Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
The new UniProt website is here! Take me to UniProt BETA

UniProtKB - P53874 (UBP10_YEAST)

Entry version 174 (29 Sep 2021)
Sequence version 2 (21 Sep 2011)
Previous versions | rss
Add a publicationFeedback
Protein

Ubiquitin carboxyl-terminal hydrolase 10

Gene

UBP10

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

Deubiquitinating enzyme involved in telomere and HM loci silencing, which is the repression of chromatin structure which leads to a stop in the transcription of nearby genes (PubMed:9755194, PubMed:10490600, PubMed:14623890).

Targets histone H2B for deubiquitination, thus helping to localize SIR2 to the telomere (PubMed:15721261, PubMed:17028327, PubMed:22056669).

At silent chromatin, including telomeres and the rDNA locus, not only maintains low H2B 'Lys-123' ubiquitination (H2BK123Ub), but also low H3 'Lys-4' and 'Lys-79' methylation (H3K4me and H3K79me, respectively) (PubMed:15721261, PubMed:15988024).

Controls the proliferating-cell nuclear antigen PCNA/POL30 deubiquitination which is crucial for keeping TLS polymerases in check as well as for down-regulating the error-free bypass (PubMed:22829782).

Deubiquitinates and stabilizes RPA190, the largest subunit of RNA polymerase I, to achieve optimal levels of ribosomes and cell growth (PubMed:22902402).

Protects also nutrient transporters such as GAP1 from ubiquitin-dependent endocytosis (PubMed:11352638).

10 Publications

<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).1 Publication 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 is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei371NucleophilePROSITE-ProRule annotation1
Active sitei691Proton acceptorPROSITE-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

  • cysteine-type endopeptidase activity Source: GO_Central
  • thiol-dependent deubiquitinase 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 functionHydrolase, Protease, Thiol protease
Biological processUbl conjugation pathway

Protein family/group databases

MEROPS protease database

More...MEROPSi		C19.088

<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 10 (EC:3.4.19.121 Publication)
Alternative name(s):
Deubiquitinating enzyme 10
Disrupter of telomere silencing protein 41 Publication
Ubiquitin thioesterase 10
Ubiquitin-specific-processing protease 10
<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:UBP10
Synonyms:DOT41 Publication
Ordered Locus Names:YNL186W
ORF Names:N1619
<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 lineageiEukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces ›
<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 XIV

Organism-specific databases

Saccharomyces Genome Database

More...SGDi		S000005130, UBP10

Eukaryotic Pathogen, Vector and Host Database Resources

More...VEuPathDBi		FungiDB:YNL186W

<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

Chromosome, Nucleus, Telomere

<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

<p>This subsection of the 'Pathology and Biotech' section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

Exhibits reduced silencing and a corresponding decrease in the level of SIR4 (PubMed:10490600). Reduces also the level of the low-affinity, high-capacity transporter of amino acids GAP1 (PubMed:11352638). Leads to alterations in expression of subtelomeric genes together with a broad change in the whole transcriptional profile, closely parallel to that induced by oxidative stress (PubMed:14623890). Results also in extrachromosomal rDNA circles (ERCs) accumulation (PubMed:17028327). Accumulates also mono- and di-ubiquitinated PCNA/POL30 in response to DNA damage and replicative stress (PubMed:22829782). Leads to reduced pre-rRNAs, mature rRNAs, and translating ribosomes (PubMed:22902402).6 Publications

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>Mutagenesisi371C → A or S: Abolishes deubiquitinating activity. 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 or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000805951 – 792Ubiquitin carboxyl-terminal hydrolase 10Add BLAST792

Proteomic databases

MaxQB - The MaxQuant DataBase

More...MaxQBi		P53874

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

More...PaxDbi		P53874

PRoteomics IDEntifications database

More...PRIDEi		P53874

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P53874

<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

Interacts with SIR4 (PubMed:10490600, PubMed:26149687).

Interacts with the proliferating-cell nuclear antigen PCNA/POL30 (PubMed:22829782).

Interacts with DHR2 and UTP22 (PubMed:22902402, PubMed:26149687).

