression, leading to the circadian pattern of clock genes expression. Therefore influences the period length and stability of the clock. Regulates genes involved in lipid metabolism such as apolipoproteins APOA1, APOA5, APOC3 and PPARG. In liver, has specific and redundant functions with RORC as positive or negative modulator of expression of genes encoding phase I and phase II proteins involved in the metabolism of lipids, steroids and xenobiotics, such as CYP7B1 and SULT2A1. Induces a rhythmic expression of some of these genes. In addition, interplays functionally with NR1H2 and NR1H3 for the regulation of genes involved in cholesterol metabolism. Also involved in the regulation of hepatic glucose metabolism through the modulation of G6PC1 and PCK1. In adipose tissue, plays a role as negative regulator of adipocyte differentiation, probably acting through dual mechanisms. May suppress CEBPB-dependent adipogenesis through direct interaction and PPARG-dependent adipogenesis through competition for DNA-binding. Downstream of IL6 and TGFB and synergistically with RORC isoform 2, is implicated in the lineage specification of uncommitted CD4(+) T-helper (T(H)) cells into T(H)17 cells, antagonizing the T(H)1 program. Probably regulates IL17 and IL17F expression on T(H) by binding to the essential enhancer conserved non-coding sequence 2 (CNS2) in the IL17-IL17F locus. Involved in hypoxia signaling by interacting with and activating the transcriptional activity of HIF1A. May inhibit cell growth in response to cellular stress. May exert an anti-inflammatory role by inducing CHUK expression and inhibiting NF-kappa-B signaling. {ECO:0000269|PubMed:10478845, ECO:0000269|PubMed:11053433, ECO:0000269|PubMed:11252722, ECO:0000269|PubMed:11554739, ECO:0000269|PubMed:12467577, ECO:0000269|PubMed:14570920, ECO:0000269|PubMed:15781255, ECO:0000269|PubMed:15790933, ECO:0000269|PubMed:16462772, ECO:0000269|PubMed:17512500, ECO:0000269|PubMed:18005000, ECO:0000269|PubMed:18354202, ECO:0000269|PubMed:18658046, ECO:0000269|PubMed:19965867, ECO:0000269|PubMed:21499262, ECO:0000269|PubMed:29656859, ECO:0000269|PubMed:7926749, ECO:0000269|PubMed:9328355, ECO:0000269|PubMed:9862959}.
uniprot
proteins
mass_dalton
58975
uniprot
proteins
mutagenesis
MUTAGEN 183; /note="T->A: Greatly increased transcriptional activity. Decrease in repression by NR1D1."; /evidence="ECO:0000269|PubMed:17512500"; MUTAGEN 183; /note="T->D,E: Some increase in transcriptional activity. No change in repression by NR1D1."; /evidence="ECO:0000269|PubMed:17512500"; MUTAGEN 183; /note="T->R: Attenuates transcriptional activity."; /evidence="ECO:0000269|PubMed:17512500"; MUTAGEN 183; /note="T->V,I: Some increase in transcriptional activity."; /evidence="ECO:0000269|PubMed:17512500"; MUTAGEN 240; /note="K->R: Loss of sumoylation."; /evidence="ECO:0000269|PubMed:19041634"; MUTAGEN 288; /note="C->Q: Less effect on transcriptional activity with cholesterol sulfate as substrate as compared to cholesterol as substrate."; /evidence="ECO:0000269|PubMed:14722075"; MUTAGEN 323; /note="C->L: About 60% loss of transcriptional activity."; /evidence="ECO:0000269|PubMed:12467577, ECO:0000269|PubMed:14722075"; MUTAGEN 330; /note="A->L: About 80% loss of transcriptional activity."; /evidence="ECO:0000269|PubMed:12467577, ECO:0000269|PubMed:14722075"; MUTAGEN 335; /note="V->R: Strongly decreases interaction with NCOA2 and MED1."; /evidence="ECO:0000269|PubMed:10478845"; MUTAGEN 339; /note="K->A: Complete loss of transcriptional activity; when associated with A-507."; /evidence="ECO:0000269|PubMed:14722075"; MUTAGEN 