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P13631 (RARG_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 176. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Retinoic acid receptor gamma

Short name=RAR-gamma
Alternative name(s):
Nuclear receptor subfamily 1 group B member 3
Gene names
Name:RARG
Synonyms:NR1B3
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length454 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Receptor for retinoic acid. Retinoic acid receptors bind as heterodimers to their target response elements in response to their ligands, all-trans or 9-cis retinoic acid, and regulate gene expression in various biological processes. The RAR/RXR heterodimers bind to the retinoic acid response elements (RARE) composed of tandem 5'-AGGTCA-3' sites known as DR1-DR5. In the absence of ligand, acts mainly as an activator of gene expression due to weak binding to corepressors. Required for limb bud development. In concert with RARA or RARB, required for skeletal growth, matrix homeostasis and growth plate function By similarity.

Subunit structure

Homodimer By similarity. Heterodimer with a RXR molecule By similarity. Binds DNA preferentially as a RAR/RXR heterodimer By similarity. Forms a complex with PUS1 and the SRA1 RNA in the nucleus By similarity.

Subcellular location

Nucleus.

Domain

Composed of three domains: a modulating N-terminal domain, a DNA-binding domain and a C-terminal ligand-binding domain.

Sequence similarities

Belongs to the nuclear hormone receptor family. NR1 subfamily.

Contains 1 nuclear receptor DNA-binding domain.

Sequence caution

The sequence CAA40548.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainZinc-finger
   LigandDNA-binding
Metal-binding
Zinc
   Molecular functionReceptor
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processHarderian gland development

Inferred from electronic annotation. Source: Ensembl

anterior/posterior pattern specification

Inferred from electronic annotation. Source: Ensembl

canonical Wnt signaling pathway

Traceable author statement PubMed 18484682. Source: BHF-UCL

cellular response to retinoic acid

Inferred from electronic annotation. Source: Ensembl

embryonic eye morphogenesis

Inferred from sequence or structural similarity. Source: BHF-UCL

embryonic hindlimb morphogenesis

Inferred from sequence or structural similarity. Source: BHF-UCL

gene expression

Traceable author statement. Source: Reactome

growth plate cartilage chondrocyte growth

Inferred from electronic annotation. Source: Ensembl

multicellular organism growth

Inferred from electronic annotation. Source: Ensembl

negative regulation of cartilage development

Inferred from electronic annotation. Source: Ensembl

negative regulation of cell proliferation

Inferred from sequence or structural similarity. Source: BHF-UCL

negative regulation of chondrocyte differentiation

Inferred from electronic annotation. Source: Ensembl

negative regulation of transcription from RNA polymerase II promoter

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of apoptotic process

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of cell proliferation

Inferred from electronic annotation. Source: Ensembl

positive regulation of programmed cell death

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of transcription from RNA polymerase II promoter

Inferred from sequence or structural similarity. Source: BHF-UCL

prostate gland epithelium morphogenesis

Inferred from electronic annotation. Source: Ensembl

regulation of cell size

Traceable author statement PubMed 18438858. Source: BHF-UCL

regulation of myelination

Inferred from electronic annotation. Source: Ensembl

response to retinoic acid

Inferred from direct assay PubMed 17943189. Source: BHF-UCL

retinoic acid receptor signaling pathway

Inferred from direct assay PubMed 17943189. Source: BHF-UCL

trachea cartilage development

Inferred from electronic annotation. Source: Ensembl

transcription initiation from RNA polymerase II promoter

Traceable author statement. Source: Reactome

   Cellular_componentintegral component of membrane

Non-traceable author statement PubMed 17943189. Source: BHF-UCL

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay PubMed 18845237. Source: UniProtKB

transcription factor complex

Inferred from sequence or structural similarity. Source: BHF-UCL

   Molecular_functionDNA binding

Inferred from sequence or structural similarity. Source: BHF-UCL

protein binding

Inferred from physical interaction PubMed 10428834PubMed 16456540PubMed 20413580. Source: UniProtKB

retinoic acid receptor activity

Inferred from electronic annotation. Source: Ensembl

retinoid X receptor binding

Inferred from sequence or structural similarity. Source: BHF-UCL

sequence-specific DNA binding

Inferred from electronic annotation. Source: InterPro

sequence-specific DNA binding transcription factor activity

Inferred from sequence or structural similarity. Source: BHF-UCL

steroid hormone receptor activity

Inferred from electronic annotation. Source: InterPro

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

SORBS3O60504-22EBI-2568901,EBI-1222956

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]

