P19793

PTMD Annotation Information


※ Protein Information

Tag Content
UniProt Accession RXRA_HUMAN; P19793;
Entrez ID 6256
GenBank Protein ID NM_001291921.1; NM_002957.5;
GenBank Nucleotide ID NP_001278850.1; NP_002948.1;
Protein Name Retinoic acid receptor RXR-alpha (Nuclear receptor subfamily 2 group B member 1) (Retinoid X receptor alpha)
Gene Name RXRA; NR2B1
Organism Homo sapiens
NCBI Taxa ID 9606
Functional DescriptionReceptor 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. The high affinity ligand for RXRs is 9-cis retinoic acid. RXRA serves as a common heterodimeric partner for a number of nuclear receptors. In the absence of ligand, the RXR-RAR heterodimers associate with a multiprotein complex containing transcription corepressors that induce histone acetylation, chromatin condensation and transcriptional suppression. On ligand binding, the corepressors dissociate from the receptors and associate with the coactivators leading to transcriptional activation. The RXRA/PPARA heterodimer is required for PPARA transcriptional activity on fatty acid oxidation genes such as ACOX1 and the P450 system genes.
Sequence
(Fasta)
MDTKHFLPLD FSTQVNSSLT SPTGRGSMAA PSLHPSLGPG IGSPGQLHSP ISTLSSPING 60
MGPPFSVISS PMGPHSMSVP TTPTLGFSTG SPQLSSPMNP VSSSEDIKPP LGLNGVLKVP 120
AHPSGNMASF TKHICAICGD RSSGKHYGVY SCEGCKGFFK RTVRKDLTYT CRDNKDCLID 180
KRQRNRCQYC RYQKCLAMGM KREAVQEERQ RGKDRNENEV ESTSSANEDM PVERILEAEL 240
AVEPKTETYV EANMGLNPSS PNDPVTNICQ AADKQLFTLV EWAKRIPHFS ELPLDDQVIL 300
LRAGWNELLI ASFSHRSIAV KDGILLATGL HVHRNSAHSA GVGAIFDRVL TELVSKMRDM 360
QMDKTELGCL RAIVLFNPDS KGLSNPAEVE ALREKVYASL EAYCKHKYPE QPGRFAKLLL 420
RLPALRSIGL KCLEHLFFFK LIGDTPIDTF LMEMLEAPHQ MT 463

※ PTM-Disease Association

NumPTMDiseaseCell TypeTypePTM SitePMID
1Serine PhosphorylationHepatocellular carcinoma/Hepatocarcinoma/HepatomaHuH7 cellUS26011826406
[Reference]: In conclusion, switching of the ubiquitin/proteasome-dependent degradation of RXRalpha by phosphorylation at serine 260 may be responsible for the aberrant growth of HCC and its suppression by retinoids.

※ Disease Cross-ref Annotation

DatabaseAnnotation
CTD (Curated)
(count: 5)
MESH:C531617 ; Amyotrophic lateral sclerosis 1
MESH:C562839 ; Mesothelioma, Malignant
MESH:D011471 ; Prostatic Neoplasms
MESH:D020426 ; Sciatic Neuropathy
MESH:D013964 ; Thyroid Neoplasms
GWASdb
(count: 17)
(view all)
rs4917350; Urinary metabolites; kidney disease
rs4917352; Urinary metabolites; kidney disease
rs12351482; Smoking initiation; nicotine dependence
rs34312136; Intelligence; attention deficit hyperactivity disorder|cognitive disorder
rs34090729; Cholesterol, total; coronary artery disease|lipid metabolism disorder|arteriosclerosis
rs34090729; Triglycerides; coronary artery disease|lipid metabolism disorder|arteriosclerosis

※ PTM Sites

PTM Modification Sites
Phosphorylation
(count: 20)
(view all)
12        HFLPLDFSTQVNSSL     dbPAF
129       HPSGNMASFTKHICA     dbPAF
147       DRSSGKHYGVYSCEG     dbPAF
150       SGKHYGVYSCEGCKG     dbPAF
17        DFSTQVNSSLTSPTG     dbPAF
20        TQVNSSLTSPTGRGS     dbPAF
Acetylation
(count: 2)
145       CGDRSSGKHYGVYSC     PLMD
417       EQPGRFAKLLLRLPA     PLMD
Ubiquitination
(count: 3)
356       VLTELVSKMRDMQMD     PLMD
364       MRDMQMDKTELGCLR     PLMD
417       EQPGRFAKLLLRLPA     PLMD
Sumoylation
(count: 1)
108       VSSSEDIKPPLGLNG     PLMD

※ Protein-Protein Interaction

NetworkInteraction
ABSource