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Protein

Ribonucleases P/MRP protein subunit POP8

Gene

POP8

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Component of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends. Also a component of RNase MRP, which cleaves pre-rRNA sequences.1 Publication

Catalytic activityi

Endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor.

GO - Molecular functioni

  1. ribonuclease P activity Source: UniProtKB-EC

GO - Biological processi

  1. intronic box C/D snoRNA processing Source: SGD
  2. mRNA cleavage Source: SGD
  3. RNA phosphodiester bond hydrolysis Source: GOC
  4. RNA phosphodiester bond hydrolysis, endonucleolytic Source: GOC
  5. rRNA processing Source: UniProtKB-KW
  6. tRNA processing Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

rRNA processing, tRNA processing

Enzyme and pathway databases

BioCyciYEAST:YBL018C-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Ribonucleases P/MRP protein subunit POP8 (EC:3.1.26.5)
Alternative name(s):
RNA-processing protein POP8
RNases P/MRP 15.5 kDa subunit
Gene namesi
Name:POP8
Ordered Locus Names:YBL018C
ORF Names:YBL0301
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311 Componenti: Chromosome II

Organism-specific databases

CYGDiYBL018c.
SGDiS000000114. POP8.

Subcellular locationi

Nucleus 1 Publication

GO - Cellular componenti

  1. cytosol Source: SGD
  2. nucleolar ribonuclease P complex Source: SGD
  3. nucleus Source: SGD
  4. ribonuclease MRP complex Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 133133Ribonucleases P/MRP protein subunit POP8PRO_0000058521Add
BLAST

Proteomic databases

MaxQBiP38208.
PaxDbiP38208.
PeptideAtlasiP38208.

Expressioni

Gene expression databases

GenevestigatoriP38208.

Interactioni

Subunit structurei

Component of nuclear RNase P and RNase MRP complexes. RNase P consists of an RNA moiety and at least 9 protein subunits including POP1, POP3, POP4, POP5, POP6, POP7, POP8, RPP1 and RPR2. RNase MRP complex consists of an RNA moiety and at least 10 protein subunits including POP1, POP3, POP4, POP5, POP6, POP7, POP8, RMP1, RPP1 and SNM1, many of which are shared with the RNase P complex.2 Publications

Protein-protein interaction databases

BioGridi32680. 114 interactions.
DIPiDIP-2033N.
IntActiP38208. 7 interactions.
MINTiMINT-486880.
STRINGi4932.YBL018C.

Structurei

3D structure databases

ProteinModelPortaliP38208.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Phylogenomic databases

eggNOGiNOG40549.
HOGENOMiHOG000000716.
InParanoidiP38208.
KOiK14528.
OMAiALKRSHG.
OrthoDBiEOG7W9S74.

Family and domain databases

InterProiIPR020347. RNase_P/MRP_POP8.
[Graphical view]
ProDomiPD082524. Ribonucleases_P/MRP_su_POP8. 1 hit.
[Graphical view] [Entries sharing at least one domain]

Sequencei

Sequence statusi: Complete.

P38208-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGKKTFREWQ YFKLSITSFD QDVDDAHAID QMTWRQWLNN ALKRSYGIFG
60 70 80 90 100
EGVEYSFLHV DDKLAYIRVN HADKDTFSSS ISTYISTDEL VGSPLTVSIL
110 120 130
QESSSLRLLE VTDDDRLWLK KVMEEEEQDC KCI
Length:133
Mass (Da):15,512
Last modified:October 1, 1994 - v1
Checksum:i9605CC5BD74AFA21
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z35779 Genomic DNA. Translation: CAA84837.1.
BK006936 Genomic DNA. Translation: DAA07102.1.
PIRiS45752.
RefSeqiNP_009535.1. NM_001178258.1.

Genome annotation databases

EnsemblFungiiYBL018C; YBL018C; YBL018C.
GeneIDi852263.
KEGGisce:YBL018C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z35779 Genomic DNA. Translation: CAA84837.1.
BK006936 Genomic DNA. Translation: DAA07102.1.
PIRiS45752.
RefSeqiNP_009535.1. NM_001178258.1.

3D structure databases

ProteinModelPortaliP38208.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi32680. 114 interactions.
DIPiDIP-2033N.
IntActiP38208. 7 interactions.
MINTiMINT-486880.
STRINGi4932.YBL018C.

Proteomic databases

MaxQBiP38208.
PaxDbiP38208.
PeptideAtlasiP38208.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYBL018C; YBL018C; YBL018C.
GeneIDi852263.
KEGGisce:YBL018C.

Organism-specific databases

CYGDiYBL018c.
SGDiS000000114. POP8.

Phylogenomic databases

eggNOGiNOG40549.
HOGENOMiHOG000000716.
InParanoidiP38208.
KOiK14528.
OMAiALKRSHG.
OrthoDBiEOG7W9S74.

Enzyme and pathway databases

BioCyciYEAST:YBL018C-MONOMER.

Miscellaneous databases

NextBioi970859.

Gene expression databases

GenevestigatoriP38208.

Family and domain databases

InterProiIPR020347. RNase_P/MRP_POP8.
[Graphical view]
ProDomiPD082524. Ribonucleases_P/MRP_su_POP8. 1 hit.
[Graphical view] [Entries sharing at least one domain]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Complete DNA sequence of yeast chromosome II."
    Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C., Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M., Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M., Cziepluch C.
    , Demolis N., Delaveau T., Doignon F., Domdey H., Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D., Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N., Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J., Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C., Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P., Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y., Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F., Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E., Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M., Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B., Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L., Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M., Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S., Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K., Mewes H.-W., Kleine K.
    EMBO J. 13:5795-5809(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  3. "Purification and characterization of the nuclear RNase P holoenzyme complex reveals extensive subunit overlap with RNase MRP."
    Chamberlain J.R., Lee Y., Lane W.S., Engelke D.R.
    Genes Dev. 12:1678-1690(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, IDENTIFICATION IN THE RNASE P COMPLEX BY MASS SPECTROMETRY.
  4. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  5. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  6. "Characterization and purification of Saccharomyces cerevisiae RNase MRP reveals a new unique protein component."
    Salinas K., Wierzbicki S., Zhou L., Schmitt M.E.
    J. Biol. Chem. 280:11352-11360(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE RNASE MRP COMPLEX BY MASS SPECTROMETRY.

Entry informationi

Entry nameiPOP8_YEAST
AccessioniPrimary (citable) accession number: P38208
Secondary accession number(s): D6VPY2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: October 1, 1994
Last modified: January 7, 2015
This is version 109 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 4870 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  2. Yeast chromosome II
    Yeast (Saccharomyces cerevisiae) chromosome II: entries and gene names

External Data

Dasty 3

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 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.