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Protein

60S ribosomal protein L32

Gene

RPL32

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 3 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

GO - Molecular functioni

  • structural constituent of ribosome Source: SGD

GO - Biological processi

  • cytoplasmic translation Source: SGD

Keywordsi

Molecular functionRibonucleoprotein, Ribosomal protein

Enzyme and pathway databases

BioCyciYEAST:G3O-28980-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 L321 Publication
Alternative name(s):
Large ribosomal subunit protein eL321 Publication
Gene namesi
Name:RPL321 Publication
Ordered Locus Names:YBL092W
ORF Names:YBL0838
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome II

Organism-specific databases

EuPathDBiFungiDB:YBL092W.
SGDiS000000188. RPL32.

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 methionineiRemoved1 Publication
ChainiPRO_00001311452 – 13060S ribosomal protein L32Add BLAST129

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei40PhosphoserineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP38061.
PRIDEiP38061.
TopDownProteomicsiP38061.

PTM databases

iPTMnetiP38061.

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

BioGridi32611. 38 interactors.
DIPiDIP-5176N.
IntActiP38061. 9 interactors.
MINTiMINT-8285132.

Structurei

Secondary structure

1130
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni20 – 24Combined sources5
Beta strandi37 – 39Combined sources3
Turni41 – 45Combined sources5
Helixi55 – 57Combined sources3
Turni61 – 65Combined sources5
Beta strandi68 – 70Combined sources3
Beta strandi72 – 78Combined sources7
Helixi79 – 82Combined sources4
Helixi83 – 85Combined sources3
Turni89 – 91Combined sources3
Beta strandi92 – 96Combined sources5
Helixi102 – 115Combined sources14
Beta strandi118 – 120Combined sources3
Turni122 – 125Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1K5Ymodel-X14-122[»]
3J6Xelectron microscopy6.10721-130[»]
3J6Yelectron microscopy6.10721-130[»]
3J77electron microscopy6.20821-130[»]
3J78electron microscopy6.30821-130[»]
3JCTelectron microscopy3.08e1-130[»]
4U3MX-ray3.00O2/o22-130[»]
4U3NX-ray3.20O2/o22-130[»]
4U3UX-ray2.90O2/o22-130[»]
4U4NX-ray3.10O2/o22-130[»]
4U4OX-ray3.60O2/o22-130[»]
4U4QX-ray3.00O2/o22-130[»]
4U4RX-ray2.80O2/o22-130[»]
4U4UX-ray3.00O2/o22-130[»]
4U4YX-ray3.20O2/o22-130[»]
4U4ZX-ray3.10O2/o22-130[»]
4U50X-ray3.20O2/o22-130[»]
4U51X-ray3.20O2/o22-130[»]
4U52X-ray3.00O2/o22-130[»]
4U53X-ray3.30O2/o22-130[»]
4U55X-ray3.20O2/o22-130[»]
4U56X-ray3.45O2/o22-130[»]
4U6FX-ray3.10O2/o22-130[»]
4V4Belectron microscopy11.70B01-130[»]
4V6Ielectron microscopy8.80Bh1-130[»]
4V7Felectron microscopy8.70d1-130[»]
4V7RX-ray4.00Bb/Db1-130[»]
4V88X-ray3.00Be/De1-130[»]
4V8Telectron microscopy8.10e1-130[»]
4V8Yelectron microscopy4.30Be2-130[»]
4V8Zelectron microscopy6.60Be2-130[»]
4V91electron microscopy3.70e1-130[»]
5APNelectron microscopy3.91e1-130[»]
5APOelectron microscopy3.41e1-130[»]
5DATX-ray3.15O2/o22-130[»]
5DC3X-ray3.25O2/o22-130[»]
5DGEX-ray3.45O2/o22-130[»]
5DGFX-ray3.30O2/o22-130[»]
5DGVX-ray3.10O2/o22-130[»]
5FCIX-ray3.40O2/o22-130[»]
5FCJX-ray3.10O2/o22-130[»]
5FL8electron microscopy9.50e1-130[»]
5GAKelectron microscopy3.88g1-130[»]
5H4Pelectron microscopy3.07e1-130[»]
5I4LX-ray3.10O2/o22-128[»]
5JCSelectron microscopy9.50e1-130[»]
5JUOelectron microscopy4.00JA1-130[»]
5JUPelectron microscopy3.50JA1-130[»]
5JUSelectron microscopy4.20JA1-130[»]
5JUTelectron microscopy4.00JA1-130[»]
5JUUelectron microscopy4.00JA1-130[»]
5LYBX-ray3.25O2/o22-128[»]
5M1Jelectron microscopy3.30e52-128[»]
5MC6electron microscopy3.80BG1-130[»]
5T62electron microscopy3.30r1-130[»]
5T6Relectron microscopy4.50r1-130[»]
5TGAX-ray3.30O2/o22-128[»]
5TGMX-ray3.50O2/o22-128[»]
ProteinModelPortaliP38061.
SMRiP38061.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP38061.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

