Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

60S ribosomal protein L5

Gene

RPL5

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

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

GO - Molecular functioni

  • 5S rRNA binding Source: SGD
  • structural constituent of ribosome Source: SGD

GO - Biological processi

  • cytoplasmic translation Source: SGD
  • ribosomal large subunit assembly Source: SGD
  • translation Source: GO_Central
Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Keywords - Ligandi

RNA-binding, rRNA-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-34030-MONOMER.
ReactomeiR-SCE-156827. L13a-mediated translational silencing of Ceruloplasmin expression.
R-SCE-1799339. SRP-dependent cotranslational protein targeting to membrane.
R-SCE-72689. Formation of a pool of free 40S subunits.
R-SCE-72706. GTP hydrolysis and joining of the 60S ribosomal subunit.
R-SCE-975956. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
R-SCE-975957. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).

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
Proteomesi
  • UP000002311 Componenti: Chromosome XVI

Organism-specific databases

EuPathDBiFungiDB:YPL131W.
SGDiS000006052. RPL5.

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00001314542 – 29760S ribosomal protein L5Add BLAST296

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Cross-linki164Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources
Modified residuei167PhosphoserineCombined sources1
Modified residuei176PhosphoserineCombined sources1
Modified residuei235PhosphoserineCombined sources1

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP26321.
PRIDEiP26321.

PTM databases

iPTMnetiP26321.

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. 107 interactors.
DIPiDIP-1790N.
IntActiP26321. 164 interactors.
MINTiMINT-8285488.

Structurei

Secondary structure

1297
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi4 – 7Combined sources4
Helixi10 – 14Combined sources5
Helixi21 – 24Combined sources4
Helixi30 – 37Combined sources8
Helixi41 – 43Combined sources3
Beta strandi50 – 56Combined sources7
Beta strandi59 – 68Combined sources10
Beta strandi71 – 79Combined sources9
Helixi80 – 86Combined sources7
Beta strandi92 – 94Combined sources3
Helixi95 – 112Combined sources18
Beta strandi116 – 118Combined sources3
Beta strandi136 – 138Combined sources3
Beta strandi145 – 147Combined sources3
Helixi159 – 168Combined sources10
Helixi177 – 179Combined sources3
Beta strandi180 – 184Combined sources5
Turni185 – 188Combined sources4
Helixi192 – 199Combined sources8
Helixi202 – 214Combined sources13
Helixi216 – 221Combined sources6
Helixi224 – 228Combined sources5
Helixi233 – 235Combined sources3
Helixi236 – 249Combined sources14
Helixi262 – 270Combined sources9
Beta strandi271 – 273Combined sources3
Helixi279 – 292Combined sources14
Turni293 – 296Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1K5Ymodel-E11-232[»]
3J6Xelectron microscopy6.10L51-297[»]
3J6Yelectron microscopy6.10L51-297[»]
3J77electron microscopy6.20L51-297[»]
3J78electron microscopy6.30L51-297[»]
3JCTelectron microscopy3.08D1-297[»]
4U3MX-ray3.00L5/l52-297[»]
4U3NX-ray3.20L5/l52-297[»]
4U3UX-ray2.90L5/l52-297[»]
4U4NX-ray3.10L5/l52-297[»]
4U4OX-ray3.60L5/l52-297[»]
4U4QX-ray3.00L5/l52-297[»]
4U4RX-ray2.80L5/l52-297[»]
4U4UX-ray3.00L5/l52-297[»]
4U4YX-ray3.20L5/l52-297[»]
4U4ZX-ray3.10L5/l52-297[»]
4U50X-ray3.20L5/l52-297[»]
4U51X-ray3.20L5/l52-297[»]
4U52X-ray3.00L5/l52-297[»]
4U53X-ray3.30L5/l52-297[»]
4U55X-ray3.20L5/l52-297[»]
4U56X-ray3.45L5/l52-297[»]
4U6FX-ray3.10L5/l52-297[»]
4V4Belectron microscopy11.70BE11-232[»]
4V6Ielectron microscopy8.80BQ1-297[»]
4V7Felectron microscopy8.70P1-297[»]
4V7RX-ray4.00BE/DE1-297[»]
4V88X-ray3.00BD/DD1-297[»]
4V8Telectron microscopy8.10D1-297[»]
4V8Yelectron microscopy4.30BD2-297[»]
4V8Zelectron microscopy6.60BD2-297[»]
4V91electron microscopy3.70D1-297[»]
5APNelectron microscopy3.91D1-297[»]
5APOelectron microscopy3.41D1-297[»]
5DATX-ray3.15L5/l52-297[»]
5DC3X-ray3.25L5/l52-297[»]
5FCIX-ray3.40L5/l52-297[»]
5FCJX-ray3.10L5/l52-297[»]
5FL8electron microscopy9.50D1-297[»]
5GAKelectron microscopy3.88H1-297[»]
5I4LX-ray3.10L5/l52-297[»]
5JUOelectron microscopy4.00I1-297[»]
5JUPelectron microscopy3.50I1-297[»]
5JUSelectron microscopy4.20I1-297[»]
5JUTelectron microscopy4.00I1-297[»]
5JUUelectron microscopy4.00I1-297[»]
ProteinModelPortaliP26321.
SMRiP26321.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP26321.

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L18P family.Curated

Phylogenomic databases

GeneTreeiENSGT00390000008456.
HOGENOMiHOG000105947.
InParanoidiP26321.
KOiK02932.
OMAiDDEERYN.
OrthoDBiEOG092C44EY.

