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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: -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

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

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
PaxDbiP49166
PRIDEiP49166

PTM databases

CarbonylDBiP49166

Interactioni

Subunit structurei

Component of the large ribosomal subunit (LSU). 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, 214 interactors
DIPiDIP-2135N
IntActiP49166, 1 interactor
MINTiP49166
STRINGi4932.YLR185W

Structurei

Secondary structure

188
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni20 – 22Combined sources3
Turni29 – 32Combined sources4
Beta strandi33 – 37Combined sources5
Beta strandi41 – 43Combined sources3
Helixi51 – 56Combined sources6
Helixi67 – 69Combined sources3
Helixi70 – 76Combined sources7

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[»]
5MEIX-ray3.50AK/DL2-88[»]
5NDGX-ray3.70O7/o72-85[»]
5NDVX-ray3.30O7/o72-88[»]
5NDWX-ray3.70O7/o72-88[»]
5OBMX-ray3.40O7/o72-88[»]
5ON6X-ray3.10AK/DL2-88[»]
5T62electron microscopy3.30w1-88[»]
5T6Relectron microscopy4.50w1-88[»]
5TBWX-ray3.00AK/DL2-88[»]
5TGAX-ray3.30O7/o72-88[»]
5TGMX-ray3.50O7/o72-88[»]
5Z3Gelectron microscopy3.65n1-88[»]
6C0Felectron microscopy3.70j1-88[»]
6CB1electron microscopy4.60j1-88[»]
6ELZelectron microscopy3.30j1-88[»]
6EM1electron microscopy3.60j1-88[»]
6EM3electron microscopy3.20j1-88[»]
6EM4electron microscopy4.10j1-88[»]
6EM5electron microscopy4.30j1-88[»]
6FT6electron microscopy3.90j1-88[»]
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
OMAiYPAAKMR
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

Similar proteinsi

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 23, 2018
This is version 147 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
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Main funding by: National Institutes of Health