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Protein

Retinoic acid receptor gamma

Gene

RARG

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

Functioni

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).By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi90 – 15566Nuclear receptorPROSITE-ProRule annotationAdd
BLAST
Zinc fingeri90 – 11021NR C4-typePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri126 – 15025NR C4-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. DNA binding Source: BHF-UCL
  2. retinoic acid receptor activity Source: Ensembl
  3. retinoid X receptor binding Source: BHF-UCL
  4. RNA polymerase II regulatory region sequence-specific DNA binding Source: Ensembl
  5. sequence-specific DNA binding transcription factor activity Source: BHF-UCL
  6. steroid hormone receptor activity Source: InterPro
  7. zinc ion binding Source: InterPro

GO - Biological processi

  1. anterior/posterior pattern specification Source: Ensembl
  2. canonical Wnt signaling pathway Source: BHF-UCL
  3. cellular response to retinoic acid Source: Ensembl
  4. embryonic camera-type eye development Source: Ensembl
  5. embryonic eye morphogenesis Source: BHF-UCL
  6. embryonic hindlimb morphogenesis Source: BHF-UCL
  7. face development Source: Ensembl
  8. gene expression Source: Reactome
  9. glandular epithelial cell development Source: Ensembl
  10. growth plate cartilage chondrocyte growth Source: Ensembl
  11. Harderian gland development Source: Ensembl
  12. multicellular organism growth Source: Ensembl
  13. negative regulation of apoptotic process Source: Ensembl
  14. negative regulation of cell proliferation Source: BHF-UCL
  15. negative regulation of chondrocyte differentiation Source: Ensembl
  16. negative regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
  17. neural tube closure Source: Ensembl
  18. positive regulation of apoptotic process Source: BHF-UCL
  19. positive regulation of cell proliferation Source: Ensembl
  20. positive regulation of programmed cell death Source: BHF-UCL
  21. positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
  22. prostate gland epithelium morphogenesis Source: Ensembl
  23. regulation of cell size Source: BHF-UCL
  24. regulation of myelination Source: Ensembl
  25. response to retinoic acid Source: BHF-UCL
  26. retinal pigment epithelium development Source: Ensembl
  27. retinoic acid receptor signaling pathway Source: BHF-UCL
  28. trachea cartilage development Source: Ensembl
  29. transcription initiation from RNA polymerase II promoter Source: Reactome
  30. transmembrane transport Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Receptor

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding, Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_15525. Nuclear Receptor transcription pathway.
REACT_267785. Signaling by Retinoic Acid.
REACT_268444. Orphan transporters.
SignaLinkiP13631.

Names & Taxonomyi

Protein namesi
Recommended name:
Retinoic acid receptor gamma
Short name:
RAR-gamma
Alternative name(s):
Nuclear receptor subfamily 1 group B member 3
Gene namesi
Name:RARG
Synonyms:NR1B3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 12

Organism-specific databases

HGNCiHGNC:9866. RARG.

Subcellular locationi

GO - Cellular componenti

  1. integral component of membrane Source: BHF-UCL
  2. nuclear chromatin Source: Ensembl
  3. nucleoplasm Source: HPA
  4. nucleus Source: UniProtKB
  5. transcription factor complex Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA34227.

Chemistry

DrugBankiDB00459. Acitretin.
DB00210. Adapalene.
DB00523. Alitretinoin.
DB00799. Tazarotene.
DB00755. Tretinoin.

Polymorphism and mutation databases

BioMutaiRARG.
DMDMi133498.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 454454Retinoic acid receptor gammaPRO_0000053472Add
BLAST

Proteomic databases

MaxQBiP13631.
PaxDbiP13631.
PRIDEiP13631.

PTM databases

PhosphoSiteiP13631.

Expressioni

Gene expression databases

BgeeiP13631.
CleanExiHS_RARG.
ExpressionAtlasiP13631. baseline and differential.
GenevestigatoriP13631.

Organism-specific databases

HPAiHPA053883.

Interactioni

Subunit structurei

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

Binary interactionsi

WithEntry#Exp.IntActNotes
SORBS3O60504-22EBI-2568901,EBI-1222956

Protein-protein interaction databases

BioGridi111851. 32 interactions.
IntActiP13631. 16 interactions.
MINTiMINT-3007936.
STRINGi9606.ENSP00000332695.