357; /note="K->A: Increased transcriptional activity. No effect on protein degradation."; /evidence="ECO:0000269|PubMed:14570920"; MUTAGEN 361; /note="L->F: Small reduction in transcriptional activity. No protein degradation."; /evidence="ECO:0000269|PubMed:14570920"; MUTAGEN 364; /note="V->G: Greatly reduced transcriptional activity. Protects from protein degradation."; /evidence="ECO:0000269|PubMed:14570920"; MUTAGEN 371; /note="A->Q: Almost total loss of transcriptional activity."; /evidence="ECO:0000269|PubMed:12467577"; MUTAGEN 399; /note="F->W: Slight loss of transcriptional activity."; /evidence="ECO:0000269|PubMed:12467577"; MUTAGEN 441; /note="K->R: No effect on sumoylation."; /evidence="ECO:0000269|PubMed:19041634"; MUTAGEN 484; /note="H->W: Almost total loss of transcriptional activity."; /evidence="ECO:0000269|PubMed:12467577"; MUTAGEN 507; /note="Y->A: Complete loss of transcriptional activity; when associated with A-339."; /evidence="ECO:0000269|PubMed:12467577"; MUTAGEN 507; /note="Y->F: About 40% loss of transcriptional activity."; /evidence="ECO:0000269|PubMed:12467577"; MUTAGEN 509; /note="E->K: Abolishes transcriptional activity. Protects from protein degradation."; /evidence="ECO:0000269|PubMed:14570920, ECO:0000269|PubMed:14722075"; MUTAGEN 510..511; /note="LF->AA: Decreases interaction with NCOA2. Loss of interaction with FOXP3."; /evidence="ECO:0000269|PubMed:10478845, ECO:0000269|PubMed:18354202
uniprot
proteins
post_translational_modification
PTM: Phosphorylation by conventional PKCs in neurons inhibits transcriptional activity. Phosphorylated on Thr-183 by MAPK1/ERK1 in vitro. {ECO:0000269|PubMed:17512500, ECO:0000269|PubMed:18005000}.; PTM: Sumoylated by SENP1 and SENP2. Sumoylation, promoted by PIAS2, PIAS3, PIAS4 but not PIAS1, enhances the transcriptional activity. Desumoylated by SENP1. {ECO:0000269|PubMed:19041634}.; PTM: Ubiquitinated, leading to its degradation by the proteasome. Proteasomal degradation is required for efficient transcriptional activity and is prevented by HR. {ECO:0000269|PubMed:14570920}.; PTM: [Isoform 1]: Monomethylated at Lys-38 by EZH2, this creates a degron recognized by a DCX (DDB1-DCAF1/VPRBP-CUL4A-RBX1) E3 ubiquitin ligase complex. {ECO:0000269|PubMed:14570920}.
uniprot
proteins
protein_family
NR1 subfamily
uniprot
proteins
protein_family
Nuclear hormone receptor family
uniprot
proteins
pubmed
10478845
uniprot
proteins
pubmed
11053433
uniprot
proteins
pubmed
11252722
uniprot
proteins
pubmed
11554739
uniprot
proteins
pubmed
12467577
uniprot
proteins
pubmed
14570920
uniprot
proteins
pubmed
14722075
uniprot
proteins
pubmed
14742449
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15781255
uniprot
proteins
pubmed
15790933
uniprot
proteins
pubmed
16462772
uniprot
proteins
pubmed
16572171
uniprot
proteins
pubmed
16959974
uniprot
proteins
pubmed
17512500
uniprot
proteins
pubmed
18005000
uniprot
proteins
pubmed
18354202
uniprot
proteins
pubmed
18658046
uniprot
proteins
pubmed
19041634
uniprot
proteins
pubmed
19381306
uniprot
proteins
pubmed
19965867
uniprot
proteins
pubmed
21499262
uniprot
proteins
pubmed
21628546
uniprot
proteins
pubmed
22170608
uniprot
proteins
pubmed
22789990
uniprot
proteins
pubmed
23063525
uniprot
proteins
pubmed
29656859
uniprot
proteins
pubmed
7916608
uniprot
proteins
pubmed
7926749
uniprot
proteins
pubmed
9328355
uniprot
proteins
pubmed
9862959
uniprot
proteins
sequence_length
523
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00407, ECO:0000269|PubMed:18005000, ECO:0000269|PubMed:18354202, ECO:0000269|PubMed:18658046}.
uniprot
proteins