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P32571

- UBP4_YEAST

UniProt

P32571 - UBP4_YEAST

Protein

Ubiquitin carboxyl-terminal hydrolase 4

Gene

DOA4

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 150 (01 Oct 2014)
      Sequence version 2 (01 Feb 1994)
      Previous versions | rss
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    Functioni

    Ubiquitin thioesterase that acts at the late endosome/prevacuolar compartment to recover ubiquitin from ubiquitinated membrane proteins en route to the vacuole. Removes also ubiquitin from soluble proteins targeted to proteasomes. Is essential to maintain a normal level of free ubiquitin. Involved in the ammonium-induced down-regulation of the GAP1 permease and the UME3 destruction in response to oxidative stress. Has a role in the RAD9 checkpoint response to TOP1 poisons. Required for promoting coordination of DNA replication and avoids DNA overreplication.19 Publications

    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).

    Enzyme regulationi

    RFU1 is an inhibitor of deubiquitination activity.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei571 – 5711Nucleophile
    Active sitei880 – 8801Proton acceptorPROSITE-ProRule annotation

    GO - Molecular functioni

    1. protein binding Source: IntAct
    2. ubiquitin-specific protease activity Source: SGD

    GO - Biological processi

    1. endocytosis Source: SGD
    2. free ubiquitin chain depolymerization Source: SGD
    3. intralumenal vesicle formation Source: SGD
    4. regulation of DNA replication Source: SGD
    5. ubiquitin-dependent protein catabolic process Source: SGD
    6. ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway Source: SGD
    7. ubiquitin homeostasis Source: SGD

    Keywords - Molecular functioni

    Hydrolase, Protease, Thiol protease

    Keywords - Biological processi

    Ubl conjugation pathway

    Enzyme and pathway databases

    BioCyciYEAST:G3O-29676-MONOMER.

    Protein family/group databases

    MEROPSiC19.005.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ubiquitin carboxyl-terminal hydrolase 4 (EC:3.4.19.12)
    Alternative name(s):
    Deubiquitinating enzyme 4
    Ubiquitin thioesterase 4
    Ubiquitin-specific-processing protease 4
    Vacuole biogenesis protein SSV7
    Gene namesi
    Name:DOA4
    Synonyms:DOS1, MUT4, NPI2, SSV7, UBP4
    Ordered Locus Names:YDR069C
    ORF Names:D4270, YD8554.02C, YD9609.23C
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome IV

    Organism-specific databases

    CYGDiYDR069c.
    SGDiS000002476. DOA4.

    Subcellular locationi

    Cytoplasm. Late endosome membrane; Peripheral membrane protein
    Note: Recruited to the late endosome by BRO1.

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Cytoplasm, Endosome, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi571 – 5711C → S or A: Impairs deubiquitination activity and protein sorting into the MVB pathway. 2 Publications
    Mutagenesisi826 – 8261Y → A: Impairs deubiquitination activity and binding to BRO1; when associated with A-827 and A-829. 1 Publication
    Mutagenesisi827 – 8271P → A: Impairs deubiquitination activity and binding to BRO1; when associated with A-826 and A-829. 1 Publication
    Mutagenesisi829 – 8291L → A: Impairs deubiquitination activity and binding to BRO1; when associated with A-826 and A-827. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 926926Ubiquitin carboxyl-terminal hydrolase 4PRO_0000080589Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei443 – 4431Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP32571.
    PaxDbiP32571.

    Expressioni

    Gene expression databases

    GenevestigatoriP32571.

    Interactioni

    Subunit structurei

    Interacts with BRO1, RFU1 and VPS32. Associates with the 26S proteasome.5 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    BRO1P4858215EBI-19840,EBI-3768
    RFU1Q080032EBI-19840,EBI-2353109

    Protein-protein interaction databases

    BioGridi32124. 120 interactions.
    DIPiDIP-5298N.
    IntActiP32571. 27 interactions.
    MINTiMINT-550253.
    STRINGi4932.YDR069C.

