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Protein

60S ribosomal protein L31-A

Gene

RPL31A

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

Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel.1 Publication

Miscellaneous

There are 2 genes for eL31 in yeast.Curated

GO - Molecular functioni

  • structural constituent of ribosome Source: SGD

GO - Biological processi

  • cytoplasmic translation Source: SGD
  • regulation of translational fidelity Source: SGD

Keywordsi

Molecular functionRibonucleoprotein, Ribosomal protein

Enzyme and pathway databases

BioCyciYEAST:G3O-29486-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 L31-A1 Publication
Alternative name(s):
L34
Large ribosomal subunit protein eL31-A1 Publication
YL28
Gene namesi
Name:RPL31A1 Publication
Synonyms:RPL34, RPL34A
Ordered Locus Names:YDL075W
ORF Names:D2478
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome IV

Organism-specific databases

EuPathDBiFungiDB:YDL075W.
SGDiS000002233. RPL31A.

Subcellular locationi

GO - Cellular componenti

  • cytosolic large ribosomal subunit Source: SGD

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved2 Publications
ChainiPRO_00001537882 – 11360S ribosomal protein L31-AAdd BLAST112

Proteomic databases

MaxQBiP0C2H8.
PRIDEiP0C2H8.
TopDownProteomicsiP0C2H8.

PTM databases

iPTMnetiP0C2H8.

Interactioni

Subunit structurei

Component of the small ribosomal subunit (SSU). Mature yeast ribosomes consist of a small (40S) and a large (60S) subunit. The 40S small subunit contains 1 molecule of ribosomal RNA (18S rRNA) and 33 different proteins (encoded by 57 genes). The large 60S subunit contains 3 rRNA molecules (25S, 5.8S and 5S rRNA) and 46 different proteins (encoded by 81 genes) (PubMed:9559554, PubMed:22096102).1 Publication1 Publication

Protein-protein interaction databases

BioGridi31986. 58 interactors.
DIPiDIP-5135N.
IntActiP0C2H8. 1 interactor.
MINTiMINT-8285615.

Structurei

Secondary structure

1113
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi9 – 15Combined sources7
Helixi16 – 20Combined sources5
Turni25 – 27Combined sources3
Helixi28 – 44Combined sources17
Beta strandi49 – 51Combined sources3
Helixi53 – 60Combined sources8
Helixi64 – 66Combined sources3
Beta strandi69 – 79Combined sources11
Beta strandi86 – 95Combined sources10
Beta strandi101 – 103Combined sources3
Beta strandi107 – 109Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1K5Ymodel-W6-83[»]
2WW9electron microscopy8.60M1-113[»]
2WWAelectron microscopy8.90M1-113[»]
2WWBelectron microscopy6.48M1-113[»]
3J6Xelectron microscopy6.10711-113[»]
3J6Yelectron microscopy6.10711-113[»]
3J77electron microscopy6.20811-113[»]
3J78electron microscopy6.30811-113[»]
3JCTelectron microscopy3.08d1-113[»]
4U3MX-ray3.00O1/o12-113[»]
4U3NX-ray3.20O1/o12-113[»]
4U3UX-ray2.90O1/o12-113[»]
4U4NX-ray3.10O1/o12-113[»]
4U4OX-ray3.60O1/o12-113[»]
4U4QX-ray3.00O1/o12-113[»]
4U4RX-ray2.80O1/o12-113[»]
4U4UX-ray3.00O1/o12-113[»]
4U4YX-ray3.20O1/o12-113[»]
4U4ZX-ray3.10O1/o12-113[»]
4U50X-ray3.20O1/o12-113[»]
4U51X-ray3.20O1/o12-113[»]
4U52X-ray3.00O1/o12-113[»]
4U53X-ray3.30O1/o12-113[»]
4U55X-ray3.20O1/o12-113[»]
4U56X-ray3.45O1/o12-113[»]
4U6FX-ray3.10O1/o12-113[»]
4V4Belectron microscopy11.70BW2-113[»]
4V6Ielectron microscopy8.80Bg1-113[»]
4V7Felectron microscopy8.70c1-113[»]
4V7RX-ray4.00Ba/Da1-113[»]
4V88X-ray3.00Bd/Dd1-113[»]
4V8Telectron microscopy8.10d1-113[»]
4V8Yelectron microscopy4.30Bd2-113[»]
4V8Zelectron microscopy6.60Bd2-113[»]
4V91electron microscopy3.70d1-113[»]
5APNelectron microscopy3.91d1-113[»]
5APOelectron microscopy3.41d1-113[»]
5DATX-ray3.15O1/o12-113[»]
5DC3X-ray3.25O1/o12-113[»]
5DGEX-ray3.45O1/o12-113[»]
5DGFX-ray3.30O1/o12-113[»]
5DGVX-ray3.10O1/o12-113[»]
5FCIX-ray3.40O1/o12-113[»]
5FCJX-ray3.10O1/o12-113[»]
5FL8electron microscopy9.50d1-113[»]
5GAKelectron microscopy3.88f4-112[»]
5H4Pelectron microscopy3.07d1-113[»]
5I4LX-ray3.10O1/o14-112[»]
5JCSelectron microscopy9.50d1-113[»]
5JUOelectron microscopy4.00IA1-113[»]
5JUPelectron microscopy3.50IA1-113[»]
5JUSelectron microscopy4.20IA1-113[»]
5JUTelectron microscopy4.00IA1-113[»]
5JUUelectron microscopy4.00IA1-113[»]
5LYBX-ray3.25O1/o14-112[»]
5M1Jelectron microscopy3.30d54-112[»]
5MC6electron microscopy3.80BC1-113[»]
5T62electron microscopy3.30q1-113[»]
5T6Relectron microscopy4.50q1-113[»]
5TGAX-ray3.30O1/o14-112[»]
5TGMX-ray3.50O1/o14-112[»]
ProteinModelPortaliP0C2H8.
SMRiP0C2H8.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0C2H8.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

