Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Nuclear receptor ROR-alpha

Gene

RORA

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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, 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, ARNTL/BMAL1, NPAS2 and CRY1. Competes with NR1D1 for binding to their shared DNA response element on some clock genes such as ARNTL/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 G6PC 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.18 Publications

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
DNA bindingi73 – 138Nuclear receptorPROSITE-ProRule annotationAdd BLAST66
Zinc fingeri73 – 93NR C4-typePROSITE-ProRule annotationAdd BLAST21
Zinc fingeri109 – 133NR C4-typePROSITE-ProRule annotationAdd BLAST25

GO - Molecular functioni

  • core promoter sequence-specific DNA binding Source: UniProtKB
  • DNA binding Source: UniProtKB
  • oxysterol binding Source: UniProtKB
  • RNA polymerase II regulatory region sequence-specific DNA binding Source: MGI
  • RNA polymerase II transcription factor activity, ligand-activated sequence-specific DNA binding Source: InterPro
  • sequence-specific DNA binding Source: UniProtKB
  • steroid hormone receptor activity Source: InterPro
  • transcription coactivator binding Source: UniProtKB
  • transcription corepressor binding Source: UniProtKB
  • transcription factor activity, direct ligand regulated sequence-specific DNA binding Source: UniProtKB
  • transcription factor activity, sequence-specific DNA binding Source: UniProtKB
  • transcription factor binding Source: UniProtKB
  • zinc ion binding Source: InterPro

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Activator, Receptor

Keywords - Biological processi

Biological rhythms, Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding, Metal-binding, Zinc

Enzyme and pathway databases

BioCyciZFISH:ENSG00000069667-MONOMER.
ReactomeiR-HSA-1368082. RORA activates gene expression.
R-HSA-1368108. BMAL1:CLOCK,NPAS2 activates circadian gene expression.
R-HSA-1989781. PPARA activates gene expression.
R-HSA-383280. Nuclear Receptor transcription pathway.
R-HSA-400253. Circadian Clock.
SignaLinkiP35398.
SIGNORiP35398.

Names & Taxonomyi

Protein namesi
Recommended name:
Nuclear receptor ROR-alpha
Alternative name(s):
Nuclear receptor RZR-alpha
Nuclear receptor subfamily 1 group F member 1
RAR-related orphan receptor A
Retinoid-related orphan receptor-alpha
Gene namesi
Name:RORA
Synonyms:NR1F1, RZRA
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 15

Organism-specific databases

HGNCiHGNC:10258. RORA.

Subcellular locationi

GO - Cellular componenti

  • nucleoplasm Source: Reactome
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi183T → A: Greatly increased transcriptional activity. Decrease in repression by NR1D1. 1 Publication1
Mutagenesisi183T → D or E: Some increase in transcriptional activity. No change in repression by NR1D1. 1 Publication1
Mutagenesisi183T → R: Attenuates transcriptional activity. 1 Publication1
Mutagenesisi183T → V or I: Some increase in transcriptional activity. 1 Publication1
Mutagenesisi240K → R: Loss of sumoylation. 1 Publication1
Mutagenesisi288C → Q: Less effect on transcriptional activity with cholesterol sulfate as substrate as compared to cholesterol as substrate. 1 Publication1
Mutagenesisi323C → L: About 60% loss of transcriptional activity. 2 Publications1
Mutagenesisi330A → L: About 80% loss of transcriptional activity. 2 Publications1
Mutagenesisi335V → R: Strongly decreases interaction with NCOA2 and MED1. 1 Publication1
Mutagenesisi339K → A: Complete loss of transcriptional activity; when associated with A-507. 1 Publication1
Mutagenesisi357K → A: Increased transcriptional activity. No effect on protein degradation. 1 Publication1
Mutagenesisi361L → F: Small reduction in transcriptional activity. No protein degradation. 1 Publication1
Mutagenesisi364V → G: Greatly reduced transcriptional activity. Protects from protein degradation. 1 Publication1
Mutagenesisi371A → Q: Almost total loss of transcriptional activity. 1 Publication1
Mutagenesisi399F → W: Slight loss of transcriptional activity. 1 Publication1
Mutagenesisi441K → R: No effect on sumoylation. 1 Publication1
Mutagenesisi484H → W: Almost total loss of transcriptional activity. 1 Publication1
Mutagenesisi507Y → A: Complete loss of transcriptional activity; when associated with A-339. 1 Publication1
Mutagenesisi507Y → F: About 40% loss of transcriptional activity. 1 Publication1
Mutagenesisi509E → K: Abolishes transcriptional activity. Protects from protein degradation. 2 Publications1
Mutagenesisi510 – 511LF → AA: Decreases interaction with NCOA2. Loss of interaction with FOXP3. 2 Publications2

Organism-specific databases

DisGeNETi6095.
OpenTargetsiENSG00000069667.
PharmGKBiPA34630.