    Structurei

    3D structure databases

    ProteinModelPortaliP32571.
    SMRiP32571. Positions 563-922.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini205 – 328124RhodanesePROSITE-ProRule annotationAdd
    BLAST
    Domaini562 – 923362USPAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi386 – 3927Poly-Gln

    Domaini

    Residues 1-208 are essential for the localization to the late endosome and constitute a late endosome localization (LEL) domain.1 Publication

    Sequence similaritiesi

    Belongs to the peptidase C19 family.Curated
    Contains 1 rhodanese domain.PROSITE-ProRule annotation
    Contains 1 USP domain.Curated

    Phylogenomic databases

    eggNOGiCOG5533.
    GeneTreeiENSGT00750000117363.
    HOGENOMiHOG000248489.
    KOiK11839.
    OMAiEDLNQCG.
    OrthoDBiEOG7R2BSX.

    Family and domain databases

    Gene3Di3.40.250.10. 1 hit.
    InterProiIPR018200. Pept_C19ubi-hydrolase_C_CS.
    IPR001394. Peptidase_C19_UCH.
    IPR001763. Rhodanese-like_dom.
    IPR028889. UCH/PAN2.
    [Graphical view]
    PfamiPF00581. Rhodanese. 1 hit.
    PF00443. UCH. 1 hit.
    [Graphical view]
    SMARTiSM00450. RHOD. 1 hit.
    [Graphical view]
    SUPFAMiSSF52821. SSF52821. 1 hit.
    PROSITEiPS50206. RHODANESE_3. 1 hit.
    PS00972. USP_1. 1 hit.
    PS00973. USP_2. 1 hit.
    PS50235. USP_3. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P32571-1 [UniParc]FASTAAdd to Basket

    « Hide

    MEQNIISTIR DECIRHRSKY LTIAQLTAIA EAKINEFIIT GKAKDQDLSS    50
    LLDKCIDILS IYKKNSKDIK NIISCKNKGA MISSNSVMII QLNYVYYKVI 100
    HIIVTTNIPH LSEFAKIKLH KSTSDEGNGN NNNNEFQLMN IYNTLLETLL 150
    KDENIAKIKS FIKSSIKQTK LNHEQEECNL MRTGSYITSN QLNSLISSSA 200
    NSASSQMEIL LIDIRSRLEF NKSHIDTKNI ICLEPISFKM SYSDHDLEKK 250
    SLITSPNSEI KMFQSRNLFK FIILYTDANE YNVKQQSVLL DILVNHSFEK 300
    PISDDFTKIF ILESGFPGWL KSNYGRQVSS SFPSNNNIKD DSVYINGNTS 350
    GLSLQHLPKM SPSIRHSMDD SMKEMLVAPT PLNHLQQQQQ QQSDNDHVLK 400
    RSSSFKKLFS NYTSPNPKNS NSNLYSISSL SISSSPSPLP LHSPDPVKGN 450
    SLPINYPETP HLWKNSETDF MTNQREQLNH NSFAHIAPIN TKAITSPSRT 500
    ATPKLQRFPQ TISMNLNMNS NGHSSATSTI QPSCLSLSNN DSLDHTDVTP 550
    TSSHNYDLDF AVGLENLGNS CYMNCIIQCI LGTHELTQIF LDDSYAKHIN 600
    INSKLGSKGI LAKYFARLVH MMYKEQVDGS KKISISPIKF KLACGSVNSL 650
    FKTASQQDCQ EFCQFLLDGL HEDLNQCGSN PPLKELSQEA EARREKLSLR 700
    IASSIEWERF LTTDFSVIVD LFQGQYASRL KCKVCSHTST TYQPFTVLSI 750
    PIPKKNSRNN ITIEDCFREF TKCENLEVDE QWLCPHCEKR QPSTKQLTIT 800
    RLPRNLIVHL KRFDNLLNKN NDFVIYPFLL DLTPFWANDF DGVFPPGVND 850
    DELPIRGQIP PFKYELYGVA CHFGTLYGGH YTAYVKKGLK KGWLYFDDTK 900
    YKPVKNKADA INSNAYVLFY HRVYGV 926
    Length:926
    Mass (Da):105,192
    Last modified:February 1, 1994 - v2
    Checksum:iB863FE6062510F3C
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti327 – 3271Q → K in AAA35105. 1 PublicationCurated
    Sequence conflicti345 – 3451I → F in AAA35105. 1 PublicationCurated
    Sequence conflicti375 – 3784MLVA → TASW in AAA35105. 1 PublicationCurated
    Sequence conflicti383 – 3831N → I in AAA35105. 1 PublicationCurated
    Sequence conflicti407 – 4071K → T in AAA35105. 1 PublicationCurated
    Sequence conflicti543 – 57028LDHTD…NLGNS → FRSYEMLHQLLLIIMTLISR LVWENLEIP in AAA35105. 1 PublicationCuratedAdd
    BLAST
    Sequence conflicti580 – 5801I → T in AAA35105. 1 PublicationCurated
    Sequence conflicti836 – 8361W → G in AAA35105. 1 PublicationCurated
    Sequence conflicti897 – 8971D → N in AAA35105. 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U02518 Genomic DNA. Translation: AAC48915.1.
    L08070 Genomic DNA. Translation: AAA35105.1.
    Z49209 Genomic DNA. Translation: CAA89098.1.
    Z46796 Genomic DNA. Translation: CAA86791.1.
    Z74365 Genomic DNA. Translation: CAA98887.1.
    X84162 Genomic DNA. Translation: CAA58985.1.
    BK006938 Genomic DNA. Translation: DAA11915.1.
    PIRiS39344.
    RefSeqiNP_010354.3. NM_001180377.3.

