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P26321

- RL5_YEAST

UniProt

P26321 - RL5_YEAST

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Protein

60S ribosomal protein L5

Gene
RPL5, RPL1, RPL1A, YPL131W, LPI14W
Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Binds 5S RNA and is required for 60S subunit assembly.UniRule annotation

GO - Molecular functioni

  1. 5S rRNA binding Source: SGD
  2. protein binding Source: IntAct
  3. structural constituent of ribosome Source: SGD

GO - Biological processi

  1. cytoplasmic translation Source: SGD
  2. ribosomal large subunit assembly Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Keywords - Ligandi

RNA-binding, rRNA-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-34030-MONOMER.
ReactomeiREACT_188965. SRP-dependent cotranslational protein targeting to membrane.
REACT_189050. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
REACT_189183. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
REACT_217188. Formation of a pool of free 40S subunits.

Names & Taxonomyi

Protein namesi
Recommended name:
60S ribosomal protein L5
Alternative name(s):
L1
L1a
Ribosomal 5S RNA-binding protein
YL3
Gene namesi
Name:RPL5
Synonyms:RPL1, RPL1A
Ordered Locus Names:YPL131W
ORF Names:LPI14W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome XVI

Organism-specific databases

SGDiS000006052. RPL5.

Subcellular locationi

Cytoplasm. Nucleus
Note: The SYO1/RPL11/RPL5 complex is transported into the nucleus by KAP104.2 Publications

GO - Cellular componenti

  1. cytosolic large ribosomal subunit Source: SGD
  2. nucleus Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 29729660S ribosomal protein L5UniRule annotationPRO_0000131454Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei167 – 1671Phosphoserine1 Publication
Modified residuei176 – 1761Phosphoserine1 Publication
Modified residuei235 – 2351Phosphoserine2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP26321.
PaxDbiP26321.
PeptideAtlasiP26321.

Expressioni

Gene expression databases

GenevestigatoriP26321.

Interactioni

Subunit structurei

Component of the large ribosomal subunit. Mature ribosomes consist of a small (40S) and a large (60S) subunit. The 40S subunit contains 32 different proteins (encoded by 56 genes) and 1 molecule of RNA (18S). The 60S subunit contains 46 different proteins (encoded by 81 genes) and 3 molecules of RNA (25S, 5.8S and 5S). Forms a heterotrimeric complex with SYO1 and RPL11A or RPL11B. Interaction of this complex with KAP104 allows the nuclear import of the heterotrimer.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
NOG1Q028922EBI-15398,EBI-12105

Protein-protein interaction databases

BioGridi36050. 135 interactions.
DIPiDIP-1790N.
IntActiP26321. 163 interactions.
MINTiMINT-8285488.
STRINGi4932.YPL131W.

Structurei

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1K5Ymodel-E11-232[»]
1S1Ielectron microscopy11.70E11-232[»]
1VW8electron microscopy6.10E1-297[»]
1VWUelectron microscopy6.10E1-297[»]
3IZSelectron microscopy-Q1-297[»]
3J65electron microscopy8.70P1-297[»]
3O58X-ray4.00E1-297[»]
3O5HX-ray4.00E1-297[»]
3U5EX-ray3.00D1-297[»]
3U5IX-ray3.00D1-297[»]
4B6Aelectron microscopy8.10D1-297[»]
4BYNelectron microscopy4.30D2-297[»]
4BYUelectron microscopy6.60D2-297[»]
4CUWelectron microscopy3.70D1-297[»]
ProteinModelPortaliP26321.
SMRiP26321. Positions 2-297.

Miscellaneous databases

EvolutionaryTraceiP26321.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0256.
GeneTreeiENSGT00390000008456.
HOGENOMiHOG000105947.
KOiK02932.
OMAiKAYGITH.
OrthoDBiEOG7DJSXQ.

Family and domain databases

HAMAPiMF_01337_A. Ribosomal_L18_A.
InterProiIPR005485. Rbsml_L5_euk/L18_arc.
IPR025607. Rbsml_L5e/L18P_C.
IPR005484. Ribosomal_L18/L5.
[Graphical view]
PANTHERiPTHR23410. PTHR23410. 1 hit.
PfamiPF14204. Ribosomal_L18_c. 1 hit.
PF00861. Ribosomal_L18p. 1 hit.
[Graphical view]
PRINTSiPR00058. RIBOSOMALL5.

