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Protein

Nuclear receptor ROR-gamma

Gene

RORC

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 cellular differentiation, immunity, peripheral 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 gene regulatory regions to modulate their transcriptional expression, depending on the tissue, time and promoter contexts. Regulates the circadian expression of clock genes such as CRY1, ARNTL/BMAL1 and NR1D1 in peripheral tissues and in a tissue-selective manner. 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 RORC-mediated activation of the expression, leading to the circadian pattern of clock genes expression. Therefore influences the period length and stability of the clock. Involved in the regulation of the rhythmic expression of genes involved in glucose and lipid metabolism, including PLIN2 and AVPR1A. Negative regulator of adipocyte differentiation through the regulation of early phase genes expression, such as MMP3. Controls adipogenesis as well as adipocyte size and modulates insulin sensitivity in obesity. In liver, has specific and redundant functions with RORA 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 SULT1E1. Also plays also a role in the regulation of hepatocyte glucose metabolism through the regulation of G6PC and PCK1. Regulates the rhythmic expression of PROX1 and promotes its nuclear localization (By similarity).By similarity
Isoform 2: Essential for thymopoiesis and the development of several secondary lymphoid tissues, including lymph nodes and Peyer's patches. Required for the generation of LTi (lymphoid tissue inducer) cells. Regulates thymocyte survival through DNA-binding on ROREs of target gene promoter regions and recruitment of coactivaros via the AF-2. Also plays a key role, downstream of IL6 and TGFB and synergistically with RORA, for 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. May also play a role in the pre-TCR activation cascade leading to the maturation of alpha/beta T-cells and may participate in the regulation of DNA accessibility in the TCR-J(alpha) locus.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi31 – 9666Nuclear receptorPROSITE-ProRule annotationAdd
BLAST
Zinc fingeri31 – 5121NR C4-typePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri67 – 9125NR C4-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. direct ligand regulated sequence-specific DNA binding transcription factor activity Source: UniProtKB
  2. DNA binding Source: UniProtKB
  3. ligand-activated sequence-specific DNA binding RNA polymerase II transcription factor activity Source: ProtInc
  4. oxysterol binding Source: UniProtKB
  5. sequence-specific DNA binding Source: UniProtKB
  6. sequence-specific DNA binding transcription factor activity Source: UniProtKB
  7. steroid hormone receptor activity Source: InterPro
  8. zinc ion binding Source: InterPro

GO - Biological processi

  1. adipose tissue development Source: UniProtKB
  2. cellular response to sterol Source: UniProtKB
  3. circadian regulation of gene expression Source: UniProtKB
  4. gene expression Source: Reactome
  5. intracellular receptor signaling pathway Source: GOC
  6. lymph node development Source: UniProtKB
  7. negative regulation of thymocyte apoptotic process Source: UniProtKB
  8. Peyer's patch development Source: UniProtKB
  9. positive regulation of circadian rhythm Source: UniProtKB
  10. positive regulation of transcription, DNA-templated Source: UniProtKB
  11. protein phosphorylation Source: Ensembl
  12. regulation of fat cell differentiation Source: UniProtKB
  13. regulation of gamma-delta T cell differentiation Source: Ensembl
  14. regulation of glucose metabolic process Source: UniProtKB
  15. regulation of steroid metabolic process Source: UniProtKB
  16. regulation of transcription involved in cell fate commitment Source: UniProtKB
  17. T cell differentiation in thymus Source: Ensembl
  18. T-helper 17 cell differentiation Source: UniProtKB
  19. T-helper cell differentiation Source: UniProtKB
  20. transcription initiation from RNA polymerase II promoter Source: Reactome
  21. xenobiotic metabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Activator, Developmental protein, Receptor

Keywords - Biological processi

Biological rhythms, Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding, Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_15525. Nuclear Receptor transcription pathway.

Names & Taxonomyi

Protein namesi
Recommended name:
Nuclear receptor ROR-gamma
Alternative name(s):
Nuclear receptor RZR-gamma
Nuclear receptor subfamily 1 group F member 3
RAR-related orphan receptor C
Retinoid-related orphan receptor-gamma
Gene namesi
Name:RORC
Synonyms:NR1F3, RORG, RZRG
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:10260. RORC.

Subcellular locationi

Nucleus Curated

GO - Cellular componenti

  1. nucleoplasm Source: Reactome
  2. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi327 – 3271A → F: Completely abolishes transcriptional activity. 1 Publication
Mutagenesisi378 – 3781F → Q: Completely abolishes transcriptional activity. 1 Publication
Mutagenesisi397 – 3971I → N: Nearly abolishes transcriptional activity. 1 Publication

Organism-specific databases

PharmGKBiPA34632.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 518518Nuclear receptor ROR-gammaPRO_0000053517Add
BLAST

Proteomic databases

PaxDbiP51449.
PRIDEiP51449.

