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Q80U87

- UBP8_MOUSE

UniProt

Q80U87 - UBP8_MOUSE

Protein

Ubiquitin carboxyl-terminal hydrolase 8

Gene

Usp8

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 108 (01 Oct 2014)
      Sequence version 2 (01 Mar 2004)
      Previous versions | rss
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    Functioni

    Hydrolase that can remove conjugated ubiquitin from proteins and therefore plays an important regulatory role at the level of protein turnover by preventing degradation. Converts both 'Lys-48' an 'Lys-63'-linked ubiquitin chains. Catalytic activity is enhanced in the M phase. Involved in cell proliferation. Required to enter into S phase in response to serum stimulation. May regulate T-cell anergy mediated by RNF128 via the formation of a complex containing RNF128 and OTUB1. Probably regulates the stability of STAM2 and RASGRF1. Regulates endosomal ubiquitin dynamics, cargo sorting, membrane traffic at early endosomes, and maintenance of ESCRT-0 stability. The level of protein ubiquitination on endosomes is essential for maintaining the morphology of the organelle. Deubiquitinates EPS15 and controles tyrosine kinase stability. Removes conjugated ubiquitin from EGFR thus regulating EGFR degradation and downstream MAPK signaling. Involved in acrosome biogenesis through interaction with the spermatid ESCRT-0 complex and microtubules. Deubiquitinates BIRC6/bruce and KIF23/MKLP1 By similarity.By similarity

    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).

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei748 – 7481Nucleophile
    Active sitei1029 – 10291Proton acceptorPROSITE-ProRule annotation

    GO - Molecular functioni

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

    GO - Biological processi

    1. cell cycle Source: UniProtKB-KW
    2. endosome organization Source: UniProtKB
    3. protein deubiquitination Source: UniProtKB
    4. Ras protein signal transduction Source: MGI
    5. ubiquitin-dependent protein catabolic process Source: InterPro

    Keywords - Molecular functioni

    Hydrolase, Protease, Thiol protease

    Keywords - Biological processi

    Cell cycle, Ubl conjugation pathway

    Enzyme and pathway databases

    ReactomeiREACT_199061. Downregulation of ERBB2:ERBB3 signaling.
    REACT_213035. regulation of FZD by ubiquitination.

    Protein family/group databases

    MEROPSiC19.011.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ubiquitin carboxyl-terminal hydrolase 8 (EC:3.4.19.12)
    Alternative name(s):
    Deubiquitinating enzyme 8
    Ubiquitin isopeptidase Y
    Short name:
    mUBPy
    Ubiquitin thioesterase 8
    Ubiquitin-specific-processing protease 8
    Gene namesi
    Name:Usp8
    Synonyms:Kiaa0055, Ubpy
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 2

    Organism-specific databases

    MGIiMGI:1934029. Usp8.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: UniProtKB
    2. extrinsic component of endosome membrane Source: UniProtKB
    3. intracellular Source: MGI
    4. midbody Source: MGI
    5. nucleus Source: UniProtKB-SubCell
    6. plasma membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Endosome, Membrane, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi405 – 4051P → A: Abolishes interaction with the SH3 domain of STAM2. 1 Publication
    Mutagenesisi406 – 4061Q → A: Does not affect interaction with the SH3 domain of STAM2. 1 Publication
    Mutagenesisi407 – 4071V → A: Reduces interaction with the SH3 domain of STAM2. 1 Publication
    Mutagenesisi408 – 4081D → A: Reduces interaction with the SH3 domain of STAM2. 1 Publication
    Mutagenesisi409 – 4091R → A: Abolishes interaction with the SH3 domain of STAM2. 1 Publication
    Mutagenesisi410 – 4101T → A: Does not affect interaction with the SH3 domain of STAM2. 1 Publication
    Mutagenesisi411 – 4111K → A: Does not affect interaction with the SH3 domain of STAM2. 1 Publication
    Mutagenesisi412 – 4121K → A: Abolishes interaction with the SH3 domain of STAM2. 1 Publication
    Mutagenesisi413 – 4131P → A: Abolishes interaction with the SH3 domain of STAM2. 1 Publication
    Mutagenesisi680 – 6801S → A: Abolishes the interaction with YWHAE and leads to accumulation in the nucleus. 2 Publications
    Mutagenesisi748 – 7481C → A: Impairs deubiquitination of EPS15, RNF128 and RNF41. 4 Publications
    Mutagenesisi907 – 9071T → A: Reduces stabilization activity on RNF41. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 10801080Ubiquitin carboxyl-terminal hydrolase 8PRO_0000080628Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei160 – 1601PhosphoserineBy similarity
    Modified residuei446 – 4461PhosphoserineBy similarity
    Modified residuei569 – 5691PhosphothreonineBy similarity
    Modified residuei680 – 6801Phosphoserine3 Publications
    Modified residuei681 – 6811PhosphoserineBy similarity
    Modified residuei907 – 9071Phosphothreonine2 Publications

