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UniProtKB - P05740 (RL17A_YEAST)

Entry version 193 (25 May 2022)
Sequence version 4 (23 Jan 2007)
Previous versions | rss
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Protein

60S ribosomal protein L17-A

Gene

RPL17A

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

There are 2 genes for uL22 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

  • structural constituent of ribosome Source: SGD
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

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-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%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:
60S ribosomal protein L17-A1 Publication
Alternative name(s):
L20A
Large ribosomal subunit protein uL22-A1 Publication
YL17
<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:RPL17A1 Publication
Synonyms:RPL17, RPL20A
Ordered Locus Names:YKL180W
<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		S000001663, RPL17A

Eukaryotic Pathogen, Vector and Host Database Resources

More...VEuPathDBi		FungiDB:YKL180W

<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 <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">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 methionineiRemoved2 Publications
<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_00001253472 – 18460S ribosomal protein L17-AAdd BLAST183

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">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-linki46Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources
<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 residuei70PhosphothreonineCombined sources1

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQB - The MaxQuant DataBase

More...MaxQBi		P05740

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

More...PaxDbi		P05740

PRoteomics IDEntifications database

More...PRIDEi		P05740

PTM databases

CarbonylDB database of protein carbonylation sites

More...CarbonylDBi		P05740

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P05740

<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 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). uL22 is associated with the polypeptide exit tunnel (PubMed:9559554, PubMed:22096102).

1 Publication1 Publication

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		33959, 210 interactors

Database of interacting proteins

More...DIPi		DIP-5529N

Protein interaction database and analysis system

More...IntActi		P05740, 59 interactors

Molecular INTeraction database

More...MINTi		P05740

STRING: functional protein association networks

More...STRINGi		4932.YKL180W

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...RNActi		P05740, 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

1184
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

AlphaFold Protein Structure Database

More...AlphaFoldDBi		P05740

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

More...SMRi		P05740

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		P05740

<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 universal ribosomal protein uL22 family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG3353, Eukaryota

Ensembl GeneTree

More...GeneTreei		ENSGT00950000183010

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_083987_0_0_1

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P05740

Identification of Orthologs from Complete Genome Data

More...OMAi		REPDNIT

Family and domain databases

Conserved Domains Database

More...CDDi		cd00336, Ribosomal_L22, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		3.90.470.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR001063, Ribosomal_L22
IPR018260, Ribosomal_L22/L17_CS
IPR005721, Ribosomal_L22/L17_euk/arc
IPR036394, Ribosomal_L22/L17_sf

The PANTHER Classification System

More...PANTHERi		PTHR11593, PTHR11593, 1 hit

Pfam protein domain database

More...Pfami		View protein in Pfam
PF00237, Ribosomal_L22, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF54843, SSF54843, 1 hit

TIGRFAMs; a protein family database

More...TIGRFAMsi		TIGR01038, uL22_arch_euk, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS00464, RIBOSOMAL_L22, 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.

<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 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.

P05740-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MARYGATSTN PAKSASARGS YLRVSFKNTR ETAQAINGWE LTKAQKYLEQ 
        60         70         80         90        100
VLDHQRAIPF RRFNSSIGRT AQGKEFGVTK ARWPAKSVKF VQGLLQNAAA 
       110        120        130        140        150
NAEAKGLDAT KLYVSHIQVN QAPKQRRRTY RAHGRINKYE SSPSHIELVV 
       160        170        180 
TEKEEAVAKA AEKKVVRLTS RQRGRIAAQK RIAA
Length:184
Mass (Da):20,549
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:iB8902DD90714671D
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 conflicti104 – 114AKGLDATKLYV → VCQEYYMFSTR in CAA52258 (PubMed:8154185).CuratedAdd BLAST11

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
Z28180 Genomic DNA Translation: CAA82023.1
Z28179 Genomic DNA Translation: CAA82022.1
X74151 Genomic DNA Translation: CAA52258.1
BK006944 Genomic DNA Translation: DAA08987.1

Protein sequence database of the Protein Information Resource

More...PIRi		S38012

NCBI Reference Sequences

More...RefSeqi		NP_012741.1, NM_001179746.1

Genome annotation databases

Ensembl fungal genome annotation project

More...EnsemblFungii		YKL180W_mRNA; YKL180W; YKL180W

Database of genes from NCBI RefSeq genomes

More...GeneIDi		853674

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		sce:YKL180W

<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
Z28180 Genomic DNA Translation: CAA82023.1
Z28179 Genomic DNA Translation: CAA82022.1
X74151 Genomic DNA Translation: CAA52258.1
BK006944 Genomic DNA Translation: DAA08987.1
PIRiS38012
RefSeqiNP_012741.1, NM_001179746.1

