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Protein

60S ribosomal protein L3

Gene

RPL3

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

GO - Molecular functioni

  • 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

Enzyme and pathway databases

BioCyciYEAST:G3O-33603-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 L3
Alternative name(s):
Maintenance of killer protein 8
RP1
Trichodermin resistance protein
YL1
Gene namesi
Name:RPL3
Synonyms:MAK8, TCM1
Ordered Locus Names:YOR063W
ORF Names:YOR29-14
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XV

Organism-specific databases

EuPathDBiFungiDB:YOR063W.
SGDiS000005589. RPL3.

Subcellular locationi

GO - Cellular componenti

  • cytosolic large ribosomal subunit Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Disruption phenotypei

A mutant confers resistance to trichodermin, a trichotecene toxin produced by plant-pathogenic fungi.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved2 Publications
Chaini2 – 38738660S ribosomal protein L3PRO_0000077251Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei24 – 241PhosphoserineCombined sources
Cross-linki39 – 39Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources
Modified residuei103 – 1031PhosphothreonineCombined sources
Cross-linki136 – 136Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources
Modified residuei156 – 1561PhosphoserineCombined sources
Modified residuei243 – 2431Pros-methylhistidine1 Publication
Modified residuei297 – 2971PhosphoserineCombined sources

Keywords - PTMi

Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP14126.
PRIDEiP14126.

PTM databases

iPTMnetiP14126.

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).1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
SRV2P175553EBI-15364,EBI-4024

Protein-protein interaction databases

BioGridi34462. 115 interactions.
DIPiDIP-6264N.
IntActiP14126. 109 interactions.
MINTiMINT-604187.

Structurei

Secondary structure

1
387
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi14 – 163Combined sources
Beta strandi23 – 264Combined sources
Beta strandi37 – 393Combined sources
Beta strandi44 – 5916Combined sources
Turni66 – 694Combined sources
Beta strandi70 – 8011Combined sources
Beta strandi84 – 9310Combined sources
Beta strandi100 – 1067Combined sources
Helixi112 – 1154Combined sources
Helixi116 – 1183Combined sources
Turni122 – 1243Combined sources
Turni129 – 1335Combined sources
Helixi134 – 1374Combined sources
Beta strandi139 – 1413Combined sources
Helixi142 – 15312Combined sources
Beta strandi156 – 1638Combined sources
Helixi166 – 1683Combined sources
Beta strandi178 – 1825Combined sources
Beta strandi185 – 1873Combined sources
Helixi188 – 19710Combined sources
Turni198 – 2003Combined sources
Beta strandi201 – 2033Combined sources
Helixi205 – 2073Combined sources
Beta strandi214 – 2207Combined sources
Beta strandi223 – 2275Combined sources
Helixi229 – 2335Combined sources
Beta strandi246 – 2483Combined sources
Beta strandi255 – 2595Combined sources
Beta strandi268 – 2714Combined sources
Beta strandi274 – 28613Combined sources
Turni291 – 2944Combined sources
Turni297 – 2993Combined sources
Turni312 – 3143Combined sources
Beta strandi321 – 3266Combined sources
Beta strandi335 – 3406Combined sources
Turni349 – 3513Combined sources
Beta strandi356 – 3594Combined sources
Turni364 – 3674Combined sources
Helixi373 – 3808Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1K5Ymodel-C8-366[»]
3J6Xelectron microscopy6.10L31-387[»]
3J6Yelectron microscopy6.10L31-387[»]
3J77electron microscopy6.20L31-387[»]
3J78electron microscopy6.30L31-387[»]
3JCTelectron microscopy3.08B1-387[»]
4U3MX-ray3.00L3/l32-387[»]
4U3NX-ray3.20L3/l32-387[»]
4U3UX-ray2.90L3/l32-387[»]
4U4NX-ray3.10L3/l32-387[»]
4U4OX-ray3.60L3/l32-387[»]
4U4QX-ray3.00L3/l32-387[»]
4U4RX-ray2.80L3/l32-387[»]
4U4UX-ray3.00L3/l32-387[»]
4U4YX-ray3.20L3/l32-387[»]
4U4ZX-ray3.10L3/l32-387[»]
4U50X-ray3.20L3/l32-387[»]
4U51X-ray3.20L3/l32-387[»]
4U52X-ray3.00L3/l32-387[»]
4U53X-ray3.30L3/l32-387[»]
4U55X-ray3.20L3/l32-387[»]
4U56X-ray3.45L3/l32-387[»]
4U6FX-ray3.10L3/l32-387[»]
4V4Belectron microscopy11.70BC2-387[»]
4V6Ielectron microscopy8.80BC1-387[»]
4V7Felectron microscopy8.70C1-387[»]
4V7RX-ray4.00BC/DC1-387[»]
4V88X-ray3.00BB/DB1-387[»]
4V8Telectron microscopy8.10B1-387[»]
4V8Yelectron microscopy4.30BB2-387[»]
4V8Zelectron microscopy6.60BB2-387[»]
4V91electron microscopy3.70B1-387[»]
5APNelectron microscopy3.91B1-387[»]
5APOelectron microscopy3.41B1-387[»]
5DC3X-ray3.25L3/l32-387[»]
5FCIX-ray3.40L3/l32-387[»]
5FCJX-ray3.10L3/l32-387[»]
5FL8electron microscopy9.50B1-387[»]
5GAKelectron microscopy3.88F1-387[»]
5I4LX-ray3.10L3/l32-387[»]
ProteinModelPortaliP14126.
SMRiP14126. Positions 9-354.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP14126.

