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Protein

Ribosome biogenesis protein RLP7

Gene

RLP7

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

Involved in the biogenesis of the 60S ribosomal subunit. May act as a specificity factor that binds precursor rRNAs and tethers the enzymes that carry out the early 5' to 3' exonucleolytic reactions that generate the mature rRNAs.1 Publication

GO - Molecular functioni

  • rRNA binding Source: SGD

GO - Biological processi

  • exonucleolytic trimming to generate mature 5'-end of 5.8S rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) Source: SGD
  • maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) Source: SGD
  • ribosomal large subunit biogenesis Source: SGD
Complete GO annotation...

Keywords - Biological processi

Ribosome biogenesis

Keywords - Ligandi

RNA-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-33044-MONOMER.
ReactomeiREACT_290856. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
REACT_302067. L13a-mediated translational silencing of Ceruloplasmin expression.
REACT_307259. Formation of a pool of free 40S subunits.
REACT_314339. SRP-dependent cotranslational protein targeting to membrane.
REACT_332565. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
REACT_343353. Peptide chain elongation.
REACT_346847. GTP hydrolysis and joining of the 60S ribosomal subunit.

Names & Taxonomyi

Protein namesi
Recommended name:
Ribosome biogenesis protein RLP7
Alternative name(s):
Ribosomal protein L7-like
Gene namesi
Name:RLP7
Synonyms:RPL7
Ordered Locus Names:YNL002C
ORF Names:N2014
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311 Componenti: Chromosome XIV

Organism-specific databases

CYGDiYNL002c.
EuPathDBiFungiDB:YNL002C.
SGDiS000004947. RLP7.

Subcellular locationi

GO - Cellular componenti

  • nucleolus Source: SGD
  • preribosome, large subunit precursor Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 322321Ribosome biogenesis protein RLP7PRO_0000104658Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine1 Publication
Modified residuei14 – 141Phosphoserine1 Publication
Modified residuei120 – 1201Phosphothreonine3 Publications
Modified residuei278 – 2781Phosphoserine2 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP40693.
PaxDbiP40693.
PeptideAtlasiP40693.

Interactioni

Protein-protein interaction databases

BioGridi35823. 374 interactions.
DIPiDIP-6476N.
IntActiP40693. 34 interactions.
MINTiMINT-8285428.
STRINGi4932.YNL002C.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4V7Felectron microscopy8.70r/s1-322[»]
ProteinModelPortaliP40693.
SMRiP40693. Positions 140-196.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L30P family.Curated

Phylogenomic databases

eggNOGiCOG1841.
HOGENOMiHOG000170917.
InParanoidiP40693.
KOiK02937.
OMAiPFKLNRE.
OrthoDBiEOG7TBCCW.

Family and domain databases

Gene3Di3.30.1390.20. 2 hits.
InterProiIPR018038. Ribosomal_L30_CS.
IPR016082. Ribosomal_L30_ferredoxin-like.
[Graphical view]
PfamiPF00327. Ribosomal_L30. 1 hit.
[Graphical view]
SUPFAMiSSF55129. SSF55129. 1 hit.
PROSITEiPS00634. RIBOSOMAL_L30. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P40693-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSTQDSKAQ TLNSNPEILL RKRRNADRTR IERQELAKKK REEQIKKKRS
60 70 80 90 100
NKNKFVRAES IVAKTLATSR EKERIKRVSI LEDKKAKNET QHIASGKDFI
110 120 130 140 150
LKITEKANGA EENSVDLEET EEEEDDGLIR EKTTYDGKPA LLFIVRVRGP
160 170 180 190 200
LAVNIPNKAF KILSLLRLVE TNTGVFVKLT KNVYPLLKVI APYVVIGKPS
210 220 230 240 250
LSSIRSLIQK RGRIIYKGEN EAEPHEIVLN DNNIVEEQLG DHGIICVEDI
260 270 280 290 300
IHEIATMGES FSVCNFFLQP FKLNREVSGF GSLNRLRKIK QREAESRTRQ
310 320
FSNAATAPVI EVDIDSLLAK LN
Length:322
Mass (Da):36,559
Last modified:February 1, 1995 - v1
Checksum:i64714DDFAFB90B5D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L19167 Genomic DNA. Translation: AAA34982.1.
X77114 Genomic DNA. Translation: CAA54376.1.
Z71278 Genomic DNA. Translation: CAA95861.1.
AY693031 Genomic DNA. Translation: AAT93050.1.
BK006947 Genomic DNA. Translation: DAA10541.1.
PIRiS38194.
RefSeqiNP_014396.3. NM_001182841.3.

