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Protein

60S ribosomal protein L37-A

Gene

RPL37A

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

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

Present with 21800 molecules/cell in log phase SD medium.1 Publication
There are 2 genes for eL37 in yeast.Curated

Cofactori

Zn2+1 PublicationNote: Binds 1 zinc ion per subunit.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi19Zinc1 Publication1
Metal bindingi22Zinc1 Publication1
Metal bindingi34Zinc1 Publication1
Metal bindingi37Zinc1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri19 – 37C4-typeSequence analysisAdd BLAST19

GO - Molecular functioni

GO - Biological processi

  • cleavage in ITS2 between 5.8S rRNA and LSU-rRNA of tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) Source: SGD
  • cytoplasmic translation Source: SGD
  • translation Source: GO_Central

Keywordsi

Molecular functionRibonucleoprotein, Ribosomal protein, RNA-binding, rRNA-binding
LigandMetal-binding, Zinc

Enzyme and pathway databases

BioCyciYEAST:G3O-32308-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 L37-A1 Publication
Alternative name(s):
L43
Large ribosomal subunit protein eL37-A1 Publication
YL35
YP55
Gene namesi
Name:RPL37A1 Publication
Synonyms:RPL35A
Ordered Locus Names:YLR185W
ORF Names:L9470.6
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XII

Organism-specific databases

EuPathDBiFungiDB:YLR185W.
SGDiS000004175. RPL37A.

Subcellular locationi

GO - Cellular componenti

  • cytosolic large ribosomal subunit Source: SGD
  • preribosome, large subunit precursor Source: SGD

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00001397222 – 8860S ribosomal protein L37-AAdd BLAST87

Proteomic databases

MaxQBiP49166.
PRIDEiP49166.

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

BioGridi31455. 209 interactors.
DIPiDIP-2135N.
IntActiP49166. 1 interactor.
MINTiMINT-8285347.

Structurei

Secondary structure

188
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi5 – 8Combined sources4
Beta strandi15 – 17Combined sources3
Turni20 – 22Combined sources3
Beta strandi24 – 28Combined sources5
Turni29 – 32Combined sources4
Turni35 – 37Combined sources3
Beta strandi41 – 43Combined sources3
Helixi48 – 50Combined sources3
Helixi51 – 57Combined sources7
Helixi67 – 69Combined sources3
Helixi70 – 75Combined sources6
Turni76 – 78Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1K5Ymodel-Z2-53[»]
3J6Xelectron microscopy6.10771-88[»]
3J6Yelectron microscopy6.10771-88[»]
3J77electron microscopy6.20871-88[»]
3J78electron microscopy6.30871-88[»]
3JCTelectron microscopy3.08j1-88[»]
4U3MX-ray3.00O7/o72-88[»]
4U3NX-ray3.20O7/o72-88[»]
4U3UX-ray2.90O7/o72-88[»]
4U4NX-ray3.10O7/o72-88[»]
4U4OX-ray3.60O7/o72-88[»]
4U4QX-ray3.00O7/o72-88[»]
4U4RX-ray2.80O7/o72-88[»]
4U4UX-ray3.00O7/o72-88[»]
4U4YX-ray3.20O7/o72-88[»]
4U4ZX-ray3.10O7/o72-88[»]
4U50X-ray3.20O7/o72-88[»]
4U51X-ray3.20O7/o72-88[»]
4U52X-ray3.00O7/o72-88[»]
4U53X-ray3.30O7/o72-88[»]
4U55X-ray3.20O7/o72-88[»]
4U56X-ray3.45O7/o72-88[»]
4U6FX-ray3.10O7/o72-88[»]
4V4Belectron microscopy11.70BY2-88[»]
4V6Ielectron microscopy8.80Bl1-88[»]
4V7Felectron microscopy8.70h1-88[»]
4V7RX-ray4.00Bd/Dd1-88[»]
4V88X-ray3.00Bj/Dj1-88[»]
4V8Telectron microscopy8.10j1-88[»]
4V8Yelectron microscopy4.30Bj2-88[»]
4V8Zelectron microscopy6.60Bj2-88[»]
4V91electron microscopy3.70j1-88[»]
5APNelectron microscopy3.91j1-88[»]
5APOelectron microscopy3.41j1-88[»]
5DATX-ray3.15O7/o72-88[»]
5DC3X-ray3.25O7/o72-88[»]
5DGEX-ray3.45O7/o72-88[»]
5DGFX-ray3.30O7/o72-88[»]
5DGVX-ray3.10O7/o72-88[»]
5FCIX-ray3.40O7/o72-88[»]
5FCJX-ray3.10O7/o72-88[»]
5FL8electron microscopy9.50j1-88[»]
5GAKelectron microscopy3.88l1-88[»]
5H4Pelectron microscopy3.07j1-88[»]
5I4LX-ray3.10O7/o72-88[»]
5JCSelectron microscopy9.50j1-88[»]
5JUOelectron microscopy4.00OA1-88[»]
5JUPelectron microscopy3.50OA1-88[»]
5JUSelectron microscopy4.20OA1-88[»]
5JUTelectron microscopy4.00OA1-88[»]
5JUUelectron microscopy4.00OA1-88[»]
5LYBX-ray3.25O7/o72-88[»]
5M1Jelectron microscopy3.30j52-88[»]
5MC6electron microscopy3.80AF1-88[»]
5T62electron microscopy3.30w1-88[»]
5T6Relectron microscopy4.50w1-88[»]
5TGAX-ray3.30O7/o72-88[»]
5TGMX-ray3.50O7/o72-88[»]
ProteinModelPortaliP49166.
SMRiP49166.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP49166.

