Hmdb loader

Showing Protein Retinoic acid receptor RXR-alpha (HMDBP01926)

IdentificationBiological propertiesGene propertiesProtein propertiesExternal linksReferencesXMLShow 5 metabolites
Identification
HMDB Protein ID HMDBP01926
Secondary Accession Numbers
  • 7334
Name Retinoic acid receptor RXR-alpha
Synonyms
  1. Nuclear receptor subfamily 2 group B member 1
  2. Retinoid X receptor alpha
Gene Name RXRA
Protein Type Enzyme
Biological Properties
General Function Involved in sequence-specific DNA binding transcription factor activity
Specific Function Nuclear hormone receptor. Involved in the retinoic acid response pathway. Binds 9-cis retinoic acid (9C-RA). ARF6 acts as a key regulator of the tissue-specific adipocyte P2 (aP2) enhancer
Pathways Not Available
Reactions Not Available
GO Classification
Component
organelle
membrane-bounded organelle
intracellular membrane-bounded organelle
nucleus
Function
ion binding
cation binding
metal ion binding
binding
transition metal ion binding
zinc ion binding
receptor activity
molecular transducer activity
signal transducer activity
nucleic acid binding
dna binding
sequence-specific dna binding
ligand-dependent nuclear receptor activity
steroid hormone receptor activity
sequence-specific dna binding transcription factor activity
Process
biological regulation
regulation of biological process
regulation of metabolic process
regulation of macromolecule metabolic process
regulation of gene expression
regulation of transcription
regulation of transcription, dna-dependent
Cellular Location
  1. Nucleus
Gene Properties
Chromosome Location Chromosome:9
Locus 9q34.3
SNPs RXRA
Gene Sequence 
>1389 bp
ATGGACACCAAACATTTCCTGCCGCTCGATTTCTCCACCCAGGTGAACTCCTCCCTCACC
TCCCCGACGGGGCGAGGCTCCATGGCTGCCCCCTCGCTGCACCCGTCCCTGGGGCCTGGC
ATCGGCTCCCCGGGACAGCTGCATTCTCCCATCAGCACCCTGAGCTCCCCCATCAACGGC
ATGGGCCCGCCTTTCTCGGTCATCAGCTCCCCCATGGGCCCCCACTCCATGTCGGTGCCC
ACCACACCCACCCTGGGCTTCAGCACTGGCAGCCCCCAGCTCAGCTCACCTATGAACCCC
GTCAGCAGCAGCGAGGACATCAAGCCCCCCCTGGGCCTCAATGGCGTCCTCAAGGTCCCC
GCCCACCCCTCAGGAAACATGGCTTCCTTCACCAAGCACATCTGCGCCATCTGCGGGGAC
CGCTCCTCAGGCAAGCACTATGGAGTGTACAGCTGCGAGGGGTGCAAGGGCTTCTTCAAG
CGGACGGTGCGCAAGGACCTGACCTACACCTGCCGCGACAACAAGGACTGCCTGATTGAC
AAGCGGCAGCGGAACCGGTGCCAGTACTGCCGCTACCAGAAGTGCCTGGCCATGGGCATG
AAGCGGGAAGCCGTGCAGGAGGAGCGGCAGCGTGGCAAGGACCGGAACGAGAATGAGGTG
GAGTCGACCAGCAGCGCCAACGAGGACATGCCGGTGGAGAGGATCCTGGAGGCTGAGCTG
GCCGTGGAGCCCAAGACCGAGACCTACGTGGAGGCAAACATGGGGCTGAACCCCAGCTCG
CCGAACGACCCTGTCACCAACATTTGCCAAGCAGCCGACAAACAGCTTTTCACCCTGGTG
GAGTGGGCCAAGCGGATCCCACACTTCTCAGAGCTGCCCCTGGACGACCAGGTCATCCTG
CTGCGGGCAGGCTGGAATGAGCTGCTCATCGCCTCCTTCTCCCACCGCTCCATCGCCGTG
AAGGACGGGATCCTCCTGGCCACCGGGCTGCACGTCCACCGGAACAGCGCCCACAGCGCA
GGGGTGGGCGCCATCTTTGACAGGGTGCTGACGGAGCTTGTGTCCAAGATGCGGGACATG
CAGATGGACAAGACGGAGCTGGGCTGCCTGCGCGCCATCGTCCTCTTTAACCCTGACTCC
AAGGGGCTCTCGAACCCGGCCGAGGTGGAGGCGCTGAGGGAGAAGGTCTATGCGTCCTTG
GAGGCCTACTGCAAGCACAAGTACCCAGAGCAGCCGGGAAGGTTCGCTAAGCTCTTGCTC
CGCCTGCCGGCTCTGCGCTCCATCGGGCTCAAATGCCTGGAACATCTCTTCTTCTTCAAG
CTCATCGGGGACACACCCATTGACACCTTCCTTATGGAGATGCTGGAGGCGCCGCACCAA
ATGACTTAG
Protein Properties
Number of Residues 462
Molecular Weight 50810.8
Theoretical pI 7.86
Pfam Domain Function
Signals
  • None
Transmembrane Regions
  • None
Protein Sequence 
>Retinoic acid receptor RXR-alpha
MDTKHFLPLDFSTQVNSSLTSPTGRGSMAAPSLHPSLGPGIGSPGQLHSPISTLSSPING
MGPPFSVISSPMGPHSMSVPTTPTLGFSTGSPQLSSPMNPVSSSEDIKPPLGLNGVLKVP
AHPSGNMASFTKHICAICGDRSSGKHYGVYSCEGCKGFFKRTVRKDLTYTCRDNKDCLID
KRQRNRCQYCRYQKCLAMGMKREAVQEERQRGKDRNENEVESTSSANEDMPVERILEAEL
AVEPKTETYVEANMGLNPSSPNDPVTNICQAADKQLFTLVEWAKRIPHFSELPLDDQVIL
LRAGWNELLIASFSHRSIAVKDGILLATGLHVHRNSAHSAGVGAIFDRVLTELVSKMRDM
