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P52479

- UBP10_MOUSE

UniProt

P52479 - UBP10_MOUSE

Protein

Ubiquitin carboxyl-terminal hydrolase 10

Gene

Usp10

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 121 (01 Oct 2014)
      Sequence version 3 (23 Mar 2010)
      Previous versions | rss
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    Functioni

    Hydrolase that can remove conjugated ubiquitin from target proteins such as p53/TP53, BECN1, SNX3 and CFTR. Acts as an essential regulator of p53/TP53 stability: in unstressed cells, specifically deubiquitinates p53/TP53 in the cytoplasm, leading to counteract MDM2 action and stabilize p53/TP53. Following DNA damage, translocates to the nucleus and deubiquitinates p53/TP53, leading to regulate the p53/TP53-dependent DNA damage response. Component of a regulatory loop that controls autophagy and p53/TP53 levels: mediates deubiquitination of BECN1, a key regulator of autophagy, leading to stabilize the PIK3C3/VPS34-containing complexes. In turn, PIK3C3/VPS34-containing complexes regulate USP10 stability, suggesting the existence of a regulatory system by which PIK3C3/VPS34-containing complexes regulate p53/TP53 protein levels via USP10 and USP13. Does not deubiquitinate MDM2. Deubiquitinates CFTR in early endosomes, enhancing its endocytic recycling 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).

    Enzyme regulationi

    Specifically inhibited by spautin-1 (specific and potent autophagy inhibitor-1), a derivative of MBCQ that binds to USP10 and inhibits deubiquitinase activity. Regulated by PIK3C3/VPS34-containing complexes By similarity.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei418 – 4181NucleophilePROSITE-ProRule annotation
    Active sitei743 – 7431Proton acceptorPROSITE-ProRule annotation

    GO - Molecular functioni

    1. cysteine-type endopeptidase activity Source: UniProtKB
    2. ion channel binding Source: UniProtKB
    3. p53 binding Source: UniProtKB
    4. ubiquitin-specific protease activity Source: UniProtKB
    5. ubiquitin thiolesterase activity Source: UniProtKB

    GO - Biological processi

    1. autophagy Source: UniProtKB-KW
    2. DNA damage response, signal transduction by p53 class mediator Source: UniProtKB
    3. DNA repair Source: UniProtKB-KW
    4. protein deubiquitination Source: UniProtKB
    5. regulation of autophagy Source: UniProtKB
    6. ubiquitin-dependent protein catabolic process Source: InterPro

    Keywords - Molecular functioni

    Hydrolase, Protease, Thiol protease

    Keywords - Biological processi

    Autophagy, DNA damage, DNA repair, Ubl conjugation pathway

    Protein family/group databases

    MEROPSiC19.018.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ubiquitin carboxyl-terminal hydrolase 10 (EC:3.4.19.12)
    Alternative name(s):
    Deubiquitinating enzyme 10
    Ubiquitin thioesterase 10
    Ubiquitin-specific-processing protease 10
    Gene namesi
    Name:Usp10
    Synonyms:Kiaa0190, Ode-1, Uchrp
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 8

    Organism-specific databases

    MGIiMGI:894652. Usp10.

    Subcellular locationi

    Cytoplasm By similarity. Nucleus By similarity. Early endosome By similarity
    Note: Cytoplasmic in normal conditions. After DNA damage, translocates to the nucleus following phosphorylation by ATM By similarity.By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. early endosome Source: UniProtKB
    3. intermediate filament cytoskeleton Source: Ensembl
    4. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Endosome, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 792791Ubiquitin carboxyl-terminal hydrolase 10PRO_0000080630Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanineBy similarity
    Modified residuei24 – 241PhosphothreonineBy similarity
    Modified residuei223 – 2231PhosphoserineBy similarity
    Modified residuei330 – 3301Phosphoserine; by ATMBy similarity
    Modified residuei359 – 3591Phosphoserine1 Publication
    Modified residuei364 – 3641PhosphoserineBy similarity
    Modified residuei570 – 5701Phosphoserine3 Publications

    Post-translational modificationi

    Phosphorylated by ATM following DNA damage, leading to stablization and translocation it to the nucleus.By similarity
    Ubiquitinated. Deubiquitinated by USP13 By similarity.By similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiP52479.
    PRIDEiP52479.

    PTM databases

    PhosphoSiteiP52479.

    Expressioni

    Gene expression databases

    ArrayExpressiP52479.
    BgeeiP52479.
    CleanExiMM_USP10.
    GenevestigatoriP52479.

    Interactioni

    Subunit structurei

    Interacts with G3BP, which may regulate its function. Interacts with p53/TP53, SNX3 and CFTR By similarity.By similarity

    Protein-protein interaction databases

    BioGridi204424. 3 interactions.
    IntActiP52479. 4 interactions.
    MINTiMINT-1870263.

