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Q14694

- UBP10_HUMAN

UniProt

Q14694 - UBP10_HUMAN

Protein

Ubiquitin carboxyl-terminal hydrolase 10

Gene

USP10

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 142 (01 Oct 2014)
      Sequence version 2 (01 Nov 1997)
      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.5 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).1 Publication

    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.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei424 – 4241Nucleophile
    Active sitei749 – 7491Proton 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. poly(A) RNA binding Source: UniProtKB
    5. protein binding Source: UniProtKB
    6. ubiquitin-specific protease activity Source: UniProtKB
    7. 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
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 16

    Organism-specific databases

    HGNCiHGNC:12608. USP10.

    Subcellular locationi

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

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Cytoplasm, Endosome, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi42 – 421T → A: Abolishes phosphorylation by ATM; when associated with A-337. 1 Publication
    Mutagenesisi42 – 421T → E: Phospho-mimetic mutant that translocates to the nucleus in absence of genotoxic stress; when associated with D-337. 1 Publication
    Mutagenesisi337 – 3371S → A: Abolishes phosphorylation by ATM; when associated with A-42. 1 Publication
    Mutagenesisi337 – 3371S → D: Phospho-mimetic mutant that translocates to the nucleus in absence of genotoxic stress; when associated with E-42. 1 Publication
    Mutagenesisi424 – 4241C → A: Abolishes de-ubiquitinating activity. 3 Publications

    Organism-specific databases

    PharmGKBiPA37234.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 798797Ubiquitin carboxyl-terminal hydrolase 10PRO_0000080629Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine1 Publication
    Modified residuei24 – 241Phosphothreonine1 Publication
    Modified residuei42 – 421Phosphothreonine; by ATM1 Publication
    Modified residuei100 – 1001Phosphothreonine1 Publication
    Modified residuei226 – 2261Phosphoserine1 Publication
    Modified residuei337 – 3371Phosphoserine; by ATM1 Publication
    Modified residuei365 – 3651Phosphoserine2 Publications
    Modified residuei370 – 3701Phosphoserine3 Publications
    Modified residuei563 – 5631Phosphoserine1 Publication
    Modified residuei576 – 5761Phosphoserine7 Publications

    Post-translational modificationi

    Phosphorylated by ATM following DNA damage, leading to stablization and translocation it to the nucleus.10 Publications
    Ubiquitinated. Deubiquitinated by USP13.1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ14694.
    PaxDbiQ14694.
    PRIDEiQ14694.

    PTM databases

    PhosphoSiteiQ14694.

    Expressioni

    Tissue specificityi

    Widely expressed.1 Publication

    Inductioni

    Following DNA damage. Down-regulated in renal cell carcinomas.1 Publication

    Gene expression databases

    ArrayExpressiQ14694.
    BgeeiQ14694.
    CleanExiHS_USP10.
    GenevestigatoriQ14694.

    Organism-specific databases

    HPAiHPA006731.
    HPA006749.

    Interactioni

    Subunit structurei

    Interacts with G3BP, which may regulate its function. Interacts with p53/TP53, SNX3 and CFTR.4 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ZC3H12AQ5D1E85EBI-2510389,EBI-747793

    Protein-protein interaction databases

    BioGridi114554. 34 interactions.
    IntActiQ14694. 16 interactions.
    MINTiMINT-3030173.
    STRINGi9606.ENSP00000219473.

    Structurei

    3D structure databases

    ProteinModelPortaliQ14694.
    SMRiQ14694. Positions 416-796.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini415 – 795381USPAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni2 – 10099Interaction with p53/TP53Add
    BLAST

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG5533.
    HOGENOMiHOG000285959.
    HOVERGENiHBG059823.
    InParanoidiQ14694.
    KOiK11841.
    OMAiGQEYQRI.
    OrthoDBiEOG7Z69BX.
    PhylomeDBiQ14694.
    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 (3)i

    Sequence statusi: Complete.

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

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q14694-1) [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

