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Entry version 184 (11 Dec 2019)
Sequence version 4 (23 Jan 2007)
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Protein

60S ribosomal protein L4-A

Gene

RPL4A

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 (PubMed:22096102). uL4 participates in the regulation of the accumulation of its own mRNA (PubMed:2065661).1 Publication1 Publication

Miscellaneous

There are 2 genes for uL4 in yeast.Curated

<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

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

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
YEAST:G3O-29009-MONOMER

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-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)

<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 L4-A1 Publication
Alternative name(s):
<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:RPL4A1 Publication
Synonyms:RPL2, RPL2A
Ordered Locus Names:YBR031W
ORF Names:YBR0315
<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 II

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...
EuPathDBi
FungiDB:YBR031W

Saccharomyces Genome Database

More...
SGDi
S000000235 RPL4A

<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 & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Nucleus

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi95R → E: Leads to a slower growth at higher temperatures but allows RPL4 assembly into the 60S subunit; when associated with E-98. 1 Publication1
Mutagenesisi98R → E: Leads to a slower growth at higher temperatures but allows RPL4 assembly into the 60S subunit; when associated with E-95. 1 Publication1
Mutagenesisi289I → A: Leads to an inefficient release from ACL4 with a delayed assembly into the 60S subunit; when associated with A-290 and A-295. 1 Publication1
Mutagenesisi290I → A: Leads to an inefficient release from ACL4 with a delayed assembly into the 60S subunit; when associated with A-289 and A-295. 1 Publication1
Mutagenesisi295I → A: Leads to an inefficient release from ACL4 with a delayed assembly into the 60S subunit; when associated with A-289 and A-290. 1 Publication1
Mutagenesisi314K → A: Significantly diminished nuclear localization; when associated with A-315 and A-319. 1 Publication1
Mutagenesisi315K → A: Significantly diminished nuclear localization; when associated with A-314 and A-319. 1 Publication1
Mutagenesisi319K → A: Significantly diminished nuclear localization; when associated with A-314 and A-315. 1 Publication1
Mutagenesisi332K → E: Leads to an inefficient release from ACL4 with a delayed assembly into the 60S subunit; when associated with A-334. 1 Publication1
Mutagenesisi334F → A: Leads to an inefficient release from ACL4 with a delayed assembly into the 60S subunit; when associated with e-332. 1 Publication1

<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_00001293672 – 36260S ribosomal protein L4-AAdd BLAST361

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei2N-acetylserine1 Publication1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

N-terminally acetylated by acetyltransferase NatA.1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQB - The MaxQuant DataBase

More...
MaxQBi
P10664

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

More...
PaxDbi
P10664

PRoteomics IDEntifications database

More...
PRIDEi
P10664

Consortium for Top Down Proteomics

More...
TopDownProteomicsi
P10664

PTM databases

CarbonylDB database of protein carbonylation sites

More...
CarbonylDBi
P10664

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P10664

<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). uL4 is associated with the polypeptide exit tunnel (PubMed:9559554, PubMed:22096102). uL4 interacts with its chaperone ACL4 and the nuclear import receptor KAP104 (PubMed:25936803).

1 Publication2 Publications

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
32733, 266 interactors

Database of interacting proteins

More...
DIPi
DIP-8314N

Protein interaction database and analysis system

More...
IntActi
P10664, 217 interactors

Molecular INTeraction database

More...
MINTi
P10664

STRING: functional protein association networks

More...
STRINGi
4932.YBR031W

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...
RNActi
P10664 protein

<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

1362
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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

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SMRi
P10664

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

<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

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni277 – 362C-terminal-extended nuclear localization signal1 PublicationAdd BLAST86

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The eukaryote-specific C-terminal extension harbors a nuclear import signal and delivers the ACL4-uL4/RPL4 complex to the pre-ribosome, triggering uL4 release from ACL4 and incorporation into the 60S ribosomal subunit.1 Publication

<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

Phylogenomic databases

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000107331

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P10664

KEGG Orthology (KO)

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KOi
K02930

Identification of Orthologs from Complete Genome Data

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OMAi
GRLTIWT

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.40.1370.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR025755 Ribos_L4_C_dom
IPR002136 Ribosomal_L4/L1e
IPR013000 Ribosomal_L4/L1e_euk/arc_CS
IPR023574 Ribosomal_L4_dom_sf

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF14374 Ribos_L4_asso_C, 1 hit
PF00573 Ribosomal_L4, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF52166 SSF52166, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00939 RIBOSOMAL_L1E, 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>. The information is filed in different subsections. The current subsections and their content are listed below:<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.

P10664-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSRPQVTVHS LTGEATANAL PLPAVFSAPI RPDIVHTVFT SVNKNKRQAY
60 70 80 90 100
AVSEKAGHQT SAESWGTGRA VARIPRVGGG GTGRSGQGAF GNMCRGGRMF
110 120 130 140 150
APTKTWRKWN VKVNHNEKRY ATASAIAATA VASLVLARGH RVEKIPEIPL
160 170 180 190 200
VVSTDLESIQ KTKEAVAALK AVGAHSDLLK VLKSKKLRAG KGKYRNRRWT
210 220 230 240 250
QRRGPLVVYA EDNGIVKALR NVPGVETANV ASLNLLQLAP GAHLGRFVIW
260 270 280 290 300
TEAAFTKLDQ VWGSETVASS KVGYTLPSHI ISTSDVTRII NSSEIQSAIR
310 320 330 340 350
PAGQATQKRT HVLKKNPLKN KQVLLRLNPY AKVFAAEKLG SKKAEKTGTK
360
PAAVFTETLK HD
Length:362
Mass (Da):39,092
Last modified:January 23, 2007 - v4
<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:i37D0942A10AAE89F
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 conflicti38V → L in AAA34974 (PubMed:2834365).Curated1
Sequence conflicti144K → T in AAA34974 (PubMed:2834365).Curated1
Sequence conflicti157E → D in AAA34974 (PubMed:2834365).Curated1
Sequence conflicti224G → S in AAA34974 (PubMed:2834365).Curated1
Sequence conflicti241G → S in AAA34974 (PubMed:2834365).Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
X76078 Genomic DNA Translation: CAA53687.1
J03195 Genomic DNA Translation: AAA34974.1
Z35900 Genomic DNA Translation: CAA84973.1
BK006936 Genomic DNA Translation: DAA07152.1

Protein sequence database of the Protein Information Resource

More...
PIRi
S45887

NCBI Reference Sequences

More...
RefSeqi
NP_009587.1, NM_001178379.1

Genome annotation databases

Ensembl fungal genome annotation project

More...
EnsemblFungii
YBR031W_mRNA; YBR031W; YBR031W

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
852319

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
sce:YBR031W

<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
X76078 Genomic DNA Translation: CAA53687.1
J03195 Genomic DNA Translation: AAA34974.1
Z35900 Genomic DNA Translation: CAA84973.1
BK006936 Genomic DNA Translation: DAA07152.1
PIRiS45887
RefSeqiNP_009587.1, NM_001178379.1