Chemistry databases

ChEMBLiCHEMBL5868.
GuidetoPHARMACOLOGYi598.

Polymorphism and mutation databases

BioMutaiRORA.
DMDMi548814.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000535121 – 523Nuclear receptor ROR-alphaAdd BLAST523

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei38N6-methyllysine1 Publication1
Modified residuei183Phosphothreonine; by MAPK11 Publication1
Cross-linki240Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)1 Publication

Post-translational modificationi

Phosphorylation by conventional PKCs in neurons inhibits transcriptional activity. Phosphorylated on Thr-183 by MAPK1/ERK1 in vitro.2 Publications
Sumoylated by SENP1 and SENP2. Sumoylation, promoted by PIAS2, PIAS3, PIAS4 but not PIAS1, enhances the transcriptional activity. Desumoylated by SENP1.1 Publication
Ubiquitinated, leading to its degradation by the proteasome. Proteasomal degradation is required for efficient transcriptional activity and is prevented by HR.1 Publication
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.1 Publication

Keywords - PTMi

Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiP35398.
PeptideAtlasiP35398.
PRIDEiP35398.

PTM databases

iPTMnetiP35398.
PhosphoSitePlusiP35398.

Expressioni

Tissue specificityi

Widely expressed in a number of tissues. Expressed in both regulatory T-cells (Treg) and effector T-cells (Teff).2 Publications

Inductioni

Induced by oxidative stress and DNA damage. Isoform 4 is induced by hypoxia (through transactivation by HIF1A and SP1), but not isoform 1.2 Publications

Gene expression databases

BgeeiENSG00000069667.
CleanExiHS_RORA.
ExpressionAtlasiP35398. baseline and differential.
GenevisibleiP35398. HS.

Organism-specific databases

HPAiCAB009861.

Interactioni

Subunit structurei

Monomer. Interacts (via the DNA-binding domain) with HIF1A; the interaction enhances HIF1A transcription under hypoxia through increasing protein stability. Interacts with CEBPB; the interaction disrupts the interaction CEBPB:EP300. Interacts with the coactivators NCOA2, PPARGC1A (via LXXLL motif), EP300 and MED1. Interacts with the corepressor NCOR1. Interacts with MAGED1 and CTNNB1. Interacts with CRY1 and PER2. Interacts (via AF-2 motif) with PROX1 (By similarity). Interacts with NRIP1. Isoform 4 interacts (via AF-2 motif) with isoform 1 of FOXP3 (via LXXLL motif).By similarity10 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
FOXP3Q9BZS15EBI-11295807,EBI-983719
GFAPP141363EBI-748689,EBI-744302
NR0B1P518432EBI-748689,EBI-946109

GO - Molecular functioni

  • transcription coactivator binding Source: UniProtKB
  • transcription corepressor binding Source: UniProtKB
  • transcription factor binding Source: UniProtKB

Protein-protein interaction databases

BioGridi112022. 24 interactors.
DIPiDIP-29938N.
IntActiP35398. 8 interactors.
MINTiMINT-2855668.
STRINGi9606.ENSP00000261523.

Chemistry databases

BindingDBiP35398.

Structurei

Secondary structure

1523
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi271 – 286Combined sources16
Helixi292 – 297Combined sources6
Turni298 – 300Combined sources3
Helixi305 – 313Combined sources9
Helixi316 – 340Combined sources25
Turni342 – 346Combined sources5
Helixi349 – 367Combined sources19
Helixi368 – 371Combined sources4
Turni374 – 377Combined sources4
Beta strandi378 – 381Combined sources4
Beta strandi384 – 386Combined sources3
Helixi388 – 394Combined sources7
Helixi397 – 411Combined sources15
Turni412 – 414Combined sources3
Helixi417 – 428Combined sources12
Helixi439 – 460Combined sources22
Helixi466 – 494Combined sources29
Helixi496 – 502Combined sources7
Helixi505 – 510Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1N83X-ray1.63A271-523[»]
1S0XX-ray2.20A271-523[»]
4S15X-ray1.90A/B269-523[»]
ProteinModelPortaliP35398.
SMRiP35398.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP35398.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni139 – 271HingeAdd BLAST133
Regioni272 – 523Ligand-bindingAdd BLAST252

