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Entry version 182 (13 Nov 2019)
Sequence version 1 (01 Nov 1995)
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Protein

Ubiquitin carboxyl-terminal hydrolase RPN11

Gene

RPN11

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 lid subcomplex of the 26S proteasome, a multiprotein complex involved in the ATP-dependent degradation of ubiquitinated proteins. RPN11 is the only catalytically active member of the lid and serves as the essential deubiquitinase of the proteasome.3 Publications

Miscellaneous

Present with 16400 molecules/cell in log phase SD medium.1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

  • Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal). EC:3.4.19.12

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi109Zinc; catalyticPROSITE-ProRule annotation1
Metal bindingi111Zinc; catalyticPROSITE-ProRule annotation1
Metal bindingi122Zinc; catalyticPROSITE-ProRule annotation1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

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

Molecular functionHydrolase, Metalloprotease, Protease, Thiol protease
Biological processUbl conjugation pathway
LigandMetal-binding, Zinc

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
YEAST:G3O-30457-MONOMER

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-SCE-1236978 Cross-presentation of soluble exogenous antigens (endosomes)
R-SCE-5668541 TNFR2 non-canonical NF-kB pathway
R-SCE-5689603 UCH proteinases
R-SCE-5689880 Ub-specific processing proteases
R-SCE-6798695 Neutrophil degranulation

Protein family/group databases

MEROPS protease database

More...
MEROPSi
M67.001

<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:
Ubiquitin carboxyl-terminal hydrolase RPN11 (EC:3.4.19.12)
Alternative name(s):
26S proteasome regulatory subunit RPN11
Protein MPR1
<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:RPN11
Synonyms:MPR1
Ordered Locus Names:YFR004W
<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 VI

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...
EuPathDBi
FungiDB:YFR004W

Saccharomyces Genome Database

More...
SGDi
S000001900 RPN11

<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

Proteasome

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

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi109H → A: Stabilizes ubiquitin pathway substrates; when associated wirh Ala-111. 1 Publication1
Mutagenesisi111H → A: Stabilizes ubiquitin pathway substrates; when associated wirh Ala-109. 1 Publication1

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘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_00002139601 – 306Ubiquitin carboxyl-terminal hydrolase RPN11Add BLAST306

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 residuei1N-acetylmethionine1 Publication1

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

N-acetylated by NAT3.1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQB - The MaxQuant DataBase

More...
MaxQBi
P43588

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

More...
PaxDbi
P43588

PRoteomics IDEntifications database

More...
PRIDEi
P43588

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P43588

<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 lid subcomplex of the 19S proteasome regulatory particle complex (also named PA700 complex). The 26S proteasome consists of a 20S proteasome core and two 19S regulatory subunits.

Interacts directly with RPN8 and STS1.

4 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
31152, 1226 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...
ComplexPortali
CPX-2262 26S Proteasome complex

Database of interacting proteins

More...
DIPi
DIP-1573N

Protein interaction database and analysis system

More...
IntActi
P43588, 37 interactors

Molecular INTeraction database

More...
MINTi
P43588

STRING: functional protein association networks

More...
STRINGi
4932.YFR004W

<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

1306
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
P43588

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

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini27 – 162MPNPROSITE-ProRule annotationAdd BLAST136

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>Motifi109 – 122JAMM motifPROSITE-ProRule annotationAdd BLAST14

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

The JAMM motif is required for the deubiquitination and degradation of ubiquitinated substrates.1 Publication

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the peptidase M67A family.Curated

Phylogenomic databases

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000183690

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P43588

KEGG Orthology (KO)

More...
KOi
K03030

Identification of Orthologs from Complete Genome Data

More...
OMAi
VFQTRMM

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR000555 JAMM/MPN+_dom
IPR037518 MPN
IPR035299 PSMD14
IPR024969 Rpn11/EIF3F_C

The PANTHER Classification System

More...
PANTHERi
PTHR10410:SF22 PTHR10410:SF22, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF01398 JAB, 1 hit
PF13012 MitMem_reg, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00232 JAB_MPN, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS50249 MPN, 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.

P43588-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MERLQRLMMN SKVGSADTGR DDTKETVYIS SIALLKMLKH GRAGVPMEVM
60 70 80 90 100
GLMLGEFVDD YTVNVVDVFA MPQSGTGVSV EAVDDVFQAK MMDMLKQTGR
110 120 130 140 150
DQMVVGWYHS HPGFGCWLSS VDVNTQKSFE QLNSRAVAVV VDPIQSVKGK
160 170 180 190 200
VVIDAFRLID TGALINNLEP RQTTSNTGLL NKANIQALIH GLNRHYYSLN
210 220 230 240 250
IDYHKTAKET KMLMNLHKEQ WQSGLKMYDY EEKEESNLAA TKSMVKIAEQ
260 270 280 290 300
YSKRIEEEKE LTEEELKTRY VGRQDPKKHL SETADETLEN NIVSVLTAGV

NSVAIK
Length:306
Mass (Da):34,398
Last modified:November 1, 1995 - 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:i9DDE8BD74890894D
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 varianti208K → Q in strain: NRRL Y-53. 1
Natural varianti239A → T in strain: NRRL Y-53. 1
Natural varianti262T → S in strain: NRRL Y-53. 1
Natural varianti280 – 281LS → IF in strain: NRRL Y-53. 2