Family & Domainsi

Sequence similaritiesi

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri19 – 37C4-typeSequence analysisAdd BLAST19

Keywords - Domaini

Zinc-finger

Phylogenomic databases

GeneTreeiENSGT00390000005254.
HOGENOMiHOG000111076.
InParanoidiP49166.
KOiK02922.
OMAiHIQKHEC.
OrthoDBiEOG092C5XPX.

Family and domain databases

Gene3Di2.20.25.30. 1 hit.
HAMAPiMF_00547. Ribosomal_L37e. 1 hit.
InterProiView protein in InterPro
IPR011331. Ribosomal_L37ae/L37e.
IPR001569. Ribosomal_L37e.
IPR018267. Ribosomal_L37e_CS.
IPR011332. Ribosomal_zn-bd.
PfamiView protein in Pfam
PF01907. Ribosomal_L37e. 1 hit.
ProDomiView protein in ProDom or Entries sharing at least one domain
PD005132. Ribosomal_L37e. 1 hit.
SUPFAMiSSF57829. SSF57829. 1 hit.
PROSITEiView protein in PROSITE
PS01077. RIBOSOMAL_L37E. 1 hit.

Sequencei

Sequence statusi: Complete.

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

P49166-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGKGTPSFGK RHNKSHTLCN RCGRRSFHVQ KKTCSSCGYP AAKTRSYNWG
60 70 80
AKAKRRHTTG TGRMRYLKHV SRRFKNGFQT GSASKASA
Length:88
Mass (Da):9,850
Last modified:January 23, 2007 - v2
Checksum:i274D249361EBE5E5
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti73R → RR AA sequence (Ref. 3) Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U17246 Genomic DNA. Translation: AAB67458.1.
BK006945 Genomic DNA. Translation: DAA09504.1.
PIRiS51430.
RefSeqiNP_013286.1. NM_001182072.1.