    Post-translational modificationi

    Phosphorylation of Ser-680 is essential for interaction with YWHAE and for cytosol localization. Undergoes dephosphorylation at Ser-680 in the M phase. Tyrosine-phosphorylated in its N-terminal half in an EGFR-dependent manner.4 Publications
    Ubiquitinated. Inactive form is mostly monoubiquitinated, but polyubiquitination happens too. Ubiquitination is increased in EGF-stimulated cells. Ubiquitination of active form is undetectable, suggesting a possibility that USP8 deubiquitinates itself, thereby regulating its own function.1 Publication

    Keywords - PTMi

    Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ80U87.
    PaxDbiQ80U87.
    PRIDEiQ80U87.

    PTM databases

    PhosphoSiteiQ80U87.

    Expressioni

    Tissue specificityi

    Highly expressed in testis. Expressed at intermediate level in brain.2 Publications

    Gene expression databases

    ArrayExpressiQ80U87.
    BgeeiQ80U87.
    CleanExiMM_USP8.
    GenevestigatoriQ80U87.

    Interactioni

    Subunit structurei

    Forms a ternary complex with RNF128 and OTUB1. Interacts (via C-terminal UCH catalytic domain) with OTUB1 isoform 1. Interacts with STAM2 (via SH3 domain). Interacts with DNAJB3, EGFR, EPS15, RASGRF1, RNF41, YWHAE, YWHAG and YWHAZ. Interacts with NBR1, RASGRF1, RNF41 and IST1 By similarity. Associates with the ESCRT-0 complex and with microtubules. Interacts with BIRC6/bruce and KIF23/MKLP1.By similarity9 Publications

    Protein-protein interaction databases

    BioGridi220000. 11 interactions.
    IntActiQ80U87. 7 interactions.
    MINTiMINT-144852.

    Structurei

    Secondary structure

    1
    1080
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi704 – 7063

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1UJ0X-ray1.70B699-709[»]
    ProteinModelPortaliQ80U87.
    SMRiQ80U87. Positions 6-132, 181-316, 718-1072.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini33 – 11684MITAdd
    BLAST
    Domaini195 – 313119RhodanesePROSITE-ProRule annotationAdd
    BLAST
    Domaini739 – 1071333USPAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi405 – 4139SH3-binding

    Domaini

    The MIT domain is required for endosomal localization, CHMP1B-binding, maintenance of ESCRT-0 stability and EGFR degradation.By similarity
    The rhodanese domain is sufficent for RNF41-binding.

    Sequence similaritiesi

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

    Keywords - Domaini

    SH3-binding

    Phylogenomic databases

    eggNOGiCOG5533.
    GeneTreeiENSGT00750000117363.
    HOGENOMiHOG000231497.
    HOVERGENiHBG012631.
    KOiK11839.
    OrthoDBiEOG7FR7GN.

    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.
    IPR015063. USP8_dimer.
    [Graphical view]
    PfamiPF00581. Rhodanese. 1 hit.
    PF00443. UCH. 1 hit.
    PF08969. USP8_dimer. 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.

