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Entry version 172 (13 Feb 2019)
Sequence version 3 (05 Oct 2010)
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Protein

60S ribosomal protein L28

Gene

RPL28

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

<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

  • RNA binding Source: SGD
  • structural constituent of ribosome Source: GO_Central

GO - Biological processi

  • cytoplasmic translation Source: SGD

<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

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

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BioCyci
YEAST:G3O-30602-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 L281 Publication
Alternative name(s):
L27a
L29
RP44
RP62
YL24
<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:RPL281 Publication
Synonyms:CYH2
Ordered Locus Names:YGL103W
<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 VII

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...
EuPathDBi
FungiDB:YGL103W

Saccharomyces Genome Database

More...
SGDi
S000003071 RPL28

<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_00001049042 – 14960S ribosomal protein L28Add BLAST148

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki96Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources

Keywords - PTMi

Isopeptide bond, Ubl conjugation

Proteomic databases

MaxQB - The MaxQuant DataBase

More...
MaxQBi
P02406

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

More...
PaxDbi
P02406

PRoteomics IDEntifications database

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PRIDEi
P02406

PTM databases

CarbonylDB database of protein carbonylation sites

More...
CarbonylDBi
P02406

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P02406

<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
33147, 281 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...
ComplexPortali
CPX-1601 60S cytosolic large ribosomal subunit

The Eukaryotic Linear Motif resource for Functional Sites in Proteins

More...
ELMi
P02406

Protein interaction database and analysis system

More...
IntActi
P02406, 32 interactors

Molecular INTeraction database

More...
MINTi
P02406

STRING: functional protein association networks

More...
STRINGi
4932.YGL103W

<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

1149
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-V6-148[»]
3J6Xelectron microscopy6.10681-149[»]
3J6Yelectron microscopy6.10681-149[»]
3J77electron microscopy6.20781-149[»]
3J78electron microscopy6.30781-149[»]
3JCTelectron microscopy3.08a1-149[»]
4U3MX-ray3.00N8/n82-149[»]
4U3NX-ray3.20N8/n82-149[»]
4U3UX-ray2.90N8/n82-149[»]
4U4NX-ray3.10N8/n82-149[»]
4U4OX-ray3.60N8/n82-149[»]
4U4QX-ray3.00N8/n82-149[»]
4U4RX-ray2.80N8/n82-149[»]
4U4UX-ray3.00N8/n82-149[»]
4U4YX-ray3.20N8/n82-149[»]
4U4ZX-ray3.10N8/n82-149[»]
4U50X-ray3.20N8/n82-149[»]
4U51X-ray3.20N8/n82-149[»]
4U52X-ray3.00N8/n82-149[»]
4U53X-ray3.30N8/n82-149[»]
4U55X-ray3.20N8/n82-149[»]
4U56X-ray3.45N8/n82-149[»]
4U6FX-ray3.10N8/n82-149[»]
4V4Belectron microscopy11.70BV2-149[»]
4V6Ielectron microscopy8.80BO1-149[»]
4V7Felectron microscopy8.70N1-149[»]
4V7RX-ray4.00BY/DY1-149[»]
4V88X-ray3.00Ba/Da1-149[»]
4V8Telectron microscopy8.10a1-149[»]
4V8Yelectron microscopy4.30Ba2-149[»]
4V8Zelectron microscopy6.60Ba2-149[»]
4V91electron microscopy3.70a1-149[»]
5APNelectron microscopy3.91a1-149[»]
5APOelectron microscopy3.41a1-149[»]
5DATX-ray3.15N8/n82-149[»]
5DC3X-ray3.25N8/n82-149[»]
5DGEX-ray3.45N8/n82-149[»]
5DGFX-ray3.30N8/n82-149[»]
5DGVX-ray3.10N8/n82-149[»]
5FCIX-ray3.40N8/n82-149[»]
5FCJX-ray3.10N8/n82-149[»]
5FL8electron microscopy9.50a1-149[»]
5GAKelectron microscopy3.88c1-149[»]
5H4Pelectron microscopy3.07a1-149[»]
5I4LX-ray3.10N8/n82-149[»]
5JCSelectron microscopy9.50a1-149[»]
5JUOelectron microscopy4.00FA1-149[»]
5JUPelectron microscopy3.50FA1-149[»]
5JUSelectron microscopy4.20FA1-149[»]
5JUTelectron microscopy4.00FA1-149[»]
5JUUelectron microscopy4.00FA1-149[»]
5LYBX-ray3.25N8/n82-149[»]
5M1Jelectron microscopy3.30a52-149[»]
5MC6electron microscopy3.80AR1-149[»]
5MEIX-ray3.50AB/DC2-149[»]
5NDGX-ray3.70N8/n82-149[»]
5NDVX-ray3.30N8/n82-149[»]
5NDWX-ray3.70N8/n82-149[»]
5OBMX-ray3.40N8/n82-149[»]
5ON6X-ray3.10AB/DC2-149[»]
5T62electron microscopy3.30n1-149[»]
5T6Relectron microscopy4.50n1-149[»]
5TBWX-ray3.00AB/DC2-149[»]
5TGAX-ray3.30N8/n82-149[»]
5TGMX-ray3.50N8/n82-149[»]
6ELZelectron microscopy3.30a1-149[»]
6FT6electron microscopy3.90a1-149[»]
6GQ1electron microscopy4.40a2-149[»]
6GQBelectron microscopy3.90a2-149[»]
6GQVelectron microscopy4.00a2-149[»]
6HD7electron microscopy3.40c1-149[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...
ProteinModelPortali
P02406