GeneTreeiENSGT00390000014729.
HOGENOMiHOG000231288.
InParanoidiP38061.
KOiK02912.
OMAiQKGIDSC.
OrthoDBiEOG092C5E5Z.

Family and domain databases

CDDicd00513. Ribosomal_L32_L32e. 1 hit.
InterProiView protein in InterPro
IPR001515. Ribosomal_L32e.
IPR018263. Ribosomal_L32e_CS.
PfamiView protein in Pfam
PF01655. Ribosomal_L32e. 1 hit.
ProDomiView protein in ProDom or Entries sharing at least one domain
PD003823. Ribosomal_L32e. 1 hit.
SMARTiView protein in SMART
SM01393. Ribosomal_L32e. 1 hit.
SUPFAMiSSF52042. SSF52042. 1 hit.
PROSITEiView protein in PROSITE
PS00580. RIBOSOMAL_L32E. 1 hit.

Sequencei

Sequence statusi: Complete.

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

P38061-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASLPHPKIV KKHTKKFKRH HSDRYHRVAE NWRKQKGIDS VVRRRFRGNI
60 70 80 90 100
SQPKIGYGSN KKTKFLSPSG HKTFLVANVK DLETLTMHTK TYAAEIAHNI
110 120 130
SAKNRVVILA RAKALGIKVT NPKGRLALEA
Length:130
Mass (Da):14,771
Last modified:October 1, 1994 - v1
Checksum:i5C5EDD87D6841976
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X79489 Genomic DNA. Translation: CAA56010.1.
Z35853 Genomic DNA. Translation: CAA84914.1.
AY558291 Genomic DNA. Translation: AAS56617.1.
EF123124 mRNA. Translation: ABM97468.1.
BK006936 Genomic DNA. Translation: DAA07031.1.
PIRiS45410.
RefSeqiNP_009460.1. NM_001178332.1.

