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O43159 (RRP8_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 115. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ribosomal RNA-processing protein 8

EC=2.1.1.-
Alternative name(s):
Cerebral protein 1
Nucleomethylin
Gene names
Name:RRP8
Synonyms:KIAA0409, NML
ORF Names:hucep-1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length456 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.11

Subunit structure

Component of the eNoSC complex, composed of SIRT1, SUV39H1 and RRP8. Ref.11

Subcellular location

Nucleusnucleolus. Note: Localizes at rDNA locus. Ref.4 Ref.5 Ref.11

Sequence similarities

Belongs to the methyltransferase superfamily. RRP8 family.

Sequence caution

The sequence BAA23705.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processrRNA processing
Transcription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityPolymorphism
   LigandS-adenosyl-L-methionine
   Molecular functionChromatin regulator
Methyltransferase
Repressor
Transferase
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcellular response to glucose starvation

Inferred from mutant phenotype PubMed 21471221. Source: UniProtKB

chromatin modification

Inferred from electronic annotation. Source: UniProtKB-KW

chromatin silencing at rDNA

Inferred from direct assay Ref.11. Source: UniProtKB

intrinsic apoptotic signaling pathway by p53 class mediator

Inferred from mutant phenotype PubMed 21471221. Source: UniProtKB

positive regulation of cell cycle arrest

Inferred from mutant phenotype PubMed 21471221. Source: UniProtKB

rRNA processing

Inferred from electronic annotation. Source: UniProtKB-KW

regulation of transcription by glucose

Inferred from mutant phenotype PubMed 21471221. Source: UniProtKB

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentchromatin silencing complex

Inferred from direct assay Ref.11. Source: UniProtKB

cytoplasm

Inferred from direct assay. Source: HPA

nucleolus

Inferred from direct assay Ref.11. Source: UniProtKB

nucleus

Inferred from direct assay. Source: HPA

plasma membrane

Inferred from direct assay. Source: HPA

rDNA heterochromatin

Inferred from direct assay Ref.11. Source: UniProtKB

   Molecular_functionS-adenosylmethionine-dependent methyltransferase activity

Traceable author statement Ref.11. Source: UniProtKB

methylated histone residue binding

Inferred from direct assay Ref.11. Source: UniProtKB

poly(A) RNA binding

Inferred from direct assay PubMed 22658674PubMed 22681889. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

SIRT1Q96EB63EBI-2008793,EBI-1802965
SUV39H1O434633EBI-2008793,EBI-349968

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 456456Ribosomal RNA-processing protein 8
PRO_0000084090

Regions

Compositional bias65 – 706Poly-Glu

Sites

Binding site2811S-adenosyl-L-methionine
Binding site3161S-adenosyl-L-methionine; via carbonyl oxygen
Binding site3341S-adenosyl-L-methionine
Binding site3461S-adenosyl-L-methionine
Binding site3471S-adenosyl-L-methionine
Binding site3631S-adenosyl-L-methionine; via carbonyl oxygen

Amino acid modifications

Modified residue621Phosphoserine Ref.7 Ref.9
Modified residue641Phosphoserine Ref.7 Ref.9
Modified residue1711Phosphoserine Ref.7
Modified residue2231Phosphoserine Ref.7

Natural variations

Natural variant1451A → P.
Corresponds to variant rs11040934 [ dbSNP | Ensembl ].
VAR_051034
Natural variant3291P → S.
Corresponds to variant rs17834692 [ dbSNP | Ensembl ].
VAR_051035

Secondary structure

.................................. 456
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O43159 [UniParc].

Last modified April 26, 2005. Version 2.
Checksum: 49251E2A488DA1C4

FASTA45650,715
        10         20         30         40         50         60 
MFEEPEWAEA APVAAGLGPV ISRPPPAASS QNKGSKRRQL LATLRALEAA SLSQHPPSLC 

        70         80         90        100        110        120 
ISDSEEEEEE RKKKCPKKAS FASASAEVGK KGKKKCQKQG PPCSDSEEEV ERKKKCHKQA 

       130        140        150        160        170        180 
LVGSDSAEDE KRKRKCQKHA PINSAQHLDN VDQTGPKAWK GSTTNDPPKQ SPGSTSPKPP 

       190        200        210        220        230        240 
HTLSRKQWRN RQKNKRRCKN KFQPPQVPDQ APAEAPTEKT EVSPVPRTDS HEARAGALRA 

       250        260        270        280        290        300 
RMAQRLDGAR FRYLNEQLYS GPSSAAQRLF QEDPEAFLLY HRGFQSQVKK WPLQPVDRIA 