    Structurei

    3D structure databases

    ProteinModelPortaliP52479.
    SMRiP52479. Positions 410-790.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini409 – 789381USPAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni2 – 9998Interaction with p53/TP53By similarityAdd
    BLAST

    Sequence similaritiesi

    Belongs to the peptidase C19 family. USP10 subfamily.Curated
    Contains 1 USP domain.Curated

    Phylogenomic databases

    GeneTreeiENSGT00550000074994.
    HOVERGENiHBG059823.
    InParanoidiQ6ZQG9.
    KOiK11841.
    OMAiGQEYQRI.
    OrthoDBiEOG7Z69BX.
    PhylomeDBiP52479.
    TreeFamiTF323203.

    Family and domain databases

    InterProiIPR018200. Pept_C19ubi-hydrolase_C_CS.
    IPR001394. Peptidase_C19_UCH.
    IPR028889. UCH/PAN2.
    IPR028767. USP10.
    [Graphical view]
    PANTHERiPTHR24006:SF69. PTHR24006:SF69. 1 hit.
    PfamiPF00443. UCH. 1 hit.
    [Graphical view]
    PROSITEiPS00972. USP_1. 1 hit.
    PS00973. USP_2. 1 hit.
    PS50235. USP_3. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P52479-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MALHNPQYIF GDFSPDEFNQ FFVTPRSSVE LPPYSGTLCS IQAEDELPDG    50
    QEHQRIEFGV DEVIEPSEGL PPTPSYSISS TLNPQAPEFI LGCTTSKKIP 100
    EAVEKDETYS SIDQYPASAL ALESNSNAEA ETLENDSGAG GLGQRERKKK 150
    KKRPPGYYSY LKDGGEDSAS PATLVNGHAT SVGTSGEAVE DAEFMDVLPP 200
    VMPRTCDSPQ NPVDFISGPV PDSPFPRTLG GDARTAGLCE GCHEADFEQP 250
    CLPADSLLRT AGTQPYVGTD TTENFAVANG KILESPGEDT AANGAELHTD 300
    EGADLDPAKP ESQSPPAESA LSASGAIPIS QPAKSWASLF HDSKPSASSP 350
    MAYVETKCSP PVPSPLASEK QMEVKEGLVP VSEDPVAIKI AELLETVTLI 400
    HKPVSLQPRG LINKGNWCYI NATLQALVAC PPMYHLMKFI PLYSKVQRPC 450
    TSTPMIDSFV RLMNEFTNMP VPPKPRQALG DKIVRDIRPG AAFEPTYIYR 500
    LLTVIKSSLS EKGRQEDAEE YLGFILNGLH EEMLSLKKLL SPTHEKHSVS 550
    NGPRSDLIED EELEDTGKGS EDEWEQVGPK NKTSITRQAD FVQTPITGIF 600
    GGHIRSVVYQ QSSKESATLQ LFFTLQLDIQ SDKIRTVQDA LESLVARESV 650
    QGYTTKTKQE VEVSRRVTLE KLPPVLVLHL KRFVYEKTGG CQKLVKNIDY 700
    PVDLEISREL LSPGIKNKNF KCQRTYRLFA VVYHHGNSAT GGHYTTDVFQ 750
    IGLNGWLRID DQTVKVINQY QVVKPPADRT AYLLYYRRVD LL 792
    Length:792
    Mass (Da):87,022
    Last modified:March 23, 2010 - v3
    Checksum:i02D07A8194215D09
    GO
    Isoform 2 (identifier: P52479-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         49-49: D → DA

    Show »
    Length:793
    Mass (Da):87,093
    Checksum:iAC67428E5DBC3D9F
    GO

    Sequence cautioni

    The sequence BAC97893.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti72 – 721P → R in AAH07134. (PubMed:15489334)Curated
    Sequence conflicti101 – 1011E → D in AAH07134. (PubMed:15489334)Curated
    Sequence conflicti293 – 2931N → S in AAH07134. (PubMed:15489334)Curated
    Sequence conflicti347 – 3471A → S in AAH07134. (PubMed:15489334)Curated
    Sequence conflicti448 – 4481R → G in BAE34291. (PubMed:16141072)Curated
    Sequence conflicti472 – 4721P → T in BAE32139. (PubMed:16141072)Curated
    Sequence conflicti528 – 5281G → R in BAE38053. (PubMed:16141072)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei49 – 491D → DA in isoform 2. 2 PublicationsVSP_038870

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D84096 mRNA. Translation: BAA12220.1.
    AK129083 mRNA. Translation: BAC97893.1. Different initiation.
    AK153675 mRNA. Translation: BAE32139.1.
    AK157970 mRNA. Translation: BAE34291.1.
    AK165156 mRNA. Translation: BAE38053.1.
    AK172443 mRNA. Translation: BAE43006.1.
    CH466525 Genomic DNA. Translation: EDL11620.1.
    BC007134 mRNA. Translation: AAH07134.1.
    CCDSiCCDS40495.1. [P52479-2]
    RefSeqiNP_033488.1. NM_009462.1. [P52479-2]
    XP_006530910.1. XM_006530847.1. [P52479-1]
    UniGeneiMm.256910.
    Mm.421337.

    Genome annotation databases

    EnsembliENSMUST00000108988; ENSMUSP00000104616; ENSMUSG00000031826. [P52479-1]
    ENSMUST00000144458; ENSMUSP00000123590; ENSMUSG00000031826. [P52479-2]
    GeneIDi22224.
    KEGGimmu:22224.
    UCSCiuc009nqn.1. mouse. [P52479-2]
    uc009nqo.1. mouse. [P52479-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D84096 mRNA. Translation: BAA12220.1 .
    AK129083 mRNA. Translation: BAC97893.1 . Different initiation.
    AK153675 mRNA. Translation: BAE32139.1 .
    AK157970 mRNA. Translation: BAE34291.1 .
    AK165156 mRNA. Translation: BAE38053.1 .
    AK172443 mRNA. Translation: BAE43006.1 .
    CH466525 Genomic DNA. Translation: EDL11620.1 .
    BC007134 mRNA. Translation: AAH07134.1 .
    CCDSi CCDS40495.1. [P52479-2 ]
    RefSeqi NP_033488.1. NM_009462.1. [P52479-2 ]
    XP_006530910.1. XM_006530847.1. [P52479-1 ]
    UniGenei Mm.256910.
    Mm.421337.

    3D structure databases

    ProteinModelPortali P52479.
    SMRi P52479. Positions 410-790.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 204424. 3 interactions.
    IntActi P52479. 4 interactions.
    MINTi MINT-1870263.

    Protein family/group databases

    MEROPSi C19.018.

    PTM databases

    PhosphoSitei P52479.

    Proteomic databases

    MaxQBi P52479.
    PRIDEi P52479.

    Protocols and materials databases

    DNASUi 22224.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000108988 ; ENSMUSP00000104616 ; ENSMUSG00000031826 . [P52479-1 ]
    ENSMUST00000144458 ; ENSMUSP00000123590 ; ENSMUSG00000031826 . [P52479-2 ]
    GeneIDi 22224.
    KEGGi mmu:22224.
    UCSCi uc009nqn.1. mouse. [P52479-2 ]
    uc009nqo.1. mouse. [P52479-1 ]

    Organism-specific databases

    CTDi 9100.
    MGIi MGI:894652. Usp10.
    Rougei Search...

    Phylogenomic databases

    GeneTreei ENSGT00550000074994.
    HOVERGENi HBG059823.
    InParanoidi Q6ZQG9.
    KOi K11841.
    OMAi GQEYQRI.
    OrthoDBi EOG7Z69BX.
    PhylomeDBi P52479.
    TreeFami TF323203.

    Miscellaneous databases

    ChiTaRSi USP10. mouse.
    NextBioi 302247.
    PROi P52479.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P52479.
    Bgeei P52479.
    CleanExi MM_USP10.
    Genevestigatori P52479.

    Family and domain databases

    InterProi IPR018200. Pept_C19ubi-hydrolase_C_CS.
    IPR001394. Peptidase_C19_UCH.
    IPR028889. UCH/PAN2.
    IPR028767. USP10.
    [Graphical view ]
    PANTHERi PTHR24006:SF69. PTHR24006:SF69. 1 hit.
    Pfami PF00443. UCH. 1 hit.
    [Graphical view ]
    PROSITEi PS00972. USP_1. 1 hit.
    PS00973. USP_2. 1 hit.
    PS50235. USP_3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning from a mouse osteoblastic cell line of a gene, encoding a ubiquitin carboxyl-terminal hydrolase related polypeptide, down regulated during ascorbic acid dependent differentiation."
      Ito M., Hitomi K., Tsukagoshi N.
      Submitted (APR-1996) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    2. "Prediction of the coding sequences of mouse homologues of KIAA gene: III. The complete nucleotide sequences of 500 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., Koseki H., Hiraoka S., Saga Y., Nagase T., Ohara O., Koga H.
      DNA Res. 10:167-180(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Embryonic tail.
    3. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
      Strain: C57BL/6J and NOD.
      Tissue: Inner ear, Spleen and Thymus.
    4. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
      Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    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] (ISOFORM 1).
      Tissue: Mammary tumor.
    6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-359, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic brain.
    7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-570, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    8. "Specific phosphopeptide enrichment with immobilized titanium ion affinity chromatography adsorbent for phosphoproteome analysis."
      Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.
      J. Proteome Res. 7:3957-3967(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-570, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    9. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-570, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiUBP10_MOUSE
    AccessioniPrimary (citable) accession number: P52479
    Secondary accession number(s): Q3T9L4
    , Q3TNN5, Q3TZB8, Q3U5E0, Q6ZQG9, Q91VY7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: March 23, 2010
    Last modified: October 1, 2014
    This is version 121 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

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

    External Data

    Dasty 3