Note: Isoforms differ only in their N-terminal regions.
Isoform 1 (identifier: P13631-1)

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.
Isoform 2 (identifier: P13631-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-61: MATNKERLFA...PDLPKEMASL → MYDCMETFAP...FAWPQPASLQ
Isoform 3 (identifier: P13631-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-72: Missing.
Note: No experimental confirmation available.
Isoform 4 (identifier: P13631-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-111: MATNKERLFA...YGVSSCEGCK → MLALPLPPCW...LPGRNPPACN
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 454454Retinoic acid receptor gamma
PRO_0000053472

Regions

DNA binding90 – 15566Nuclear receptor
Zinc finger90 – 11021NR C4-type
Zinc finger126 – 15025NR C4-type
Region1 – 8989Modulating
Region156 – 20146Hinge
Region202 – 421220Ligand-binding

Natural variations

Alternative sequence1 – 111111MATNK…CEGCK → MLALPLPPCWSGAPPGEEGE SAAGPWCFQHPVSLQAGSRC TTVWKRLPRVRDGCTGRPGP GPACCAEPPAAPVSPDLNLL PGRNPPACN in isoform 4.
VSP_044776
Alternative sequence1 – 7272Missing in isoform 3.
VSP_044777
Alternative sequence1 – 6161MATNK…EMASL → MYDCMETFAPGPRRLYGAAG PGAGLLRRATGGSCFAGLES FAWPQPASLQ in isoform 2.
VSP_031080
Natural variant4271S → L.
Corresponds to variant rs2229774 [ dbSNP | Ensembl ].
VAR_038554
Natural variant4301G → S in a breast cancer sample; somatic mutation. Ref.14
VAR_036061

Experimental info

Sequence conflict1181I → T in CAB60726. Ref.10
Sequence conflict1721K → R in AAG41594. Ref.11
Sequence conflict2521T → A in CAB60726. Ref.10
Sequence conflict3421M → V in BAH12478. Ref.4
Sequence conflict4211M → L in CAB60726. Ref.10

Secondary structure

............................... 454
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified January 1, 1990. Version 1.
Checksum: 1EE27B22772D4AFD

FASTA45450,342
        10         20         30         40         50         60 
MATNKERLFA AGALGPGSGY PGAGFPFAFP GALRGSPPFE MLSPSFRGLG QPDLPKEMAS 

        70         80         90        100        110        120 
LSVETQSTSS EEMVPSSPSP PPPPRVYKPC FVCNDKSSGY HYGVSSCEGC KGFFRRSIQK 

       130        140        150        160        170        180 
NMVYTCHRDK NCIINKVTRN RCQYCRLQKC FEVGMSKEAV RNDRNKKKKE VKEEGSPDSY 

       190        200        210        220        230        240 
ELSPQLEELI TKVSKAHQET FPSLCQLGKY TTNSSADHRV QLDLGLWDKF SELATKCIIK 

       250        260        270        280        290        300 
IVEFAKRLPG FTGLSIADQI TLLKAACLDI LMLRICTRYT PEQDTMTFSD GLTLNRTQMH 

       310        320        330        340        350        360 
NAGFGPLTDL VFAFAGQLLP LEMDDTETGL LSAICLICGD RMDLEEPEKV DKLQEPLLEA 

       370        380        390        400        410        420 
LRLYARRRRP SQPYMFPRML MKITDLRGIS TKGAERAITL KMEIPGPMPP LIREMLENPE 

       430        440        450 
MFEDDSSQPG PHPNASSEDE VPGGQGKGGL KSPA 

« Hide

Isoform 2 [UniParc].

Checksum: 4D709194F5111E86
Show »

FASTA44349,308
Isoform 3 [UniParc].

Checksum: 37AF909319A4B140
Show »

FASTA38242,926
Isoform 4 [UniParc].

Checksum: AA332A06D720ADB8
Show »

FASTA43247,931

References

« Hide 'large scale' references
[1]"A third human retinoic acid receptor, hRAR-gamma."
Krust A., Kastner P., Petkovich M., Zelent A., Chambon P.
Proc. Natl. Acad. Sci. U.S.A. 86:5310-5314(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]"A functional retinoic acid receptor encoded by the gene on human chromosome 12."
Ishikawa T., Umesono K., Mangelsdorf D.J., Aburatani H., Stanger B.Z., Shibasaki Y., Imawari M., Evans R.M., Takaku F.
Mol. Endocrinol. 4:837-844(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[3]"Genomic organization of the retinoic acid receptor gamma gene."
Lehmann J.M., Hoffmann B., Pfahl M.
Nucleic Acids Res. 19:573-578(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), ALTERNATIVE SPLICING.
Tissue: Placenta.
[4]"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. expand/collapse author list , 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; 3 AND 4).
Tissue: Brain, Tongue and Umbilical cord blood.
[5]"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. expand/collapse author list , 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].
[6]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"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.
[8]"Murine isoforms of retinoic acid receptor gamma with specific patterns of expression."
Kastner P., Krust A., Mendelsohn C., Garnier J.-M., Zelent A., Leroy P., Staub A., Chambon P.
Proc. Natl. Acad. Sci. U.S.A. 87:2700-2704(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-63 (ISOFORM 2).
[9]"RAR-gamma-2 expression is regulated through a retinoic acid response element embedded in Sp1 sites."
Lehmann J.M., Zhang X.K., Pfahl M.
Mol. Cell. Biol. 12:2976-2985(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-55, ALTERNATIVE SPLICING.
Tissue: Placenta.
[10]Gebhard W.
Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 74-454.
Tissue: Lung carcinoma.
[11]"Genomic organization of the human retinoic acid receptor gamma gene."
Xu H., Clifford J.L.
Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 134-191 AND 394-411.
[12]"Crystal structure of the RAR-gamma ligand-binding domain bound to all-trans retinoic acid."
Renaud J.-P., Rochel N., Ruff M., Vivat V., Chambon P., Gronemeyer H., Moras D.
Nature 378:681-689(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 178-423.
[13]"Conformational adaptation of agonists to the human nuclear receptor RAR gamma."
Klaholz B.P., Renaud J.-P., Mitschler A., Zusi C., Chambon P., Gronemeyer H., Moras D.
Nat. Struct. Biol. 5:199-202(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 178-423.
[14]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] SER-430.
+Additional computationally mapped references.

Web resources

Wikipedia

Retinoic acid receptor entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M24857 mRNA. Translation: AAA52692.1.
M57707 mRNA. Translation: AAA63254.1.
M38258 mRNA. Translation: AAA60254.1.
AK297023 mRNA. Translation: BAH12478.1.
AK297277 mRNA. Translation: BAH12537.1.
AK316259 mRNA. Translation: BAH14630.1.
AC021072 Genomic DNA. No translation available.
AC073573 Genomic DNA. No translation available.
CH471054 Genomic DNA. Translation: EAW96676.1.
BC093727 mRNA. Translation: AAH93727.1.
BC093729 mRNA. Translation: AAH93729.1.
M32074 mRNA. Translation: AAA60253.1.
X57280 Genomic DNA. Translation: CAA40548.1. Sequence problems.
AJ250835 Genomic DNA. Translation: CAB60726.1.
AY013703 Genomic DNA. Translation: AAG41594.2.
AY013704 Genomic DNA. Translation: AAG41595.1.
CCDSCCDS41790.1. [P13631-2]
CCDS58236.1. [P13631-3]
CCDS58237.1. [P13631-4]
CCDS8850.1. [P13631-1]
PIRA33903.
C35991.
RefSeqNP_000957.1. NM_000966.5. [P13631-1]
NP_001036193.1. NM_001042728.2. [P13631-2]
NP_001230659.1. NM_001243730.1. [P13631-3]
NP_001230661.1. NM_001243732.1. [P13631-4]
XP_005269113.1. XM_005269056.2. [P13631-1]
XP_005269114.1. XM_005269057.1. [P13631-1]
UniGeneHs.1497.
Hs.733399.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1EXAX-ray1.59A178-423[»]
1EXXX-ray1.67A178-423[»]
1FCXX-ray1.47A183-417[»]
1FCYX-ray1.30A183-417[»]
1FCZX-ray1.38A183-417[»]
1FD0X-ray1.38A183-417[»]
2LBDX-ray2.06A178-423[»]
3LBDX-ray2.40A178-423[»]
4LBDX-ray2.50A178-423[»]
ProteinModelPortalP13631.
SMRP13631. Positions 89-417.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111851. 32 interactions.
IntActP13631. 12 interactions.
MINTMINT-3007936.
STRING9606.ENSP00000332695.