    Genome annotation databases

    EnsemblFungiiYDR069C; YDR069C; YDR069C.
    GeneIDi851641.
    KEGGisce:YDR069C.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U02518 Genomic DNA. Translation: AAC48915.1 .
    L08070 Genomic DNA. Translation: AAA35105.1 .
    Z49209 Genomic DNA. Translation: CAA89098.1 .
    Z46796 Genomic DNA. Translation: CAA86791.1 .
    Z74365 Genomic DNA. Translation: CAA98887.1 .
    X84162 Genomic DNA. Translation: CAA58985.1 .
    BK006938 Genomic DNA. Translation: DAA11915.1 .
    PIRi S39344.
    RefSeqi NP_010354.3. NM_001180377.3.

    3D structure databases

    ProteinModelPortali P32571.
    SMRi P32571. Positions 563-922.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 32124. 120 interactions.
    DIPi DIP-5298N.
    IntActi P32571. 27 interactions.
    MINTi MINT-550253.
    STRINGi 4932.YDR069C.

    Protein family/group databases

    MEROPSi C19.005.

    Proteomic databases

    MaxQBi P32571.
    PaxDbi P32571.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YDR069C ; YDR069C ; YDR069C .
    GeneIDi 851641.
    KEGGi sce:YDR069C.

    Organism-specific databases

    CYGDi YDR069c.
    SGDi S000002476. DOA4.

    Phylogenomic databases

    eggNOGi COG5533.
    GeneTreei ENSGT00750000117363.
    HOGENOMi HOG000248489.
    KOi K11839.
    OMAi EDLNQCG.
    OrthoDBi EOG7R2BSX.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-29676-MONOMER.

    Miscellaneous databases

    NextBioi 969209.

    Gene expression databases

    Genevestigatori P32571.

    Family and domain databases

    Gene3Di 3.40.250.10. 1 hit.
    InterProi IPR018200. Pept_C19ubi-hydrolase_C_CS.
    IPR001394. Peptidase_C19_UCH.
    IPR001763. Rhodanese-like_dom.
    IPR028889. UCH/PAN2.
    [Graphical view ]
    Pfami PF00581. Rhodanese. 1 hit.
    PF00443. UCH. 1 hit.
    [Graphical view ]
    SMARTi SM00450. RHOD. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52821. SSF52821. 1 hit.
    PROSITEi PS50206. RHODANESE_3. 1 hit.
    PS00972. USP_1. 1 hit.
    PS00973. USP_2. 1 hit.
    PS50235. USP_3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    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. 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. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    20. 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.

    Entry informationi

    Entry nameiUBP4_YEAST
    AccessioniPrimary (citable) accession number: P32571
    Secondary accession number(s): D6VS55
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1993
    Last sequence update: February 1, 1994
    Last modified: October 1, 2014
    This is version 150 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Present with 428 molecules/cell in log phase SD medium.1 Publication

    Keywords - Technical termi

    Complete proteome, Reference proteome

    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

    Dasty 3