<p>Provides any useful information about the protein, mostly biological knowledge.</p><p><a href='../manual/function_section' target='_top'>More...</a></p>Functionⁱ

<p>Describes the catalytic activity of an enzyme, i.e. the chemical reaction it catalyzes. This information usually correlates with the presence of an EC (Enzyme Commission) number in the ‘Names and taxonomy’ section.</p><p><a href='../manual/catalytic_activity' target='_top'>More...</a></p>Catalytic activityⁱ

<p>Describes an enzyme regulatory mechanism and reports the components which regulate (by activation or inhibition) the reaction.</p><p><a href='../manual/enzyme_regulation' target='_top'>More...</a></p>Enzyme regulationⁱ

Sites

Feature key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
<p>Is used for enzymes and indicates the residues directly involved in catalysis.</p><p><a href='../manual/act_site' target='_top'>More...</a></p>Active sitei	571 – 571	1	Nucleophile
<p>Is used for enzymes and indicates the residues directly involved in catalysis.</p><p><a href='../manual/act_site' target='_top'>More...</a></p>Active sitei	880 – 880	1	Proton acceptorPROSITE-ProRule annotation <p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More…</a></p> Manual assertion according to rulesi PROSITE-ProRule:PRU10092 PROSITE-ProRule:PRU10093

<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><p><a href='../manual/gene_ontology' target='_top'>More...</a></p>GO - Molecular functionⁱ

1. ubiquitin-specific protease activity Source: SGD

   <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayⁱ

   • 19410548
   • 8247125

<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><p><a href='../manual/gene_ontology' target='_top'>More...</a></p>GO - Biological processⁱ

1. endocytosis Source: SGD

   <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypeⁱ

   • 9119204

2. free ubiquitin chain depolymerization Source: SGD

   <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayⁱ

   • 19410548

3. intralumenal vesicle formation Source: SGD

   <p>Inferred from Genetic Interaction</p> <p>Used to describe “traditional” genetic interactions such as suppressors and synthetic lethals as well as other techniques such as functional complementation, rescue experiments, or inferences about a gene drawn from the phenotype of a mutation in a different gene.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#igi">GO evidence code guide</a></p> Inferred from genetic interactionⁱ

   • 23444383

4. regulation of DNA replication Source: SGD

   <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypeⁱ

   • 8657109

5. ubiquitin-dependent protein catabolic process Source: SGD

   <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypeⁱ

   • 17145966

6. ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway Source: SGD

   <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypeⁱ

   • 17376168

7. ubiquitin homeostasis Source: SGD

   <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypeⁱ

   • 19410548

<p>UniProtKB Keywords constitute a <a target="_top" href="/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>Keywords - Molecular functionⁱ

<p>UniProtKB Keywords constitute a <a target="_top" href="/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>Keywords - Biological processⁱ

Enzyme and pathway databases

Protein family/group databases

<p>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><p><a href='../manual/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyⁱ

Organism-specific databases

<p>Provides information on the location and the topology of the mature protein in the cell.</p><p><a href='../manual/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationⁱ

<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><p><a href='../manual/gene_ontology' target='_top'>More...</a></p>GO - Cellular componentⁱ

1. endosome Source: SGD

   <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayⁱ

   • 17145966

2. late endosome membrane Source: UniProtKB-SubCell
3. proteasome complex Source: SGD

   <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactionⁱ

   • 10069815

<p>UniProtKB Keywords constitute a <a target="_top" href="/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>Keywords - Cellular componentⁱ

<p>Provides information on the disease(s) and phenotype(s) associated with the deficiency of a protein.</p><p><a href='../manual/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechⁱ

Mutagenesis

Feature key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
<p>Describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.</p><p><a href='../manual/mutagen' target='_top'>More...</a></p>Mutagenesisi	571 – 571	1	C → S or A: Impairs deubiquitination activity and protein sorting into the MVB pathway. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini Ref.27 "Dual mechanisms specify Doa4-mediated deubiquitination at multivesicular bodies." Richter C., West M., Odorizzi G. EMBO J. 26:2454-2464(2007) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH BRO1, MUTAGENESIS OF CYS-571; TYR-826; PRO-827 AND LEU-829. Ref.29 "Evidence for a direct role of the Doa4 deubiquitinating enzyme in protein sorting into the MVB pathway." Nikko E., Andre B. Traffic 8:566-581(2007) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, MUTAGENESIS OF CYS-571.
<p>Describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.</p><p><a href='../manual/mutagen' target='_top'>More...</a></p>Mutagenesisi	826 – 826	1	Y → A: Impairs deubiquitination activity and binding to BRO1; when associated with A-827 and A-829. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini Ref.27 "Dual mechanisms specify Doa4-mediated deubiquitination at multivesicular bodies." Richter C., West M., Odorizzi G. EMBO J. 26:2454-2464(2007) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH BRO1, MUTAGENESIS OF CYS-571; TYR-826; PRO-827 AND LEU-829.
<p>Describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.</p><p><a href='../manual/mutagen' target='_top'>More...</a></p>Mutagenesisi	827 – 827	1	P → A: Impairs deubiquitination activity and binding to BRO1; when associated with A-826 and A-829. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini Ref.27 "Dual mechanisms specify Doa4-mediated deubiquitination at multivesicular bodies." Richter C., West M., Odorizzi G. EMBO J. 26:2454-2464(2007) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH BRO1, MUTAGENESIS OF CYS-571; TYR-826; PRO-827 AND LEU-829.
<p>Describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.</p><p><a href='../manual/mutagen' target='_top'>More...</a></p>Mutagenesisi	829 – 829	1	L → A: Impairs deubiquitination activity and binding to BRO1; when associated with A-826 and A-827. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini Ref.27 "Dual mechanisms specify Doa4-mediated deubiquitination at multivesicular bodies." Richter C., West M., Odorizzi G. EMBO J. 26:2454-2464(2007) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH BRO1, MUTAGENESIS OF CYS-571; TYR-826; PRO-827 AND LEU-829.

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

Molecule processing

Feature key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
<p>Describes the extent of a polypeptide chain in the mature protein following processing.</p><p><a href='../manual/chain' target='_top'>More...</a></p>Chaini	1 – 926	926	Ubiquitin carboxyl-terminal hydrolase 4		PRO_0000080589	Add BLAST

Amino acid modifications

Feature key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
<p>Specifies the position and type of each modified residue excluding <a href="/manual/lipid">lipids</a>, <a href="/manual/carbohyd">glycans</a> and <a href="/manual/crosslnk">protein cross-links</a>.</p><p><a href='../manual/mod_res' target='_top'>More...</a></p>Modified residuei	443 – 443	1	Phosphoserine1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini Ref.30 "A multidimensional chromatography technology for in-depth phosphoproteome analysis." Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H. Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-443, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

<p>UniProtKB Keywords constitute a <a target="_top" href="/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>Keywords - PTMⁱ

Proteomic databases

<p>Provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.</p><p><a href='../manual/expression_section' target='_top'>More...</a></p>Expressionⁱ

Gene expression databases

<p>Provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.</p><p><a href='../manual/interaction_section' target='_top'>More...</a></p>Interactionⁱ

<p>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 ‘Function’ section).</p><p><a href='../manual/subunit_structure' target='_top'>More...</a></p>Subunit structureⁱ

<p>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><p><a href='../manual/binary_interactions' target='_top'>More...</a></p>Binary interactionsⁱ

Protein-protein interaction databases

<p>Provides information on the tertiary structure of a protein.</p><p><a href='../manual/structure_section' target='_top'>More...</a></p>Structureⁱ

3D structure databases

<p>Provides information on sequence similarities with other proteins and the domain(s) present in a protein.</p><p><a href='../manual/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsⁱ

Domains and Repeats

Feature key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
<p>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><p><a href='../manual/domain' target='_top'>More...</a></p>Domaini	205 – 328	124	RhodanesePROSITE-ProRule annotation <p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More…</a></p> Manual assertion according to rulesi PROSITE-ProRule:PRU00173			Add BLAST
<p>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><p><a href='../manual/domain' target='_top'>More...</a></p>Domaini	562 – 923	362	USP			Add BLAST

Compositional bias

Feature key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
<p>Describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.</p><p><a href='../manual/compbias' target='_top'>More...</a></p>Compositional biasi	386 – 392	7	Poly-Gln

<p>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><p><a href='../manual/domain_cc' target='_top'>More...</a></p>Domainⁱ

<p>Provides information about the sequence similarity with other proteins.</p><p><a href='../manual/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesⁱ

Phylogenomic databases

Family and domain databases

<p>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 length and molecular weight.</p><p><a href='../manual/sequences_section' target='_top'>More...</a></p>Sequenceⁱ

<p>Indicates if the canonical sequence displayed by default in the entry is complete or not.</p><p><a href='../manual/sequence_status' target='_top'>More...</a></p>Sequence statusⁱ: Complete.