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

More...
SMRi
P02406

Database of comparative protein structure models

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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
P02406

<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

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi7 – 13Nuclear localization signal1 Publication7
Motifi24 – 30Nuclear localization signal1 Publication7

<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

Ensembl GeneTree

More...
GeneTreei
ENSGT00390000005534

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000231263

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P02406

KEGG Orthology (KO)

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KOi
K02900

Identification of Orthologs from Complete Genome Data

More...
OMAi
WGRVGQH

Family and domain databases

HAMAP database of protein families

More...
HAMAPi
MF_01341 Ribosomal_L15, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR036227 L18e/L15P_sf
IPR030878 Ribosomal_L15
IPR001196 Ribosomal_L15_CS
IPR021131 Ribosomal_L18e/L15P

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00828 Ribosomal_L27A, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF52080 SSF52080, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00475 RIBOSOMAL_L15, 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.

P02406-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MPSRFTKTRK HRGHVSAGKG RIGKHRKHPG GRGMAGGQHH HRINMDKYHP
60 70 80 90 100
GYFGKVGMRY FHKQQAHFWK PVLNLDKLWT LIPEDKRDQY LKSASKETAP
110 120 130 140
VIDTLAAGYG KILGKGRIPN VPVIVKARFV SKLAEEKIRA AGGVVELIA
Length:149
Mass (Da):16,722
Last modified:October 5, 2010 - v3
<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:iB34C325C01E14ACB
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural varianti38Q → E Confers resistance to cycloheximide, an inhibitor of polypeptide elongation. 1 Publication1

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
X01573 Genomic DNA Translation: CAA25729.1
Z72625 Genomic DNA Translation: CAA96808.1
M19490 Genomic DNA Translation: AAA35002.1
BK006941 Genomic DNA Translation: DAA08004.1

Protein sequence database of the Protein Information Resource

More...
PIRi
A02782 R6BY29

NCBI Reference Sequences

More...
RefSeqi
NP_011412.1, NM_001180968.1

Genome annotation databases

Ensembl fungal genome annotation project

More...
EnsemblFungii
YGL103W_mRNA; YGL103W_mRNA; YGL103W

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
852775

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
sce:YGL103W

<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
X01573 Genomic DNA Translation: CAA25729.1
Z72625 Genomic DNA Translation: CAA96808.1
M19490 Genomic DNA Translation: AAA35002.1
BK006941 Genomic DNA Translation: DAA08004.1
PIRiA02782 R6BY29
RefSeqiNP_011412.1, NM_001180968.1

