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Entry version 162 (05 Jun 2019)
Sequence version 3 (23 Jan 2007)
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Protein

60S ribosomal protein L22-A

Gene

RPL22A

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score:

Annotation score:4 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 60400 molecules/cell in log phase SD medium.1 Publication
There are 2 genes for eL22 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

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

GO - Biological processi

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

Molecular functionRibonucleoprotein, Ribosomal protein

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
YEAST:G3O-32215-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 L22-A1 Publication
Alternative name(s):
L1c
RP4
YL31
<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:RPL22A1 Publication
Ordered Locus Names:YLR061W
ORF Names:L2168
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri559292 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000002311 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome XII

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...
EuPathDBi
FungiDB:YLR061W

Saccharomyces Genome Database

More...
SGDi
S000004051 RPL22A

<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

<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 methionineiRemoved2 Publications
<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_00002155142 – 12160S ribosomal protein L22-AAdd BLAST120

Proteomic databases

MaxQB - The MaxQuant DataBase

More...
MaxQBi
P05749

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

More...
PaxDbi
P05749

PRoteomics IDEntifications database

More...
PRIDEi
P05749

Consortium for Top Down Proteomics

More...
TopDownProteomicsi
P05749

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P05749

<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
31336, 391 interactors

Protein interaction database and analysis system

More...
IntActi
P05749, 5 interactors

Molecular INTeraction database

More...
MINTi
P05749

STRING: functional protein association networks

More...
STRINGi
4932.YLR061W

<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

1121
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

More...
SMRi
P05749

Database of comparative protein structure models

More...
ModBasei
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

Phylogenomic databases

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000169435

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000198396

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P05749

KEGG Orthology (KO)

More...
KOi
K02891

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.30.1360.210, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR002671 Ribosomal_L22e
IPR038526 Ribosomal_L22e_sf

The PANTHER Classification System

More...
PANTHERi
PTHR10064 PTHR10064, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF01776 Ribosomal_L22e, 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.

P05749-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MAPNTSRKQK IAKTFTVDVS SPTENGVFDP ASYAKYLIDH IKVEGAVGNL
60 70 80 90 100
GNAVTVTEDG TVVTVVSTAK FSGKYLKYLT KKYLKKNQLR DWIRFVSTKT
110 120
NEYRLAFYQV TPEEDEEEDE E
Length:121
Mass (Da):13,693
Last modified:January 23, 2007 - 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:iAFF542E484A52069
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 conflicti49N → D AA sequence (PubMed:6814480).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
X94607 Genomic DNA Translation: CAA64308.1
Z73233 Genomic DNA Translation: CAA97592.1
BK006945 Genomic DNA Translation: DAA09379.1

Protein sequence database of the Protein Information Resource

More...
PIRi
S61635

NCBI Reference Sequences

More...
RefSeqi
NP_013162.1, NM_001181948.1

Genome annotation databases

Ensembl fungal genome annotation project

More...
EnsemblFungii
YLR061W_mRNA; YLR061W_mRNA; YLR061W

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
850750

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
sce:YLR061W

<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
X94607 Genomic DNA Translation: CAA64308.1
Z73233 Genomic DNA Translation: CAA97592.1
BK006945 Genomic DNA Translation: DAA09379.1
PIRiS61635
RefSeqiNP_013162.1, NM_001181948.1

