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Protein

Ribosomal RNA-processing protein 8

Gene

RRP8

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei281S-adenosyl-L-methionineCombined sources1 Publication1
Binding sitei316S-adenosyl-L-methionine; via carbonyl oxygenCombined sources1 Publication1
Binding sitei334S-adenosyl-L-methionineCombined sources1 Publication1
Binding sitei346S-adenosyl-L-methionineCombined sources1 Publication1
Binding sitei347S-adenosyl-L-methionineCombined sources1 Publication1
Binding sitei363S-adenosyl-L-methionine; via carbonyl oxygenCombined sources1 Publication1

GO - Molecular functioni

  • methylated histone binding Source: UniProtKB
  • poly(A) RNA binding Source: UniProtKB
  • S-adenosylmethionine-dependent methyltransferase activity Source: UniProtKB

GO - Biological processi

  • cellular response to glucose starvation Source: UniProtKB
  • chromatin modification Source: UniProtKB-KW
  • chromatin silencing at rDNA Source: UniProtKB
  • intrinsic apoptotic signaling pathway by p53 class mediator Source: UniProtKB
  • positive regulation of cell cycle arrest Source: UniProtKB
  • regulation of transcription by glucose Source: UniProtKB
  • rRNA processing Source: UniProtKB-KW
  • transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator, Methyltransferase, Repressor, Transferase

Keywords - Biological processi

rRNA processing, Transcription, Transcription regulation

Keywords - Ligandi

S-adenosyl-L-methionine

Enzyme and pathway databases

BioCyciZFISH:ENSG00000132275-MONOMER.
ReactomeiR-HSA-427359. SIRT1 negatively regulates rRNA Expression.

Names & Taxonomyi

Protein namesi
Recommended name:
Ribosomal RNA-processing protein 8 (EC:2.1.1.-)
Alternative name(s):
Cerebral protein 1
Nucleomethylin
Gene namesi
Name:RRP8
Synonyms:KIAA0409, NML
ORF Names:hucep-1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 11

Organism-specific databases

HGNCiHGNC:29030. RRP8.

Subcellular locationi

GO - Cellular componenti

  • chromatin silencing complex Source: UniProtKB
  • cytoplasm Source: HPA
  • nucleolus Source: UniProtKB
  • nucleoplasm Source: Reactome
  • nucleus Source: HPA
  • plasma membrane Source: HPA
  • rDNA heterochromatin Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

DisGeNETi23378.
OpenTargetsiENSG00000132275.
PharmGKBiPA164725550.

Polymorphism and mutation databases

BioMutaiRRP8.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000840901 – 456Ribosomal RNA-processing protein 8Add BLAST456

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei62PhosphoserineCombined sources1
Modified residuei64PhosphoserineCombined sources1
Modified residuei104PhosphoserineCombined sources1
Modified residuei171PhosphoserineCombined sources1
Modified residuei176PhosphoserineCombined sources1
Modified residuei223PhosphoserineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiO43159.
MaxQBiO43159.
PaxDbiO43159.
PeptideAtlasiO43159.
PRIDEiO43159.

2D gel databases

SWISS-2DPAGEO43159.

PTM databases

iPTMnetiO43159.
PhosphoSitePlusiO43159.

Expressioni

Gene expression databases

BgeeiENSG00000132275.
CleanExiHS_KIAA0409.
ExpressionAtlasiO43159. baseline and differential.
GenevisibleiO43159. HS.

Organism-specific databases

HPAiHPA038487.
HPA057562.

Interactioni

Subunit structurei

Component of the eNoSC complex, composed of SIRT1, SUV39H1 and RRP8.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
SIRT1Q96EB63EBI-2008793,EBI-1802965
SUV39H1O434633EBI-2008793,EBI-349968

GO - Molecular functioni

  • methylated histone binding Source: UniProtKB

Protein-protein interaction databases

BioGridi116954. 115 interactors.
DIPiDIP-46686N.
IntActiO43159. 10 interactors.
MINTiMINT-4526401.
STRINGi9606.ENSP00000254605.

Structurei

Secondary structure

1456
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi244 – 260Combined sources17
Helixi263 – 272Combined sources10
Helixi274 – 288Combined sources15
Beta strandi291 – 293Combined sources3
Helixi295 – 304Combined sources10
Beta strandi312 – 316Combined sources5
Helixi321 – 325Combined sources5
Beta strandi330 – 336Combined sources7
Beta strandi342 – 345Combined sources4
Beta strandi357 – 364Combined sources8
Helixi371 – 381Combined sources11
Beta strandi382 – 392Combined sources11
Helixi394 – 396Combined sources3
Helixi400 – 409Combined sources10
Beta strandi412 – 418Combined sources7
Beta strandi425 – 431Combined sources7
Helixi444 – 446Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2ZFUX-ray2.00A/B242-456[»]
ProteinModelPortaliO43159.
SMRiO43159.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO43159.

Family & Domainsi

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi65 – 70Poly-Glu6

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG3045. Eukaryota.
ENOG4111J8Z. LUCA.
GeneTreeiENSGT00390000006189.
HOGENOMiHOG000164004.
InParanoidiO43159.
KOiK14850.
OMAiLMGTNIR.
OrthoDBiEOG091G0K2R.
PhylomeDBiO43159.
TreeFamiTF313749.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
InterProiIPR007823. RRP8.
IPR029063. SAM-dependent_MTases.
IPR023576. UbiE/COQ5_MeTrFase_CS.
[Graphical view]
PANTHERiPTHR12787. PTHR12787. 1 hit.
PfamiPF05148. Methyltransf_8. 1 hit.
[Graphical view]
SUPFAMiSSF53335. SSF53335. 1 hit.