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
2WW9electron microscopy8.60I1-184[»]
2WWAelectron microscopy8.90I1-184[»]
2WWBelectron microscopy6.48I1-184[»]
3J6Xelectron microscopy6.10571-184[»]
3J6Yelectron microscopy6.10571-184[»]
3J77electron microscopy6.20671-184[»]
3J78electron microscopy6.30671-184[»]
3JCTelectron microscopy3.08P1-184[»]
4U3MX-ray3.00M7/m72-184[»]
4U3NX-ray3.20M7/m72-184[»]
4U3UX-ray2.90M7/m72-184[»]
4U4NX-ray3.10M7/m72-184[»]
4U4OX-ray3.60M7/m72-184[»]
4U4QX-ray3.00M7/m72-184[»]
4U4RX-ray2.80M7/m72-184[»]
4U4UX-ray3.00M7/m72-184[»]
4U4YX-ray3.20M7/m72-184[»]
4U4ZX-ray3.10M7/m72-184[»]
4U50X-ray3.20M7/m72-184[»]
4U51X-ray3.20M7/m72-184[»]
4U52X-ray3.00M7/m72-184[»]
4U53X-ray3.30M7/m72-184[»]
4U55X-ray3.20M7/m72-184[»]
4U56X-ray3.45M7/m72-184[»]
4U6FX-ray3.10M7/m72-184[»]
4V4Belectron microscopy11.70BN2-184[»]
4V6Ielectron microscopy8.80BV1-170[»]
4V7Felectron microscopy8.70U1-184[»]
4V7RX-ray4.00BQ/DQ1-184[»]
4V88X-ray3.00BP/DP1-184[»]
4V8Telectron microscopy8.10P1-184[»]
4V8Yelectron microscopy4.30BP2-184[»]
4V8Zelectron microscopy6.60BP2-184[»]
4V91electron microscopy3.70P1-184[»]
5APNelectron microscopy3.91P1-184[»]
5APOelectron microscopy3.41P1-184[»]
5DATX-ray3.15M7/m72-184[»]
5DC3X-ray3.25M7/m72-184[»]
5DGEX-ray3.45M7/m72-184[»]
5DGFX-ray3.30M7/m72-184[»]
5DGVX-ray3.10M7/m72-184[»]
5FCIX-ray3.40M7/m72-184[»]
5FCJX-ray3.10M7/m72-184[»]
5FL8electron microscopy9.50P1-184[»]
5GAKelectron microscopy3.88R1-184[»]
5H4Pelectron microscopy3.07P1-184[»]
5I4LX-ray3.10M7/m72-184[»]
5JCSelectron microscopy9.50P1-184[»]
5JUOelectron microscopy4.00U1-184[»]
5JUPelectron microscopy3.50U1-184[»]
5JUSelectron microscopy4.20U1-184[»]
5JUTelectron microscopy4.00U1-184[»]
5JUUelectron microscopy4.00U1-184[»]
5LYBX-ray3.25M7/m72-184[»]
5M1Jelectron microscopy3.30P52-184[»]
5MC6electron microscopy3.80AX1-184[»]
5MEIX-ray3.50CR/x2-184[»]
5NDGX-ray3.70M7/m71-184[»]
5NDVX-ray3.30M7/m71-184[»]
5NDWX-ray3.70M7/m71-184[»]
5OBMX-ray3.40M7/m71-184[»]
5ON6X-ray3.10CR/x2-184[»]
5T62electron microscopy3.30c1-184[»]
5T6Relectron microscopy4.50c1-184[»]
5TBWX-ray3.00CR/x2-184[»]
5TGAX-ray3.30M7/m72-184[»]
5TGMX-ray3.50M7/m72-184[»]
5Z3Gelectron microscopy3.65T1-184[»]
6C0Felectron microscopy3.70P1-184[»]
6CB1electron microscopy4.60P1-184[»]
6ELZelectron microscopy3.30P1-184[»]
6EM1electron microscopy3.60P1-184[»]
6EM3electron microscopy3.20P1-184[»]
6EM4electron microscopy4.10P1-184[»]
6EM5electron microscopy4.30P1-184[»]
6FT6electron microscopy3.90P1-184[»]
6GQ1electron microscopy4.40P2-184[»]
6GQBelectron microscopy3.90P2-184[»]
6GQVelectron microscopy4.00P2-184[»]
6HD7electron microscopy3.40R1-184[»]
6HHQX-ray3.10CR/x1-184[»]
6I7Oelectron microscopy5.30AX/XX1-184[»]
6M62electron microscopy3.20P1-184[»]
6N8Jelectron microscopy3.50P1-184[»]
6N8Kelectron microscopy3.60P1-184[»]
6N8Lelectron microscopy3.60P1-184[»]
6N8Melectron microscopy3.50c1-184[»]
6N8Nelectron microscopy3.80c1-184[»]
6N8Oelectron microscopy3.50c1-184[»]
6OIGelectron microscopy3.80P2-184[»]
6Q8Yelectron microscopy3.10AX2-184[»]
6QIKelectron microscopy3.10U2-155[»]
6QT0electron microscopy3.40U1-184[»]
6QTZelectron microscopy3.50U1-184[»]
6R84electron microscopy3.6052-184[»]
6R86electron microscopy3.4052-184[»]
6R87electron microscopy3.4052-184[»]
6RI5electron microscopy3.30U1-184[»]
6RZZelectron microscopy3.20U1-184[»]
6S05electron microscopy3.90U1-184[»]
6S47electron microscopy3.28AR2-184[»]
6SNTelectron microscopy2.80v1-184[»]
6SV4electron microscopy3.30AX/XX/zX1-184[»]
6T4Qelectron microscopy2.60LP2-184[»]
6T7Ielectron microscopy3.20LP1-184[»]
6T7Telectron microscopy3.10LP1-184[»]
6T83electron microscopy4.00A/Py1-184[»]
6TB3electron microscopy2.80AX2-184[»]
6TNUelectron microscopy3.10AX2-184[»]
6WOOelectron microscopy2.90P3-182[»]
6XIQelectron microscopy4.20P1-184[»]
6XIRelectron microscopy3.20P1-184[»]
6YLGelectron microscopy3.00P1-184[»]
6YLHelectron microscopy3.10P1-184[»]
6YLXelectron microscopy3.90P1-184[»]
6YLYelectron microscopy3.80P1-184[»]
6Z6Jelectron microscopy3.40LP1-184[»]
6Z6Kelectron microscopy3.40LP1-184[»]
7AZYelectron microscopy2.88y1-184[»]
7B7Delectron microscopy3.30LR2-184[»]
7BT6electron microscopy3.12P1-184[»]
7BTBelectron microscopy3.22P1-184[»]
7NRCelectron microscopy3.90LR2-184[»]
7NRDelectron microscopy4.36LR2-184[»]
7OF1electron microscopy3.10P1-184[»]
7OH3electron microscopy3.40P1-184[»]
7OHPelectron microscopy3.90P1-184[»]
7OHQelectron microscopy3.10P1-184[»]
7OHRelectron microscopy4.72P1-184[»]
7OHSelectron microscopy4.38P1-184[»]
7OHUelectron microscopy3.70P1-184[»]
7OHVelectron microscopy3.90P1-184[»]
7OHWelectron microscopy3.50P1-184[»]
7OHXelectron microscopy3.30P1-184[»]
7OHYelectron microscopy3.90P1-184[»]
AlphaFoldDBiP05740
SMRiP05740
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi33959, 210 interactors
DIPiDIP-5529N
IntActiP05740, 59 interactors
MINTiP05740
STRINGi4932.YKL180W