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-D5-260[»]
3J6Xelectron microscopy6.10L41-362[»]
3J6Yelectron microscopy6.10L41-362[»]
3J77electron microscopy6.20L41-362[»]
3J78electron microscopy6.30L41-362[»]
3JCTelectron microscopy3.08C1-362[»]
4U3MX-ray3.00L4/l42-362[»]
4U3NX-ray3.20L4/l42-362[»]
4U3UX-ray2.90L4/l42-362[»]
4U4NX-ray3.10L4/l42-362[»]
4U4OX-ray3.60L4/l42-362[»]
4U4QX-ray3.00L4/l42-362[»]
4U4RX-ray2.80L4/l42-362[»]
4U4UX-ray3.00L4/l42-362[»]
4U4YX-ray3.20L4/l42-362[»]
4U4ZX-ray3.10L4/l42-362[»]
4U50X-ray3.20L4/l42-362[»]
4U51X-ray3.20L4/l42-362[»]
4U52X-ray3.00L4/l42-362[»]
4U53X-ray3.30L4/l42-362[»]
4U55X-ray3.20L4/l42-362[»]
4U56X-ray3.45L4/l42-362[»]
4U6FX-ray3.10L4/l42-362[»]
4V6Ielectron microscopy8.80BD1-362[»]
4V7Felectron microscopy8.70D1-362[»]
4V7RX-ray4.00BD/DD1-362[»]
4V88X-ray3.00BC/DC1-362[»]
4V8Telectron microscopy8.10C1-362[»]
4V8Yelectron microscopy4.30BC2-362[»]
4V8Zelectron microscopy6.60BC2-362[»]
4V91electron microscopy3.70C1-362[»]
5APNelectron microscopy3.91C1-362[»]
5APOelectron microscopy3.41C1-362[»]
5DATX-ray3.15L4/l42-362[»]
5DC3X-ray3.25L4/l42-362[»]
5DGEX-ray3.45L4/l42-362[»]
5DGFX-ray3.30L4/l42-362[»]
5DGVX-ray3.10L4/l42-362[»]
5FCIX-ray3.40L4/l42-362[»]
5FCJX-ray3.10L4/l42-362[»]
5FL8electron microscopy9.50C1-362[»]
5GAKelectron microscopy3.88G1-362[»]
5H4Pelectron microscopy3.07C2-362[»]
5I4LX-ray3.10L4/l42-362[»]
5JCSelectron microscopy9.50C1-362[»]
5JUOelectron microscopy4.00H1-362[»]
5JUPelectron microscopy3.50H1-362[»]
5JUSelectron microscopy4.20H1-362[»]
5JUTelectron microscopy4.00H1-362[»]
5JUUelectron microscopy4.00H1-362[»]
5LYBX-ray3.25L4/l42-362[»]
5M1Jelectron microscopy3.30C52-362[»]
5MC6electron microscopy3.80BE1-362[»]
5MEIX-ray3.50CF/l2-362[»]
5NDGX-ray3.70L4/l42-362[»]
5NDVX-ray3.30L4/l42-362[»]
5NDWX-ray3.70L4/l42-362[»]
5OBMX-ray3.40L4/l42-362[»]
5ON6X-ray3.10CF/l2-362[»]
5T62electron microscopy3.30F1-362[»]
5T6Relectron microscopy4.50F1-362[»]
5TBWX-ray3.00CF/l2-362[»]
5TGAX-ray3.30L4/l42-362[»]
5TGMX-ray3.50L4/l42-362[»]
5Z3Gelectron microscopy3.65G1-362[»]
6C0Felectron microscopy3.70C1-362[»]
6CB1electron microscopy4.60C1-362[»]
6ELZelectron microscopy3.30C1-362[»]
6EM1electron microscopy3.60C1-362[»]
6EM3electron microscopy3.20C1-362[»]
6EM4electron microscopy4.10C1-362[»]
6EM5electron microscopy4.30C1-362[»]
6FT6electron microscopy3.90C1-362[»]
6GQ1electron microscopy4.40C2-362[»]
6GQBelectron microscopy3.90C2-362[»]
6GQVelectron microscopy4.00C2-362[»]
6HD7electron microscopy3.40G1-362[»]
6HHQX-ray3.10CF/l1-362[»]
6I7Oelectron microscopy5.30BE/YE2-362[»]
6N8Jelectron microscopy3.50C1-362[»]
6N8Kelectron microscopy3.60C1-362[»]
6N8Lelectron microscopy3.60C1-362[»]
6N8Melectron microscopy3.50F1-362[»]
6N8Nelectron microscopy3.80F1-362[»]
6N8Oelectron microscopy3.50F1-362[»]
6Q8Yelectron microscopy3.10BE2-362[»]
6QIKelectron microscopy3.10D1-362[»]
6QT0electron microscopy3.40D1-362[»]
6QTZelectron microscopy3.50D1-362[»]
6R84electron microscopy3.60G2-362[»]
6R86electron microscopy3.40G2-362[»]
6R87electron microscopy3.40G2-362[»]
6RI5electron microscopy3.30D1-362[»]
6RZZelectron microscopy3.20D1-362[»]
6S05electron microscopy3.90D1-362[»]
6S47electron microscopy3.28AF2-362[»]
SMRiP10664
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGridi32733, 266 interactors
DIPiDIP-8314N
IntActiP10664, 217 interactors
MINTiP10664
STRINGi4932.YBR031W

PTM databases

CarbonylDBiP10664
iPTMnetiP10664

Proteomic databases

MaxQBiP10664
PaxDbiP10664
PRIDEiP10664
TopDownProteomicsiP10664

Genome annotation databases

EnsemblFungiiYBR031W_mRNA; YBR031W; YBR031W
GeneIDi852319
KEGGisce:YBR031W

Organism-specific databases

EuPathDBiFungiDB:YBR031W
SGDiS000000235 RPL4A

Phylogenomic databases

HOGENOMiHOG000107331
InParanoidiP10664
KOiK02930
OMAiGRLTIWT

Enzyme and pathway databases

BioCyciYEAST:G3O-29009-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

Protein Ontology

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PROi
PR:P10664
RNActiP10664 protein

Family and domain databases

Gene3Di3.40.1370.10, 1 hit
InterProiView protein in InterPro
IPR025755 Ribos_L4_C_dom
IPR002136 Ribosomal_L4/L1e
IPR013000 Ribosomal_L4/L1e_euk/arc_CS
IPR023574 Ribosomal_L4_dom_sf
PfamiView protein in Pfam
PF14374 Ribos_L4_asso_C, 1 hit
PF00573 Ribosomal_L4, 1 hit
SUPFAMiSSF52166 SSF52166, 1 hit
PROSITEiView protein in PROSITE
PS00939 RIBOSOMAL_L1E, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
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 nameiRL4A_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: P10664
Secondary accession number(s): D6VQ32
<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: July 1, 1989
Last sequence update: January 23, 2007
Last modified: December 11, 2019
This is version 184 of the entry and version 4 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, Direct protein sequencing, Reference proteome

Documents

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