PTM databases

PhosphoSiteiP51449.

Expressioni

Tissue specificityi

Isoform 1 is widely expressed in many tissues, including liver and adipose, and highly expressed in skeletal muscle. Isoform 2 is primarily expressed in immature thymocytes.

Inductioni

Up-regulated in the state of obesity.1 Publication

Gene expression databases

BgeeiP51449.
CleanExiHS_RORC.
ExpressionAtlasiP51449. baseline and differential.
GenevestigatoriP51449.

Interactioni

Subunit structurei

Interacts (via AF-2 motif) with the coactivator NCOA2 (via LXXLL motif). Interacts with the corepressor NCOR1. Interacts with CRY1. Interacts (via AF-2 motif) with the coactivators NCOA1 and PPARGC1A (via LXXLL motif) (By similarity). Interacts (via AF-2 motif) with PROX1 (By similarity).By similarity3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ArntlQ9WTL82EBI-3908771,EBI-644534From a different organism.
ClockO087852EBI-3908771,EBI-79859From a different organism.
NCOA1Q157882EBI-3908771,EBI-455189

Protein-protein interaction databases

BioGridi112024. 3 interactions.
DIPiDIP-60622N.
IntActiP51449. 24 interactions.
MINTiMINT-4720467.
STRINGi9606.ENSP00000327025.

Structurei

Secondary structure

1
518
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi267 – 28216Combined sources
Helixi289 – 2946Combined sources
Turni295 – 2973Combined sources
Helixi302 – 3098Combined sources
Helixi313 – 33725Combined sources
Helixi341 – 3433Combined sources
Helixi346 – 36419Combined sources
Helixi365 – 3684Combined sources
Turni371 – 3744Combined sources
Beta strandi375 – 3784Combined sources
Beta strandi381 – 3833Combined sources
Helixi385 – 3917Combined sources
Helixi394 – 40815Combined sources
Turni409 – 4113Combined sources
Helixi414 – 42512Combined sources
Helixi436 – 45621Combined sources
Helixi460 – 4656Combined sources
Helixi471 – 48919Combined sources
Helixi491 – 4977Combined sources
Helixi500 – 5067Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3B0WX-ray2.20A/B265-507[»]
3KYTX-ray2.35A265-507[»]
3L0JX-ray2.40A265-507[»]
3L0LX-ray1.74A/B260-507[»]
4NB6X-ray2.85A/B262-507[»]
4NIEX-ray2.01A/B263-509[»]
4QM0X-ray2.20A/C262-507[»]
4WLBX-ray1.70A/B262-507[»]
ProteinModelPortaliP51449.
SMRiP51449. Positions 31-129, 260-507.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP51449.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 3030ModulatingSequence AnalysisAdd
BLAST
Regioni97 – 268172HingeSequence AnalysisAdd
BLAST
Regioni269 – 518250Ligand-bindingAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi501 – 5066AF-2

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi121 – 13010Poly-Gln

Domaini

The AF-2 (activation function-2) motif is required for recruiting coregulators containing LXXLL motifs such as NCOA1 and NCOA2.By similarity

Sequence similaritiesi

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

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri31 – 5121NR C4-typePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri67 – 9125NR C4-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiNOG317095.
GeneTreeiENSGT00780000121834.
HOVERGENiHBG106848.
InParanoidiP51449.
KOiK08534.
PhylomeDBiP51449.
TreeFamiTF319910.

Family and domain databases

Gene3Di1.10.565.10. 2 hits.
3.30.50.10. 1 hit.
InterProiIPR008946. Nucl_hormone_rcpt_ligand-bd.
IPR000536. Nucl_hrmn_rcpt_lig-bd_core.
IPR003079. ROR_rcpt.
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]
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 (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative promoter usage. Align

Isoform 1 (identifier: P51449-1) [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