GeneTreeiENSGT00390000005200.
HOGENOMiHOG000216660.
InParanoidiP0C2H8.
KOiK02910.
OMAiDERIDTR.
OrthoDBiEOG092C5QTG.

Family and domain databases

CDDicd00463. Ribosomal_L31e. 1 hit.
Gene3Di3.10.440.10. 1 hit.
InterProiView protein in InterPro
IPR000054. Ribosomal_L31e.
IPR020052. Ribosomal_L31e_CS.
IPR023621. Ribosomal_L31e_dom.
PANTHERiPTHR10956. PTHR10956. 1 hit.
PfamiView protein in Pfam
PF01198. Ribosomal_L31e. 1 hit.
ProDomiView protein in ProDom or Entries sharing at least one domain
PD006030. Ribosomal_L31e. 1 hit.
SMARTiView protein in SMART
SM01380. Ribosomal_L31e. 1 hit.
SUPFAMiSSF54575. SSF54575. 1 hit.
PROSITEiView protein in PROSITE
PS01144. RIBOSOMAL_L31E. 1 hit.

Sequencei

Sequence statusi: Complete.

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

P0C2H8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAGLKDVVTR EYTINLHKRL HGVSFKKRAP RAVKEIKKFA KLHMGTDDVR
60 70 80 90 100
LAPELNQAIW KRGVKGVEYR LRLRISRKRN EEEDAKNPLF SYVEPVLVAS
110
AKGLQTVVVE EDA
Length:113
Mass (Da):12,953
Last modified:March 6, 2007 - v1
Checksum:i351B5ADD15DB3B5D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X01441 Genomic DNA. Translation: CAA25679.1.
Z74123 Genomic DNA. Translation: CAA98641.1.
BK006938 Genomic DNA. Translation: DAA11784.1.
PIRiS67611. R5BY1E.
RefSeqiNP_010208.1. NM_001180134.1.

