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Protein

Ribonuclease MRP protein subunit RMP1

Gene

RMP1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Functions as part of ribonuclease MRP (RNase MRP), which is involved in rRNA processing in mitochondria.1 Publication

GO - Molecular functioni

  • rRNA primary transcript binding Source: SGD

GO - Biological processi

  • maturation of 5.8S rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) Source: SGD
  • mRNA cleavage Source: SGD
Complete GO annotation...

Keywords - Biological processi

rRNA processing

Enzyme and pathway databases

BioCyciYEAST:G3O-32282-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Ribonuclease MRP protein subunit RMP1
Alternative name(s):
RNA-processing protein RMP1
RNase MRP 23.6 kDa subunit
Gene namesi
Name:RMP1Imported
Ordered Locus Names:YLR145W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311 Componenti: Chromosome XII

Organism-specific databases

CYGDiYLR145w.
EuPathDBiFungiDB:YLR145W.
SGDiS000004135. RMP1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei86 – 10823HelicalSequence AnalysisAdd
BLAST

GO - Cellular componenti

  • cytoplasm Source: UniProtKB-SubCell
  • integral component of membrane Source: UniProtKB-KW
  • nucleus Source: UniProtKB-SubCell
  • ribonuclease MRP complex Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Membrane, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi103 – 1031C → R in RMP1-6; temperature-sensitive phenotype. Defective in 5.8S rRNA processing. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 201201Ribonuclease MRP protein subunit RMP1PRO_0000270572Add
BLAST

Proteomic databases

MaxQBiQ12530.

Interactioni

Subunit structurei

Component of RNase MRP complex which 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.1 Publication

Protein-protein interaction databases

BioGridi31414. 116 interactions.
DIPiDIP-4813N.
IntActiQ12530. 9 interactions.
MINTiMINT-573400.
STRINGi4932.YLR145W.

Structurei

3D structure databases

ProteinModelPortaliQ12530.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi183 – 19311Poly-LysSequence AnalysisAdd
BLAST

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG42290.
HOGENOMiHOG000066119.
InParanoidiQ12530.
KOiK14532.
OMAiQFVTLGV.
OrthoDBiEOG7T4MXW.

Sequencei

Sequence statusi: Complete.

Q12530-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDEMDNVIRS LEQEYRLILL LNHRNKNQHR AASWYGSFNE MKRNCGQIIT
60 70 80 90 100
LFSSRRLQAK RLKDVEWVKL HRLLQRALFR QLKRWYWQFN GVIALGQFVT
110 120 130 140 150
LGCTLVTLLA NVRALYMRLW EINETEFIRC GCLIKNLPRT KAKSVVNDVE
160 170 180 190 200
ELGEIIDEDI GNNVQENELV ITSIPKPLTE NCKKKKKRKK KNKSAIDGIF

G
Length:201
Mass (Da):23,619
Last modified:November 1, 1996 - v1
Checksum:iEDE608D76402BBBC
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U53879 Genomic DNA. Translation: AAB82379.1.
Z73317 Genomic DNA. Translation: CAA97717.1.
BK006945 Genomic DNA. Translation: DAA09455.1.
PIRiS64994.
RefSeqiNP_013246.1. NM_001182032.1.

Genome annotation databases

EnsemblFungiiYLR145W; YLR145W; YLR145W.
GeneIDi850837.
KEGGisce:YLR145W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U53879 Genomic DNA. Translation: AAB82379.1.
Z73317 Genomic DNA. Translation: CAA97717.1.
BK006945 Genomic DNA. Translation: DAA09455.1.
PIRiS64994.
RefSeqiNP_013246.1. NM_001182032.1.

3D structure databases

ProteinModelPortaliQ12530.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi31414. 116 interactions.
DIPiDIP-4813N.
IntActiQ12530. 9 interactions.
MINTiMINT-573400.
STRINGi4932.YLR145W.

Proteomic databases

MaxQBiQ12530.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYLR145W; YLR145W; YLR145W.
GeneIDi850837.
KEGGisce:YLR145W.

Organism-specific databases

CYGDiYLR145w.
EuPathDBiFungiDB:YLR145W.
SGDiS000004135. RMP1.

Phylogenomic databases

eggNOGiNOG42290.
HOGENOMiHOG000066119.
InParanoidiQ12530.
KOiK14532.
OMAiQFVTLGV.
OrthoDBiEOG7T4MXW.

Enzyme and pathway databases

BioCyciYEAST:G3O-32282-MONOMER.

Miscellaneous databases

NextBioi967114.
PROiQ12530.

Family and domain databases

ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII."
    Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W., Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K., Heuss-Neitzel D., Hilbert H.
    , Hilger F., Kleine K., Koetter P., Louis E.J., Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S., Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D., Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M., Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P., Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M., Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K., Zollner A., Hani J., Hoheisel J.D.
    Nature 387:87-90(1997) [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. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  4. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  5. "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(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, IDENTIFICATION IN THE RNASE MRP COMPLEX BY MASS SPECTROMETRY, MUTAGENESIS OF CYS-103.

Entry informationi

Entry nameiRMP1_YEAST
AccessioniPrimary (citable) accession number: Q12530
Secondary accession number(s): D6VYD9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 9, 2007
Last sequence update: November 1, 1996
Last modified: June 24, 2015
This is version 92 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 556 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 XII
    Yeast (Saccharomyces cerevisiae) chromosome XII: 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.