Javascript is not enabled on this browser. This site will not work properly without Javascript.
PhosphoSitePlus Homepage Cell Signaling Technology
PhosphoSitePlus
HomeAbout PhosphoSiteUsing PhosphoSiteCuration ProcessContact
NIH-logos NIGMS Logo NIAAA Logo NCI Logo NIH Logo
Protein Page:
RARA (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitination
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
RARA is a receptor for retinoic acid, a potent mammalian morphogen and teratogen that has profound effects on vertebrate development. RARA is a member of the nuclear receptor superfamily. Controls cell function by directly regulating gene expression. Its phosphorylation is crucial for transcriptional activity. Aberrations involving RARA may be a cause of acute promyelocytic leukemia. Two splice-variant isoforms have been described. Note: This description may include information from UniProtKB.
Protein type: Nuclear receptor; Transcription factor; DNA binding protein
Cellular Component: nucleoplasm; cell surface; cell soma; perinuclear region of cytoplasm; cytoplasm; dendrite; nuclear chromatin; nucleus
Molecular Function: protein domain specific binding; protein kinase B binding; retinoic acid binding; zinc ion binding; chromatin DNA binding; translation repressor activity, nucleic acid binding; transcription coactivator activity; phosphoinositide 3-kinase regulator activity; drug binding; transcription factor binding; protein binding; enzyme binding; sequence-specific DNA binding; protein heterodimerization activity; protein kinase A binding; steroid hormone receptor activity; mRNA 5'-UTR binding; retinoic acid receptor activity; transcription corepressor activity; transcription factor activity; receptor binding
Biological Process: prostate gland development; retinoic acid receptor signaling pathway; negative regulation of translational initiation; regulation of myelination; estrogen receptor signaling pathway; positive regulation of transcription, DNA-dependent; ventricular cardiac muscle cell differentiation; regulation of synaptic plasticity; negative regulation of transcription from RNA polymerase II promoter; female pregnancy; signal transduction; protein amino acid phosphorylation; regulation of phosphoinositide 3-kinase activity; response to estradiol stimulus; response to vitamin A; germ cell development; negative regulation of granulocyte differentiation; positive regulation of interleukin-4 production; regulation of apoptosis; negative regulation of cell proliferation; Sertoli cell fate commitment; positive regulation of T-helper 2 cell differentiation; ureteric bud development; negative regulation of interferon-gamma production; positive regulation of cell proliferation; positive regulation of interleukin-13 production; positive regulation of interleukin-5 production; transcription initiation from RNA polymerase II promoter; response to retinoic acid; multicellular organism growth; positive regulation of cell cycle; positive regulation of binding; negative regulation of tumor necrosis factor production; liver development; positive regulation of phosphoinositide 3-kinase cascade; positive regulation of protein kinase B signaling cascade; response to ethanol; response to cytokine stimulus; spermatogenesis; gene expression; steroid hormone mediated signaling; positive regulation of transcription from RNA polymerase II promoter; negative regulation of transcription, DNA-dependent; positive regulation of neuron differentiation; apoptotic cell clearance
Reference #:  P10276 (UniProtKB)
Alt. Names/Synonyms: NR1B1; Nuclear receptor subfamily 1 group B member 1; nucleophosmin-retinoic acid receptor alpha fusion protein NPM-RAR long form; RAR; RAR-alpha; RARA; Retinoic acid receptor alpha; retinoic acid receptor, alpha; Retinoic acid receptor, alpha polypeptide
Gene Symbols: RARA
Molecular weight: 50,771 Da
Basal Isoelectric point: 8.21  Predict pI for various phosphorylation states
CST Pathways:  Regulation of P38 MAPKs  |  Wnt/├č-Catenin Signaling
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

RARA

Protein Structure Not Found.


STRING  |  Reactome  |  neXtProt  |  Protein Atlas  |  BioGPS  |  DISEASE  |  Scansite  |  Pfam  |  RCSB PDB  |  Phospho3D  |  Phospho.ELM  |  NetworKIN  |  Source  |  UCSD-Nature  |  GeneCards  |  UniProtKB  |  Entrez-Gene  |  Ensembl Gene  |  NURSA


Sites Implicated In
transcription, altered: S77‑p
transcription, inhibited: S77‑p, S96‑p, S219‑p, S369‑p
activity, induced: S77‑p
activity, inhibited: S96‑p, S219‑p, S369‑p
intracellular localization: S219‑p, S369‑p
molecular association, regulation: S77‑p, S219‑p, S369‑p
protein conformation: S77‑p, S369‑p
protein degradation: S77‑p, T181‑p, S445‑p, S461‑p
ubiquitination: T181‑p, S445‑p, S461‑p

Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

 
8 1 S77-p EIVPSPPsPPPLPRI
1 0 S96-p FVCQDKSsGYHYGVS
1 0 K109 VSACEGCKGFFRRSI
1 0 K166-sm RNDRNKKkKEVPkPE
1 0 K171 KKkKEVPKPECSESY
1 0 K171-sm KKkKEVPkPECSESY
0 1 Y178 kPECSESYTLtPEVG
2 0 T181-p CSESYTLtPEVGELI
1 0 S219-p NSSEQRVsLDIDLWD
2 0 R347 QDLEQPDRVDMLQEP
7 0 S369-p YVRKRRPsRPHMFPK
1 0 K399-sm AERVITLkMEIPGsM
0 1 S405-p LkMEIPGsMPPLIQE
3 0 S445-p APPPGSCsPSLSPSS
1 0 S449 GSCsPSLSPSSNRSS
1 0 S456 SPSSNRSSPATHsP_
3 0 S461-p RSSPATHsP______
  mouse

 
S77-p EIVPSPPsPPPLPRI
S96 FVCQDKSSGYHYGVS
K109-me VSACEGCkGFFRRSI
K166 RNDRNKKKKEAPkPE
K171-me KKKKEAPkPECSESy
K171 KKKKEAPKPECSESy
Y178-p kPECSESyTLTPEVG
T181 CSESyTLTPEVGELI
S219 NSSEQRVSLDIDLWD
K347-m3 QDLEQPDkVDMLQEP
S369-p YVRKRRPsRPHMFPK
K399 AERVITLKMEIPGSM
S405 LKMEIPGSMPPLIQE
S445-p APPPGSCsPSLsPSS
S449-p GSCsPSLsPSSHRSs
S456-p sPSSHRSsPATQsP_
S461-p RSsPATQsP______
  rat

 
S74 EIVPSPPSPPPLPRI
S93 FVCQDKSSGYHYGVS
K106 VSACEGCKGFFRRSI
K163 RNDRNKKKKETPKPE
K168 KKKKETPKPECSESY
K168 KKKKETPKPECSESY
Y175 KPECSESYTLTPEVG
T178 CSESYTLTPEVGELI
S216 NSSEQRVSLDIDLWD
K344 QDLEQPDKVDMLQEP
S366 YVRKRRPSRPHMFPK
K396 AERVITLKMEIPGSM
S402 LKMEIPGSMPPLIQE
S442 APPPGSCSPSLSPSS
S446 GSCSPSLSPSSHRSS
S453 SPSSHRSSPATQSP_
S458 RSSPATQSP______
Home  |  Curator Login With enhanced literature mining using Linguamatics I2E I2E Logo Produced by 3rd Millennium  |  Design by Digizyme
©2003-2013 Cell Signaling Technology, Inc.