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
X79561 Genomic DNA Translation: CAA56098.1
AY152546 Genomic DNA Translation: AAN77865.1
D50617 Genomic DNA Translation: BAA09243.1
AY692755 Genomic DNA Translation: AAT92774.1
BK006940 Genomic DNA Translation: DAA12444.1

Protein sequence database of the Protein Information Resource

More...
PIRi
S56259

NCBI Reference Sequences

More...
RefSeqi
NP_116659.1, NM_001179969.1

Genome annotation databases

Ensembl fungal genome annotation project

More...
EnsemblFungii
YFR004W_mRNA; YFR004W; YFR004W

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
850554

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
sce:YFR004W

<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
X79561 Genomic DNA Translation: CAA56098.1
AY152546 Genomic DNA Translation: AAN77865.1
D50617 Genomic DNA Translation: BAA09243.1
AY692755 Genomic DNA Translation: AAT92774.1
BK006940 Genomic DNA Translation: DAA12444.1
PIRiS56259
RefSeqiNP_116659.1, NM_001179969.1

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
3J47electron microscopy-V230-298[»]
3JCKelectron microscopy3.50G1-306[»]
3JCOelectron microscopy4.80V1-306[»]
3JCPelectron microscopy4.60V1-306[»]
4CR2electron microscopy7.70V1-306[»]
4CR3electron microscopy9.30V1-306[»]
4CR4electron microscopy8.80V1-306[»]
4O8XX-ray1.99B2-239[»]
4O8YX-ray1.95B2-239[»]
4OCLX-ray2.40B/E1-220[»]
4OCMX-ray1.99B/E1-220[»]
4OCNX-ray2.25B/E1-220[»]
4OWPX-ray2.35B2-229[»]
5A5Belectron microscopy9.50V1-306[»]
5MPBelectron microscopy7.80V1-306[»]
5MPCelectron microscopy7.70V1-306[»]
5MPDelectron microscopy4.10V1-306[»]
5MPEelectron microscopy4.50V1-306[»]
5U4PX-ray2.50B2-219[»]
5W83X-ray1.55B1-222[»]
5WVIelectron microscopy6.30V1-306[»]
5WVKelectron microscopy4.20V1-306[»]
6EF3electron microscopy4.17r1-306[»]
6FVTelectron microscopy4.10V18-306[»]
6FVUelectron microscopy4.50V18-306[»]
6FVVelectron microscopy5.40V18-306[»]
6FVWelectron microscopy4.50V18-306[»]
6FVXelectron microscopy4.90V18-306[»]
6FVYelectron microscopy6.10V18-306[»]
6J2Celectron microscopy7.00V1-306[»]
6J2Nelectron microscopy7.50V1-306[»]
6J2Qelectron microscopy3.80V1-306[»]
6J2Xelectron microscopy3.80V1-306[»]
6J30electron microscopy4.50V1-306[»]
SMRiP43588
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGridi31152, 1226 interactors
ComplexPortaliCPX-2262 26S Proteasome complex
DIPiDIP-1573N
IntActiP43588, 37 interactors
MINTiP43588
STRINGi4932.YFR004W

Protein family/group databases

MEROPSiM67.001

PTM databases

iPTMnetiP43588

Proteomic databases

MaxQBiP43588
PaxDbiP43588
PRIDEiP43588

Protocols and materials databases

ABCD curated depository of sequenced antibodies

More...
ABCDi
P43588

Genome annotation databases

EnsemblFungiiYFR004W_mRNA; YFR004W; YFR004W
GeneIDi850554
KEGGisce:YFR004W

Organism-specific databases

EuPathDBiFungiDB:YFR004W
SGDiS000001900 RPN11

Phylogenomic databases

HOGENOMiHOG000183690
InParanoidiP43588
KOiK03030
OMAiVFQTRMM

Enzyme and pathway databases

BioCyciYEAST:G3O-30457-MONOMER
ReactomeiR-SCE-1236978 Cross-presentation of soluble exogenous antigens (endosomes)
R-SCE-5668541 TNFR2 non-canonical NF-kB pathway
R-SCE-5689603 UCH proteinases
R-SCE-5689880 Ub-specific processing proteases
R-SCE-6798695 Neutrophil degranulation

Miscellaneous databases

Protein Ontology

More...
PROi
PR:P43588

Family and domain databases

InterProiView protein in InterPro
IPR000555 JAMM/MPN+_dom
IPR037518 MPN
IPR035299 PSMD14
IPR024969 Rpn11/EIF3F_C
PANTHERiPTHR10410:SF22 PTHR10410:SF22, 1 hit
PfamiView protein in Pfam
PF01398 JAB, 1 hit
PF13012 MitMem_reg, 1 hit
SMARTiView protein in SMART
SM00232 JAB_MPN, 1 hit
PROSITEiView protein in PROSITE
PS50249 MPN, 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 nameiRPN11_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: P43588
Secondary accession number(s): D6VTN4, Q8J0T5
<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, 1995
Last sequence update: November 1, 1995
Last modified: November 13, 2019
This is version 182 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, Complete proteome, Direct protein sequencing, Reference proteome

Documents

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