Genome annotation databases

EnsemblFungiiYNL002C; YNL002C; YNL002C.
GeneIDi855730.
KEGGisce:YNL002C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L19167 Genomic DNA. Translation: AAA34982.1.
X77114 Genomic DNA. Translation: CAA54376.1.
Z71278 Genomic DNA. Translation: CAA95861.1.
AY693031 Genomic DNA. Translation: AAT93050.1.
BK006947 Genomic DNA. Translation: DAA10541.1.
PIRiS38194.
RefSeqiNP_014396.3. NM_001182841.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4V7Felectron microscopy8.70r/s1-322[»]
ProteinModelPortaliP40693.
SMRiP40693. Positions 140-196.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi35823. 374 interactions.
DIPiDIP-6476N.
IntActiP40693. 34 interactions.
MINTiMINT-8285428.
STRINGi4932.YNL002C.

Proteomic databases

MaxQBiP40693.
PaxDbiP40693.
PeptideAtlasiP40693.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYNL002C; YNL002C; YNL002C.
GeneIDi855730.
KEGGisce:YNL002C.

Organism-specific databases

CYGDiYNL002c.
EuPathDBiFungiDB:YNL002C.
SGDiS000004947. RLP7.

Phylogenomic databases

eggNOGiCOG1841.
HOGENOMiHOG000170917.
InParanoidiP40693.
KOiK02937.
OMAiPFKLNRE.
OrthoDBiEOG7TBCCW.

Enzyme and pathway databases

BioCyciYEAST:G3O-33044-MONOMER.
ReactomeiREACT_290856. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
REACT_302067. L13a-mediated translational silencing of Ceruloplasmin expression.
REACT_307259. Formation of a pool of free 40S subunits.
REACT_314339. SRP-dependent cotranslational protein targeting to membrane.
REACT_332565. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
REACT_343353. Peptide chain elongation.
REACT_346847. GTP hydrolysis and joining of the 60S ribosomal subunit.

Miscellaneous databases

NextBioi980111.
PROiP40693.

Family and domain databases

Gene3Di3.30.1390.20. 2 hits.
InterProiIPR018038. Ribosomal_L30_CS.
IPR016082. Ribosomal_L30_ferredoxin-like.
[Graphical view]
PfamiPF00327. Ribosomal_L30. 1 hit.
[Graphical view]
SUPFAMiSSF55129. SSF55129. 1 hit.
PROSITEiPS00634. RIBOSOMAL_L30. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Two yeast chromosomes are related by a fossil duplication of their centromeric regions."
    Lalo D., Stettler S., Mariotte S., Slonimski P.P., Thuriaux P.
    C. R. Acad. Sci. III, Sci. Vie 316:367-373(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: S288c / GRF88.
  2. "Two distinct yeast proteins are related to the mammalian ribosomal polypeptide L7."
    Lalo D., Mariotte S., Thuriaux P.
    Yeast 9:1085-1091(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: S288c / GRF88.
  3. "Organization of the centromeric region of chromosome XIV in Saccharomyces cerevisiae."
    Lalo D., Stettler S., Mariotte S., Gendreau E., Thuriaux P.
    Yeast 10:523-533(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: S288c / GRF88.
  4. "Nucleotide sequence analysis of an 8887 bp region of the left arm of yeast chromosome XIV, encompassing the centromere sequence."
    Verhasselt P., Aert R., Voet M., Volckaert G.
    Yeast 10:945-951(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 96604 / S288c / FY1679.
  5. "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.
  6. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  7. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  8. "A nucleolar protein related to ribosomal protein L7 is required for an early step in large ribosomal subunit biogenesis."
    Dunbar D.A., Dragon F., Lee S.J., Baserga S.J.
    Proc. Natl. Acad. Sci. U.S.A. 97:13027-13032(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  9. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  10. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-120, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.
  11. "Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry."
    Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.
    Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-278, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "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-14; THR-120 AND SER-278, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-120, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. 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 nameiRLP7_YEAST
AccessioniPrimary (citable) accession number: P40693
Secondary accession number(s): D6W1H5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: June 24, 2015
This is version 133 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 7720 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Ribosomal proteins
    Ribosomal proteins families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families
  4. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  5. 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.