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi506 – 523AF-2Add BLAST18

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi166 – 169Poly-Gln4

Domaini

The AF-2 (activation function-2) motif is required for recruiting coregulators containing LXXLL motifs.By similarity

Sequence similaritiesi

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

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri73 – 93NR C4-typePROSITE-ProRule annotationAdd BLAST21
Zinc fingeri109 – 133NR C4-typePROSITE-ProRule annotationAdd BLAST25

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiKOG4216. Eukaryota.
ENOG410XUGR. LUCA.
GeneTreeiENSGT00850000132242.
HOGENOMiHOG000010200.
HOVERGENiHBG106848.
InParanoidiP35398.
KOiK08532.
OMAiNKPREVM.
OrthoDBiEOG091G0649.
TreeFamiTF319910.

Family and domain databases

Gene3Di1.10.565.10. 2 hits.
3.30.50.10. 1 hit.
InterProiIPR000536. Nucl_hrmn_rcpt_lig-bd.
IPR001723. Nuclear_hrmn_rcpt.
IPR003079. ROR_rcpt.
IPR001628. Znf_hrmn_rcpt.
IPR013088. Znf_NHR/GATA.
[Graphical view]
PfamiPF00104. Hormone_recep. 1 hit.
PF00105. zf-C4. 1 hit.
[Graphical view]
PRINTSiPR01293. RORNUCRECPTR.
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 (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative promoter usage and alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P35398-2) [UniParc]FASTAAdd to basket
Also known as: Alpha-1

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

        10         20         30         40         50
MESAPAAPDP AASEPGSSGA DAAAGSRETP LNQESARKSE PPAPVRRQSY
60 70 80 90 100
SSTSRGISVT KKTHTSQIEI IPCKICGDKS SGIHYGVITC EGCKGFFRRS
110 120 130 140 150
QQSNATYSCP RQKNCLIDRT SRNRCQHCRL QKCLAVGMSR DAVKFGRMSK
160 170 180 190 200
KQRDSLYAEV QKHRMQQQQR DHQQQPGEAE PLTPTYNISA NGLTELHDDL
210 220 230 240 250
SNYIDGHTPE GSKADSAVSS FYLDIQPSPD QSGLDINGIK PEPICDYTPA
260 270 280 290 300
SGFFPYCSFT NGETSPTVSM AELEHLAQNI SKSHLETCQY LREELQQITW
310 320 330 340 350
QTFLQEEIEN YQNKQREVMW QLCAIKITEA IQYVVEFAKR IDGFMELCQN
360 370 380 390 400
DQIVLLKAGS LEVVFIRMCR AFDSQNNTVY FDGKYASPDV FKSLGCEDFI
410 420 430 440 450
SFVFEFGKSL CSMHLTEDEI ALFSAFVLMS ADRSWLQEKV KIEKLQQKIQ
460 470 480 490 500
LALQHVLQKN HREDGILTKL ICKVSTLRAL CGRHTEKLMA FKAIYPDIVR
510 520
LHFPPLYKEL FTSEFEPAMQ IDG
Length:523
Mass (Da):58,975
Last modified:April 16, 2014 - v2
Checksum:i0FA43BBCE6E28DC7
GO
Isoform 2 (identifier: P35398-1) [UniParc]FASTAAdd to basket
Also known as: Alpha-2

The sequence of this isoform differs from the canonical sequence as follows:
     1-66: MESAPAAPDP...ISVTKKTHTS → MNEGAPGDSD...KEVQTGYMNA

Note: Produced by alternative promoter usage. Region from 23 to 71 inhibits DNA-binding and transactivation activity.
Show »
Length:556
Mass (Da):63,036
Checksum:i0D9797A147CEE8AE
GO
Isoform 3 (identifier: P35398-3) [UniParc]FASTAAdd to basket
Also known as: Alpha-3

The sequence of this isoform differs from the canonical sequence as follows:
     38-65: KSEPPAPVRRQSYSSTSRGISVTKKTHT → SSSTCSSLSRLFWSQLEHINWDGATAKNFINLREFFSFLLPALRK

Note: Produced by alternative splicing.
Show »
Length:540
Mass (Da):61,108
Checksum:i89FEA2A06D25D971
GO
Isoform 4 (identifier: P35398-4) [UniParc]FASTAAdd to basket
Also known as: Alpha-4

The sequence of this isoform differs from the canonical sequence as follows:
     1-65: MESAPAAPDPAASEPGSSGADAAAGSRETPLNQESARKSEPPAPVRRQSYSSTSRGISVTKKTHT → MMYFVIAAMK

Note: Produced by alternative promoter usage.Curated
Show »
Length:468
Mass (Da):53,556
Checksum:iFD577090E6261B16
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti368M → V in AAA02963 (PubMed:7916608).Curated1
Sequence conflicti466I → M in AAA02963 (PubMed:7916608).Curated1
Isoform 4 (identifier: P35398-4)
Sequence conflicti7A → E in AAA02963 (PubMed:7916608).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Isoform 2 (identifier: P35398-1)
Natural varianti18P → S in a colorectal cancer sample, somatic mutation. 1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0539731 – 66MESAP…KTHTS → MNEGAPGDSDLETEARVPWS IMGHCLRTGQARMSATPTPA GEGARRDELFGILQILHQCI LSSGDAFVLTGVCCSWRQNG KPPYSQKEDKEVQTGYMNA in isoform 2. 1 PublicationAdd BLAST66
Alternative sequenceiVSP_0539741 – 65MESAP…KKTHT → MMYFVIAAMK in isoform 4. 3 PublicationsAdd BLAST65
Alternative sequenceiVSP_05397538 – 65KSEPP…KKTHT → SSSTCSSLSRLFWSQLEHIN WDGATAKNFINLREFFSFLL PALRK in isoform 3. 1 PublicationAdd BLAST28

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U04897 mRNA. Translation: AAA62658.1.
U04898 mRNA. Translation: AAA62659.1.
U04899 mRNA. Translation: AAA62660.1.
L14611 mRNA. Translation: AAA02963.1.
HQ692818 mRNA. Translation: ADZ17329.1.
AC009560 Genomic DNA. No translation available.
AC012404 Genomic DNA. No translation available.
AC022898 Genomic DNA. No translation available.
AC079068 Genomic DNA. No translation available.
AC087385 Genomic DNA. No translation available.
AC107241 Genomic DNA. No translation available.
AC107905 Genomic DNA. No translation available.
CH471082 Genomic DNA. Translation: EAW77594.1.
BC008831 mRNA. Translation: AAH08831.1.
BC100987 mRNA. Translation: AAI00988.1.
BC100988 mRNA. Translation: AAI00989.1.
BC100989 mRNA. Translation: AAI00990.1.
BC100990 mRNA. Translation: AAI00991.1.
CCDSiCCDS10177.1. [P35398-2]
CCDS10179.1. [P35398-1]
CCDS45271.1. [P35398-4]
PIRiA53196.
A56856.
B53196.
C53196.
RefSeqiNP_002934.1. NM_002943.3.
NP_599022.1. NM_134260.2. [P35398-1]
NP_599023.1. NM_134261.2. [P35398-2]
NP_599024.1. NM_134262.2.
UniGeneiHs.560343.

Genome annotation databases

EnsembliENST00000261523; ENSP00000261523; ENSG00000069667. [P35398-1]
ENST00000335670; ENSP00000335087; ENSG00000069667. [P35398-2]
GeneIDi6095.
KEGGihsa:6095.
UCSCiuc002agt.5. human. [P35398-2]