Sequencei

Sequence statusi: Complete.

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

P26321-1 [UniParc]FASTAAdd to Basket

« Hide

MAFQKDAKSS AYSSRFQTPF RRRREGKTDY YQRKRLVTQH KAKYNTPKYR    50
LVVRFTNKDI ICQIISSTIT GDVVLAAAYS HELPRYGITH GLTNWAAAYA 100
TGLLIARRTL QKLGLDETYK GVEEVEGEYE LTEAVEDGPR PFKVFLDIGL 150
QRTTTGARVF GALKGASDGG LYVPHSENRF PGWDFETEEI DPELLRSYIF 200
GGHVSQYMEE LADDDEERFS ELFKGYLADD IDADSLEDIY TSAHEAIRAD 250
PAFKPTEKKF TKEQYAAESK KYRQTKLSKE ERAARVAAKI AALAGQQ 297
Length:297
Mass (Da):33,715
Last modified:October 5, 2010 - v4
Checksum:i14E3B2931C3CAE2B
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti18 – 181T → Y AA sequence 1 Publication
Sequence conflicti112 – 1121K → R in AAA35234. 1 Publication
Sequence conflicti112 – 1121K → R in AAA35236. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M65056 Genomic DNA. Translation: AAA35234.1.
M94864 Genomic DNA. Translation: AAA35236.1.
L01796 Genomic DNA. Translation: AAA34979.1.
U43703 Genomic DNA. Translation: AAB68228.1.
BK006949 Genomic DNA. Translation: DAA11302.1.
PIRiS42144.
RefSeqiNP_015194.1. NM_001183945.1.

Genome annotation databases

EnsemblFungiiYPL131W; YPL131W; YPL131W.
GeneIDi855972.
KEGGisce:YPL131W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M65056 Genomic DNA. Translation: AAA35234.1 .
M94864 Genomic DNA. Translation: AAA35236.1 .
L01796 Genomic DNA. Translation: AAA34979.1 .
U43703 Genomic DNA. Translation: AAB68228.1 .
BK006949 Genomic DNA. Translation: DAA11302.1 .
PIRi S42144.
RefSeqi NP_015194.1. NM_001183945.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1K5Y model - E 11-232 [» ]
1S1I electron microscopy 11.70 E 11-232 [» ]
1VW8 electron microscopy 6.10 E 1-297 [» ]
1VWU electron microscopy 6.10 E 1-297 [» ]
3IZS electron microscopy - Q 1-297 [» ]
3J65 electron microscopy 8.70 P 1-297 [» ]
3O58 X-ray 4.00 E 1-297 [» ]
3O5H X-ray 4.00 E 1-297 [» ]
3U5E X-ray 3.00 D 1-297 [» ]
3U5I X-ray 3.00 D 1-297 [» ]
4B6A electron microscopy 8.10 D 1-297 [» ]
4BYN electron microscopy 4.30 D 2-297 [» ]
4BYU electron microscopy 6.60 D 2-297 [» ]
4CUW electron microscopy 3.70 D 1-297 [» ]
ProteinModelPortali P26321.
SMRi P26321. Positions 2-297.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 36050. 135 interactions.
DIPi DIP-1790N.
IntActi P26321. 163 interactions.
MINTi MINT-8285488.
STRINGi 4932.YPL131W.

Proteomic databases

MaxQBi P26321.
PaxDbi P26321.
PeptideAtlasi P26321.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YPL131W ; YPL131W ; YPL131W .
GeneIDi 855972.
KEGGi sce:YPL131W.

Organism-specific databases

SGDi S000006052. RPL5.

Phylogenomic databases

eggNOGi COG0256.
GeneTreei ENSGT00390000008456.
HOGENOMi HOG000105947.
KOi K02932.
OMAi KAYGITH.
OrthoDBi EOG7DJSXQ.

Enzyme and pathway databases

BioCyci YEAST:G3O-34030-MONOMER.
Reactomei REACT_188965. SRP-dependent cotranslational protein targeting to membrane.
REACT_189050. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
REACT_189183. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
REACT_217188. Formation of a pool of free 40S subunits.