Structurei

Secondary structure

1
454
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi184 – 20017Combined sources
Helixi204 – 2063Combined sources
Helixi224 – 24623Combined sources
Helixi251 – 2533Combined sources
Helixi256 – 27722Combined sources
Turni281 – 2844Combined sources
Beta strandi285 – 2873Combined sources
Beta strandi292 – 2954Combined sources
Helixi296 – 3027Combined sources
Helixi305 – 3073Combined sources
Helixi308 – 31811Combined sources
Helixi319 – 3213Combined sources
Helixi325 – 33612Combined sources
Helixi347 – 36822Combined sources
Helixi375 – 40127Combined sources
Beta strandi404 – 4063Combined sources
Helixi410 – 4167Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP13631.
SMRiP13631. Positions 89-419.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP13631.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 8989ModulatingAdd
BLAST
Regioni156 – 20146HingeAdd
BLAST
Regioni202 – 421220Ligand-bindingAdd
BLAST

Domaini

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

Sequence similaritiesi

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

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri90 – 11021NR C4-typePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri126 – 15025NR C4-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiNOG297448.
GeneTreeiENSGT00780000121834.
HOVERGENiHBG005606.
InParanoidiP13631.
KOiK08529.
OMAiYEMTPEL.
OrthoDBiEOG738053.
PhylomeDBiP13631.
TreeFamiTF328382.

Family and domain databases

Gene3Di1.10.565.10. 1 hit.
3.30.50.10. 1 hit.
InterProiIPR008946. 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]
PfamiPF00104. Hormone_recep. 1 hit.
PF00105. zf-C4. 1 hit.
[Graphical view]
PRINTSiPR01292. RETNOICACIDR.
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 splicing. AlignAdd to basket

Note: Isoforms differ only in their N-terminal regions.

Isoform 1 (identifier: P13631-1) [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
MATNKERLFA AGALGPGSGY PGAGFPFAFP GALRGSPPFE MLSPSFRGLG
60 70 80 90 100
QPDLPKEMAS LSVETQSTSS EEMVPSSPSP PPPPRVYKPC FVCNDKSSGY
110 120 130 140 150
HYGVSSCEGC KGFFRRSIQK NMVYTCHRDK NCIINKVTRN RCQYCRLQKC
160 170 180 190 200
FEVGMSKEAV RNDRNKKKKE VKEEGSPDSY ELSPQLEELI TKVSKAHQET
210 220 230 240 250
FPSLCQLGKY TTNSSADHRV QLDLGLWDKF SELATKCIIK IVEFAKRLPG
260 270 280 290 300
FTGLSIADQI TLLKAACLDI LMLRICTRYT PEQDTMTFSD GLTLNRTQMH
310 320 330 340 350
NAGFGPLTDL VFAFAGQLLP LEMDDTETGL LSAICLICGD RMDLEEPEKV
360 370 380 390 400
DKLQEPLLEA LRLYARRRRP SQPYMFPRML MKITDLRGIS TKGAERAITL
410 420 430 440 450
KMEIPGPMPP LIREMLENPE MFEDDSSQPG PHPNASSEDE VPGGQGKGGL

KSPA
Length:454
Mass (Da):50,342
Last modified:January 1, 1990 - v1
Checksum:i1EE27B22772D4AFD
GO
Isoform 2 (identifier: P13631-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-61: MATNKERLFA...PDLPKEMASL → MYDCMETFAP...FAWPQPASLQ

Show »
Length:443
Mass (Da):49,308
Checksum:i4D709194F5111E86
GO
Isoform 3 (identifier: P13631-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-72: Missing.

Note: No experimental confirmation available.

Show »
Length:382
Mass (Da):42,926
Checksum:i37AF909319A4B140
GO
Isoform 4 (identifier: P13631-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-111: MATNKERLFA...YGVSSCEGCK → MLALPLPPCW...LPGRNPPACN

Note: No experimental confirmation available.

Show »
Length:432
Mass (Da):47,931
Checksum:iAA332A06D720ADB8
GO

Sequence cautioni

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

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti118 – 1181I → T in CAB60726 (Ref. 10) Curated
Sequence conflicti172 – 1721K → R in AAG41594 (Ref. 11) Curated
Sequence conflicti252 – 2521T → A in CAB60726 (Ref. 10) Curated
Sequence conflicti342 – 3421M → V in BAH12478 (PubMed:14702039).Curated
Sequence conflicti421 – 4211M → L in CAB60726 (Ref. 10) Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti427 – 4271S → L.
Corresponds to variant rs2229774 [ dbSNP | Ensembl ].
VAR_038554
Natural varianti430 – 4301G → S in a breast cancer sample; somatic mutation. 1 Publication
VAR_036061

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 111111MATNK…CEGCK → MLALPLPPCWSGAPPGEEGE SAAGPWCFQHPVSLQAGSRC TTVWKRLPRVRDGCTGRPGP GPACCAEPPAAPVSPDLNLL PGRNPPACN in isoform 4. 1 PublicationVSP_044776Add
BLAST
Alternative sequencei1 – 7272Missing in isoform 3. 1 PublicationVSP_044777Add
BLAST
Alternative sequencei1 – 6161MATNK…EMASL → MYDCMETFAPGPRRLYGAAG PGAGLLRRATGGSCFAGLES FAWPQPASLQ in isoform 2. 2 PublicationsVSP_031080Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS41790.1. [P13631-2]
CCDS58236.1. [P13631-3]
CCDS58237.1. [P13631-4]
CCDS8850.1. [P13631-1]
PIRiA33903.
C35991.
RefSeqiNP_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]
UniGeneiHs.1497.
Hs.733399.