Chemistry

BindingDBP13631.
ChEMBLCHEMBL2363071.
DrugBankDB00459. Acitretin.
DB00210. Adapalene.
DB00523. Alitretinoin.
DB00926. Etretinate.
DB00799. Tazarotene.
DB00755. Tretinoin.
GuidetoPHARMACOLOGY592.

PTM databases

PhosphoSiteP13631.

Polymorphism databases

DMDM133498.

Proteomic databases

MaxQBP13631.
PaxDbP13631.
PRIDEP13631.

Protocols and materials databases

DNASU5916.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000327550; ENSP00000332695; ENSG00000172819. [P13631-3]
ENST00000338561; ENSP00000343698; ENSG00000172819. [P13631-2]
ENST00000394426; ENSP00000377947; ENSG00000172819. [P13631-1]
ENST00000425354; ENSP00000388510; ENSG00000172819. [P13631-1]
ENST00000543726; ENSP00000444335; ENSG00000172819. [P13631-4]
GeneID5916.
KEGGhsa:5916.
UCSCuc001sce.3. human. [P13631-1]
uc010sob.2. human.

Organism-specific databases

CTD5916.
GeneCardsGC12M053604.
H-InvDBHIX0129677.
HGNCHGNC:9866. RARG.
HPAHPA053883.
MIM180190. gene.
neXtProtNX_P13631.
PharmGKBPA34227.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG297448.
HOVERGENHBG005606.
InParanoidP13631.
KOK08529.
OMARSPQPDQ.
OrthoDBEOG738053.
PhylomeDBP13631.
TreeFamTF328382.

Enzyme and pathway databases

ReactomeREACT_71. Gene Expression.
SignaLinkP13631.

Gene expression databases

ArrayExpressP13631.
BgeeP13631.
CleanExHS_RARG.
GenevestigatorP13631.

Family and domain databases

Gene3D1.10.565.10. 1 hit.
3.30.50.10. 1 hit.
InterProIPR008946. Nucl_hormone_rcpt_ligand-bd.
IPR000536. Nucl_hrmn_rcpt_lig-bd_core.
IPR003078. Retinoic_acid_rcpt.
IPR001723. Str_hrmn_rcpt.
IPR001628. Znf_hrmn_rcpt.
IPR013088. Znf_NHR/GATA.
[Graphical view]
PfamPF00104. Hormone_recep. 1 hit.
PF00105. zf-C4. 1 hit.
[Graphical view]
PRINTSPR01292. RETNOICACIDR.
PR00398. STRDHORMONER.
PR00047. STROIDFINGER.
SMARTSM00430. HOLI. 1 hit.
SM00399. ZnF_C4. 1 hit.
[Graphical view]
SUPFAMSSF48508. SSF48508. 1 hit.
PROSITEPS00031. NUCLEAR_REC_DBD_1. 1 hit.
PS51030. NUCLEAR_REC_DBD_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP13631.
GeneWikiRetinoic_acid_receptor_gamma.
GenomeRNAi5916.
NextBio23030.
PROP13631.
SOURCESearch...

Entry information

Entry nameRARG_HUMAN
AccessionPrimary (citable) accession number: P13631
Secondary accession number(s): B7Z492 expand/collapse secondary AC list , B7Z4F1, B7ZAE4, J3KNP6, P22932, Q15281, Q52LZ8, Q9BYX8, Q9H1I3, Q9UJ38
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 1, 1990
Last modified: July 9, 2014
This is version 176 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM