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Entry version 154 (13 Feb 2019)
Sequence version 2 (23 Jan 2007)
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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

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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

<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi19Zinc1 Publication1
Metal bindingi22Zinc1 Publication1
Metal bindingi34Zinc1 Publication1
Metal bindingi37Zinc1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section specifies the position(s) and type(s) of zinc fingers within the protein.<p><a href='/help/zn_fing' target='_top'>More...</a></p>Zinc fingeri19 – 37C4-typeSequence analysisAdd BLAST19

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

  • metal ion binding Source: UniProtKB-KW
  • rRNA binding Source: UniProtKB-KW
  • structural constituent of ribosome Source: SGD

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

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

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
YEAST:G3O-32308-MONOMER

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-SCE-156827 L13a-mediated translational silencing of Ceruloplasmin expression
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)

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
60S ribosomal protein L37-A1 Publication
Alternative name(s):
L43
YL35
YP55
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:RPL37A1 Publication
Synonyms:RPL35A
Ordered Locus Names:YLR185W
ORF Names:L9470.6
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri559292 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000002311 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome XII

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...
EuPathDBi
FungiDB:YLR185W

Saccharomyces Genome Database

More...
SGDi
S000004175 RPL37A

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>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

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemoved1 Publication
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001397222 – 8860S ribosomal protein L37-AAdd BLAST87

Proteomic databases

MaxQB - The MaxQuant DataBase

More...
MaxQBi
P49166

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
P49166

PRoteomics IDEntifications database

More...
PRIDEi
P49166

PTM databases

CarbonylDB database of protein carbonylation sites

More...
CarbonylDBi
P49166

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>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

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
31455, 227 interactors

Database of interacting proteins

More...
DIPi
DIP-2135N

Protein interaction database and analysis system

More...
IntActi
P49166, 1 interactor

Molecular INTeraction database

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MINTi
P49166

STRING: functional protein association networks

More...
STRINGi
4932.YLR185W

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

188
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
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[»]
6GQ1electron microscopy4.40j2-88[»]
6GQBelectron microscopy3.90j2-88[»]
6GQVelectron microscopy4.00j2-88[»]
6HD7electron microscopy3.40l1-88[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
P49166

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
P49166

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P49166

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Zinc finger

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

Keywords - Domaini

Zinc-finger

Phylogenomic databases

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000168926

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000111076

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P49166

KEGG Orthology (KO)

More...
KOi
K02922

Identification of Orthologs from Complete Genome Data

More...
OMAi
YPAAKMR

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
2.20.25.30, 1 hit

HAMAP database of protein families

More...
HAMAPi
MF_00547 Ribosomal_L37e, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR011331 Ribosomal_L37ae/L37e
IPR001569 Ribosomal_L37e
IPR018267 Ribosomal_L37e_CS
IPR011332 Ribosomal_zn-bd

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF01907 Ribosomal_L37e, 1 hit

ProDom; a protein domain database

More...
ProDomi
View protein in ProDom or Entries sharing at least one domain
PD005132 Ribosomal_L37e, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF57829 SSF57829, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS01077 RIBOSOMAL_L37E, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i274D249361EBE5E5
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti73R → RR AA sequence (Ref. 3) Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
U17246 Genomic DNA Translation: AAB67458.1
BK006945 Genomic DNA Translation: DAA09504.1

Protein sequence database of the Protein Information Resource

More...
PIRi
S51430

NCBI Reference Sequences

More...
RefSeqi
NP_013286.1, NM_001182072.1

Genome annotation databases

Ensembl fungal genome annotation project

More...
EnsemblFungii
YLR185W_mRNA; YLR185W_mRNA; YLR185W

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
850882

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
sce:YLR185W

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>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[»]
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[»]
6GQ1electron microscopy4.40j2-88[»]
6GQBelectron microscopy3.90j2-88[»]
6GQVelectron microscopy4.00j2-88[»]
6HD7electron microscopy3.40l1-88[»]
ProteinModelPortaliP49166
SMRiP49166
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi31455, 227 interactors
DIPiDIP-2135N
IntActiP49166, 1 interactor
MINTiP49166
STRINGi4932.YLR185W

PTM databases

CarbonylDBiP49166

Proteomic databases

MaxQBiP49166
PaxDbiP49166
PRIDEiP49166

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYLR185W_mRNA; YLR185W_mRNA; YLR185W
GeneIDi850882
KEGGisce:YLR185W

Organism-specific databases

EuPathDBiFungiDB:YLR185W
SGDiS000004175 RPL37A

Phylogenomic databases

GeneTreeiENSGT00940000168926
HOGENOMiHOG000111076
InParanoidiP49166
KOiK02922
OMAiYPAAKMR

Enzyme and pathway databases

BioCyciYEAST:G3O-32308-MONOMER
ReactomeiR-SCE-156827 L13a-mediated translational silencing of Ceruloplasmin expression
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

Protein Ontology

More...
PROi
PR: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

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiRL37A_YEAST
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P49166
Secondary accession number(s): D6VYI8
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: January 23, 2007
Last modified: February 13, 2019
This is version 154 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
  4. Yeast chromosome XII
    Yeast (Saccharomyces cerevisiae) chromosome XII: entries and gene names
  5. Ribosomal proteins
    Ribosomal proteins families and list of entries
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