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 microscopy6.10621-121[»]
3J6Yelectron microscopy6.10621-121[»]
3J77electron microscopy6.20721-121[»]
3J78electron microscopy6.30721-121[»]
3JCTelectron microscopy3.08U1-121[»]
4U3MX-ray3.00N2/n22-121[»]
4U3NX-ray3.20N2/n22-121[»]
4U3UX-ray2.90N2/n22-121[»]
4U4NX-ray3.10N2/n22-121[»]
4U4OX-ray3.60N2/n22-121[»]
4U4QX-ray3.00N2/n22-121[»]
4U4RX-ray2.80N2/n22-121[»]
4U4UX-ray3.00N2/n22-121[»]
4U4YX-ray3.20N2/n22-121[»]
4U4ZX-ray3.10N2/n22-121[»]
4U50X-ray3.20N2/n22-121[»]
4U51X-ray3.20N2/n22-121[»]
4U52X-ray3.00N2/n22-121[»]
4U53X-ray3.30N2/n22-121[»]
4U55X-ray3.20N2/n22-121[»]
4U56X-ray3.45N2/n22-121[»]
4U6FX-ray3.10N2/n22-121[»]
4V6Ielectron microscopy8.80BW1-121[»]
4V7Felectron microscopy8.70V1-121[»]
4V88X-ray3.00BU/DU1-121[»]
4V8Telectron microscopy8.10U1-121[»]
4V8Yelectron microscopy4.30BU2-121[»]
4V8Zelectron microscopy6.60BU2-121[»]
4V91electron microscopy3.70U1-121[»]
5APNelectron microscopy3.91U1-121[»]
5APOelectron microscopy3.41U1-121[»]
5DATX-ray3.15N2/n22-121[»]
5DC3X-ray3.25N2/n22-121[»]
5DGEX-ray3.45N2/n22-121[»]
5DGFX-ray3.30N2/n22-121[»]
5DGVX-ray3.10N2/n22-121[»]
5FCIX-ray3.40N2/n22-121[»]
5FCJX-ray3.10N2/n22-121[»]
5FL8electron microscopy9.50U1-121[»]
5GAKelectron microscopy3.88W1-121[»]
5H4Pelectron microscopy3.07U1-121[»]
5I4LX-ray3.10N2/n29-108[»]
5JCSelectron microscopy9.50U1-121[»]
5JUOelectron microscopy4.00Z1-121[»]
5JUPelectron microscopy3.50Z1-121[»]
5JUSelectron microscopy4.20Z1-121[»]
5JUTelectron microscopy4.00Z1-121[»]
5JUUelectron microscopy4.00Z1-121[»]
5LYBX-ray3.25N2/n29-108[»]
5M1Jelectron microscopy3.30U59-108[»]
5MC6electron microscopy3.80BL1-121[»]
5MEIX-ray3.505/CW9-108[»]
5NDGX-ray3.70N2/n211-108[»]
5NDVX-ray3.30N2/n210-108[»]
5NDWX-ray3.70N2/n29-108[»]
5OBMX-ray3.40N2/n29-108[»]
5ON6X-ray3.105/CW9-108[»]
5T62electron microscopy3.30h1-121[»]
5T6Relectron microscopy4.50h1-121[»]
5TBWX-ray3.005/CW9-108[»]
5TGAX-ray3.30N2/n29-108[»]
5TGMX-ray3.50N2/n29-108[»]
6ELZelectron microscopy3.30U1-121[»]
6EM5electron microscopy4.30U1-121[»]
6FT6electron microscopy3.90U1-121[»]
6GQ1electron microscopy4.40U9-108[»]
6GQBelectron microscopy3.90U9-108[»]
6GQVelectron microscopy4.00U9-108[»]
6HD7electron microscopy3.40W1-121[»]
6HHQX-ray3.105/CW1-121[»]
6I7Oelectron microscopy5.30BL/YL11-108[»]
6N8Jelectron microscopy3.50U1-121[»]
6N8Kelectron microscopy3.60U1-121[»]
6N8Lelectron microscopy3.60U1-121[»]
6N8Melectron microscopy3.50h1-121[»]
6N8Nelectron microscopy3.80h1-121[»]
6N8Oelectron microscopy3.50h1-121[»]
6Q8Yelectron microscopy3.10BL9-108[»]
SMRiP05749
ModBaseiSearch...

Protein-protein interaction databases

BioGridi31336, 391 interactors
IntActiP05749, 5 interactors
MINTiP05749
STRINGi4932.YLR061W

PTM databases

iPTMnetiP05749

Proteomic databases

MaxQBiP05749
PaxDbiP05749
PRIDEiP05749
TopDownProteomicsiP05749

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYLR061W_mRNA; YLR061W_mRNA; YLR061W
GeneIDi850750
KEGGisce:YLR061W

Organism-specific databases

EuPathDBiFungiDB:YLR061W
SGDiS000004051 RPL22A

Phylogenomic databases

GeneTreeiENSGT00940000169435
HOGENOMiHOG000198396
InParanoidiP05749
KOiK02891

Enzyme and pathway databases

BioCyciYEAST:G3O-32215-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

More...
PROi
PR:P05749

Family and domain databases

Gene3Di3.30.1360.210, 1 hit
InterProiView protein in InterPro
IPR002671 Ribosomal_L22e
IPR038526 Ribosomal_L22e_sf
PANTHERiPTHR10064 PTHR10064, 1 hit
PfamiView protein in Pfam
PF01776 Ribosomal_L22e, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

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 nameiRL22A_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: P05749
Secondary accession number(s): D6VY63
<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: November 1, 1988
Last sequence update: January 23, 2007
Last modified: June 5, 2019
This is version 162 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, 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 chromosome XII
    Yeast (Saccharomyces cerevisiae) chromosome XII: entries and gene names
  4. Ribosomal proteins
    Ribosomal proteins families and list of entries
  5. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
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