        10         20         30         40         50
MDRAPQRQHR ASRELLAAKK THTSQIEVIP CKICGDKSSG IHYGVITCEG
60 70 80 90 100
CKGFFRRSQR CNAAYSCTRQ QNCPIDRTSR NRCQHCRLQK CLALGMSRDA
110 120 130 140 150
VKFGRMSKKQ RDSLHAEVQK QLQQRQQQQQ EPVVKTPPAG AQGADTLTYT
160 170 180 190 200
LGLPDGQLPL GSSPDLPEAS ACPPGLLKAS GSGPSYSNNL AKAGLNGASC
210 220 230 240 250
HLEYSPERGK AEGRESFYST GSQLTPDRCG LRFEEHRHPG LGELGQGPDS
260 270 280 290 300
YGSPSFRSTP EAPYASLTEI EHLVQSVCKS YRETCQLRLE DLLRQRSNIF
310 320 330 340 350
SREEVTGYQR KSMWEMWERC AHHLTEAIQY VVEFAKRLSG FMELCQNDQI
360 370 380 390 400
VLLKAGAMEV VLVRMCRAYN ADNRTVFFEG KYGGMELFRA LGCSELISSI
410 420 430 440 450
FDFSHSLSAL HFSEDEIALY TALVLINAHR PGLQEKRKVE QLQYNLELAF
460 470 480 490 500
HHHLCKTHRQ SILAKLPPKG KLRSLCSQHV ERLQIFQHLH PIVVQAAFPP
510
LYKELFSTET ESPVGLSK
Length:518
Mass (Da):58,195
Last modified:June 21, 2004 - v2
Checksum:i7F423140BD7922BE
GO
Isoform 2 (identifier: P51449-2) [UniParc]FASTAAdd to Basket

Also known as: RORgT

The sequence of this isoform differs from the canonical sequence as follows:
     1-21: Missing.
     22-24: HTS → MRT

Show »
Length:497
Mass (Da):55,813
Checksum:i6D0048673483EA11
GO

Sequence cautioni

The sequence AAA64751.1 differs from that shown. Reason: Frameshift at position 516. Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 2121Missing in isoform 2. 1 PublicationVSP_010632Add
BLAST
Alternative sequencei22 – 243HTS → MRT in isoform 2. 1 PublicationVSP_010633

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U16997 mRNA. Translation: AAA64751.1. Frameshift.
AL834219 mRNA. Translation: CAD38900.1.
AL589765 Genomic DNA. Translation: CAI17179.1.
BC031554 mRNA. Translation: AAH31554.1.
CCDSiCCDS1004.1. [P51449-1]
CCDS30856.1. [P51449-2]
PIRiJC2494.
RefSeqiNP_001001523.1. NM_001001523.1. [P51449-2]
NP_005051.2. NM_005060.3. [P51449-1]
UniGeneiHs.256022.
Hs.607993.

Genome annotation databases

EnsembliENST00000318247; ENSP00000327025; ENSG00000143365. [P51449-1]
ENST00000356728; ENSP00000349164; ENSG00000143365. [P51449-2]
GeneIDi6097.
KEGGihsa:6097.
UCSCiuc001ezh.3. human. [P51449-1]

Polymorphism databases

DMDMi49066040.

Keywords - Coding sequence diversityi

Alternative promoter usage

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U16997 mRNA. Translation: AAA64751.1. Frameshift.
AL834219 mRNA. Translation: CAD38900.1.
AL589765 Genomic DNA. Translation: CAI17179.1.
BC031554 mRNA. Translation: AAH31554.1.
CCDSiCCDS1004.1. [P51449-1]
CCDS30856.1. [P51449-2]
PIRiJC2494.
RefSeqiNP_001001523.1. NM_001001523.1. [P51449-2]
NP_005051.2. NM_005060.3. [P51449-1]
UniGeneiHs.256022.
Hs.607993.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3B0WX-ray2.20A/B265-507[»]
3KYTX-ray2.35A265-507[»]
3L0JX-ray2.40A265-507[»]
3L0LX-ray1.74A/B260-507[»]
4NB6X-ray2.85A/B262-507[»]
4NIEX-ray2.01A/B263-509[»]
4QM0X-ray2.20A/C262-507[»]
4WLBX-ray1.70A/B262-507[»]
ProteinModelPortaliP51449.
SMRiP51449. Positions 31-129, 260-507.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112024. 3 interactions.
DIPiDIP-60622N.
IntActiP51449. 24 interactions.
MINTiMINT-4720467.
STRINGi9606.ENSP00000327025.

Chemistry

BindingDBiP51449.
ChEMBLiCHEMBL1741186.
GuidetoPHARMACOLOGYi600.

PTM databases

PhosphoSiteiP51449.

Polymorphism databases

DMDMi49066040.

Proteomic databases

PaxDbiP51449.
PRIDEiP51449.