Genome annotation databases

EnsemblFungiiYBL092W; YBL092W; YBL092W.
GeneIDi852185.
KEGGisce:YBL092W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X79489 Genomic DNA. Translation: CAA56010.1.
Z35853 Genomic DNA. Translation: CAA84914.1.
AY558291 Genomic DNA. Translation: AAS56617.1.
EF123124 mRNA. Translation: ABM97468.1.
BK006936 Genomic DNA. Translation: DAA07031.1.
PIRiS45410.
RefSeqiNP_009460.1. NM_001178332.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1K5Ymodel-X14-122[»]
3J6Xelectron microscopy6.10721-130[»]
3J6Yelectron microscopy6.10721-130[»]
3J77electron microscopy6.20821-130[»]
3J78electron microscopy6.30821-130[»]
3JCTelectron microscopy3.08e1-130[»]
4U3MX-ray3.00O2/o22-130[»]
4U3NX-ray3.20O2/o22-130[»]
4U3UX-ray2.90O2/o22-130[»]
4U4NX-ray3.10O2/o22-130[»]
4U4OX-ray3.60O2/o22-130[»]
4U4QX-ray3.00O2/o22-130[»]
4U4RX-ray2.80O2/o22-130[»]
4U4UX-ray3.00O2/o22-130[»]
4U4YX-ray3.20O2/o22-130[»]
4U4ZX-ray3.10O2/o22-130[»]
4U50X-ray3.20O2/o22-130[»]
4U51X-ray3.20O2/o22-130[»]
4U52X-ray3.00O2/o22-130[»]
4U53X-ray3.30O2/o22-130[»]
4U55X-ray3.20O2/o22-130[»]
4U56X-ray3.45O2/o22-130[»]
4U6FX-ray3.10O2/o22-130[»]
4V4Belectron microscopy11.70B01-130[»]
4V6Ielectron microscopy8.80Bh1-130[»]
4V7Felectron microscopy8.70d1-130[»]
4V7RX-ray4.00Bb/Db1-130[»]
4V88X-ray3.00Be/De1-130[»]
4V8Telectron microscopy8.10e1-130[»]
4V8Yelectron microscopy4.30Be2-130[»]
4V8Zelectron microscopy6.60Be2-130[»]
4V91electron microscopy3.70e1-130[»]
5APNelectron microscopy3.91e1-130[»]
5APOelectron microscopy3.41e1-130[»]
5DATX-ray3.15O2/o22-130[»]
5DC3X-ray3.25O2/o22-130[»]
5DGEX-ray3.45O2/o22-130[»]
5DGFX-ray3.30O2/o22-130[»]
5DGVX-ray3.10O2/o22-130[»]
5FCIX-ray3.40O2/o22-130[»]
5FCJX-ray3.10O2/o22-130[»]
5FL8electron microscopy9.50e1-130[»]
5GAKelectron microscopy3.88g1-130[»]
5H4Pelectron microscopy3.07e1-130[»]
5I4LX-ray3.10O2/o22-128[»]
5JCSelectron microscopy9.50e1-130[»]
5JUOelectron microscopy4.00JA1-130[»]
5JUPelectron microscopy3.50JA1-130[»]
5JUSelectron microscopy4.20JA1-130[»]
5JUTelectron microscopy4.00JA1-130[»]
5JUUelectron microscopy4.00JA1-130[»]
5LYBX-ray3.25O2/o22-128[»]
5M1Jelectron microscopy3.30e52-128[»]
5MC6electron microscopy3.80BG1-130[»]
5T62electron microscopy3.30r1-130[»]
5T6Relectron microscopy4.50r1-130[»]
5TGAX-ray3.30O2/o22-128[»]
5TGMX-ray3.50O2/o22-128[»]
ProteinModelPortaliP38061.
SMRiP38061.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi32611. 38 interactors.
DIPiDIP-5176N.
IntActiP38061. 9 interactors.
MINTiMINT-8285132.

PTM databases

iPTMnetiP38061.

Proteomic databases

MaxQBiP38061.
PRIDEiP38061.
TopDownProteomicsiP38061.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYBL092W; YBL092W; YBL092W.
GeneIDi852185.
KEGGisce:YBL092W.

Organism-specific databases

EuPathDBiFungiDB:YBL092W.
SGDiS000000188. RPL32.

Phylogenomic databases

GeneTreeiENSGT00390000014729.
HOGENOMiHOG000231288.
InParanoidiP38061.
KOiK02912.
OMAiQKGIDSC.
OrthoDBiEOG092C5E5Z.

Enzyme and pathway databases

BioCyciYEAST:G3O-28980-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

EvolutionaryTraceiP38061.
PROiPR:P38061.

Family and domain databases

CDDicd00513. Ribosomal_L32_L32e. 1 hit.
InterProiView protein in InterPro
IPR001515. Ribosomal_L32e.
IPR018263. Ribosomal_L32e_CS.
PfamiView protein in Pfam
PF01655. Ribosomal_L32e. 1 hit.
ProDomiView protein in ProDom or Entries sharing at least one domain
PD003823. Ribosomal_L32e. 1 hit.
SMARTiView protein in SMART
SM01393. Ribosomal_L32e. 1 hit.
SUPFAMiSSF52042. SSF52042. 1 hit.
PROSITEiView protein in PROSITE
PS00580. RIBOSOMAL_L32E. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiRL32_YEAST
AccessioniPrimary (citable) accession number: P38061
Secondary accession number(s): A2TBM1, D6VPR1
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: October 1, 1994
Last modified: May 10, 2017
This is version 142 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, 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 II
    Yeast (Saccharomyces cerevisiae) chromosome II: 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.