Genome annotation databases

EnsemblFungiiYLR185W; YLR185W; YLR185W.
GeneIDi850882.
KEGGisce:YLR185W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U17246 Genomic DNA. Translation: AAB67458.1.
BK006945 Genomic DNA. Translation: DAA09504.1.
PIRiS51430.
RefSeqiNP_013286.1. NM_001182072.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1K5Ymodel-Z2-53[»]
3J6Xelectron microscopy6.10771-88[»]
3J6Yelectron microscopy6.10771-88[»]
3J77electron microscopy6.20871-88[»]
3J78electron microscopy6.30871-88[»]
3JCTelectron microscopy3.08j1-88[»]
4U3MX-ray3.00O7/o72-88[»]
4U3NX-ray3.20O7/o72-88[»]
4U3UX-ray2.90O7/o72-88[»]
4U4NX-ray3.10O7/o72-88[»]
4U4OX-ray3.60O7/o72-88[»]
4U4QX-ray3.00O7/o72-88[»]
4U4RX-ray2.80O7/o72-88[»]
4U4UX-ray3.00O7/o72-88[»]
4U4YX-ray3.20O7/o72-88[»]
4U4ZX-ray3.10O7/o72-88[»]
4U50X-ray3.20O7/o72-88[»]
4U51X-ray3.20O7/o72-88[»]
4U52X-ray3.00O7/o72-88[»]
4U53X-ray3.30O7/o72-88[»]
4U55X-ray3.20O7/o72-88[»]
4U56X-ray3.45O7/o72-88[»]
4U6FX-ray3.10O7/o72-88[»]
4V4Belectron microscopy11.70BY2-88[»]
4V6Ielectron microscopy8.80Bl1-88[»]
4V7Felectron microscopy8.70h1-88[»]
4V7RX-ray4.00Bd/Dd1-88[»]
4V88X-ray3.00Bj/Dj1-88[»]
4V8Telectron microscopy8.10j1-88[»]
4V8Yelectron microscopy4.30Bj2-88[»]
4V8Zelectron microscopy6.60Bj2-88[»]
4V91electron microscopy3.70j1-88[»]
5APNelectron microscopy3.91j1-88[»]
5APOelectron microscopy3.41j1-88[»]
5DATX-ray3.15O7/o72-88[»]
5DC3X-ray3.25O7/o72-88[»]
5DGEX-ray3.45O7/o72-88[»]
5DGFX-ray3.30O7/o72-88[»]
5DGVX-ray3.10O7/o72-88[»]
5FCIX-ray3.40O7/o72-88[»]
5FCJX-ray3.10O7/o72-88[»]
5FL8electron microscopy9.50j1-88[»]
5GAKelectron microscopy3.88l1-88[»]
5H4Pelectron microscopy3.07j1-88[»]
5I4LX-ray3.10O7/o72-88[»]
5JCSelectron microscopy9.50j1-88[»]
5JUOelectron microscopy4.00OA1-88[»]
5JUPelectron microscopy3.50OA1-88[»]
5JUSelectron microscopy4.20OA1-88[»]
5JUTelectron microscopy4.00OA1-88[»]
5JUUelectron microscopy4.00OA1-88[»]
5LYBX-ray3.25O7/o72-88[»]
5M1Jelectron microscopy3.30j52-88[»]
5MC6electron microscopy3.80AF1-88[»]
5T62electron microscopy3.30w1-88[»]
5T6Relectron microscopy4.50w1-88[»]
5TGAX-ray3.30O7/o72-88[»]
5TGMX-ray3.50O7/o72-88[»]
ProteinModelPortaliP49166.
SMRiP49166.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi31455. 209 interactors.
DIPiDIP-2135N.
IntActiP49166. 1 interactor.
MINTiMINT-8285347.

Proteomic databases

MaxQBiP49166.
PRIDEiP49166.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYLR185W; YLR185W; YLR185W.
GeneIDi850882.
KEGGisce:YLR185W.

Organism-specific databases

EuPathDBiFungiDB:YLR185W.
SGDiS000004175. RPL37A.

Phylogenomic databases

GeneTreeiENSGT00390000005254.
HOGENOMiHOG000111076.
InParanoidiP49166.
KOiK02922.
OMAiHIQKHEC.
OrthoDBiEOG092C5XPX.

Enzyme and pathway databases

BioCyciYEAST:G3O-32308-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

EvolutionaryTraceiP49166.
PROiPR:P49166.

Family and domain databases

Gene3Di2.20.25.30. 1 hit.
HAMAPiMF_00547. Ribosomal_L37e. 1 hit.
InterProiView protein in InterPro
IPR011331. Ribosomal_L37ae/L37e.
IPR001569. Ribosomal_L37e.
IPR018267. Ribosomal_L37e_CS.
IPR011332. Ribosomal_zn-bd.
PfamiView protein in Pfam
PF01907. Ribosomal_L37e. 1 hit.
ProDomiView protein in ProDom or Entries sharing at least one domain
PD005132. Ribosomal_L37e. 1 hit.
SUPFAMiSSF57829. SSF57829. 1 hit.
PROSITEiView protein in PROSITE
PS01077. RIBOSOMAL_L37E. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiRL37A_YEAST
AccessioniPrimary (citable) accession number: P49166
Secondary accession number(s): D6VYI8
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: January 23, 2007
Last modified: May 10, 2017
This is version 137 of the entry and version 2 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 XII
    Yeast (Saccharomyces cerevisiae) chromosome XII: 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.