    Q80U87-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPAVASVPKE LYLSSSLKDL NKKTEVKPEK TSTKNYIHSA QKIFKTAEEC     50
    RLDRDEERAY VLYMKYVAVY NLIKKRPDFK QQQDYYLSIL GPANIKKAIE 100
    EAERLSESLK LRYEEAEVRK QLEEKDRREE EQLQQQKRQE MGREDSGAAA 150
    KRSVENLLDS KTKTQRINGE KSEGAAAAER GAITAKELYT MMMDKNTSLI 200
    IMDARKIQDY QHSCILDSLS VPEEAISPGV TASWIEANLS DDSKDTWKKR 250
    GSVDYVVLLD WFSSAKDLLL GTTLRSLKDA LFKWESKTVL RHEPLVLEGG 300
    YENWLLCYPQ FTTNAKVTPP PRSRAEEVSV SLDFTYPSLE EPVPSKLPTQ 350
    MPPPPIETNE KALLVTDQDE KLRLSTQPAL AGPGAAPRAE ASPIIQPAPA 400
    TKSVPQVDRT KKPSVKLPED HRIKSENTDQ SGRVLSDRST KPVFPSPTTM 450
    LTDEEKARIH QETALLMEKN KQEKELWDKQ QKEQKEKLRR EEQERKAGKT 500
    QDADERDSTE NQHKAKDGQE KKDSKQTKTE DRELSADGAQ EATGTQRQSK 550
    SEHEASDAKV PVEGKRCPTS EAQKRPADVS PASVSGELNA GKAQREPLTR 600
    ARSEEMGRIV PGLPLGWAKF LDPITGTFRY YHSPTNTVHM YPPEMAPSSA 650
    PPSTPPTHKV KPQVPAERDR EPSKLKRSYS SPDITQALQE EEKRRPAVTP 700
    MVNRENKPPC YPKAEISRLS ASQIRNLNPV FGGSGPALTG LRNLGNTCYM 750
    NSILQCLCNA PHLADYFNRN CYQDDINRSN LLGHKGEVAE EFGIIMKALW 800
    TGQYRYISPK DFKVTIGKIN DQFAGSSQQD SQELLLFLMD GLHEDLNKAD 850
    NRKRHKEENN EHLDDLQAAE HAWQKHKQLN ESIIVALFQG QFKSTVQCLT 900
    CRRRSRTFEA FMYLSLPLAS TSKCTLQDCL RLFSKEEKLT DNNRFYCSHC 950
    RARRDSLKKI EIWKLPPVLL VHLKRFSYDG RWKQKLQTSV DFPLENLDLS 1000
    QYVIGPKNSL KKYNLFSVSN HYGGLDGGHY TAYCKNAARQ RWFKFDDHEV 1050
    SDISVSSVRS SAAYILFYTS LGPRITDVAT 1080
    Length:1,080
    Mass (Da):122,611
    Last modified:March 1, 2004 - v2
    Checksum:i7F458E3B1AF0B7FA
    GO

    Sequence cautioni

    The sequence BAC65477.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti139 – 1391Q → P in AAD38869. (PubMed:11500497)Curated
    Sequence conflicti151 – 1511K → R in BAB18534. (PubMed:10982817)Curated
    Sequence conflicti349 – 3491T → A in BAB18534. (PubMed:10982817)Curated
    Sequence conflicti370 – 3701E → G in BAB18534. (PubMed:10982817)Curated
    Sequence conflicti557 – 5571D → N in BAB18534. (PubMed:10982817)Curated
    Sequence conflicti576 – 5761P → L in BAB18534. (PubMed:10982817)Curated
    Sequence conflicti837 – 8371F → S in BAB18534. (PubMed:10982817)Curated
    Sequence conflicti865 – 8739DLQAAEHAW → EPAGGRARL in BAB18534. (PubMed:10982817)Curated
    Sequence conflicti885 – 8862VA → RL in BAB18534. (PubMed:10982817)Curated
    Sequence conflicti894 – 8941S → A in BAB18534. (PubMed:10982817)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB045709 mRNA. Translation: BAB18534.1.
    AF057146 mRNA. Translation: AAD38869.1.
    AK122195 mRNA. Translation: BAC65477.1. Different initiation.
    AL732330 Genomic DNA. Translation: CAM14544.1.
    BC027052 mRNA. Translation: AAH27052.1.
    BC050947 mRNA. Translation: AAH50947.1.
    BC061465 mRNA. Translation: AAH61465.1.
    BC066126 mRNA. Translation: AAH66126.1.
    CCDSiCCDS16687.1.
    RefSeqiNP_062703.2. NM_019729.3.
    UniGeneiMm.272629.
    Mm.490069.