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1K5Ymodel-V6-148[»]
3J6Xelectron microscopy6.10681-149[»]
3J6Yelectron microscopy6.10681-149[»]
3J77electron microscopy6.20781-149[»]
3J78electron microscopy6.30781-149[»]
3JCTelectron microscopy3.08a1-149[»]
4U3MX-ray3.00N8/n82-149[»]
4U3NX-ray3.20N8/n82-149[»]
4U3UX-ray2.90N8/n82-149[»]
4U4NX-ray3.10N8/n82-149[»]
4U4OX-ray3.60N8/n82-149[»]
4U4QX-ray3.00N8/n82-149[»]
4U4RX-ray2.80N8/n82-149[»]
4U4UX-ray3.00N8/n82-149[»]
4U4YX-ray3.20N8/n82-149[»]
4U4ZX-ray3.10N8/n82-149[»]
4U50X-ray3.20N8/n82-149[»]
4U51X-ray3.20N8/n82-149[»]
4U52X-ray3.00N8/n82-149[»]
4U53X-ray3.30N8/n82-149[»]
4U55X-ray3.20N8/n82-149[»]
4U56X-ray3.45N8/n82-149[»]
4U6FX-ray3.10N8/n82-149[»]
4V4Belectron microscopy11.70BV2-149[»]
4V6Ielectron microscopy8.80BO1-149[»]
4V7Felectron microscopy8.70N1-149[»]
4V7RX-ray4.00BY/DY1-149[»]
4V88X-ray3.00Ba/Da1-149[»]
4V8Telectron microscopy8.10a1-149[»]
4V8Yelectron microscopy4.30Ba2-149[»]
4V8Zelectron microscopy6.60Ba2-149[»]
4V91electron microscopy3.70a1-149[»]
5APNelectron microscopy3.91a1-149[»]
5APOelectron microscopy3.41a1-149[»]
5DATX-ray3.15N8/n82-149[»]
5DC3X-ray3.25N8/n82-149[»]
5DGEX-ray3.45N8/n82-149[»]
5DGFX-ray3.30N8/n82-149[»]
5DGVX-ray3.10N8/n82-149[»]
5FCIX-ray3.40N8/n82-149[»]
5FCJX-ray3.10N8/n82-149[»]
5FL8electron microscopy9.50a1-149[»]
5GAKelectron microscopy3.88c1-149[»]
5H4Pelectron microscopy3.07a1-149[»]
5I4LX-ray3.10N8/n82-149[»]
5JCSelectron microscopy9.50a1-149[»]
5JUOelectron microscopy4.00FA1-149[»]
5JUPelectron microscopy3.50FA1-149[»]
5JUSelectron microscopy4.20FA1-149[»]
5JUTelectron microscopy4.00FA1-149[»]
5JUUelectron microscopy4.00FA1-149[»]
5LYBX-ray3.25N8/n82-149[»]
5M1Jelectron microscopy3.30a52-149[»]
5MC6electron microscopy3.80AR1-149[»]
5MEIX-ray3.50AB/DC2-149[»]
5NDGX-ray3.70N8/n82-149[»]
5NDVX-ray3.30N8/n82-149[»]
5NDWX-ray3.70N8/n82-149[»]
5OBMX-ray3.40N8/n82-149[»]
5ON6X-ray3.10AB/DC2-149[»]
5T62electron microscopy3.30n1-149[»]
5T6Relectron microscopy4.50n1-149[»]
5TBWX-ray3.00AB/DC2-149[»]
5TGAX-ray3.30N8/n82-149[»]
5TGMX-ray3.50N8/n82-149[»]
6ELZelectron microscopy3.30a1-149[»]
6FT6electron microscopy3.90a1-149[»]
6GQ1electron microscopy4.40a2-149[»]
6GQBelectron microscopy3.90a2-149[»]
6GQVelectron microscopy4.00a2-149[»]
6HD7electron microscopy3.40c1-149[»]
ProteinModelPortaliP02406
SMRiP02406
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi33147, 281 interactors
ComplexPortaliCPX-1601 60S cytosolic large ribosomal subunit
ELMiP02406
IntActiP02406, 32 interactors
MINTiP02406
STRINGi4932.YGL103W

PTM databases

CarbonylDBiP02406
iPTMnetiP02406

Proteomic databases

MaxQBiP02406
PaxDbiP02406
PRIDEiP02406

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYGL103W_mRNA; YGL103W_mRNA; YGL103W
GeneIDi852775
KEGGisce:YGL103W

Organism-specific databases

EuPathDBiFungiDB:YGL103W
SGDiS000003071 RPL28

Phylogenomic databases

GeneTreeiENSGT00390000005534
HOGENOMiHOG000231263
InParanoidiP02406
KOiK02900
OMAiWGRVGQH

Enzyme and pathway databases

BioCyciYEAST:G3O-30602-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

EvolutionaryTraceiP02406

Protein Ontology

More...
PROi
PR:P02406

Family and domain databases

HAMAPiMF_01341 Ribosomal_L15, 1 hit
InterProiView protein in InterPro
IPR036227 L18e/L15P_sf
IPR030878 Ribosomal_L15
IPR001196 Ribosomal_L15_CS
IPR021131 Ribosomal_L18e/L15P
PfamiView protein in Pfam
PF00828 Ribosomal_L27A, 1 hit
SUPFAMiSSF52080 SSF52080, 1 hit
PROSITEiView protein in PROSITE
PS00475 RIBOSOMAL_L15, 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 nameiRL28_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: P02406
Secondary accession number(s): D6VU43
<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 21, 1986
Last sequence update: October 5, 2010
Last modified: February 13, 2019
This is version 172 of the entry and version 3 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, Reference proteome

Documents

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