PTM databases

CarbonylDBiP05740
iPTMnetiP05740

Proteomic databases

MaxQBiP05740
PaxDbiP05740
PRIDEiP05740

Genome annotation databases

EnsemblFungiiYKL180W_mRNA; YKL180W; YKL180W
GeneIDi853674
KEGGisce:YKL180W

Organism-specific databases

SGDiS000001663, RPL17A
VEuPathDBiFungiDB:YKL180W

Phylogenomic databases

eggNOGiKOG3353, Eukaryota
GeneTreeiENSGT00950000183010
HOGENOMiCLU_083987_0_0_1
InParanoidiP05740
OMAiREPDNIT

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-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

EvolutionaryTraceiP05740

Protein Ontology

More...PROi		PR:P05740
RNActiP05740, protein

Family and domain databases

CDDicd00336, Ribosomal_L22, 1 hit
Gene3Di3.90.470.10, 1 hit
InterProiView protein in InterPro
IPR001063, Ribosomal_L22
IPR018260, Ribosomal_L22/L17_CS
IPR005721, Ribosomal_L22/L17_euk/arc
IPR036394, Ribosomal_L22/L17_sf
PANTHERiPTHR11593, PTHR11593, 1 hit
PfamiView protein in Pfam
PF00237, Ribosomal_L22, 1 hit
SUPFAMiSSF54843, SSF54843, 1 hit
TIGRFAMsiTIGR01038, uL22_arch_euk, 1 hit
PROSITEiView protein in PROSITE
PS00464, RIBOSOMAL_L22, 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 nameiRL17A_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: P05740
Secondary accession number(s): D6VX21
<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: November 1, 1988
Last sequence update: January 23, 2007
Last modified: May 25, 2022
This is version 193 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. 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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