    Genome annotation databases

    EnsembliENSMUST00000028841; ENSMUSP00000028841; ENSMUSG00000027363.
    GeneIDi84092.
    KEGGimmu:84092.
    UCSCiuc008meb.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB045709 mRNA. Translation: BAB18534.1 .
    AF057146 mRNA. Translation: AAD38869.1 .
    AK122195 mRNA. Translation: BAC65477.1 . Different initiation.
    AL732330 Genomic DNA. Translation: CAM14544.1 .
    BC027052 mRNA. Translation: AAH27052.1 .
    BC050947 mRNA. Translation: AAH50947.1 .
    BC061465 mRNA. Translation: AAH61465.1 .
    BC066126 mRNA. Translation: AAH66126.1 .
    CCDSi CCDS16687.1.
    RefSeqi NP_062703.2. NM_019729.3.
    UniGenei Mm.272629.
    Mm.490069.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1UJ0 X-ray 1.70 B 699-709 [» ]
    ProteinModelPortali Q80U87.
    SMRi Q80U87. Positions 6-132, 181-316, 718-1072.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 220000. 11 interactions.
    IntActi Q80U87. 7 interactions.
    MINTi MINT-144852.

    Protein family/group databases

    MEROPSi C19.011.

    PTM databases

    PhosphoSitei Q80U87.

    Proteomic databases

    MaxQBi Q80U87.
    PaxDbi Q80U87.
    PRIDEi Q80U87.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000028841 ; ENSMUSP00000028841 ; ENSMUSG00000027363 .
    GeneIDi 84092.
    KEGGi mmu:84092.
    UCSCi uc008meb.2. mouse.

    Organism-specific databases

    CTDi 9101.
    MGIi MGI:1934029. Usp8.
    Rougei Search...

    Phylogenomic databases

    eggNOGi COG5533.
    GeneTreei ENSGT00750000117363.
    HOGENOMi HOG000231497.
    HOVERGENi HBG012631.
    KOi K11839.
    OrthoDBi EOG7FR7GN.

    Enzyme and pathway databases

    Reactomei REACT_199061. Downregulation of ERBB2:ERBB3 signaling.
    REACT_213035. regulation of FZD by ubiquitination.

    Miscellaneous databases

    NextBioi 350878.
    PROi Q80U87.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q80U87.
    Bgeei Q80U87.
    CleanExi MM_USP8.
    Genevestigatori Q80U87.