3 Publications

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		35647, 235 interactors

Database of interacting proteins

More...DIPi		DIP-6664N

Protein interaction database and analysis system

More...IntActi		P53874, 22 interactors

Molecular INTeraction database

More...MINTi		P53874

STRING: functional protein association networks

More...STRINGi		4932.YNL186W

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...RNActi		P53874, 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

3D structure databases

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

More...SMRi		P53874

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>Domaini362 – 733USPPROSITE-ProRule annotationAdd BLAST372

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni2 – 27DHR2-binding module1 PublicationAdd BLAST26
Regioni64 – 87DisorderedSequence analysisAdd BLAST24
Regioni103 – 320DisorderedSequence analysisAdd BLAST218
Regioni109 – 145SIR4-binding module1 PublicationAdd BLAST37
Regioni167 – 208UTP22-binding module1 PublicationAdd BLAST42
Regioni526 – 563DisorderedSequence analysisAdd BLAST38
Regioni749 – 792DisorderedSequence analysisAdd BLAST44

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes the position of regions of compositional bias within the protein and the particular type of amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi115 – 129Polar residuesSequence analysisAdd BLAST15
Compositional biasi130 – 172Basic and acidic residuesSequence analysisAdd BLAST43
Compositional biasi173 – 192Acidic residuesSequence analysisAdd BLAST20
Compositional biasi208 – 225Basic and acidic residuesSequence analysisAdd BLAST18
Compositional biasi226 – 253Acidic residuesSequence analysisAdd BLAST28
Compositional biasi254 – 271Basic and acidic residuesSequence analysisAdd BLAST18
Compositional biasi272 – 295Polar residuesSequence analysisAdd BLAST24
Compositional biasi296 – 316Basic and acidic residuesSequence analysisAdd BLAST21
Compositional biasi531 – 563Polar residuesSequence analysisAdd BLAST33
Compositional biasi749 – 772Polar residuesSequence analysisAdd BLAST24
Compositional biasi773 – 792Basic residuesSequence analysisAdd BLAST20

<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

Residues 2-27 within the N-terminal intrinsically disordered regions (IDR) constitute the binding module for DHR2 which is required to coordinate the UBP10-DHR2 interaction (PubMed:26149687).1 Publication
Residues 109-145 within the N-terminal intrinsically disordered regions (IDR) constitute the binding module for SIR4 which required to coordinate the UBP10-SIR4 interaction, but also to direct UBP10's functional role in telomere chromatin silencing (PubMed:26149687).1 Publication
Residues 167-208 within the N-terminal intrinsically disordered regions (IDR) constitute the binding module for UTP22 which is required to coordinate the UBP10-UTP22 interaction (PubMed:26149687).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 C19 family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG1870, Eukaryota

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_016013_1_1_1

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P53874

Identification of Orthologs from Complete Genome Data

More...OMAi		HKTTNAL

Family and domain databases

Database of protein disorder

More...DisProti		DP01189

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR038765, Papain-like_cys_pep_sf
IPR001394, Peptidase_C19_UCH
IPR018200, USP_CS
IPR028889, USP_dom

Pfam protein domain database

More...Pfami		View protein in Pfam
PF00443, UCH, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF54001, SSF54001, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS00973, USP_2, 1 hit
PS50235, USP_3, 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.