Protocols and materials databases

DNASUi6097.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000318247; ENSP00000327025; ENSG00000143365. [P51449-1]
ENST00000356728; ENSP00000349164; ENSG00000143365. [P51449-2]
GeneIDi6097.
KEGGihsa:6097.
UCSCiuc001ezh.3. human. [P51449-1]

Organism-specific databases

CTDi6097.
GeneCardsiGC01M151778.
HGNCiHGNC:10260. RORC.
MIMi602943. gene.
neXtProtiNX_P51449.
PharmGKBiPA34632.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG317095.
GeneTreeiENSGT00780000121834.
HOVERGENiHBG106848.
InParanoidiP51449.
KOiK08534.
PhylomeDBiP51449.
TreeFamiTF319910.

Enzyme and pathway databases

ReactomeiREACT_15525. Nuclear Receptor transcription pathway.

Miscellaneous databases

EvolutionaryTraceiP51449.
GeneWikiiRAR-related_orphan_receptor_gamma.
GenomeRNAii6097.
NextBioi23717.
PROiP51449.
SOURCEiSearch...

Gene expression databases

BgeeiP51449.
CleanExiHS_RORC.
ExpressionAtlasiP51449. baseline and differential.
GenevestigatoriP51449.

Family and domain databases

Gene3Di1.10.565.10. 2 hits.
3.30.50.10. 1 hit.
InterProiIPR008946. Nucl_hormone_rcpt_ligand-bd.
IPR000536. Nucl_hrmn_rcpt_lig-bd_core.
IPR003079. ROR_rcpt.
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]
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...

Publicationsi

« Hide 'large scale' publications
  1. "ROR gamma: the third member of ROR/RZR orphan receptor subfamily that is highly expressed in skeletal muscle."
    Hirose T., Smith R.J., Jetten A.M.
    Biochem. Biophys. Res. Commun. 205:1976-1983(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Skeletal muscle.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Lymph node.
  3. "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].
  4. "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: Colon and Kidney.
  5. "Retinoid-related orphan receptors (RORs): critical roles in development, immunity, circadian rhythm, and cellular metabolism."
    Jetten A.M.
    Nucl. Recept. Signal. 7:3-35(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON FUNCTION.
  6. "A second class of nuclear receptors for oxysterols: Regulation of RORalpha and RORgamma activity by 24S-hydroxycholesterol (cerebrosterol)."
    Wang Y., Kumar N., Crumbley C., Griffin P.R., Burris T.P.
    Biochim. Biophys. Acta 1801:917-923(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME REGULATION, INTERACTION WITH NCOA2.
  7. "Modulation of retinoic acid receptor-related orphan receptor alpha and gamma activity by 7-oxygenated sterol ligands."
    Wang Y., Kumar N., Solt L.A., Richardson T.I., Helvering L.M., Crumbley C., Garcia-Ordonez R.D., Stayrook K.R., Zhang X., Novick S., Chalmers M.J., Griffin P.R., Burris T.P.
    J. Biol. Chem. 285:5013-5025(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN GLUCOSE METABOLISM REGULATION, IDENTIFICATION OF LIGANDS.
  8. "Adipogenesis and insulin sensitivity in obesity are regulated by retinoid-related orphan receptor gamma."
    Meissburger B., Ukropec J., Roeder E., Beaton N., Geiger M., Teupser D., Civan B., Langhans W., Nawroth P.P., Gasperikova D., Rudofsky G., Wolfrum C.
    EMBO Mol. Med. 3:637-651(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION BY OBESITY.
  9. Cited for: FUNCTION IN T(H)17 CELLS DIFFERENTIATION, IDENTIFICATION OF LIGANDS.
  10. "Cryptochromes mediate rhythmic repression of the glucocorticoid receptor."
    Lamia K.A., Papp S.J., Yu R.T., Barish G.D., Uhlenhaut N.H., Jonker J.W., Downes M., Evans R.M.
    Nature 480:552-556(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CRY1.
  11. "Action of RORs and their ligands in (patho)physiology."
    Solt L.A., Burris T.P.
    Trends Endocrinol. Metab. 23:619-627(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON FUNCTION AND LIGANDS.
  12. "Structural basis for hydroxycholesterols as natural ligands of orphan nuclear receptor RORgamma."
    Jin L., Martynowski D., Zheng S., Wada T., Xie W., Li Y.
    Mol. Endocrinol. 24:923-929(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.74 ANGSTROMS) OF 260-507 IN COMPLEX WITH HYDROXYCHOLESTEROLS, FUNCTION TRANSCRIPTION ACTIVATOR, MUTAGENESIS OF ALA-327; PHE-378 AND ILE-397.

Entry informationi

Entry nameiRORG_HUMAN
AccessioniPrimary (citable) accession number: P51449
Secondary accession number(s): Q5SZR9, Q8N5V7, Q8NCY8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: June 21, 2004
Last modified: February 4, 2015
This is version 139 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

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 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.