dbPAF Protein Information

Tag Content
dbPAF ID dbPAF-0001459
Uniprot Accession O43159; RRP8_HUMAN; Q7KZ78; Q9BVM6;
Genbank Protein ID NP_056139.1;
Genbank Nucleotide ID NM_015324.3;
Protein Name Ribosomal RNA-processing protein 8
Protein Synonyms/Alias Cerebral protein 1;Nucleomethylin;
Gene Name RRP8
Gene Synonyms/Alias KIAA0409;NML;hucep-1;
Organism Homo sapiens(Human)
NCBI Taxa ID 9606
Functional Description
(View all)		 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.
Phosphorylation Sites
 dbPAF PTMs: 24 (View all)
PositionPeptidesSourceReferences ( PMIDs )
43KRRQLLATLRALEAAPHOSIDA;PhosphoSitePlus21081558; 22135298
51LRALEAASLSQHPPSdbPTM 3.0;HPRD 9;SysPTM 2.0;curated17081983; 16381945; 23193290; 18988627; 19366988; 23090842;
53ALEAASLSQHPPSLCdbPTM 3.0;HPRD 9;PhosphoSitePlus;SysPTM 2.0;curated17081983; 16381945; 23193290; 18988627; 22135298; 19366988;
58SLSQHPPSLCISDSEdbPTM 3.0;Phospho.ELM 9.0;HPRD 9;PhosphoSitePlus;SysPTM 2.0;curated18669648; 16381945; 23193290; 17081983; 18988627; 22135298;
62HPPSLCISDSEEEEEdbPTM 3.0;Phospho.ELM 9.0;HPRD 9;PHOSIDA;PhosphoPep 2.0;PhosphoSitePlus;SysPTM 2.0;UniProt;curated17081983; 18220336; 18669648; 19413330; 19690332; 16381945;
64PSLCISDSEEEEEERdbPTM 3.0;Phospho.ELM 9.0;HPRD 9;PHOSIDA;PhosphoPep 2.0;PhosphoSitePlus;SysPTM 2.0;UniProt;curated17081983; 18220336; 18669648; 19413330; 19690332; 16381945;
80KKCPKKASFASASAEPhosphoSitePlus;curated22135298; 25627689; 20873877; 22817900
83PKKASFASASAEVGKPhosphoSitePlus;curated22135298; 25627689; 20873877
85KASFASASAEVGKKGPhosphoSitePlus;curated22135298; 25627689
104QKQGPPCSDSEEEVEdbPTM 3.0;Phospho.ELM 9.0;HPRD 9;PHOSIDA;PhosphoSitePlus;SysPTM 2.0;curated17081983; 19413330; 16381945; 23193290; 20164059; 20363803;
106QGPPCSDSEEEVERKdbPTM 3.0;Phospho.ELM 9.0;HPRD 9;PHOSIDA;PhosphoSitePlus;SysPTM 2.0;curated17081983; 19413330; 16381945; 23193290; 19691289; 20164059;
124HKQALVGSDSAEDEKdbPTM 3.0;Phospho.ELM 9.0;HPRD 9;PhosphoSitePlus;SysPTM 2.0;curated17287340; 19413330; 16381945; 23193290; 21406692; 19691289;
126QALVGSDSAEDEKRKdbPTM 3.0;Phospho.ELM 9.0;HPRD 9;PhosphoPep 2.0;PhosphoSitePlus;SysPTM 2.0;curated17287340; 19007248; 19413330; 16381945; 23193290; 20068231;
162GPKAWKGSTTNDPPKPhosphoSitePlus;curated22135298; 24732914
163PKAWKGSTTNDPPKQPhosphoSitePlus22135298
171TNDPPKQSPGSTSPKdbPTM 3.0;Phospho.ELM 9.0;HPRD 9;PHOSIDA;PhosphoPep 2.0;PhosphoSitePlus;SysPTM 2.0;UniProt;curated16565220; 18669648; 16381945; 23193290; 20068231; 18988627;
174PPKQSPGSTSPKPPHdbPTM 3.0;HPRD 9;PhosphoSitePlus;curated20068231; 16381945; 23193290; 18988627; 22135298; 25627689;
175PKQSPGSTSPKPPHTdbPTM 3.0;Phospho.ELM 9.0;HPRD 9;PhosphoPep 2.0;PhosphoSitePlus;SysPTM 2.0;curated18669648; 16381945; 23193290; 18988627; 19060867; 22135298;
176KQSPGSTSPKPPHTLdbPTM 3.0;Phospho.ELM 9.0;HPRD 9;PHOSIDA;PhosphoPep 2.0;PhosphoSitePlus;SysPTM 2.0;curated16565220; 16381945; 23193290; 18669648; 17081983; 18988627;
182TSPKPPHTLSRKQWRcurated24961811; 24732914
Sequence
(Fasta)		MFEEPEWAEA APVAAGLGPV ISRPPPAASS QNKGSKRRQL LATLRALEAA SLSQHPPSLC 60
ISDSEEEEEE RKKKCPKKAS FASASAEVGK KGKKKCQKQG PPCSDSEEEV ERKKKCHKQA 120
LVGSDSAEDE KRKRKCQKHA PINSAQHLDN VDQTGPKAWK GSTTNDPPKQ SPGSTSPKPP 180
HTLSRKQWRN RQKNKRRCKN KFQPPQVPDQ APAEAPTEKT EVSPVPRTDS HEARAGALRA 240
RMAQRLDGAR FRYLNEQLYS GPSSAAQRLF QEDPEAFLLY HRGFQSQVKK WPLQPVDRIA 300
RDLRQRPASL VVADFGCGDC RLASSIRNPV HCFDLASLDP RVTVCDMAQV PLEDESVDVA 360
VFCLSLMGTN IRDFLEEANR VLKPGGLLKV AEVSSRFEDV RTFLRAVTKL GFKIVSKDLT 420
NSHFFLFDFQ KTGPPLVGPK AQLSGLQLQP CLYKRR 457
Keyword

KW-0002--3D-structure
KW-0156--Chromatin regulator
KW-0181--Complete proteome
KW-0489--Methyltransferase
KW-0539--Nucleus
KW-0597--Phosphoprotein
KW-0621--Polymorphism
KW-1185--Reference proteome
KW-0678--Repressor
KW-0698--rRNA processing
KW-0949--S-adenosyl-L-methionine
KW-0804--Transcription
KW-0805--Transcription regulation
KW-0808--Transferase
Interpro

IPR007823--Methyltransferase-rel
IPR029063--SAM-dependent_MTases
IPR023576--UbiE/COQ5_MeTrFase_CS
PROSITE
Pfam

PF05148--Methyltransf_8
Gene Ontology

GO:0005677--C:chromatin silencing complex
GO:0005737--C:cytoplasm
GO:0005730--C:nucleolus
GO:0005654--C:nucleoplasm
GO:0005634--C:nucleus
GO:0005886--C:plasma membrane
GO:0033553--C:rDNA heterochromatin
GO:0035064--F:methylated histone binding
GO:0044822--F:poly(A) RNA binding
GO:0008757--F:S-adenosylmethionine-dependent methyltransferase activity
GO:0042149--P:cellular response to glucose starvation
GO:0016568--P:chromatin modification
GO:0000183--P:chromatin silencing at rDNA
GO:0010467--P:gene expression
GO:0072332--P:intrinsic apoptotic signaling pathway by p53 class mediator
GO:0045814--P:negative regulation of gene expression, epigenetic
GO:0071158--P:positive regulation of cell cycle arrest
GO:0040029--P:regulation of gene expression, epigenetic
GO:0046015--P:regulation of transcription by glucose
GO:0006364--P:rRNA processing
GO:0006351--P:transcription, DNA-templated