    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.
    IPR015063. USP8_dimer.
    [Graphical view ]
    Pfami PF00581. Rhodanese. 1 hit.
    PF00443. UCH. 1 hit.
    PF08969. USP8_dimer. 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. "A deubiquitinating enzyme UBPY interacts with the Src homology 3 domain of Hrs-binding protein via a novel binding motif PX(V/I)(D/N)RXXKP."
      Kato M., Miyazawa K., Kitamura N.
      J. Biol. Chem. 275:37481-37487(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], SH3-BINDING, INTERACTION WITH STAM2, MUTAGENESIS OF PRO-405; GLN-406; VAL-407; ASP-408; ARG-409; THR-410; LYS-411; LYS-412 AND PRO-413.
    2. "Cloning and characterization of mouse UBPy, a deubiquitinating enzyme that interacts with the ras guanine nucleotide exchange factor CDC25(Mm)/Ras-GRF1."
      Gnesutta N., Ceriani M., Innocenti M., Mauri I., Zippel R., Sturani E., Borgonovo B., Berruti G., Martegani E.
      J. Biol. Chem. 276:39448-39454(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, INTERACTION WITH RASGRF1.
      Tissue: Embryo.
    3. "Prediction of the coding sequences of mouse homologues of KIAA gene: II. The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
      Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S., Nakajima D., Nagase T., Ohara O., Koga H.
      DNA Res. 10:35-48(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Brain.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6.
      Tissue: Brain and Kidney.
    6. "Stabilization of the E3 ubiquitin ligase Nrdp1 by the deubiquitinating enzyme USP8."
      Wu X., Yen L., Irwin L., Sweeney C., Carraway K.L. III
      Mol. Cell. Biol. 24:7748-7757(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH RNF41, FUNCTION, MUTAGENESIS OF CYS-748.
    7. Cited for: INTERACTION WITH OTUB1 AND RNF128, MUTAGENESIS OF CYS-748.
    8. "The deubiquitinating enzyme mUBPy interacts with the sperm-specific molecular chaperone MSJ-1: the relation with the proteasome, acrosome, and centrosome in mouse male germ cells."
      Berruti G., Martegani E.
      Biol. Reprod. 72:14-21(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY, INTERACTION WITH DNAJB3.
    9. "Regulation of epidermal growth factor receptor down-regulation by UBPY-mediated deubiquitination at endosomes."
      Mizuno E., Iura T., Mukai A., Yoshimori T., Kitamura N., Komada M.
      Mol. Biol. Cell 16:5163-5174(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, UBIQUITINATION, MUTAGENESIS OF CYS-748.
    10. "A deubiquitinating enzyme UBPY regulates the level of protein ubiquitination on endosomes."
      Mizuno E., Kobayashi K., Yamamoto A., Kitamura N., Komada M.
      Traffic 7:1017-1031(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF CYS-748, INTERACTION WITH ESP15.
    11. "UBPY-mediated epidermal growth factor receptor (EGFR) de-ubiquitination promotes EGFR degradation."
      Alwan H.A., van Leeuwen J.E.
      J. Biol. Chem. 282:1658-1669(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION, INTERACTION WITH EGFR, FUNCTION.
    12. "Identification of 14-3-3epsilon substrates from embryonic murine brain."
      Ballif B.A., Cao Z., Schwartz D., Carraway K.L. III, Gygi S.P.
      J. Proteome Res. 5:2372-2379(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-680, INTERACTION WITH YWHAE, MUTAGENESIS OF SER-680, SUBCELLULAR LOCATION.
    13. "14-3-3-dependent inhibition of the deubiquitinating activity of UBPY and its cancellation in the M phase."
      Mizuno E., Kitamura N., Komada M.
      Exp. Cell Res. 313:3624-3634(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, PHOSPHORYLATION AT SER-680, INTERACTION WITH YWHAE; YWHAG AND YWHAZ, MUTAGENESIS OF SER-680, SUBCELLULAR LOCATION.
    14. "Neuregulin-induced ErbB3 downregulation is mediated by a protein stability cascade involving the E3 ubiquitin ligase Nrdp1."
      Cao Z., Wu X., Yen L., Sweeney C., Carraway K.L. III
      Mol. Cell. Biol. 27:2180-2188(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, PHOSPHORYLATION AT THR-907, MUTAGENESIS OF THR-907.
    15. "Essential role of ubiquitin-specific protease 8 for receptor tyrosine kinase stability and endocytic trafficking in vivo."
      Niendorf S., Oksche A., Kisser A., Lohler J., Prinz M., Schorle H., Feller S., Lewitzky M., Horak I., Knobeloch K.P.
      Mol. Cell. Biol. 27:5029-5039(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    16. "The phagosomal proteome in interferon-gamma-activated macrophages."
      Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
      Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. "USP8, a regulator of endosomal sorting, is involved in mouse acrosome biogenesis through interaction with the spermatid ESCRT-0 complex and microtubules."
      Berruti G., Ripolone M., Ceriani M.
      Biol. Reprod. 82:930-939(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, ASSOCIATION WITH THE ESCRT-0 COMPLEX, MICROTUBULE-BINDING.

    Entry informationi

    Entry nameiUBP8_MOUSE
    AccessioniPrimary (citable) accession number: Q80U87
    Secondary accession number(s): A2AI53
    , Q80YP2, Q8R0D3, Q9EQU1, Q9WVP5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 1, 2004
    Last sequence update: March 1, 2004
    Last modified: October 1, 2014
    This is version 108 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. Peptidase families
      Classification of peptidase families and list of entries
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

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