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L3P family.Curated

Phylogenomic databases

GeneTreeiENSGT00390000017606.
HOGENOMiHOG000107319.
InParanoidiP14126.
KOiK02925.
OMAiVPRIRSW.
OrthoDBiEOG092C2SEF.

Family and domain databases

InterProiIPR000597. Ribosomal_L3.
IPR019926. Ribosomal_L3_CS.
IPR009000. Transl_B-barrel.
[Graphical view]
PfamiPF00297. Ribosomal_L3. 1 hit.
[Graphical view]
SUPFAMiSSF50447. SSF50447. 1 hit.
PROSITEiPS00474. RIBOSOMAL_L3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P14126-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSHRKYEAPR HGHLGFLPRK RAASIRARVK AFPKDDRSKP VALTSFLGYK
60 70 80 90 100
AGMTTIVRDL DRPGSKFHKR EVVEAVTVVD TPPVVVVGVV GYVETPRGLR
110 120 130 140 150
SLTTVWAEHL SDEVKRRFYK NWYKSKKKAF TKYSAKYAQD GAGIERELAR
160 170 180 190 200
IKKYASVVRV LVHTQIRKTP LAQKKAHLAE IQLNGGSISE KVDWAREHFE
210 220 230 240 250
KTVAVDSVFE QNEMIDAIAV TKGHGFEGVT HRWGTKKLPR KTHRGLRKVA
260 270 280 290 300
CIGAWHPAHV MWSVARAGQR GYHSRTSINH KIYRVGKGDD EANGATSFDR
310 320 330 340 350
TKKTITPMGG FVHYGEIKND FIMVKGCIPG NRKRIVTLRK SLYTNTSRKA
360 370 380
LEEVSLKWID TASKFGKGRF QTPAEKHAFM GTLKKDL
Length:387
Mass (Da):43,758
Last modified:January 23, 2007 - v4
Checksum:i986769A218E9698A
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti255 – 2551W → C in AAA88732 (PubMed:6305925).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J01351 Genomic DNA. Translation: AAA88732.1.
Z74971 Genomic DNA. Translation: CAA99256.1.
Z70678 Genomic DNA. Translation: CAA94548.1.
BK006948 Genomic DNA. Translation: DAA10842.1.
PIRiS66946. R5BY4E.
RefSeqiNP_014706.1. NM_001183482.1.