    MALHSPQYIF GDFSPDEFNQ FFVTPRSSVE LPPYSGTVLC GTQAVDKLPD    50
    GQEYQRIEFG VDEVIEPSDT LPRTPSYSIS STLNPQAPEF ILGCTASKIT 100
    PDGITKEASY GSIDCQYPGS ALALDGSSNV EAEVLENDGV SGGLGQRERK 150
    KKKKRPPGYY SYLKDGGDDS ISTEALVNGH ANSAVPNSVS AEDAEFMGDM 200
    PPSVTPRTCN SPQNSTDSVS DIVPDSPFPG ALGSDTRTAG QPEGGPGADF 250
    GQSCFPAEAG RDTLSRTAGA QPCVGTDTTE NLGVANGQIL ESSGEGTATN 300
    GVELHTTESI DLDPTKPESA SPPADGTGSA SGTLPVSQPK SWASLFHDSK 350
    PSSSSPVAYV ETKYSPPAIS PLVSEKQVEV KEGLVPVSED PVAIKIAELL 400
    ENVTLIHKPV SLQPRGLINK GNWCYINATL QALVACPPMY HLMKFIPLYS 450
    KVQRPCTSTP MIDSFVRLMN EFTNMPVPPK PRQALGDKIV RDIRPGAAFE 500
    PTYIYRLLTV NKSSLSEKGR QEDAEEYLGF ILNGLHEEML NLKKLLSPSN 550
    EKLTISNGPK NHSVNEEEQE EQGEGSEDEW EQVGPRNKTS VTRQADFVQT 600
    PITGIFGGHI RSVVYQQSSK ESATLQPFFT LQLDIQSDKI RTVQDALESL 650
    VARESVQGYT TKTKQEVEIS RRVTLEKLPP VLVLHLKRFV YEKTGGCQKL 700
    IKNIEYPVDL EISKELLSPG VKNKNFKCHR TYRLFAVVYH HGNSATGGHY 750
    TTDVFQIGLN GWLRIDDQTV KVINQYQVVK PTAERTAYLL YYRRVDLL 798
    Length:798
    Mass (Da):87,134
    Last modified:November 1, 1997 - v2
    Checksum:iE6BA77E2B5CE2B3F
    GO
    Isoform 2 (identifier: Q14694-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-1: M → MCSKDTVLSVCALYWRKGIQSHTPLIGAWRRGKQREQPEDRGVPMKRAA

    Show »
    Length:846
    Mass (Da):92,597
    Checksum:i01C2CD6FC3709AE4
    GO
    Isoform 3 (identifier: Q14694-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-6: MALHSP → MPWLPSPGIG

    Note: No experimental confirmation available.

    Show »
    Length:802
    Mass (Da):87,533
    Checksum:iCBA33D0F268AEF5A
    GO

    Sequence cautioni

    The sequence CAD97644.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti108 – 1081A → V in BAG61546. (PubMed:14702039)Curated
    Sequence conflicti263 – 2631T → A in BAG61546. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti200 – 2001M → V.1 Publication
    Corresponds to variant rs1862792 [ dbSNP | Ensembl ].
    VAR_015859
    Natural varianti203 – 2031S → P.1 Publication
    Corresponds to variant rs2326391 [ dbSNP | Ensembl ].
    VAR_015860
    Natural varianti204 – 2041V → L.1 Publication
    Corresponds to variant rs1812061 [ dbSNP | Ensembl ].
    VAR_015861

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 66MALHSP → MPWLPSPGIG in isoform 3. 1 PublicationVSP_038868
    Alternative sequencei1 – 11M → MCSKDTVLSVCALYWRKGIQ SHTPLIGAWRRGKQREQPED RGVPMKRAA in isoform 2. 1 PublicationVSP_038869

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D80012 mRNA. Translation: BAA11507.1.
    AK299618 mRNA. Translation: BAG61546.1.
    AK315570 mRNA. Translation: BAG37945.1.
    AL162049 mRNA. Translation: CAB82392.2.
    BX537402 mRNA. Translation: CAD97644.1. Different initiation.
    AC009116 Genomic DNA. No translation available.
    AC025280 Genomic DNA. No translation available.
    BC000263 mRNA. Translation: AAH00263.1.
    CCDSiCCDS45537.1. [Q14694-1]
    CCDS62004.1. [Q14694-3]
    RefSeqiNP_001259004.1. NM_001272075.1. [Q14694-3]
    NP_005144.2. NM_005153.2. [Q14694-1]
    UniGeneiHs.136778.

    Genome annotation databases

    EnsembliENST00000219473; ENSP00000219473; ENSG00000103194. [Q14694-1]
    ENST00000570191; ENSP00000457411; ENSG00000103194. [Q14694-3]
    GeneIDi9100.
    KEGGihsa:9100.
    UCSCiuc002fii.3. human. [Q14694-1]
    uc010voe.2. human. [Q14694-3]

    Polymorphism databases

    DMDMi2501458.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D80012 mRNA. Translation: BAA11507.1 .
    AK299618 mRNA. Translation: BAG61546.1 .
    AK315570 mRNA. Translation: BAG37945.1 .
    AL162049 mRNA. Translation: CAB82392.2 .
    BX537402 mRNA. Translation: CAD97644.1 . Different initiation.
    AC009116 Genomic DNA. No translation available.
    AC025280 Genomic DNA. No translation available.
    BC000263 mRNA. Translation: AAH00263.1 .
    CCDSi CCDS45537.1. [Q14694-1 ]
    CCDS62004.1. [Q14694-3 ]
    RefSeqi NP_001259004.1. NM_001272075.1. [Q14694-3 ]
    NP_005144.2. NM_005153.2. [Q14694-1 ]
    UniGenei Hs.136778.

