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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; cytoplasm; plasma membrane; nucleolus; nucleus 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®

Select Structure to View Below RRP8 2ZFU - A/B=242-456 (human)

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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

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	23		S62-p	HPPsLCIsDsEEEEE
0	23		S64-p	PsLCIsDsEEEEEER
0	1		K78-a	RKKKCPKkASFASAS
0	9		S104-p	QKQGPPCsDsEEEVE
0	10		S106-p	QGPPCsDsEEEVERK
0	2		S124-p	HKQALVGsDsAEDEK
0	2		S126-p	QALVGsDsAEDEKRK
0	3		S171-p	TNDPPKQsPGSTsPK
0	4		S176-p	KQsPGSTsPKPPHTL
0	1		P179	PGSTsPKPPHTLSRK
0	6		S223-p	PTEKTEVsPVPRTDS
0	1		A233	PRTDSHEARAGALRA
0	1		S286-p	LYHRGFQsQVKKWPL

	mouse
T43	KRRHLLATLRALEAA
S58-p	SLSQQTPsLPGsDsE
S62-p	QTPsLPGsDsEEEEE
S64-p	PsLPGsDsEEEEEVG
R79	RKKRHLQRPSLASVS
S105-p	QKQAPSIsDSEGKEI
S107	QAPSIsDSEGKEIRR
G125	RQAPPLGGVSAGEEK
S127	APPLGGVSAGEEKGK
S172-p	TIDPSKPsPESMsPN
S177-p	KPsPESMsPNsSHTL
S180-p	PESMsPNsSHTLSRK
P224	SIEETEVPPVPKSDS
S234-p	PKSDSQEsRAGALRA
R287	LYHRGFQRQVKKWPL

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