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UniProtKB - P35997 (RS27A_YEAST)

Entry version 168 (25 May 2022)
Sequence version 1 (01 Jun 1994)
Previous versions | rss
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Protein

40S ribosomal protein S27-A

Gene

RPS27A

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 43300 molecules/cell in log phase SD medium.1 Publication
There are 2 genes for eS27 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+CuratedNote: Binds 1 zinc ion per subunit.Curated

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> 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 fingeri37 – 59C4-typeSequence analysisAdd BLAST23

<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

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<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
LigandMetal-binding, Zinc

Enzyme and pathway databases

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-6791226, Major pathway of rRNA processing in the nucleolus and cytosol
R-SCE-72689, Formation of a pool of free 40S subunits
R-SCE-72695, Formation of the ternary complex, and subsequently, the 43S complex
R-SCE-72702, Ribosomal scanning and start codon recognition
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%5Fand%5Ftaxonomy%5Fsection">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:
40S ribosomal protein S27-A1 Publication
Alternative name(s):
RP61
Small ribosomal subunit protein eS27-A1 Publication
YS20
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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:RPS27A1 Publication
Ordered Locus Names:YKL156W
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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 lineageiEukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces ›
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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%5Fmanual">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 XI

Organism-specific databases

Saccharomyces Genome Database

More...SGDi		S000001639, RPS27A

Eukaryotic Pathogen, Vector and Host Database Resources

More...VEuPathDBi		FungiDB:YKL156W

<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

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 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001490661 – 8240S ribosomal protein S27-AAdd BLAST82

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 residuei40S-methylcysteine1 Publication1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">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

The N-terminus is not modified.1 Publication

Keywords - PTMi

Methylation

Proteomic databases

MaxQB - The MaxQuant DataBase

More...MaxQBi		P35997

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

More...PaxDbi		P35997

PRoteomics IDEntifications database

More...PRIDEi		P35997

Consortium for Top Down Proteomics

More...TopDownProteomicsi		P35997

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P35997

<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%5Fsection">'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%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Component of the small ribosomal subunit (SSU). Mature yeast ribosomes consist of a small (40S) and a large (60S) subunit. The 40S small subunit contains 1 molecule of ribosomal RNA (18S rRNA) and 33 different proteins (encoded by 57 genes). The large 60S subunit contains 3 rRNA molecules (25S, 5.8S and 5S rRNA) and 46 different proteins (encoded by 81 genes) (PubMed:9559554, PubMed:22096102).

1 Publication1 Publication

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		33981, 713 interactors

Protein interaction database and analysis system

More...IntActi		P35997, 11 interactors

Molecular INTeraction database

More...MINTi		P35997

STRING: functional protein association networks

More...STRINGi		4932.YKL156W

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...RNActi		P35997, 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

182
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

AlphaFold Protein Structure Database

More...AlphaFoldDBi		P35997

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

More...SMRi		P35997

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

<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

Belongs to the eukaryotic ribosomal protein eS27 family.Curated

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri37 – 59C4-typeSequence analysisAdd BLAST23

Keywords - Domaini

Zinc-finger

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG1779, Eukaryota

Ensembl GeneTree

More...GeneTreei		ENSGT00940000167938

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_130128_3_0_1

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P35997

Identification of Orthologs from Complete Genome Data

More...OMAi		LHPAIDF

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		2.20.25.100, 1 hit

HAMAP database of protein families

More...HAMAPi		MF_00371, Ribosomal_S27e, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR000592, Ribosomal_S27
IPR023407, Ribosomal_S27_Zn-bd_dom_sf
IPR011332, Ribosomal_zn-bd

The PANTHER Classification System

More...PANTHERi		PTHR11594, PTHR11594, 1 hit

Pfam protein domain database

More...Pfami		View protein in Pfam
PF01667, Ribosomal_S27e, 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
PS01168, RIBOSOMAL_S27E, 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%5Flength">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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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.

