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Protein Page:
RRP8 (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
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; cytoplasm; plasma membrane; nucleolus; nucleus
Molecular Function: protein binding; S-adenosylmethionine-dependent methyltransferase activity; methylated histone residue binding
Biological Process: methylation; 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.


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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

 
0 2 T43-p KRRQLLAtLRALEAA
0 10 S58-p SLSQHPPsLCIsDsE
0 27 S62-p HPPsLCIsDsEEEEE
0 27 S64-p PsLCIsDsEEEEEER
0 1 K78-ac RKKKCPKkAsFAsAS
0 1 S80-p KKCPKkAsFAsASAE
0 1 S83-p PKkAsFAsASAEVGK
0 12 S104-p QKQGPPCsDsEEEVE
0 11 S106-p QGPPCsDsEEEVERK
0 2 S124-p HKQALVGsDsAEDEK
0 4 S126-p QALVGsDsAEDEKRK
0 2 S162-p GPKAWKGstTNDPPK
0 2 T163-p PKAWKGstTNDPPKQ
0 1 T164 KAWKGstTNDPPKQs
0 6 S171-p TNDPPKQsPGstsPK
0 2 S174-p PPKQsPGstsPKPPH
0 1 T175-p PKQsPGstsPKPPHT
0 7 S176-p KQsPGstsPKPPHTL
0 2 - gap
0 8 S223-p PTEKTEVsPVPRTDS
0 1 - gap
0 2 S286-p LYHRGFQsQVKKWPL
  mouse

 
T43 KRRHLLATLRALEAA
S58-p SLSQQTPsLPGsDsE
S62-p QTPsLPGsDsEEEEE
S64-p PsLPGsDsEEEEEVG
R79 RKKRHLQRPSLASVS
S81 KRHLQRPSLASVSKE
S84 LQRPSLASVSKEVGK
S105-p QKQAPSIsDSEGKEI
S107 QAPSIsDSEGKEIRR
- gap
S127 APPLGGVSAGEEKGK
S162-p TVHNSRTstAtIDPS
T163-p VHNSRTstAtIDPSK
T165-p NSRTstAtIDPSKPs
S172-p tIDPSKPsPEsMsPN
S175-p PSKPsPEsMsPNsSH
- gap
S177-p KPsPEsMsPNsSHTL
S180-p PEsMsPNsSHTLSRK
- gap
S234-p PKSDSQEsRAGALRA
- gap
  rat

 
T43 KRRHLLATLRALEAA
S58 SLSQQCPSLPGsDsE
S62-p QCPSLPGsDsEEEEE
S64-p PSLPGsDsEEEEEVG
R79 RKKRHFQRSSLANVS
S81 KRHFQRSSLANVSKE
- gap
S105 QKQAPFISDSEGKEV
S107 QAPFISDSEGKEVER
- gap
S127 APPLGGISAGEEKGK
S162 TVHNSRTSTATLDPP
T163 VHNSRTSTATLDPPK
T165 NSRTSTATLDPPKSS
S172 TLDPPKSSRESASPN
- gap
- gap
S177 KSSRESASPNSSHTL
S180 RESASPNSSHTLSRK
- gap
T234 PKSDSQETRAGALRA
- gap
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