Genome annotation databases

EnsembliENST00000338561; ENSP00000343698; ENSG00000172819. [P13631-2]
ENST00000394426; ENSP00000377947; ENSG00000172819. [P13631-3]
ENST00000425354; ENSP00000388510; ENSG00000172819. [P13631-1]
ENST00000543726; ENSP00000444335; ENSG00000172819. [P13631-4]
GeneIDi5916.
KEGGihsa:5916.
UCSCiuc001sce.3. human. [P13631-1]
uc010sob.2. human.

Polymorphism and mutation databases

BioMutaiRARG.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Wikipedia

Retinoic acid receptor entry

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS41790.1. [P13631-2]
CCDS58236.1. [P13631-3]
CCDS58237.1. [P13631-4]
CCDS8850.1. [P13631-1]
PIRiA33903.
C35991.
RefSeqiNP_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]
UniGeneiHs.1497.
Hs.733399.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP13631.
SMRiP13631. Positions 89-419.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111851. 32 interactions.
IntActiP13631. 16 interactions.
MINTiMINT-3007936.
STRINGi9606.ENSP00000332695.

Chemistry

BindingDBiP13631.
ChEMBLiCHEMBL2363071.
DrugBankiDB00459. Acitretin.
DB00210. Adapalene.
DB00523. Alitretinoin.
DB00799. Tazarotene.
DB00755. Tretinoin.
GuidetoPHARMACOLOGYi592.

PTM databases

PhosphoSiteiP13631.

Polymorphism and mutation databases

BioMutaiRARG.
DMDMi133498.

Proteomic databases

MaxQBiP13631.
PaxDbiP13631.
PRIDEiP13631.

Protocols and materials databases

DNASUi5916.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000338561; ENSP00000343698; ENSG00000172819. [P13631-2]
ENST00000394426; ENSP00000377947; ENSG00000172819. [P13631-3]
ENST00000425354; ENSP00000388510; ENSG00000172819. [P13631-1]
ENST00000543726; ENSP00000444335; ENSG00000172819. [P13631-4]
GeneIDi5916.
KEGGihsa:5916.
UCSCiuc001sce.3. human. [P13631-1]
uc010sob.2. human.

Organism-specific databases

CTDi5916.
GeneCardsiGC12M053604.
H-InvDBHIX0129677.
HGNCiHGNC:9866. RARG.
HPAiHPA053883.
MIMi180190. gene.
neXtProtiNX_P13631.
PharmGKBiPA34227.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG297448.
GeneTreeiENSGT00780000121834.
HOVERGENiHBG005606.
InParanoidiP13631.
KOiK08529.
OMAiYEMTPEL.
OrthoDBiEOG738053.
PhylomeDBiP13631.
TreeFamiTF328382.

Enzyme and pathway databases

ReactomeiREACT_15525. Nuclear Receptor transcription pathway.
REACT_267785. Signaling by Retinoic Acid.
REACT_268444. Orphan transporters.
SignaLinkiP13631.

Miscellaneous databases

ChiTaRSiRARG. human.
EvolutionaryTraceiP13631.
GeneWikiiRetinoic_acid_receptor_gamma.
GenomeRNAii5916.
NextBioi23030.
PROiP13631.
SOURCEiSearch...

Gene expression databases

BgeeiP13631.
CleanExiHS_RARG.
ExpressionAtlasiP13631. baseline and differential.
GenevestigatoriP13631.

Family and domain databases

Gene3Di1.10.565.10. 1 hit.
3.30.50.10. 1 hit.
InterProiIPR008946. 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]
PfamiPF00104. Hormone_recep. 1 hit.
PF00105. zf-C4. 1 hit.
[Graphical view]
PRINTSiPR01292. RETNOICACIDR.
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. 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.
    , 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.
    , 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. 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. Cited for: VARIANT [LARGE SCALE ANALYSIS] SER-430.

Entry informationi

Entry nameiRARG_HUMAN
AccessioniPrimary (citable) accession number: P13631
Secondary accession number(s): B7Z492
, B7Z4F1, B7ZAE4, J3KNP6, P22932, Q15281, Q52LZ8, Q9BYX8, Q9H1I3, Q9UJ38
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 1, 1990
Last modified: April 29, 2015
This is version 185 of the entry and version 1 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 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. 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.