P35997-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MVLVQDLLHP TAASEARKHK LKTLVQGPRS YFLDVKCPGC LNITTVFSHA 
        60         70         80 
QTAVTCESCS TILCTPTGGK AKLSEGTSFR RK
Length:82
Mass (Da):8,879
Last modified:June 1, 1994 - v1
<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:iFCA80130CFCEC91E
GO

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
Z26877 Genomic DNA No translation available.
Z28156 Genomic DNA Translation: CAA81998.1
Z28155 Genomic DNA Translation: CAA81997.1
BK006944 Genomic DNA Translation: DAA09008.1

Protein sequence database of the Protein Information Resource

More...PIRi		S37986

NCBI Reference Sequences

More...RefSeqi		NP_012766.1, NM_001179722.1

Genome annotation databases

Ensembl fungal genome annotation project

More...EnsemblFungii		YKL156W_mRNA; YKL156W; YKL156W

Database of genes from NCBI RefSeq genomes

More...GeneIDi		853700

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		sce:YKL156W

<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
Z26877 Genomic DNA No translation available.
Z28156 Genomic DNA Translation: CAA81998.1
Z28155 Genomic DNA Translation: CAA81997.1
BK006944 Genomic DNA Translation: DAA09008.1
PIRiS37986
RefSeqiNP_012766.1, NM_001179722.1

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
3J6Xelectron microscopy6.10271-82[»]
3J6Yelectron microscopy6.10271-82[»]
3J77electron microscopy6.20271-82[»]
3J78electron microscopy6.30271-82[»]
4U3MX-ray3.00D7/d72-82[»]
4U3NX-ray3.20D7/d72-82[»]
4U3UX-ray2.90D7/d72-82[»]
4U4NX-ray3.10D7/d72-82[»]
4U4OX-ray3.60D7/d72-82[»]
4U4QX-ray3.00D7/d72-82[»]
4U4RX-ray2.80D7/d72-82[»]
4U4UX-ray3.00D7/d72-82[»]
4U4YX-ray3.20D7/d72-82[»]
4U4ZX-ray3.10D7/d72-82[»]
4U50X-ray3.20D7/d72-82[»]
4U51X-ray3.20D7/d72-82[»]
4U52X-ray3.00D7/d72-82[»]
4U53X-ray3.30D7/d72-82[»]
4U55X-ray3.20D7/d72-82[»]
4U56X-ray3.45D7/d72-82[»]
4U6FX-ray3.10D7/d72-82[»]
4V6Ielectron microscopy8.80AX1-82[»]
4V88X-ray3.00Ab/Cb1-82[»]
4V8Yelectron microscopy4.30A11-82[»]
4V8Zelectron microscopy6.60A11-82[»]
4V92electron microscopy3.70b2-82[»]
5DATX-ray3.15D7/d72-82[»]
5DC3X-ray3.25D7/d72-82[»]
5DGEX-ray3.45D7/d72-82[»]
5DGFX-ray3.30D7/d72-82[»]
5DGVX-ray3.10D7/d72-82[»]
5FCIX-ray3.40D7/d72-82[»]
5FCJX-ray3.10D7/d72-82[»]
5I4LX-ray3.10D7/d72-82[»]
5JUOelectron microscopy4.00YB1-82[»]
5JUPelectron microscopy3.50YB1-82[»]
5JUSelectron microscopy4.20YB1-82[»]
5JUTelectron microscopy4.00YB1-82[»]
5JUUelectron microscopy4.00YB1-82[»]
5LL6electron microscopy3.90f1-82[»]
5LYBX-ray3.25D7/d72-82[»]
5M1Jelectron microscopy3.30b22-82[»]
5MC6electron microscopy3.80f1-82[»]
5MEIX-ray3.50c/d72-82[»]
5NDGX-ray3.70D7/d72-82[»]
5NDVX-ray3.30D7/d72-82[»]
5NDWX-ray3.70D7/d72-82[»]
5OBMX-ray3.40D7/d72-82[»]
5ON6X-ray3.10c/d72-82[»]
5TBWX-ray3.00c/d72-82[»]
5TGAX-ray3.30D7/d72-82[»]
5TGMX-ray3.50D7/d72-82[»]
5WYJelectron microscopy8.70Sc1-82[»]
5WYKelectron microscopy4.50Sc1-82[»]
6EMLelectron microscopy3.60f1-82[»]
6FAIelectron microscopy3.40b1-82[»]
6GQ1electron microscopy4.40AR2-82[»]
6GQBelectron microscopy3.90AR2-82[»]
6GQVelectron microscopy4.00AR2-82[»]
6HHQX-ray3.10c/d71-82[»]
6I7Oelectron microscopy5.30f/fb2-82[»]
6KE6electron microscopy3.40Sc1-82[»]
6LQPelectron microscopy3.20Sc1-82[»]
6LQQelectron microscopy4.10Sc1-82[»]
6LQRelectron microscopy8.60Sc1-82[»]
6LQSelectron microscopy3.80Sc1-82[»]
6LQTelectron microscopy4.90Sc1-82[»]
6Q8Yelectron microscopy3.10f2-82[»]
6RBDelectron microscopy3.47b1-82[»]
6RBEelectron microscopy3.80b1-82[»]
6S47electron microscopy3.28Bc2-82[»]
6SNTelectron microscopy2.80b1-82[»]
6SV4electron microscopy3.30f/fb/fc1-82[»]
6T4Qelectron microscopy2.60Sb2-82[»]
6T7Ielectron microscopy3.20Sb1-82[»]
6T7Telectron microscopy3.10Sb1-82[»]
6T83electron microscopy4.002/bb1-82[»]
6TB3electron microscopy2.80f2-82[»]
6TNUelectron microscopy3.10f2-82[»]
6WDRelectron microscopy3.70b2-82[»]
6WOOelectron microscopy2.90bb2-82[»]
6XIQelectron microscopy4.20AR1-82[»]
6XIRelectron microscopy3.20AR1-82[»]
6Y7Celectron microscopy3.80b1-82[»]
6Z6Jelectron microscopy3.40Sb1-82[»]
6Z6Kelectron microscopy3.40Sb1-82[»]
6ZCEelectron microscopy5.30c1-82[»]
6ZQAelectron microscopy4.40Db1-82[»]
6ZQBelectron microscopy3.90Db1-82[»]
6ZQCelectron microscopy3.80Db1-82[»]
6ZQDelectron microscopy3.80Db1-82[»]
6ZQEelectron microscopy7.10Db1-82[»]
6ZQFelectron microscopy4.90Db1-82[»]
6ZQGelectron microscopy3.50Db1-82[»]
6ZU9electron microscopy6.20f1-82[»]
6ZVIelectron microscopy3.00L2-82[»]
7A1Gelectron microscopy3.00f2-82[»]
7AJTelectron microscopy4.60Db1-82[»]
7AJUelectron microscopy3.80Db1-82[»]
7B7Delectron microscopy3.30f2-82[»]
7D4Ielectron microscopy4.00Sc1-82[»]
7D5Telectron microscopy6.00Sc1-82[»]
7D63electron microscopy12.30Sc1-82[»]
7NRCelectron microscopy3.90Sf2-82[»]
7NRDelectron microscopy4.36Sf2-82[»]
7OSAX-ray3.00eS271-82[»]
7OSMX-ray3.00eS271-82[»]
7RR5electron microscopy3.23Sb1-82[»]
AlphaFoldDBiP35997
SMRiP35997
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi33981, 713 interactors
IntActiP35997, 11 interactors
MINTiP35997
STRINGi4932.YKL156W