Sequencei

Sequence statusi: Complete.

O43159-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFEEPEWAEA APVAAGLGPV ISRPPPAASS QNKGSKRRQL LATLRALEAA
60 70 80 90 100
SLSQHPPSLC ISDSEEEEEE RKKKCPKKAS FASASAEVGK KGKKKCQKQG
110 120 130 140 150
PPCSDSEEEV ERKKKCHKQA LVGSDSAEDE KRKRKCQKHA PINSAQHLDN
160 170 180 190 200
VDQTGPKAWK GSTTNDPPKQ SPGSTSPKPP HTLSRKQWRN RQKNKRRCKN
210 220 230 240 250
KFQPPQVPDQ APAEAPTEKT EVSPVPRTDS HEARAGALRA RMAQRLDGAR
260 270 280 290 300
FRYLNEQLYS GPSSAAQRLF QEDPEAFLLY HRGFQSQVKK WPLQPVDRIA
310 320 330 340 350
RDLRQRPASL VVADFGCGDC RLASSIRNPV HCFDLASLDP RVTVCDMAQV
360 370 380 390 400
PLEDESVDVA VFCLSLMGTN IRDFLEEANR VLKPGGLLKV AEVSSRFEDV
410 420 430 440 450
RTFLRAVTKL GFKIVSKDLT NSHFFLFDFQ KTGPPLVGPK AQLSGLQLQP

CLYKRR
Length:456
Mass (Da):50,715
Last modified:April 26, 2005 - v2
Checksum:i49251E2A488DA1C4
GO

Sequence cautioni

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

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_051034145A → P.Corresponds to variant rs11040934dbSNPEnsembl.1
Natural variantiVAR_051035329P → S.Corresponds to variant rs17834692dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D87060 mRNA. Translation: BAB46916.1.
AB007869 mRNA. Translation: BAA23705.1. Different initiation.
BC001071 mRNA. Translation: AAH01071.1.
CCDSiCCDS31411.1.
RefSeqiNP_056139.1. NM_015324.3.
UniGeneiHs.652255.

Genome annotation databases

EnsembliENST00000254605; ENSP00000254605; ENSG00000132275.
GeneIDi23378.
KEGGihsa:23378.
UCSCiuc001med.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D87060 mRNA. Translation: BAB46916.1.
AB007869 mRNA. Translation: BAA23705.1. Different initiation.
BC001071 mRNA. Translation: AAH01071.1.
CCDSiCCDS31411.1.
RefSeqiNP_056139.1. NM_015324.3.
UniGeneiHs.652255.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2ZFUX-ray2.00A/B242-456[»]
ProteinModelPortaliO43159.
SMRiO43159.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi116954. 115 interactors.
DIPiDIP-46686N.
IntActiO43159. 10 interactors.
MINTiMINT-4526401.
STRINGi9606.ENSP00000254605.

PTM databases

iPTMnetiO43159.
PhosphoSitePlusiO43159.

Polymorphism and mutation databases

BioMutaiRRP8.

2D gel databases

SWISS-2DPAGEO43159.

Proteomic databases

EPDiO43159.
MaxQBiO43159.
PaxDbiO43159.
PeptideAtlasiO43159.
PRIDEiO43159.

Protocols and materials databases

DNASUi23378.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000254605; ENSP00000254605; ENSG00000132275.
GeneIDi23378.
KEGGihsa:23378.
UCSCiuc001med.4. human.

Organism-specific databases

CTDi23378.
DisGeNETi23378.
GeneCardsiRRP8.
HGNCiHGNC:29030. RRP8.
HPAiHPA038487.
HPA057562.
MIMi615818. gene.
neXtProtiNX_O43159.
OpenTargetsiENSG00000132275.
PharmGKBiPA164725550.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3045. Eukaryota.
ENOG4111J8Z. LUCA.
GeneTreeiENSGT00390000006189.
HOGENOMiHOG000164004.
InParanoidiO43159.
KOiK14850.
OMAiLMGTNIR.
OrthoDBiEOG091G0K2R.
PhylomeDBiO43159.
TreeFamiTF313749.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000132275-MONOMER.
ReactomeiR-HSA-427359. SIRT1 negatively regulates rRNA Expression.

Miscellaneous databases

EvolutionaryTraceiO43159.
GeneWikiiKIAA0409.
GenomeRNAii23378.
PROiO43159.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000132275.
CleanExiHS_KIAA0409.
ExpressionAtlasiO43159. baseline and differential.
GenevisibleiO43159. HS.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
InterProiIPR007823. RRP8.
IPR029063. SAM-dependent_MTases.
IPR023576. UbiE/COQ5_MeTrFase_CS.
[Graphical view]
PANTHERiPTHR12787. PTHR12787. 1 hit.
PfamiPF05148. Methyltransf_8. 1 hit.
[Graphical view]
SUPFAMiSSF53335. SSF53335. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiRRP8_HUMAN
AccessioniPrimary (citable) accession number: O43159
Secondary accession number(s): Q7KZ78, Q9BVM6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 26, 2005
Last sequence update: April 26, 2005
Last modified: November 30, 2016
This is version 143 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 11
    Human chromosome 11: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.