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Protein

M-phase phosphoprotein 6 homolog

Gene

MPP6

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

Involved in surveillance of pre-rRNAs and pre-mRNAs, and the degradation of cryptic non-coding RNAs (ncRNA) derived from intergenic regions and the ribosomal DNA spacer heterochromatin. Binds RNA.1 Publication

GO - Molecular functioni

  1. poly(U) RNA binding Source: SGD

GO - Biological processi

  1. exonucleolytic trimming to generate mature 3'-end of 5.8S rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) Source: SGD
  2. nuclear mRNA surveillance of mRNA 3'-end processing Source: SGD
  3. nuclear mRNA surveillance of spliceosomal pre-mRNA splicing Source: SGD
  4. nuclear polyadenylation-dependent CUT catabolic process Source: SGD
  5. nuclear polyadenylation-dependent rRNA catabolic process Source: SGD
Complete GO annotation...

Keywords - Biological processi

rRNA processing

Keywords - Ligandi

RNA-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-33338-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
M-phase phosphoprotein 6 homolog
Alternative name(s):
Exosome-associated RNA-binding protein MPP6
Gene namesi
Name:MPP6
Ordered Locus Names:YNR024W
ORF Names:N3230
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311 Componenti: Chromosome XIV

Organism-specific databases

CYGDiYNR024w.
EuPathDBiFungiDB:YNR024W.
SGDiS000005307. MPP6.

Subcellular locationi

  1. Nucleus 4 Publications

  2. Note: Colocalizes with the nuclear exosome and ribosomes.

GO - Cellular componenti

  1. cytosol Source: SGD
  2. nucleus Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Disruption phenotypei

Lethal in combination with the absence of either RRP6 or its cofactor RRP47. Weak but detectable stabilization of unspliced pre-mRNAs, and stronger stabilization is detected for mRNAs with defects in 3' cleavage and polyadenylation.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 186185M-phase phosphoprotein 6 homologPRO_0000203474Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine1 Publication
Modified residuei42 – 421Phosphoserine1 Publication
Modified residuei150 – 1501Phosphoserine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP53725.
PaxDbiP53725.

Expressioni

Gene expression databases

GenevestigatoriP53725.

Interactioni

Protein-protein interaction databases

BioGridi35849. 37 interactions.
DIPiDIP-4263N.
IntActiP53725. 1 interaction.
MINTiMINT-567258.
STRINGi4932.YNR024W.

Structurei

3D structure databases

ProteinModelPortaliP53725.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Phylogenomic databases

InParanoidiP53725.
KOiK12594.
OMAiNMKFMKF.
OrthoDBiEOG7V76K9.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P53725-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSANNGVTGK LSSRVMNMKF MKFGKTDDEE SSNSNTPSNI NSDVEPIEQK
60 70 80 90 100
GKLFGLDDSA WDLNSYKDDL KKISGKEKKK VKRVVYKKRP NLIISNVGYS
110 120 130 140 150
ELRKPEGVIS GRKTFGDNSD DSGSRKRKFD EGEQNEDEKR DAKDKEFTGS
160 170 180
QDDGEDEYDL DKLFKDSIKK KKTNHNGKNK NRNSKK
Length:186
Mass (Da):21,142
Last modified:October 1, 1996 - v1
Checksum:iB1DEE530E6F9379C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z71639 Genomic DNA. Translation: CAA96303.1.
BK006947 Genomic DNA. Translation: DAA10565.1.
PIRiS63355.
RefSeqiNP_014421.3. NM_001183201.3.

Genome annotation databases

EnsemblFungiiYNR024W; YNR024W; YNR024W.
GeneIDi855758.
KEGGisce:YNR024W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z71639 Genomic DNA. Translation: CAA96303.1.
BK006947 Genomic DNA. Translation: DAA10565.1.
PIRiS63355.
RefSeqiNP_014421.3. NM_001183201.3.

3D structure databases

ProteinModelPortaliP53725.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi35849. 37 interactions.
DIPiDIP-4263N.
IntActiP53725. 1 interaction.
MINTiMINT-567258.
STRINGi4932.YNR024W.

Proteomic databases

MaxQBiP53725.
PaxDbiP53725.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYNR024W; YNR024W; YNR024W.
GeneIDi855758.
KEGGisce:YNR024W.

Organism-specific databases

CYGDiYNR024w.
EuPathDBiFungiDB:YNR024W.
SGDiS000005307. MPP6.

Phylogenomic databases

InParanoidiP53725.
KOiK12594.
OMAiNMKFMKF.
OrthoDBiEOG7V76K9.

Enzyme and pathway databases

BioCyciYEAST:G3O-33338-MONOMER.

Miscellaneous databases

NextBioi980187.
PROiP53725.

Gene expression databases

GenevestigatoriP53725.

Family and domain databases

ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its evolutionary implications."
    Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K., Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K., Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M., Beinhauer J.D., Boskovic J., Buitrago M.J.
    , Bussereau F., Coster F., Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F., Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C., Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A., Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H., Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L., Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R., Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D., Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A., Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C., Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F., Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G., Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M., Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.
    Nature 387:93-98(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. "Systematic identification and functional screens of uncharacterized proteins associated with eukaryotic ribosomal complexes."
    Fleischer T.C., Weaver C.M., McAfee K.J., Jennings J.L., Link A.J.
    Genes Dev. 20:1294-1307(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  6. "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
    Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
    J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.
  7. "A yeast exosome cofactor, Mpp6, functions in RNA surveillance and in the degradation of noncoding RNA transcripts."
    Milligan L., Decourty L., Saveanu C., Rappsilber J., Ceulemans H., Jacquier A., Tollervey D.
    Mol. Cell. Biol. 28:5446-5457(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, RNA-BINDING, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, IDENTIFICATION BY MASS SPECTROMETRY.
  8. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
    Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
    Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-42 AND SER-150, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "Comparative multiplexed mass spectrometric analyses of endogenously expressed yeast nuclear and cytoplasmic exosomes."
    Synowsky S.A., van Wijk M., Raijmakers R., Heck A.J.
    J. Mol. Biol. 385:1300-1313(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
  10. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
    Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
    Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiMPP6_YEAST
AccessioniPrimary (citable) accession number: P53725
Secondary accession number(s): D6W1J9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: April 29, 2015
This is version 91 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 1350 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 XIV
    Yeast (Saccharomyces cerevisiae) chromosome XIV: 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.