QMDKTELGCLRAIVLFNPDSKGLSNPAEVEALREKVYASLEAYCKHKYPEQPGRFAKLLL
RLPALRSIGLKCLEHLFFFKLIGDTPIDTFLMEMLEAPHQMT
GenBank ID Protein 35885
UniProtKB/Swiss-Prot ID P19793
UniProtKB/Swiss-Prot Entry Name RXRA_HUMAN
PDB IDs
GenBank Gene ID X52773
GeneCard ID RXRA
GenAtlas ID RXRA
HGNC ID HGNC:10477
References
General References
  1. Chen H, Lin RJ, Schiltz RL, Chakravarti D, Nash A, Nagy L, Privalsky ML, Nakatani Y, Evans RM: Nuclear receptor coactivator ACTR is a novel histone acetyltransferase and forms a multimeric activation complex with P/CAF and CBP/p300. Cell. 1997 Aug 8;90(3):569-80. [PubMed:9267036 ]
  2. Lee SK, Anzick SL, Choi JE, Bubendorf L, Guan XY, Jung YK, Kallioniemi OP, Kononen J, Trent JM, Azorsa D, Jhun BH, Cheong JH, Lee YC, Meltzer PS, Lee JW: A nuclear factor, ASC-2, as a cancer-amplified transcriptional coactivator essential for ligand-dependent transactivation by nuclear receptors in vivo. J Biol Chem. 1999 Nov 26;274(48):34283-93. [PubMed:10567404 ]
  3. Bu H, Kashireddy P, Chang J, Zhu YT, Zhang Z, Zheng W, Rao SM, Zhu YJ: ERBP, a novel estrogen receptor binding protein enhancing the activity of estrogen receptor. Biochem Biophys Res Commun. 2004 Apr 23;317(1):54-9. [PubMed:15047147 ]
  4. Mangelsdorf DJ, Ong ES, Dyck JA, Evans RM: Nuclear receptor that identifies a novel retinoic acid response pathway. Nature. 1990 May 17;345(6272):224-9. [PubMed:2159111 ]
  5. Heyman RA, Mangelsdorf DJ, Dyck JA, Stein RB, Eichele G, Evans RM, Thaller C: 9-cis retinoic acid is a high affinity ligand for the retinoid X receptor. Cell. 1992 Jan 24;68(2):397-406. [PubMed:1310260 ]
  6. Mathur M, Tucker PW, Samuels HH: PSF is a novel corepressor that mediates its effect through Sin3A and the DNA binding domain of nuclear hormone receptors. Mol Cell Biol. 2001 Apr;21(7):2298-311. [PubMed:11259580 ]
  7. Takano Y, Adachi S, Okuno M, Muto Y, Yoshioka T, Matsushima-Nishiwaki R, Tsurumi H, Ito K, Friedman SL, Moriwaki H, Kojima S, Okano Y: The RING finger protein, RNF8, interacts with retinoid X receptor alpha and enhances its transcription-stimulating activity. J Biol Chem. 2004 Apr 30;279(18):18926-34. Epub 2004 Feb 23. [PubMed:14981089 ]
  8. Singh RR, Gururaj AE, Vadlamudi RK, Kumar R: 9-cis-retinoic acid up-regulates expression of transcriptional coregulator PELP1, a novel coactivator of the retinoid X receptor alpha pathway. J Biol Chem. 2006 Jun 2;281(22):15394-404. Epub 2006 Mar 30. [PubMed:16574651 ]
  9. Choi SJ, Chung SS, Rho EJ, Lee HW, Lee MH, Choi HS, Seol JH, Baek SH, Bang OS, Chung CH: Negative modulation of RXRalpha transcriptional activity by small ubiquitin-related modifier (SUMO) modification and its reversal by SUMO-specific protease SUSP1. J Biol Chem. 2006 Oct 13;281(41):30669-77. Epub 2006 Aug 15. [PubMed:16912044 ]
  10. Lee MS, Sem DS, Kliewer SA, Provencal J, Evans RM, Wright PE: NMR assignments and secondary structure of the retinoid X receptor alpha DNA-binding domain. Evidence for the novel C-terminal helix. Eur J Biochem. 1994 Sep 1;224(2):639-50. [PubMed:7925381 ]
  11. Rastinejad F, Perlmann T, Evans RM, Sigler PB: Structural determinants of nuclear receptor assembly on DNA direct repeats. Nature. 1995 May 18;375(6528):203-11. [PubMed:7746322 ]
  12. Bourguet W, Ruff M, Chambon P, Gronemeyer H, Moras D: Crystal structure of the ligand-binding domain of the human nuclear receptor RXR-alpha. Nature. 1995 Jun 1;375(6530):377-82. [PubMed:7760929 ]
  13. Holmbeck SM, Foster MP, Casimiro DR, Sem DS, Dyson HJ, Wright PE: High-resolution solution structure of the retinoid X receptor DNA-binding domain. J Mol Biol. 1998 Aug 14;281(2):271-84. [PubMed:9698548 ]