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:
RRP8 (human)

Overview
RRP8 Essential component of the eNoSC (energy-dependent nucleolar silencing) complex, a complex that mediates silencing of rDNA in response to intracellular energy status and acts by recruiting histone-modifying enzymes. The eNoSC complex is able to sense the energy status of cell: upon glucose starvation, elevation of NAD(+)/NADP(+) ratio activates SIRT1, leading to histone H3 deacetylation followed by dimethylation of H3 at 'Lys- 9' (H3K9me2) by SUV39H1 and the formation of silent chromatin in the rDNA locus. In the complex, RRP8 binds to H3K9me2 and probably acts as a methyltransferase. Its substrates are however unknown. Component of the eNoSC complex, composed of SIRT1, SUV39H1 and RRP8. Belongs to the methyltransferase superfamily. RRP8 family. Note: This description may include information from UniProtKB.
Protein type: EC 2.1.1.-
Cellular Component: chromatin silencing complex; nucleolus
Molecular Function: protein binding; S-adenosylmethionine-dependent methyltransferase activity; methylated histone residue binding
Biological Process: chromatin silencing at rDNA; cellular response to glucose starvation; transcription, DNA-dependent; chromatin modification; regulation of transcription by glucose; rRNA processing
Reference #:  O43159 (UniProtKB)
Alt. Names/Synonyms: Cerebral protein 1; KIAA0409; NML; Nucleomethylin; ribosomal RNA processing 8, methyltransferase, homolog (yeast); Ribosomal RNA-processing protein 8; RRP8; RRP8 methyltransferase homolog
Gene Symbols: RRP8
Molecular weight: 50,715 Da
Basal Isoelectric point: 9.51  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

RRP8

Protein Structure Not Found.


STRING  |  Scansite  |  Phospho.ELM  |  NetworKIN  |  Pfam  |  RCSB PDB  |  Phospho3D  |  UniProtKB  |  Entrez-Gene  |  GenPept  |  Ensembl Gene


Modification Sites and Domains  

Modification Sites in Parent Protein, Orthologs, and Isoforms  
 

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

 
0 2 T43-p KRRQLLAtLRALEAA
0 9 S58-p SLSQHPPsLCIsDsE
0 26 S62-p HPPsLCIsDsEEEEE
0 26 S64-p PsLCIsDsEEEEEER
0 11 S104-p QKQGPPCsDsEEEVE
0 10 S106-p QGPPCsDsEEEVERK
0 2 S124-p HKQALVGsDsAEDEK
0 3 S126-p QALVGsDsAEDEKRK
0 4 S171-p TNDPPKQsPGSTsPK
0 5 S176-p KQsPGSTsPKPPHTL
0 1 - gap
0 7 S223-p PTEKTEVsPVPRTDS
0 1 - gap
0 1 S286-p LYHRGFQsQVKKWPL
  mouse

 
T43 KRRHLLATLRALEAA
S58-p SLSQQTPsLPGsDsE
S62-p QTPsLPGsDsEEEEE
S64-p PsLPGsDsEEEEEVG
S105-p QKQAPSIsDSEGKEI
S107 QAPSIsDSEGKEIRR
- gap
S127 APPLGGVSAGEEKGK
S172-p TIDPSKPsPESMsPN
S177-p KPsPESMsPNsSHTL
S180-p PESMsPNsSHTLSRK
- gap
S234-p PKSDSQEsRAGALRA
- gap
  rat

 
T43 KRRHLLATLRALEAA
S58 SLSQQCPSLPGsDsE
S62-p QCPSLPGsDsEEEEE
S64-p PSLPGsDsEEEEEVG
S105 QKQAPFISDSEGKEV
S107 QAPFISDSEGKEVER
- gap
S127 APPLGGISAGEEKGK
S172 TLDPPKSSRESASPN
S177 KSSRESASPNSSHTL
S180 RESASPNSSHTLSRK
- gap
T234 PKSDSQETRAGALRA
- gap
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.