Keywords - Coding sequence diversityi

Alternative promoter usage, Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U04897 mRNA. Translation: AAA62658.1.
U04898 mRNA. Translation: AAA62659.1.
U04899 mRNA. Translation: AAA62660.1.
L14611 mRNA. Translation: AAA02963.1.
HQ692818 mRNA. Translation: ADZ17329.1.
AC009560 Genomic DNA. No translation available.
AC012404 Genomic DNA. No translation available.
AC022898 Genomic DNA. No translation available.
AC079068 Genomic DNA. No translation available.
AC087385 Genomic DNA. No translation available.
AC107241 Genomic DNA. No translation available.
AC107905 Genomic DNA. No translation available.
CH471082 Genomic DNA. Translation: EAW77594.1.
BC008831 mRNA. Translation: AAH08831.1.
BC100987 mRNA. Translation: AAI00988.1.
BC100988 mRNA. Translation: AAI00989.1.
BC100989 mRNA. Translation: AAI00990.1.
BC100990 mRNA. Translation: AAI00991.1.
CCDSiCCDS10177.1. [P35398-2]
CCDS10179.1. [P35398-1]
CCDS45271.1. [P35398-4]
PIRiA53196.
A56856.
B53196.
C53196.
RefSeqiNP_002934.1. NM_002943.3.
NP_599022.1. NM_134260.2. [P35398-1]
NP_599023.1. NM_134261.2. [P35398-2]
NP_599024.1. NM_134262.2.
UniGeneiHs.560343.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1N83X-ray1.63A271-523[»]
1S0XX-ray2.20A271-523[»]
4S15X-ray1.90A/B269-523[»]
ProteinModelPortaliP35398.
SMRiP35398.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112022. 24 interactors.
DIPiDIP-29938N.
IntActiP35398. 8 interactors.
MINTiMINT-2855668.
STRINGi9606.ENSP00000261523.

Chemistry databases

BindingDBiP35398.
ChEMBLiCHEMBL5868.
GuidetoPHARMACOLOGYi598.

PTM databases

iPTMnetiP35398.
PhosphoSitePlusiP35398.

Polymorphism and mutation databases

BioMutaiRORA.
DMDMi548814.

Proteomic databases

PaxDbiP35398.
PeptideAtlasiP35398.
PRIDEiP35398.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000261523; ENSP00000261523; ENSG00000069667. [P35398-1]
ENST00000335670; ENSP00000335087; ENSG00000069667. [P35398-2]
GeneIDi6095.
KEGGihsa:6095.
UCSCiuc002agt.5. human. [P35398-2]

Organism-specific databases

CTDi6095.
DisGeNETi6095.
GeneCardsiRORA.
HGNCiHGNC:10258. RORA.
HPAiCAB009861.
MIMi600825. gene.
neXtProtiNX_P35398.
OpenTargetsiENSG00000069667.
PharmGKBiPA34630.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG4216. Eukaryota.
ENOG410XUGR. LUCA.
GeneTreeiENSGT00850000132242.
HOGENOMiHOG000010200.
HOVERGENiHBG106848.
InParanoidiP35398.
KOiK08532.
OMAiNKPREVM.
OrthoDBiEOG091G0649.
TreeFamiTF319910.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000069667-MONOMER.
ReactomeiR-HSA-1368082. RORA activates gene expression.
R-HSA-1368108. BMAL1:CLOCK,NPAS2 activates circadian gene expression.
R-HSA-1989781. PPARA activates gene expression.
R-HSA-383280. Nuclear Receptor transcription pathway.
R-HSA-400253. Circadian Clock.
SignaLinkiP35398.
SIGNORiP35398.

Miscellaneous databases

ChiTaRSiRORA. human.
EvolutionaryTraceiP35398.
GeneWikiiRAR-related_orphan_receptor_alpha.
GenomeRNAii6095.
PROiP35398.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000069667.
CleanExiHS_RORA.
ExpressionAtlasiP35398. baseline and differential.
GenevisibleiP35398. HS.

Family and domain databases

Gene3Di1.10.565.10. 2 hits.
3.30.50.10. 1 hit.
InterProiIPR000536. Nucl_hrmn_rcpt_lig-bd.
IPR001723. Nuclear_hrmn_rcpt.
IPR003079. ROR_rcpt.
IPR001628. Znf_hrmn_rcpt.
IPR013088. Znf_NHR/GATA.
[Graphical view]
PfamiPF00104. Hormone_recep. 1 hit.
PF00105. zf-C4. 1 hit.
[Graphical view]
PRINTSiPR01293. RORNUCRECPTR.
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]
ProtoNetiSearch...

Entry informationi

Entry nameiRORA_HUMAN
AccessioniPrimary (citable) accession number: P35398
Secondary accession number(s): P35397
, P35399, P45445, Q495X4, Q96H83
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: April 16, 2014
Last modified: November 2, 2016
This is version 175 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 15
    Human chromosome 15: 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.