        10         20         30         40         50
MEQNIISTIR DECIRHRSKY LTIAQLTAIA EAKINEFIIT GKAKDQDLSS 
        60         70         80         90        100
LLDKCIDILS IYKKNSKDIK NIISCKNKGA MISSNSVMII QLNYVYYKVI 
       110        120        130        140        150
HIIVTTNIPH LSEFAKIKLH KSTSDEGNGN NNNNEFQLMN IYNTLLETLL 
       160        170        180        190        200
KDENIAKIKS FIKSSIKQTK LNHEQEECNL MRTGSYITSN QLNSLISSSA 
       210        220        230        240        250
NSASSQMEIL LIDIRSRLEF NKSHIDTKNI ICLEPISFKM SYSDHDLEKK 
       260        270        280        290        300
SLITSPNSEI KMFQSRNLFK FIILYTDANE YNVKQQSVLL DILVNHSFEK 
       310        320        330        340        350
PISDDFTKIF ILESGFPGWL KSNYGRQVSS SFPSNNNIKD DSVYINGNTS 
       360        370        380        390        400
GLSLQHLPKM SPSIRHSMDD SMKEMLVAPT PLNHLQQQQQ QQSDNDHVLK 
       410        420        430        440        450
RSSSFKKLFS NYTSPNPKNS NSNLYSISSL SISSSPSPLP LHSPDPVKGN 
       460        470        480        490        500
SLPINYPETP HLWKNSETDF MTNQREQLNH NSFAHIAPIN TKAITSPSRT 
       510        520        530        540        550
ATPKLQRFPQ TISMNLNMNS NGHSSATSTI QPSCLSLSNN DSLDHTDVTP 
       560        570        580        590        600
TSSHNYDLDF AVGLENLGNS CYMNCIIQCI LGTHELTQIF LDDSYAKHIN 
       610        620        630        640        650
INSKLGSKGI LAKYFARLVH MMYKEQVDGS KKISISPIKF KLACGSVNSL 
       660        670        680        690        700
FKTASQQDCQ EFCQFLLDGL HEDLNQCGSN PPLKELSQEA EARREKLSLR 
       710        720        730        740        750
IASSIEWERF LTTDFSVIVD LFQGQYASRL KCKVCSHTST TYQPFTVLSI 
       760        770        780        790        800
PIPKKNSRNN ITIEDCFREF TKCENLEVDE QWLCPHCEKR QPSTKQLTIT 
       810        820        830        840        850
RLPRNLIVHL KRFDNLLNKN NDFVIYPFLL DLTPFWANDF DGVFPPGVND 
       860        870        880        890        900
DELPIRGQIP PFKYELYGVA CHFGTLYGGH YTAYVKKGLK KGWLYFDDTK 
       910        920 
YKPVKNKADA INSNAYVLFY HRVYGV                       

Experimental Info

Feature key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
<p>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><p><a href='../manual/conflict' target='_top'>More...</a></p>Sequence conflicti	327 – 327	1	Q → K in AAA35105. 1 Publication Ref.2 Latterich M. Submitted (JAN-1993) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Curated
<p>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><p><a href='../manual/conflict' target='_top'>More...</a></p>Sequence conflicti	345 – 345	1	I → F in AAA35105. 1 Publication Ref.2 Latterich M. Submitted (JAN-1993) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Curated
<p>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><p><a href='../manual/conflict' target='_top'>More...</a></p>Sequence conflicti	375 – 378	4	MLVA → TASW in AAA35105. 1 Publication Ref.2 Latterich M. Submitted (JAN-1993) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Curated
<p>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><p><a href='../manual/conflict' target='_top'>More...</a></p>Sequence conflicti	383 – 383	1	N → I in AAA35105. 1 Publication Ref.2 Latterich M. Submitted (JAN-1993) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Curated
<p>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><p><a href='../manual/conflict' target='_top'>More...</a></p>Sequence conflicti	407 – 407	1	K → T in AAA35105. 1 Publication Ref.2 Latterich M. Submitted (JAN-1993) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Curated
<p>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><p><a href='../manual/conflict' target='_top'>More...</a></p>Sequence conflicti	543 – 570	28	LDHTD…NLGNS → FRSYEMLHQLLLIIMTLISR LVWENLEIP in AAA35105. 1 Publication Ref.2 Latterich M. Submitted (JAN-1993) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Curated			Add BLAST
<p>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><p><a href='../manual/conflict' target='_top'>More...</a></p>Sequence conflicti	580 – 580	1	I → T in AAA35105. 1 Publication Ref.2 Latterich M. Submitted (JAN-1993) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Curated
<p>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><p><a href='../manual/conflict' target='_top'>More...</a></p>Sequence conflicti	836 – 836	1	W → G in AAA35105. 1 Publication Ref.2 Latterich M. Submitted (JAN-1993) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Curated
<p>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><p><a href='../manual/conflict' target='_top'>More...</a></p>Sequence conflicti	897 – 897	1	D → N in AAA35105. 1 Publication Ref.2 Latterich M. Submitted (JAN-1993) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Curated

Sequence databases

Genome annotation databases

<p>Is used to point to information related to entries and found in data collections other than UniProtKB.</p><p><a href='../manual/cross_references_section' target='_top'>More...</a></p> Cross-referencesⁱ

Sequence databases

3D structure databases

Protein-protein interaction databases

Protein family/group databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Gene expression databases

Family and domain databases

<p>Contains the literature citations that are the sources of data used to annotate the entry. Each reference is numbered and contains several subsections allowing a precise description of a given citation.</p><p><a href='../manual/publications_section' target='_top'>More...</a></p>Publicationsⁱ

1. "The yeast DOA4 gene encodes a deubiquitinating enzyme related to a product of the human tre-2 oncogene."
   Papa F.R., Hochstrasser M.
   Nature 366:313-319(1993) [PubMed] [Europe PMC] [Abstract]
   Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
2. Latterich M.
   Submitted (JAN-1993) to the EMBL/GenBank/DDBJ databases
   Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
3. "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."
   Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T.

   , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.
   Nature 387:75-78(1997) [PubMed] [Europe PMC] [Abstract]
   Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
   Strain: ATCC 204508 / S288c.
   
4. "The reference genome sequence of Saccharomyces cerevisiae: Then and now."
   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.
   G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
   Cited for: GENOME REANNOTATION.
   Strain: ATCC 204508 / S288c.
   
5. "Nucleotide sequence analysis of a 32,500 bp region of the right arm of Saccharomyces cerevisiae chromosome IV."
   Brandt P., Ramlow S., Otto B., Bloecker H.
   Yeast 12:85-90(1996) [PubMed] [Europe PMC] [Abstract]
   Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 36-926.
   Strain: ATCC 204508 / S288c.
   
6. "Coordinating DNA replication to produce one copy of the genome requires genes that act in ubiquitin metabolism."
   Singer J.D., Manning B.M., Formosa T.
   Mol. Cell. Biol. 16:1356-1366(1996) [PubMed] [Europe PMC] [Abstract]
   Cited for: FUNCTION.
7. "Ubiquitin lys63 is involved in ubiquitination of a yeast plasma membrane protein."
   Galan J.-M., Haguenauer-Tsapis R.
   EMBO J. 16:5847-5854(1997) [PubMed] [Europe PMC] [Abstract]
   Cited for: FUNCTION.
8. "Catabolite inactivation of the yeast maltose transporter requires ubiquitin-ligase npi1/rsp5 and ubiquitin-hydrolase npi2/doa4."
   Lucero P., Lagunas R.
   FEMS Microbiol. Lett. 147:273-277(1997) [PubMed] [Europe PMC] [Abstract]
   Cited for: FUNCTION.
9. "Role for the ubiquitin-proteasome system in the vacuolar degradation of Ste6p, the a-factor transporter in Saccharomyces cerevisiae."
   Loayza D., Michaelis S.
   Mol. Cell. Biol. 18:779-789(1998) [PubMed] [Europe PMC] [Abstract]
   Cited for: FUNCTION.
10. "NH4+-induced down-regulation of the Saccharomyces cerevisiae Gap1p permease involves its ubiquitination with lysine-63-linked chains."
    Springael J.-Y., Galan J.-M., Haguenauer-Tsapis R., Andre B.
    J. Cell Sci. 112:1375-1383(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
11. "Interaction of the Doa4 deubiquitinating enzyme with the yeast 26S proteasome."
    Papa F.R., Amerik A.Y., Hochstrasser M.
    Mol. Biol. Cell 10:741-756(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: ASSOCIATION WITH THE 26S PROTEASOME.
12. "The Doa4 deubiquitinating enzyme is required for ubiquitin homeostasis in yeast."
    Swaminathan S., Amerik A.Y., Hochstrasser M.
    Mol. Biol. Cell 10:2583-2594(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
13. "Oxidative stress-induced destruction of the yeast C-type cyclin Ume3p requires phosphatidylinositol-specific phospholipase C and the 26S proteasome."
    Cooper K.F., Mallory M.J., Strich R.
    Mol. Cell. Biol. 19:3338-3348(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
14. "The Doa4 deubiquitinating enzyme is functionally linked to the vacuolar protein-sorting and endocytic pathways."
    Amerik A.Y., Nowak J., Swaminathan S., Hochstrasser M.
    Mol. Biol. Cell 11:3365-3380(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
15. "Glucose-induced monoubiquitination of the Saccharomyces cerevisiae galactose transporter is sufficient to signal its internalization."
    Horak J., Wolf D.H.
    J. Bacteriol. 183:3083-3088(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
16. "Uptake of the ATP-binding cassette (ABC) transporter Ste6 into the yeast vacuole is blocked in the doa4 Mutant."
    Losko S., Kopp F., Kranz A., Koelling R.
    Mol. Biol. Cell 12:1047-1059(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
17. "Deubiquitination step in the endocytic pathway of yeast plasma membrane proteins: crucial role of Doa4p ubiquitin isopeptidase."
    Dupre S., Haguenauer-Tsapis R.
    Mol. Cell. Biol. 21:4482-4494(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
18. "Permease recycling and ubiquitination status reveal a particular role for Bro1 in the multivesicular body pathway."
    Nikko E., Marini A.-M., Andre B.
    J. Biol. Chem. 278:50732-50743(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
19. "Global analysis of protein localization in budding yeast."
    Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K.
    Nature 425:686-691(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
20. "Global analysis of protein expression in yeast."
    Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
    Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
21. "The deubiquitinating enzyme Doa4p protects cells from DNA topoisomerase I poisons."
    Fiorani P., Reid R.J.D., Schepis A., Jacquiau H.R., Guo H., Thimmaiah P., Benedetti P., Bjornsti M.-A.
    J. Biol. Chem. 279:21271-21281(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
22. "Bro1 coordinates deubiquitination in the multivesicular body pathway by recruiting Doa4 to endosomes."
    Luhtala N., Odorizzi G.
    J. Cell Biol. 166:717-729(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH BRO1.
23. "Protein-protein interactions of ESCRT complexes in the yeast Saccharomyces cerevisiae."
    Bowers K., Lottridge J., Helliwell S.B., Goldthwaite L.M., Luzio J.P., Stevens T.H.
    Traffic 5:194-210(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH VPS32.
24. "Did2 coordinates Vps4-mediated dissociation of ESCRT-III from endosomes."
    Nickerson D.P., West M., Odorizzi G.
    J. Cell Biol. 175:715-720(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
25. "A conserved late endosome-targeting signal required for Doa4 deubiquitylating enzyme function."
    Amerik A.Y., Sindhi N., Hochstrasser M.
    J. Cell Biol. 175:825-835(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, DOMAIN.
26. "Amino acids regulate retrieval of the yeast general amino acid permease from the vacuolar targeting pathway."
    Rubio-Texeira M., Kaiser C.A.
    Mol. Biol. Cell 17:3031-3050(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
27. "Dual mechanisms specify Doa4-mediated deubiquitination at multivesicular bodies."
    Richter C., West M., Odorizzi G.
    EMBO J. 26:2454-2464(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH BRO1, MUTAGENESIS OF CYS-571; TYR-826; PRO-827 AND LEU-829.
28. "Split-ubiquitin two-hybrid assay to analyze protein-protein interactions at the endosome: application to Saccharomyces cerevisiae Bro1 interacting with ESCRT complexes, the Doa4 ubiquitin hydrolase, and the Rsp5 ubiquitin ligase."
    Nikko E., Andre B.
    Eukaryot. Cell 6:1266-1277(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH BRO1, SUBCELLULAR LOCATION.
29. "Evidence for a direct role of the Doa4 deubiquitinating enzyme in protein sorting into the MVB pathway."
    Nikko E., Andre B.
    Traffic 8:566-581(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF CYS-571.
30. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
    Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
    Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-443, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
31. "An inhibitor of a deubiquitinating enzyme regulates ubiquitin homeostasis."
    Kimura Y., Yashiroda H., Kudo T., Koitabashi S., Murata S., Kakizuka A., Tanaka K.
    Cell 137:549-559(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME REGULATION, INTERACTION WITH RFU1.

<p>Provides general information on the entry.</p><p><a href='../manual/entry_information_section' target='_top'>More...</a></p>Entry informationⁱ

<p>Contains any relevant information that doesn’t fit in any other defined sections</p><p><a href='../manual/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousⁱ

Miscellaneous

<p>UniProtKB Keywords constitute a <a target="_top" href="/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>Keywords - Technical termⁱ

Documents

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

External Data

<p>Provides links to the UniProt Reference Clusters (<a href="/help/uniref">UniRef</a>). UniRef consists of clusters for UniProtKB sequences (including isoforms) and selected UniParc sequences, in order to obtain complete coverage of the sequence space at resolutions of 100%, 90% and 50% identity.</p><p><a href='../manual/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsⁱ