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Protein

Ribosomal RNA-processing protein 8

Gene

Rrp8

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 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 (By similarity).By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei282 – 2821S-adenosyl-L-methionineBy similarity
Binding sitei317 – 3171S-adenosyl-L-methionine; via carbonyl oxygenBy similarity
Binding sitei335 – 3351S-adenosyl-L-methionineBy similarity
Binding sitei347 – 3471S-adenosyl-L-methionineBy similarity
Binding sitei348 – 3481S-adenosyl-L-methionineBy similarity
Binding sitei364 – 3641S-adenosyl-L-methionine; via carbonyl oxygenBy similarity

GO - Molecular functioni

GO - Biological processi

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

ReactomeiR-MMU-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 homolog
Gene namesi
Name:Rrp8
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 7

Organism-specific databases

MGIiMGI:1914251. Rrp8.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 457457Ribosomal RNA-processing protein 8PRO_0000084091Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei62 – 621PhosphoserineCombined sources
Modified residuei64 – 641PhosphoserineCombined sources
Modified residuei105 – 1051PhosphoserineBy similarity
Modified residuei172 – 1721PhosphoserineBy similarity
Modified residuei177 – 1771PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ9DB85.
MaxQBiQ9DB85.
PaxDbiQ9DB85.
PeptideAtlasiQ9DB85.
PRIDEiQ9DB85.

PTM databases

iPTMnetiQ9DB85.
PhosphoSiteiQ9DB85.

Expressioni

Gene expression databases

BgeeiQ9DB85.
CleanExiMM_1500003O22RIK.
ExpressionAtlasiQ9DB85. baseline and differential.
GenevisibleiQ9DB85. MM.

Interactioni

Subunit structurei

Component of the eNoSC complex, composed of SIRT1, SUV39H1 and RRP8.By similarity

GO - Molecular functioni

Protein-protein interaction databases

BioGridi221741. 2 interactions.
IntActiQ9DB85. 1 interaction.
MINTiMINT-4128130.
STRINGi10090.ENSMUSP00000095752.

Structurei

3D structure databases

ProteinModelPortaliQ9DB85.
SMRiQ9DB85. Positions 245-455.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi65 – 695Poly-Glu

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG3045. Eukaryota.
ENOG4111J8Z. LUCA.
GeneTreeiENSGT00390000006189.
HOGENOMiHOG000164004.
InParanoidiQ9DB85.
KOiK14850.
OrthoDBiEOG7PGDRQ.
PhylomeDBiQ9DB85.
TreeFamiTF313749.

Family and domain databases

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

Sequencei

Sequence statusi: Complete.

Q9DB85-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFEEPEWVEA APAIVGLGAA TAQVRPATAP PVKGRKRRHL LATLRALEAA
60 70 80 90 100
SLSQQTPSLP GSDSEEEEEV GRKKRHLQRP SLASVSKEVG KKRKGKCQKQ
110 120 130 140 150
APSISDSEGK EIRRKCHRQA PPLGGVSAGE EKGKRKCQEY SSLHLTQPLD
160 170 180 190 200
SVDQTVHNSR TSTATIDPSK PSPESMSPNS SHTLSRKQWR NRQKNKRRHK
210 220 230 240 250
NKFRPLQTPE QAPPKASIEE TEVPPVPKSD SQESRAGALR ARMTQRLDGA
260 270 280 290 300
RFRYLNEQLY SGPSSAARRL FQEDPEAFLL YHRGFQRQVK KWPLHPVDRI
310 320 330 340 350
AKDLRQKPAS LVVADFGCGD CRLASSVRNP VHCFDLASLD PRVTVCDMAQ
360 370 380 390 400
VPLEDESVDV AVFCLSLMGT NIRDFLEEAN RVLKTGGLLK VAEVSSRFED
410 420 430 440 450
IRTFLGAVTK LGFKIIYKDL TNSHFFLFDF EKTGPPRVGP KAQLSGLKLQ

PCLYKRR
Length:457
Mass (Da):51,066
Last modified:June 1, 2001 - v1
Checksum:iA9DB8CB932E1DB3C
GO

Sequence cautioni

The sequence BAC37008.1 differs from that shown. Reason: Frameshift at position 22. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti30 – 301P → R in BAE41665 (PubMed:16141072).Curated
Sequence conflicti30 – 301P → R in BAE42891 (PubMed:16141072).Curated
Sequence conflicti30 – 301P → R in BAE42874 (PubMed:16141072).Curated
Sequence conflicti151 – 1511S → N in BAE41665 (PubMed:16141072).Curated
Sequence conflicti151 – 1511S → N in BAE42891 (PubMed:16141072).Curated
Sequence conflicti151 – 1511S → N in BAE42874 (PubMed:16141072).Curated
Sequence conflicti173 – 1731P → H in BAE32883 (PubMed:16141072).Curated
Sequence conflicti268 – 2681R → Q in BAE41665 (PubMed:16141072).Curated
Sequence conflicti268 – 2681R → Q in BAE42891 (PubMed:16141072).Curated
Sequence conflicti268 – 2681R → Q in BAE42874 (PubMed:16141072).Curated
Sequence conflicti370 – 3701T → N in BAE32883 (PubMed:16141072).Curated
Sequence conflicti385 – 3851T → P in BAE41665 (PubMed:16141072).Curated
Sequence conflicti385 – 3851T → P in BAE42891 (PubMed:16141072).Curated
Sequence conflicti385 – 3851T → P in BAE42874 (PubMed:16141072).Curated
Sequence conflicti394 – 3941V → A in BAE41665 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK005138 mRNA. Translation: BAB23836.1.
AK045361 mRNA. Translation: BAC32326.1.
AK077786 mRNA. Translation: BAC37008.1. Frameshift.
AK154858 mRNA. Translation: BAE32883.1.
AK170257 mRNA. Translation: BAE41665.1.
AK172189 mRNA. Translation: BAE42874.1.
AK172224 mRNA. Translation: BAE42891.1.
BC022923 mRNA. Translation: AAH22923.1.
BC046799 mRNA. Translation: AAH46799.1.
CCDSiCCDS21658.1.
RefSeqiNP_080173.1. NM_025897.2.
UniGeneiMm.231400.

Genome annotation databases

EnsembliENSMUST00000033179; ENSMUSP00000033179; ENSMUSG00000030888.
GeneIDi101867.
KEGGimmu:101867.
UCSCiuc009iyz.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK005138 mRNA. Translation: BAB23836.1.
AK045361 mRNA. Translation: BAC32326.1.
AK077786 mRNA. Translation: BAC37008.1. Frameshift.
AK154858 mRNA. Translation: BAE32883.1.
AK170257 mRNA. Translation: BAE41665.1.
AK172189 mRNA. Translation: BAE42874.1.
AK172224 mRNA. Translation: BAE42891.1.
BC022923 mRNA. Translation: AAH22923.1.
BC046799 mRNA. Translation: AAH46799.1.
CCDSiCCDS21658.1.
RefSeqiNP_080173.1. NM_025897.2.
UniGeneiMm.231400.

3D structure databases

ProteinModelPortaliQ9DB85.
SMRiQ9DB85. Positions 245-455.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi221741. 2 interactions.
IntActiQ9DB85. 1 interaction.
MINTiMINT-4128130.
STRINGi10090.ENSMUSP00000095752.

PTM databases

iPTMnetiQ9DB85.
PhosphoSiteiQ9DB85.

Proteomic databases

EPDiQ9DB85.
MaxQBiQ9DB85.
PaxDbiQ9DB85.
PeptideAtlasiQ9DB85.
PRIDEiQ9DB85.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000033179; ENSMUSP00000033179; ENSMUSG00000030888.
GeneIDi101867.
KEGGimmu:101867.
UCSCiuc009iyz.2. mouse.

Organism-specific databases

CTDi23378.
MGIiMGI:1914251. Rrp8.

Phylogenomic databases

eggNOGiKOG3045. Eukaryota.
ENOG4111J8Z. LUCA.
GeneTreeiENSGT00390000006189.
HOGENOMiHOG000164004.
InParanoidiQ9DB85.
KOiK14850.
OrthoDBiEOG7PGDRQ.
PhylomeDBiQ9DB85.
TreeFamiTF313749.

Enzyme and pathway databases

ReactomeiR-MMU-427359. SIRT1 negatively regulates rRNA Expression.

Miscellaneous databases

PROiQ9DB85.
SOURCEiSearch...

Gene expression databases

BgeeiQ9DB85.
CleanExiMM_1500003O22RIK.
ExpressionAtlasiQ9DB85. baseline and differential.
GenevisibleiQ9DB85. MM.

Family and domain databases

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

Publicationsi

  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J and NOD.
    Tissue: Cerebellum, Corpora quadrigemina and Spleen.
  2. "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].
    Strain: C57BL/6J and FVB/N.
    Tissue: Brain and Kidney.
  3. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-62 AND SER-64, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  4. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-62; SER-64 AND SER-177, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Kidney, Liver, Lung, Pancreas, Spleen and Testis.

Entry informationi

Entry nameiRRP8_MOUSE
AccessioniPrimary (citable) accession number: Q9DB85
Secondary accession number(s): Q3T9X9
, Q3TDD7, Q3U3A5, Q8BHW3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 26, 2005
Last sequence update: June 1, 2001
Last modified: July 6, 2016
This is version 109 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. 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.