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P13631

- RARG_HUMAN

UniProt

P13631 - RARG_HUMAN

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Protein
Retinoic acid receptor gamma
Gene
RARG, NR1B3
Organism
Homo sapiens (Human)
Status
Reviewed - 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.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi90 – 15566Nuclear receptor
Add
BLAST
Zinc fingeri90 – 11021NR C4-type
Add
BLAST
Zinc fingeri126 – 15025NR C4-type
Add
BLAST

GO - Molecular functioni

  1. DNA binding Source: BHF-UCL
  2. protein binding Source: UniProtKB
  3. retinoic acid receptor activity Source: Ensembl
  4. retinoid X receptor binding Source: BHF-UCL
  5. sequence-specific DNA binding Source: InterPro
  6. sequence-specific DNA binding transcription factor activity Source: BHF-UCL
  7. steroid hormone receptor activity Source: InterPro
  8. zinc ion binding Source: InterPro

GO - Biological processi

  1. Harderian gland development Source: Ensembl
  2. anterior/posterior pattern specification Source: Ensembl
  3. canonical Wnt signaling pathway Source: BHF-UCL
  4. cellular response to retinoic acid Source: Ensembl
  5. embryonic eye morphogenesis Source: BHF-UCL
  6. embryonic hindlimb morphogenesis Source: BHF-UCL
  7. gene expression Source: Reactome
  8. growth plate cartilage chondrocyte growth Source: Ensembl
  9. multicellular organism growth Source: Ensembl
  10. negative regulation of cartilage development Source: Ensembl
  11. negative regulation of cell proliferation Source: BHF-UCL
  12. negative regulation of chondrocyte differentiation Source: Ensembl
  13. negative regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
  14. positive regulation of apoptotic process Source: BHF-UCL
  15. positive regulation of cell proliferation Source: Ensembl
  16. positive regulation of programmed cell death Source: BHF-UCL
  17. positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
  18. prostate gland epithelium morphogenesis Source: Ensembl
  19. regulation of cell size Source: BHF-UCL
  20. regulation of myelination Source: Ensembl
  21. response to retinoic acid Source: BHF-UCL
  22. retinoic acid receptor signaling pathway Source: BHF-UCL
  23. trachea cartilage development Source: Ensembl
  24. transcription initiation from RNA polymerase II promoter 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.
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: Chromosome 12

Organism-specific databases

HGNCiHGNC:9866. RARG.

Subcellular locationi

GO - Cellular componenti

  1. integral component of membrane Source: BHF-UCL
  2. nucleoplasm Source: Reactome
  3. nucleus Source: UniProtKB
  4. transcription factor complex Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA34227.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 454454Retinoic acid receptor gamma
PRO_0000053472Add
BLAST

Proteomic databases

MaxQBiP13631.
PaxDbiP13631.
PRIDEiP13631.

PTM databases

PhosphoSiteiP13631.

Expressioni

Gene expression databases

ArrayExpressiP13631.
BgeeiP13631.
CleanExiHS_RARG.
GenevestigatoriP13631.

Organism-specific databases

HPAiHPA053883.

Interactioni

Subunit structurei

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.

Binary interactionsi

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

Protein-protein interaction databases

BioGridi111851. 32 interactions.
IntActiP13631. 12 interactions.
MINTiMINT-3007936.
STRINGi9606.ENSP00000332695.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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 89-417.

Miscellaneous databases

EvolutionaryTraceiP13631.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 8989Modulating
Add
BLAST
Regioni156 – 20146Hinge
Add
BLAST
Regioni202 – 421220Ligand-binding
Add
BLAST

Domaini

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

Sequence similaritiesi

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiNOG297448.
HOVERGENiHBG005606.
InParanoidiP13631.
KOiK08529.
OMAiRSPQPDQ.
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. Align

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

MATNKERLFA AGALGPGSGY PGAGFPFAFP GALRGSPPFE MLSPSFRGLG    50
QPDLPKEMAS LSVETQSTSS EEMVPSSPSP PPPPRVYKPC FVCNDKSSGY 100
HYGVSSCEGC KGFFRRSIQK NMVYTCHRDK NCIINKVTRN RCQYCRLQKC 150
FEVGMSKEAV RNDRNKKKKE VKEEGSPDSY ELSPQLEELI TKVSKAHQET 200
FPSLCQLGKY TTNSSADHRV QLDLGLWDKF SELATKCIIK IVEFAKRLPG 250
FTGLSIADQI TLLKAACLDI LMLRICTRYT PEQDTMTFSD GLTLNRTQMH 300
NAGFGPLTDL VFAFAGQLLP LEMDDTETGL LSAICLICGD RMDLEEPEKV 350
DKLQEPLLEA LRLYARRRRP SQPYMFPRML MKITDLRGIS TKGAERAITL 400
KMEIPGPMPP LIREMLENPE MFEDDSSQPG PHPNASSEDE VPGGQGKGGL 450
KSPA 454
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.

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.
VSP_044776Add
BLAST
Alternative sequencei1 – 7272Missing in isoform 3.
VSP_044777Add
BLAST
Alternative sequencei1 – 6161MATNK…EMASL → MYDCMETFAPGPRRLYGAAG PGAGLLRRATGGSCFAGLES FAWPQPASLQ in isoform 2.
VSP_031080Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti118 – 1181I → T in CAB60726. 1 Publication
Sequence conflicti172 – 1721K → R in AAG41594. 1 Publication
Sequence conflicti252 – 2521T → A in CAB60726. 1 Publication
Sequence conflicti342 – 3421M → V in BAH12478. 1 Publication
Sequence conflicti421 – 4211M → L in CAB60726. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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

EnsembliENST00000327550; ENSP00000332695; ENSG00000172819. [P13631-3]
ENST00000338561; ENSP00000343698; ENSG00000172819. [P13631-2]
ENST00000394426; ENSP00000377947; ENSG00000172819. [P13631-1]
ENST00000425354; ENSP00000388510; ENSG00000172819. [P13631-1]
ENST00000543726; ENSP00000444335; ENSG00000172819. [P13631-4]
GeneIDi5916.
KEGGihsa:5916.
UCSCiuc001sce.3. human. [P13631-1]
uc010sob.2. human.

Polymorphism databases

DMDMi133498.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Wikipedia

Retinoic acid receptor entry

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS41790.1. [P13631-2 ]
CCDS58236.1. [P13631-3 ]
CCDS58237.1. [P13631-4 ]
CCDS8850.1. [P13631-1 ]
PIRi A33903.
C35991.
RefSeqi NP_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 ]
UniGenei Hs.1497.
Hs.733399.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1EXA X-ray 1.59 A 178-423 [» ]
1EXX X-ray 1.67 A 178-423 [» ]
1FCX X-ray 1.47 A 183-417 [» ]
1FCY X-ray 1.30 A 183-417 [» ]
1FCZ X-ray 1.38 A 183-417 [» ]
1FD0 X-ray 1.38 A 183-417 [» ]
2LBD X-ray 2.06 A 178-423 [» ]
3LBD X-ray 2.40 A 178-423 [» ]
4LBD X-ray 2.50 A 178-423 [» ]
ProteinModelPortali P13631.
SMRi P13631. Positions 89-417.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111851. 32 interactions.
IntActi P13631. 12 interactions.
MINTi MINT-3007936.
STRINGi 9606.ENSP00000332695.

Chemistry

BindingDBi P13631.
ChEMBLi CHEMBL2363071.
DrugBanki DB00459. Acitretin.
DB00210. Adapalene.
DB00523. Alitretinoin.
DB00926. Etretinate.
DB00799. Tazarotene.
DB00755. Tretinoin.
GuidetoPHARMACOLOGYi 592.

PTM databases

PhosphoSitei P13631.

Polymorphism databases

DMDMi 133498.

Proteomic databases

MaxQBi P13631.
PaxDbi P13631.
PRIDEi P13631.

Protocols and materials databases

DNASUi 5916.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000327550 ; ENSP00000332695 ; ENSG00000172819 . [P13631-3 ]
ENST00000338561 ; ENSP00000343698 ; ENSG00000172819 . [P13631-2 ]
ENST00000394426 ; ENSP00000377947 ; ENSG00000172819 . [P13631-1 ]
ENST00000425354 ; ENSP00000388510 ; ENSG00000172819 . [P13631-1 ]
ENST00000543726 ; ENSP00000444335 ; ENSG00000172819 . [P13631-4 ]
GeneIDi 5916.
KEGGi hsa:5916.
UCSCi uc001sce.3. human. [P13631-1 ]
uc010sob.2. human.

Organism-specific databases

CTDi 5916.
GeneCardsi GC12M053604.
H-InvDB HIX0129677.
HGNCi HGNC:9866. RARG.
HPAi HPA053883.
MIMi 180190. gene.
neXtProti NX_P13631.
PharmGKBi PA34227.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG297448.
HOVERGENi HBG005606.
InParanoidi P13631.
KOi K08529.
OMAi RSPQPDQ.
OrthoDBi EOG738053.
PhylomeDBi P13631.
TreeFami TF328382.

Enzyme and pathway databases

Reactomei REACT_15525. Nuclear Receptor transcription pathway.
SignaLinki P13631.

Miscellaneous databases

EvolutionaryTracei P13631.
GeneWikii Retinoic_acid_receptor_gamma.
GenomeRNAii 5916.
NextBioi 23030.
PROi P13631.
SOURCEi Search...

Gene expression databases

ArrayExpressi P13631.
Bgeei P13631.
CleanExi HS_RARG.
Genevestigatori P13631.

Family and domain databases

Gene3Di 1.10.565.10. 1 hit.
3.30.50.10. 1 hit.
InterProi IPR008946. 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 ]
Pfami PF00104. Hormone_recep. 1 hit.
PF00105. zf-C4. 1 hit.
[Graphical view ]
PRINTSi PR01292. RETNOICACIDR.
PR00398. STRDHORMONER.
PR00047. STROIDFINGER.
SMARTi SM00430. HOLI. 1 hit.
SM00399. ZnF_C4. 1 hit.
[Graphical view ]
SUPFAMi SSF48508. SSF48508. 1 hit.
PROSITEi PS00031. NUCLEAR_REC_DBD_1. 1 hit.
PS51030. NUCLEAR_REC_DBD_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: September 3, 2014
This is version 177 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

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