Genome annotation databases

EnsemblFungiiYDL075W; YDL075W; YDL075W.
GeneIDi851484.
KEGGisce:YDL075W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X01441 Genomic DNA. Translation: CAA25679.1.
Z74123 Genomic DNA. Translation: CAA98641.1.
BK006938 Genomic DNA. Translation: DAA11784.1.
PIRiS67611. R5BY1E.
RefSeqiNP_010208.1. NM_001180134.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1K5Ymodel-W6-83[»]
2WW9electron microscopy8.60M1-113[»]
2WWAelectron microscopy8.90M1-113[»]
2WWBelectron microscopy6.48M1-113[»]
3J6Xelectron microscopy6.10711-113[»]
3J6Yelectron microscopy6.10711-113[»]
3J77electron microscopy6.20811-113[»]
3J78electron microscopy6.30811-113[»]
3JCTelectron microscopy3.08d1-113[»]
4U3MX-ray3.00O1/o12-113[»]
4U3NX-ray3.20O1/o12-113[»]
4U3UX-ray2.90O1/o12-113[»]
4U4NX-ray3.10O1/o12-113[»]
4U4OX-ray3.60O1/o12-113[»]
4U4QX-ray3.00O1/o12-113[»]
4U4RX-ray2.80O1/o12-113[»]
4U4UX-ray3.00O1/o12-113[»]
4U4YX-ray3.20O1/o12-113[»]
4U4ZX-ray3.10O1/o12-113[»]
4U50X-ray3.20O1/o12-113[»]
4U51X-ray3.20O1/o12-113[»]
4U52X-ray3.00O1/o12-113[»]
4U53X-ray3.30O1/o12-113[»]
4U55X-ray3.20O1/o12-113[»]
4U56X-ray3.45O1/o12-113[»]
4U6FX-ray3.10O1/o12-113[»]
4V4Belectron microscopy11.70BW2-113[»]
4V6Ielectron microscopy8.80Bg1-113[»]
4V7Felectron microscopy8.70c1-113[»]
4V7RX-ray4.00Ba/Da1-113[»]
4V88X-ray3.00Bd/Dd1-113[»]
4V8Telectron microscopy8.10d1-113[»]
4V8Yelectron microscopy4.30Bd2-113[»]
4V8Zelectron microscopy6.60Bd2-113[»]
4V91electron microscopy3.70d1-113[»]
5APNelectron microscopy3.91d1-113[»]
5APOelectron microscopy3.41d1-113[»]
5DATX-ray3.15O1/o12-113[»]
5DC3X-ray3.25O1/o12-113[»]
5DGEX-ray3.45O1/o12-113[»]
5DGFX-ray3.30O1/o12-113[»]
5DGVX-ray3.10O1/o12-113[»]
5FCIX-ray3.40O1/o12-113[»]
5FCJX-ray3.10O1/o12-113[»]
5FL8electron microscopy9.50d1-113[»]
5GAKelectron microscopy3.88f4-112[»]
5H4Pelectron microscopy3.07d1-113[»]
5I4LX-ray3.10O1/o14-112[»]
5JCSelectron microscopy9.50d1-113[»]
5JUOelectron microscopy4.00IA1-113[»]
5JUPelectron microscopy3.50IA1-113[»]
5JUSelectron microscopy4.20IA1-113[»]
5JUTelectron microscopy4.00IA1-113[»]
5JUUelectron microscopy4.00IA1-113[»]
5LYBX-ray3.25O1/o14-112[»]
5M1Jelectron microscopy3.30d54-112[»]
5MC6electron microscopy3.80BC1-113[»]
5T62electron microscopy3.30q1-113[»]
5T6Relectron microscopy4.50q1-113[»]
5TGAX-ray3.30O1/o14-112[»]
5TGMX-ray3.50O1/o14-112[»]
ProteinModelPortaliP0C2H8.
SMRiP0C2H8.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi31986. 58 interactors.
DIPiDIP-5135N.
IntActiP0C2H8. 1 interactor.
MINTiMINT-8285615.

PTM databases

iPTMnetiP0C2H8.

Proteomic databases

MaxQBiP0C2H8.
PRIDEiP0C2H8.
TopDownProteomicsiP0C2H8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYDL075W; YDL075W; YDL075W.
GeneIDi851484.
KEGGisce:YDL075W.

Organism-specific databases

EuPathDBiFungiDB:YDL075W.
SGDiS000002233. RPL31A.

Phylogenomic databases

GeneTreeiENSGT00390000005200.
HOGENOMiHOG000216660.
InParanoidiP0C2H8.
KOiK02910.
OMAiDERIDTR.
OrthoDBiEOG092C5QTG.

Enzyme and pathway databases

BioCyciYEAST:G3O-29486-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

EvolutionaryTraceiP0C2H8.
PROiPR:P0C2H8.

Family and domain databases

CDDicd00463. Ribosomal_L31e. 1 hit.
Gene3Di3.10.440.10. 1 hit.
InterProiView protein in InterPro
IPR000054. Ribosomal_L31e.
IPR020052. Ribosomal_L31e_CS.
IPR023621. Ribosomal_L31e_dom.
PANTHERiPTHR10956. PTHR10956. 1 hit.
PfamiView protein in Pfam
PF01198. Ribosomal_L31e. 1 hit.
ProDomiView protein in ProDom or Entries sharing at least one domain
PD006030. Ribosomal_L31e. 1 hit.
SMARTiView protein in SMART
SM01380. Ribosomal_L31e. 1 hit.
SUPFAMiSSF54575. SSF54575. 1 hit.
PROSITEiView protein in PROSITE
PS01144. RIBOSOMAL_L31E. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiRL31A_YEAST
AccessioniPrimary (citable) accession number: P0C2H8
Secondary accession number(s): D6VRS4, P04649, Q3E7B8
Entry historyiIntegrated into UniProtKB/Swiss-Prot: March 6, 2007
Last sequence update: March 6, 2007
Last modified: May 10, 2017
This is version 93 of the entry and version 1 of the sequence. See 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 IV
    Yeast (Saccharomyces cerevisiae) chromosome IV: 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.