PTM databases

iPTMnetiP35997

Proteomic databases

MaxQBiP35997
PaxDbiP35997
PRIDEiP35997
TopDownProteomicsiP35997

Genome annotation databases

EnsemblFungiiYKL156W_mRNA; YKL156W; YKL156W
GeneIDi853700
KEGGisce:YKL156W

Organism-specific databases

SGDiS000001639, RPS27A
VEuPathDBiFungiDB:YKL156W

Phylogenomic databases

eggNOGiKOG1779, Eukaryota
GeneTreeiENSGT00940000167938
HOGENOMiCLU_130128_3_0_1
InParanoidiP35997
OMAiLHPAIDF

Enzyme and pathway databases

ReactomeiR-SCE-156827, L13a-mediated translational silencing of Ceruloplasmin expression
R-SCE-1799339, SRP-dependent cotranslational protein targeting to membrane
R-SCE-6791226, Major pathway of rRNA processing in the nucleolus and cytosol
R-SCE-72689, Formation of a pool of free 40S subunits
R-SCE-72695, Formation of the ternary complex, and subsequently, the 43S complex
R-SCE-72702, Ribosomal scanning and start codon recognition
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

More...PROi		PR:P35997
RNActiP35997, protein

Family and domain databases

Gene3Di2.20.25.100, 1 hit
HAMAPiMF_00371, Ribosomal_S27e, 1 hit
InterProiView protein in InterPro
IPR000592, Ribosomal_S27
IPR023407, Ribosomal_S27_Zn-bd_dom_sf
IPR011332, Ribosomal_zn-bd
PANTHERiPTHR11594, PTHR11594, 1 hit
PfamiView protein in Pfam
PF01667, Ribosomal_S27e, 1 hit
SUPFAMiSSF57829, SSF57829, 1 hit
PROSITEiView protein in PROSITE
PS01168, RIBOSOMAL_S27E, 1 hit

MobiDB: a database of protein disorder and mobility annotations

More...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 nameiRS27A_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: P35997
Secondary accession number(s): D6VX42
<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%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: May 25, 2022
This is version 168 of the entry and version 1 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, Reference proteome

Documents

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