Miscellaneous databases

EvolutionaryTracei P26321.
NextBioi 980789.
PROi P26321.

Gene expression databases

Genevestigatori P26321.

Family and domain databases

HAMAPi MF_01337_A. Ribosomal_L18_A.
InterProi IPR005485. Rbsml_L5_euk/L18_arc.
IPR025607. Rbsml_L5e/L18P_C.
IPR005484. Ribosomal_L18/L5.
[Graphical view ]
PANTHERi PTHR23410. PTHR23410. 1 hit.
Pfami PF14204. Ribosomal_L18_c. 1 hit.
PF00861. Ribosomal_L18p. 1 hit.
[Graphical view ]
PRINTSi PR00058. RIBOSOMALL5.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Structure of the yeast ribosomal 5 S RNA-binding protein YL3."
    Tang B., Nazar R.N.
    J. Biol. Chem. 266:6120-6123(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. "Unbalanced regulation of the ribosomal 5 S RNA-binding protein in Saccharomyces cerevisiae expressing mutant 5 S rRNAs."
    Tang B., Nazar R.N.
    J. Biol. Chem. 267:17738-17742(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Yeast ribosomal protein L1 is required for the stability of newly synthesized 5S rRNA and the assembly of 60S ribosomal subunits."
    Deshmukh M.P., Tsay Y.F., Paulovich A.G., Woolford J.L. Jr.
    Mol. Cell. Biol. 13:2835-2845(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI."
    Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W., Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D., Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E., Churcher C.M.
    , Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H., DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N., Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K., Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M., Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A., Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S., Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D., Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S., Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B., Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A., Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R., Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A., Vo D.H., Hani J.
    Nature 387:103-105(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  5. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  6. "The 5-S RNA binding protein from yeast (Saccharomyces cerevisiae) ribosomes. Evolution of the eukaryotic 5-S RNA binding protein."
    Nazar R.N., Yaguchi M., Willick G.E., Rollin C.F., Roy C.
    Eur. J. Biochem. 102:573-582(1979) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-31 AND 219-253.
  7. "The list of cytoplasmic ribosomal proteins of Saccharomyces cerevisiae."
    Planta R.J., Mager W.H.
    Yeast 14:471-477(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NOMENCLATURE, SUBUNIT.
  8. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  9. "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 SER-235, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.
  10. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "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 SER-167; SER-176 AND SER-235, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "Sites of ubiquitin attachment in Saccharomyces cerevisiae."
    Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.
    Proteomics 12:236-240(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. Cited for: INTERACTION WITH RPL11A; RPL11B AND SYO1, SUBCELLULAR LOCATION.
  15. "Structure of the 80S ribosome from Saccharomyces cerevisiae -- tRNA-ribosome and subunit-subunit interactions."
    Spahn C.M.T., Beckmann R., Eswar N., Penczek P.A., Sali A., Blobel G., Frank J.
    Cell 107:373-386(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: 3D-STRUCTURE MODELING OF 11-232, ELECTRON MICROSCOPY.
  16. "Domain movements of elongation factor eEF2 and the eukaryotic 80S ribosome facilitate tRNA translocation."
    Spahn C.M.T., Gomez-Lorenzo M.G., Grassucci R.A., Joergensen R., Andersen G.R., Beckmann R., Penczek P.A., Ballesta J.P.G., Frank J.
    EMBO J. 23:1008-1019(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: 3D-STRUCTURE MODELING OF 11-232, ELECTRON MICROSCOPY.
  17. "Crystal structure of the eukaryotic ribosome."
    Ben-Shem A., Jenner L., Yusupova G., Yusupov M.
    Science 330:1203-1209(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (4.0 ANGSTROMS) OF 80S RIBOSOME.
  18. Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 80S RIBOSOME.

Entry informationi

Entry nameiRL5_YEAST
AccessioniPrimary (citable) accession number: P26321
Secondary accession number(s): D6W3N6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: October 5, 2010
Last modified: September 3, 2014
This is version 134 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, 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 XVI
    Yeast (Saccharomyces cerevisiae) chromosome XVI: entries and gene names

External Data

Dasty 3

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