Family and domain databases

HAMAPiMF_01337_A. Ribosomal_L18_A. 1 hit.
InterProiIPR005485. Rbsml_L5_euk/L18_arc.
IPR025607. Rbsml_L5e/L18P_C.
[Graphical view]
PANTHERiPTHR23410. PTHR23410. 1 hit.
PfamiPF14204. Ribosomal_L18_c. 1 hit.
PF17144. Ribosomal_L5e. 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

        10         20         30         40         50
MAFQKDAKSS AYSSRFQTPF RRRREGKTDY YQRKRLVTQH KAKYNTPKYR
60 70 80 90 100
LVVRFTNKDI ICQIISSTIT GDVVLAAAYS HELPRYGITH GLTNWAAAYA
110 120 130 140 150
TGLLIARRTL QKLGLDETYK GVEEVEGEYE LTEAVEDGPR PFKVFLDIGL
160 170 180 190 200
QRTTTGARVF GALKGASDGG LYVPHSENRF PGWDFETEEI DPELLRSYIF
210 220 230 240 250
GGHVSQYMEE LADDDEERFS ELFKGYLADD IDADSLEDIY TSAHEAIRAD
260 270 280 290
PAFKPTEKKF TKEQYAAESK KYRQTKLSKE ERAARVAAKI AALAGQQ
Length:297
Mass (Da):33,715
Last modified:October 5, 2010 - v4
Checksum:i14E3B2931C3CAE2B
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti18T → Y AA sequence (PubMed:393511).Curated1
Sequence conflicti112K → R in AAA35234 (PubMed:2007570).Curated1
Sequence conflicti112K → R in AAA35236 (PubMed:1325447).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1K5Ymodel-E11-232[»]
3J6Xelectron microscopy6.10L51-297[»]
3J6Yelectron microscopy6.10L51-297[»]
3J77electron microscopy6.20L51-297[»]
3J78electron microscopy6.30L51-297[»]
3JCTelectron microscopy3.08D1-297[»]
4U3MX-ray3.00L5/l52-297[»]
4U3NX-ray3.20L5/l52-297[»]
4U3UX-ray2.90L5/l52-297[»]
4U4NX-ray3.10L5/l52-297[»]
4U4OX-ray3.60L5/l52-297[»]
4U4QX-ray3.00L5/l52-297[»]
4U4RX-ray2.80L5/l52-297[»]
4U4UX-ray3.00L5/l52-297[»]
4U4YX-ray3.20L5/l52-297[»]
4U4ZX-ray3.10L5/l52-297[»]
4U50X-ray3.20L5/l52-297[»]
4U51X-ray3.20L5/l52-297[»]
4U52X-ray3.00L5/l52-297[»]
4U53X-ray3.30L5/l52-297[»]
4U55X-ray3.20L5/l52-297[»]
4U56X-ray3.45L5/l52-297[»]
4U6FX-ray3.10L5/l52-297[»]
4V4Belectron microscopy11.70BE11-232[»]
4V6Ielectron microscopy8.80BQ1-297[»]
4V7Felectron microscopy8.70P1-297[»]
4V7RX-ray4.00BE/DE1-297[»]
4V88X-ray3.00BD/DD1-297[»]
4V8Telectron microscopy8.10D1-297[»]
4V8Yelectron microscopy4.30BD2-297[»]
4V8Zelectron microscopy6.60BD2-297[»]
4V91electron microscopy3.70D1-297[»]
5APNelectron microscopy3.91D1-297[»]
5APOelectron microscopy3.41D1-297[»]
5DATX-ray3.15L5/l52-297[»]
5DC3X-ray3.25L5/l52-297[»]
5FCIX-ray3.40L5/l52-297[»]
5FCJX-ray3.10L5/l52-297[»]
5FL8electron microscopy9.50D1-297[»]
5GAKelectron microscopy3.88H1-297[»]
5I4LX-ray3.10L5/l52-297[»]
5JUOelectron microscopy4.00I1-297[»]
5JUPelectron microscopy3.50I1-297[»]
5JUSelectron microscopy4.20I1-297[»]
5JUTelectron microscopy4.00I1-297[»]
5JUUelectron microscopy4.00I1-297[»]
ProteinModelPortaliP26321.
SMRiP26321.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi36050. 107 interactors.
DIPiDIP-1790N.
IntActiP26321. 164 interactors.
MINTiMINT-8285488.

PTM databases

iPTMnetiP26321.

Proteomic databases

MaxQBiP26321.
PRIDEiP26321.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

EuPathDBiFungiDB:YPL131W.
SGDiS000006052. RPL5.

Phylogenomic databases

GeneTreeiENSGT00390000008456.
HOGENOMiHOG000105947.
InParanoidiP26321.
KOiK02932.
OMAiDDEERYN.
OrthoDBiEOG092C44EY.

Enzyme and pathway databases

BioCyciYEAST:G3O-34030-MONOMER.
ReactomeiR-SCE-156827. L13a-mediated translational silencing of Ceruloplasmin expression.
R-SCE-1799339. SRP-dependent cotranslational protein targeting to membrane.
R-SCE-72689. Formation of a pool of free 40S subunits.
R-SCE-72706. GTP hydrolysis and joining of the 60S ribosomal subunit.
R-SCE-975956. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
R-SCE-975957. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).

Miscellaneous databases

EvolutionaryTraceiP26321.
PROiP26321.

Family and domain databases

HAMAPiMF_01337_A. Ribosomal_L18_A. 1 hit.
InterProiIPR005485. Rbsml_L5_euk/L18_arc.
IPR025607. Rbsml_L5e/L18P_C.
[Graphical view]
PANTHERiPTHR23410. PTHR23410. 1 hit.
PfamiPF14204. Ribosomal_L18_c. 1 hit.
PF17144. Ribosomal_L5e. 1 hit.
[Graphical view]
PRINTSiPR00058. RIBOSOMALL5.
ProtoNetiSearch...

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: November 30, 2016
This is version 160 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

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 one 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.