Genome annotation databases

EnsemblFungiiYOR063W; YOR063W; YOR063W.
GeneIDi854229.
KEGGisce:YOR063W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J01351 Genomic DNA. Translation: AAA88732.1.
Z74971 Genomic DNA. Translation: CAA99256.1.
Z70678 Genomic DNA. Translation: CAA94548.1.
BK006948 Genomic DNA. Translation: DAA10842.1.
PIRiS66946. R5BY4E.
RefSeqiNP_014706.1. NM_001183482.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1K5Ymodel-C8-366[»]
3J6Xelectron microscopy6.10L31-387[»]
3J6Yelectron microscopy6.10L31-387[»]
3J77electron microscopy6.20L31-387[»]
3J78electron microscopy6.30L31-387[»]
3JCTelectron microscopy3.08B1-387[»]
4U3MX-ray3.00L3/l32-387[»]
4U3NX-ray3.20L3/l32-387[»]
4U3UX-ray2.90L3/l32-387[»]
4U4NX-ray3.10L3/l32-387[»]
4U4OX-ray3.60L3/l32-387[»]
4U4QX-ray3.00L3/l32-387[»]
4U4RX-ray2.80L3/l32-387[»]
4U4UX-ray3.00L3/l32-387[»]
4U4YX-ray3.20L3/l32-387[»]
4U4ZX-ray3.10L3/l32-387[»]
4U50X-ray3.20L3/l32-387[»]
4U51X-ray3.20L3/l32-387[»]
4U52X-ray3.00L3/l32-387[»]
4U53X-ray3.30L3/l32-387[»]
4U55X-ray3.20L3/l32-387[»]
4U56X-ray3.45L3/l32-387[»]
4U6FX-ray3.10L3/l32-387[»]
4V4Belectron microscopy11.70BC2-387[»]
4V6Ielectron microscopy8.80BC1-387[»]
4V7Felectron microscopy8.70C1-387[»]
4V7RX-ray4.00BC/DC1-387[»]
4V88X-ray3.00BB/DB1-387[»]
4V8Telectron microscopy8.10B1-387[»]
4V8Yelectron microscopy4.30BB2-387[»]
4V8Zelectron microscopy6.60BB2-387[»]
4V91electron microscopy3.70B1-387[»]
5APNelectron microscopy3.91B1-387[»]
5APOelectron microscopy3.41B1-387[»]
5DC3X-ray3.25L3/l32-387[»]
5FCIX-ray3.40L3/l32-387[»]
5FCJX-ray3.10L3/l32-387[»]
5FL8electron microscopy9.50B1-387[»]
5GAKelectron microscopy3.88F1-387[»]
5I4LX-ray3.10L3/l32-387[»]
ProteinModelPortaliP14126.
SMRiP14126. Positions 9-354.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi34462. 115 interactions.
DIPiDIP-6264N.
IntActiP14126. 109 interactions.
MINTiMINT-604187.

PTM databases

iPTMnetiP14126.

Proteomic databases

MaxQBiP14126.
PRIDEiP14126.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYOR063W; YOR063W; YOR063W.
GeneIDi854229.
KEGGisce:YOR063W.

Organism-specific databases

EuPathDBiFungiDB:YOR063W.
SGDiS000005589. RPL3.

Phylogenomic databases

GeneTreeiENSGT00390000017606.
HOGENOMiHOG000107319.
InParanoidiP14126.
KOiK02925.
OMAiVPRIRSW.
OrthoDBiEOG092C2SEF.

Enzyme and pathway databases

BioCyciYEAST:G3O-33603-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

EvolutionaryTraceiP14126.
PROiP14126.

Family and domain databases

InterProiIPR000597. Ribosomal_L3.
IPR019926. Ribosomal_L3_CS.
IPR009000. Transl_B-barrel.
[Graphical view]
PfamiPF00297. Ribosomal_L3. 1 hit.
[Graphical view]
SUPFAMiSSF50447. SSF50447. 1 hit.
PROSITEiPS00474. RIBOSOMAL_L3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiRL3_YEAST
AccessioniPrimary (citable) accession number: P14126
Secondary accession number(s): D6W2C6, Q08459
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 23, 2007
Last modified: September 7, 2016
This is version 167 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 450 molecules/cell in log phase SD medium.1 Publication

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 XV
    Yeast (Saccharomyces cerevisiae) chromosome XV: 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.