P53874-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MTTQESIKPL VDRILSNPLQ FNAAMISNKS NNNDTSAAPE NSSYIVIGKQ 
        60         70         80         90        100
HNNNSNSTAI AATAESKQIK ENNLIDRPNG KKTNTVPKSM AEALLLYTSK 
       110        120        130        140        150
NDKDAADATG AKKSAELSTE LSTEPPSSSS EDDKVGKEEE EEGEIFHEAR 
       160        170        180        190        200
DYVEPRKASL KERDNADKGD GEDIGEDIGE DIGEDIGEDI GEDIGENLGS 
       210        220        230        240        250
PLATIDDSSN ENEKEKRKEL STSISSDDEI EDDEDEDDMD YDSSAMEKEL 
       260        270        280        290        300
PEEEENDSSS KISEGEKKSL YQDLMENSTV EVNRYEPVNN TKENGNRNPK 
       310        320        330        340        350
GEEEEEEEEE LKHKSRSITP PVTISNLSNF YQFNENINDR GSLNSTRIVK 
       360        370        380        390        400
NWGDKFTNLK PRGLLNHGVT CYTNAAVQAM LHIPSIQHYL FDILMGKYDS 
       410        420        430        440        450
TISKNSVSYT LAETSKKMWL PVSKNPRKNV SASYINPKHL ISRLDDINCM 
       460        470        480        490        500
MSEWQQEDSH EYFMSLMSRL QEDSVPKGHK LIESIIYDIF GGLLKQIVTC 
       510        520        530        540        550
KSCGSISKTE QPFYDLSLHL KGKKKLDPNS DLSSDSINGT SATTSTTTSN 
       560        570        580        590        600
AATKPSLSSS SSVNLNNGSP FAAASDLSSA NRRFSIEKSI KDFFNPELIK 
       610        620        630        640        650
VDKEQKGYVC EKCHKTTNAV KHSSILRAPE TLLVHLKKFR FNGTSSSKMK 
       660        670        680        690        700
QAVSYPMFLD LTEYCESKEL PVKYQLLSVV VHEGRSLSSG HYIAHCKQPD 
       710        720        730        740        750
GSWATYDDEY INIISERDVL KEPNAYYLLY TRLTPKSVPL PLAKSAMATG 
       760        770        780        790 
NVTSKSKQEQ AVNEPNNRPL KINSKKNNRK KWKKNKKRKF TK
Length:792
Mass (Da):88,531
Last modified:September 21, 2011 - v2
<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:iAA2DE6DB0C560E37
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 conflicti310E → D in CAA96080 (PubMed:9169873).Curated1

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
Z71462 Genomic DNA Translation: CAA96080.1
BK006947 Genomic DNA Translation: DAA10367.2

Protein sequence database of the Protein Information Resource

More...PIRi		S63141

NCBI Reference Sequences

More...RefSeqi		NP_014213.2, NM_001183024.2

Genome annotation databases

Ensembl fungal genome annotation project

More...EnsemblFungii		YNL186W_mRNA; YNL186W; YNL186W

Database of genes from NCBI RefSeq genomes

More...GeneIDi		855535

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		sce:YNL186W

<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
Z71462 Genomic DNA Translation: CAA96080.1
BK006947 Genomic DNA Translation: DAA10367.2
PIRiS63141
RefSeqiNP_014213.2, NM_001183024.2

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
6RR0X-ray2.18H/I/J/K/L/M/N117-128[»]
SMRiP53874
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi35647, 235 interactors
DIPiDIP-6664N
IntActiP53874, 22 interactors
MINTiP53874
STRINGi4932.YNL186W

Protein family/group databases

MEROPSiC19.088

PTM databases

iPTMnetiP53874

Proteomic databases

MaxQBiP53874
PaxDbiP53874
PRIDEiP53874

Genome annotation databases

EnsemblFungiiYNL186W_mRNA; YNL186W; YNL186W
GeneIDi855535
KEGGisce:YNL186W

Organism-specific databases

SGDiS000005130, UBP10
VEuPathDBiFungiDB:YNL186W

Phylogenomic databases

eggNOGiKOG1870, Eukaryota
HOGENOMiCLU_016013_1_1_1
InParanoidiP53874
OMAiHKTTNAL

Miscellaneous databases

Protein Ontology

More...PROi		PR:P53874
RNActiP53874, protein

Family and domain databases

DisProtiDP01189
InterProiView protein in InterPro
IPR038765, Papain-like_cys_pep_sf
IPR001394, Peptidase_C19_UCH
IPR018200, USP_CS
IPR028889, USP_dom
PfamiView protein in Pfam
PF00443, UCH, 1 hit
SUPFAMiSSF54001, SSF54001, 1 hit
PROSITEiView protein in PROSITE
PS00973, USP_2, 1 hit
PS50235, USP_3, 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 nameiUBP10_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: P53874
Secondary accession number(s): D6W101
<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: October 1, 1996
Last sequence update: September 21, 2011
Last modified: September 29, 2021
This is version 174 of the entry and version 2 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 XIV
    Yeast (Saccharomyces cerevisiae) chromosome XIV: entries and gene names
  3. Peptidase families
    Classification of peptidase 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
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again