       310        320        330        340        350        360 
RDLRQRPASL VVADFGCGDC RLASSIRNPV HCFDLASLDP RVTVCDMAQV PLEDESVDVA 

       370        380        390        400        410        420 
VFCLSLMGTN IRDFLEEANR VLKPGGLLKV AEVSSRFEDV RTFLRAVTKL GFKIVSKDLT 

       430        440        450 
NSHFFLFDFQ KTGPPLVGPK AQLSGLQLQP CLYKRR 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and characterization of a novel gene which is expressed in the human brain."
Yazaki M., Takayama K., Matsumoto K., Yoshimoto M.
Submitted (AUG-1996) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Brain.
[2]"Prediction of the coding sequences of unidentified human genes. VIII. 78 new cDNA clones from brain which code for large proteins in vitro."
Ishikawa K., Nagase T., Nakajima D., Seki N., Ohira M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
DNA Res. 4:307-313(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain.
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]"Functional proteomic analysis of human nucleolus."
Scherl A., Coute Y., Deon C., Calle A., Kindbeiter K., Sanchez J.-C., Greco A., Hochstrasser D.F., Diaz J.-J.
Mol. Biol. Cell 13:4100-4109(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[5]"Directed proteomic analysis of the human nucleolus."
Andersen J.S., Lyon C.E., Fox A.H., Leung A.K.L., Lam Y.W., Steen H., Mann M., Lamond A.I.
Curr. Biol. 12:1-11(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION.
[6]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[7]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-62; SER-64; SER-171 AND SER-223, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[8]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[9]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-62 AND SER-64, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[10]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"Epigenetic control of rDNA loci in response to intracellular energy status."
Murayama A., Ohmori K., Fujimura A., Minami H., Yasuzawa-Tanaka K., Kuroda T., Oie S., Daitoku H., Okuwaki M., Nagata K., Fukamizu A., Kimura K., Shimizu T., Yanagisawa J.
Cell 133:627-639(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 242-456 IN COMPLEX WITH S-ADENOSYL-L-HOMOCYSTEINE, IDENTIFICATION IN THE ENOSC COMPLEX, FUNCTION, SUBCELLULAR LOCATION, H3K9ME2-BINDING.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D87060 mRNA. Translation: BAB46916.1.
AB007869 mRNA. Translation: BAA23705.1. Different initiation.
BC001071 mRNA. Translation: AAH01071.1.
RefSeqNP_056139.1. NM_015324.3.
UniGeneHs.652255.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2ZFUX-ray2.00A/B242-456[»]
ProteinModelPortalO43159.
SMRO43159. Positions 243-454.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116954. 4 interactions.
DIPDIP-46686N.
IntActO43159. 3 interactions.
MINTMINT-4526401.
STRING9606.ENSP00000254605.

PTM databases

PhosphoSiteO43159.

2D gel databases

SWISS-2DPAGEO43159.

Proteomic databases

PaxDbO43159.
PeptideAtlasO43159.
PRIDEO43159.

Protocols and materials databases

DNASU23378.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000254605; ENSP00000254605; ENSG00000132275.
GeneID23378.
KEGGhsa:23378.
UCSCuc001med.3. human.

Organism-specific databases

CTD23378.
GeneCardsGC11M006577.
HGNCHGNC:29030. RRP8.
HPAHPA038487.
neXtProtNX_O43159.
PharmGKBPA164725550.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0500.
HOGENOMHOG000164004.
InParanoidO43159.
KOK14850.
OMALMGTNIR.
OrthoDBEOG7PGDRQ.
PhylomeDBO43159.
TreeFamTF313749.

Gene expression databases

ArrayExpressO43159.
BgeeO43159.
CleanExHS_KIAA0409.
GenevestigatorO43159.

Family and domain databases

InterProIPR007823. Methyltransferase-rel.
IPR023576. UbiE/COQ5_MeTrFase_CS.
[Graphical view]
PANTHERPTHR12787. PTHR12787. 1 hit.
PfamPF05148. Methyltransf_8. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceO43159.
GeneWikiKIAA0409.
GenomeRNAi23378.
NextBio45466.
PROO43159.

Entry information

Entry nameRRP8_HUMAN
AccessionPrimary (citable) accession number: O43159
Secondary accession number(s): Q7KZ78, Q9BVM6
Entry history
Integrated into UniProtKB/Swiss-Prot: April 26, 2005
Last sequence update: April 26, 2005
Last modified: April 16, 2014
This is version 115 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 11

Human chromosome 11: entries, gene names and cross-references to MIM