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P26321 (RL5_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 133. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
60S ribosomal protein L5
Alternative name(s):
L1
L1a
Ribosomal 5S RNA-binding protein
YL3
Gene names
Name:RPL5
Synonyms:RPL1, RPL1A
Ordered Locus Names:YPL131W
ORF Names:LPI14W
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length297 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Binds 5S RNA and is required for 60S subunit assembly. HAMAP-Rule MF_01337_A

Subunit structure

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. Ref.7

Subcellular location

Cytoplasm. Nucleus. Note: The SYO1/RPL11/RPL5 complex is transported into the nucleus by KAP104. Ref.8 Ref.14

Sequence similarities

Belongs to the ribosomal protein L18P family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

NOG1Q028922EBI-15398,EBI-12105

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.6
Chain2 – 29729660S ribosomal protein L5 HAMAP-Rule MF_01337_A
PRO_0000131454

Amino acid modifications

Modified residue1671Phosphoserine Ref.11
Modified residue1761Phosphoserine Ref.11
Modified residue2351Phosphoserine Ref.9 Ref.11

Experimental info

Sequence conflict181T → Y AA sequence Ref.6
Sequence conflict1121K → R in AAA35234. Ref.1
Sequence conflict1121K → R in AAA35236. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P26321 [UniParc].

Last modified October 5, 2010. Version 4.
Checksum: 14E3B2931C3CAE2B

FASTA29733,715
        10         20         30         40         50         60 
MAFQKDAKSS AYSSRFQTPF RRRREGKTDY YQRKRLVTQH KAKYNTPKYR LVVRFTNKDI 

        70         80         90        100        110        120 
ICQIISSTIT GDVVLAAAYS HELPRYGITH GLTNWAAAYA TGLLIARRTL QKLGLDETYK 

       130        140        150        160        170        180 
GVEEVEGEYE LTEAVEDGPR PFKVFLDIGL QRTTTGARVF GALKGASDGG LYVPHSENRF 

       190        200        210        220        230        240 
PGWDFETEEI DPELLRSYIF GGHVSQYMEE LADDDEERFS ELFKGYLADD IDADSLEDIY 

       250        260        270        280        290 
TSAHEAIRAD PAFKPTEKKF TKEQYAAESK KYRQTKLSKE ERAARVAAKI AALAGQQ 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
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]"Global analysis of protein localization in budding yeast."
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K.
Nature 425:686-691(2003) [PubMed] [Europe PMC] [Abstract]
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]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
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]"Synchronizing nuclear import of ribosomal proteins with ribosome assembly."
Kressler D., Bange G., Ogawa Y., Stjepanovic G., Bradatsch B., Pratte D., Amlacher S., Strauss D., Yoneda Y., Katahira J., Sinning I., Hurt E.
Science 338:666-671(2012) [PubMed] [Europe PMC] [Abstract]
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]"The structure of the eukaryotic ribosome at 3.0 A resolution."
Ben-Shem A., Garreau de Loubresse N., Melnikov S., Jenner L., Yusupova G., Yusupov M.
Science 334:1524-1529(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 80S RIBOSOME.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRS42144.
RefSeqNP_015194.1. NM_001183945.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1K5Ymodel-E11-232[»]
1S1Ielectron microscopy11.70E11-232[»]
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[»]
ProteinModelPortalP26321.
SMRP26321. Positions 2-297.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid36050. 135 interactions.
DIPDIP-1790N.
IntActP26321. 163 interactions.
MINTMINT-8285488.
STRING4932.YPL131W.

Proteomic databases

MaxQBP26321.
PaxDbP26321.
PeptideAtlasP26321.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYPL131W; YPL131W; YPL131W.
GeneID855972.
KEGGsce:YPL131W.

Organism-specific databases

SGDS000006052. RPL5.

Phylogenomic databases

eggNOGCOG0256.
GeneTreeENSGT00390000008456.
HOGENOMHOG000105947.
KOK02932.
OMAKAYGITH.
OrthoDBEOG7DJSXQ.

Enzyme and pathway databases

BioCycYEAST:G3O-34030-MONOMER.

Gene expression databases

GenevestigatorP26321.

Family and domain databases

HAMAPMF_01337_A. Ribosomal_L18_A.
InterProIPR005485. Rbsml_L5_euk/L18_arc.
IPR025607. Rbsml_L5e/L18P_C.
IPR005484. Ribosomal_L18/L5.
[Graphical view]
PANTHERPTHR23410. PTHR23410. 1 hit.
PfamPF14204. Ribosomal_L18_c. 1 hit.
PF00861. Ribosomal_L18p. 1 hit.
[Graphical view]
PRINTSPR00058. RIBOSOMALL5.
ProtoNetSearch...

Other

EvolutionaryTraceP26321.
NextBio980789.
PROP26321.

Entry information

Entry nameRL5_YEAST
AccessionPrimary (citable) accession number: P26321
Secondary accession number(s): D6W3N6
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: October 5, 2010
Last modified: June 11, 2014
This is version 133 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome XVI

Yeast (Saccharomyces cerevisiae) chromosome XVI: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families

Ribosomal proteins

Ribosomal proteins families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references