    3D structure databases

    ProteinModelPortali Q14694.
    SMRi Q14694. Positions 416-796.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114554. 34 interactions.
    IntActi Q14694. 16 interactions.
    MINTi MINT-3030173.
    STRINGi 9606.ENSP00000219473.

    Protein family/group databases

    MEROPSi C19.018.

    PTM databases

    PhosphoSitei Q14694.

    Polymorphism databases

    DMDMi 2501458.

    Proteomic databases

    MaxQBi Q14694.
    PaxDbi Q14694.
    PRIDEi Q14694.

    Protocols and materials databases

    DNASUi 9100.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000219473 ; ENSP00000219473 ; ENSG00000103194 . [Q14694-1 ]
    ENST00000570191 ; ENSP00000457411 ; ENSG00000103194 . [Q14694-3 ]
    GeneIDi 9100.
    KEGGi hsa:9100.
    UCSCi uc002fii.3. human. [Q14694-1 ]
    uc010voe.2. human. [Q14694-3 ]

    Organism-specific databases

    CTDi 9100.
    GeneCardsi GC16P084734.
    H-InvDB HIX0173245.
    HGNCi HGNC:12608. USP10.
    HPAi HPA006731.
    HPA006749.
    MIMi 609818. gene.
    neXtProti NX_Q14694.
    PharmGKBi PA37234.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5533.
    HOGENOMi HOG000285959.
    HOVERGENi HBG059823.
    InParanoidi Q14694.
    KOi K11841.
    OMAi GQEYQRI.
    OrthoDBi EOG7Z69BX.
    PhylomeDBi Q14694.
    TreeFami TF323203.

    Miscellaneous databases

    ChiTaRSi USP10. human.
    GeneWikii USP10.
    GenomeRNAii 9100.
    NextBioi 34113.
    PROi Q14694.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q14694.
    Bgeei Q14694.
    CleanExi HS_USP10.
    Genevestigatori Q14694.

    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. "Ras-GAP SH3 domain binding protein (G3BP) is a modulator of USP10, a novel human ubiquitin specific protease."
      Soncini C., Berdo I., Draetta G.
      Oncogene 20:3869-3879(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, INTERACTION WITH G3BP, MUTAGENESIS OF CYS-424.
    2. "Prediction of the coding sequences of unidentified human genes. V. The coding sequences of 40 new genes (KIAA0161-KIAA0200) deduced by analysis of cDNA clones from human cell line KG-1."
      Nagase T., Seki N., Ishikawa K., Tanaka A., Nomura N.
      DNA Res. 3:17-24(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Bone marrow.
    3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
      Tissue: Brain and Placenta.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT VAL-200.
      Tissue: Melanoma and Retina.
    5. "The sequence and analysis of duplication-rich human chromosome 16."
      Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.
      , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
      Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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), VARIANTS PRO-203 AND LEU-204.
      Tissue: Brain.
    7. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-576, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    8. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
      Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
      Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-365 AND SER-370, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    9. "Toward a global characterization of the phosphoproteome in prostate cancer cells: identification of phosphoproteins in the LNCaP cell line."
      Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S.
      Electrophoresis 28:2027-2034(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-576, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Prostate cancer.
    10. "Quantitative phosphoproteome profiling of Wnt3a-mediated signaling network: indicating the involvement of ribonucleoside-diphosphate reductase M2 subunit phosphorylation at residue serine 20 in canonical Wnt signal transduction."
      Tang L.-Y., Deng N., Wang L.-S., Dai J., Wang Z.-L., Jiang X.-S., Li S.-J., Li L., Sheng Q.-H., Wu D.-Q., Li L., Zeng R.
      Mol. Cell. Proteomics 6:1952-1967(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-576, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic kidney.
    11. "Vasopressin-inducible ubiquitin-specific protease 10 increases ENaC cell surface expression by deubiquitylating and stabilizing sorting nexin 3."
      Boulkroun S., Ruffieux-Daidie D., Vitagliano J.J., Poirot O., Charles R.P., Lagnaz D., Firsov D., Kellenberger S., Staub O.
      Am. J. Physiol. 295:F889-F900(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH SNX3.
    12. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-100; SER-226 AND SER-370, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. "Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography."
      Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J.
      Proteomics 8:1346-1361(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-576, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    14. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. "The deubiquitinating enzyme USP10 regulates the post-endocytic sorting of cystic fibrosis transmembrane conductance regulator in airway epithelial cells."
      Bomberger J.M., Barnaby R.L., Stanton B.A.
      J. Biol. Chem. 284:18778-18789(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH CFTR, MUTAGENESIS OF CYS-424.
    16. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-563 AND SER-576, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    17. "USP10 regulates p53 localization and stability by deubiquitinating p53."
      Yuan J., Luo K., Zhang L., Cheville J.C., Lou Z.
      Cell 140:384-396(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, INDUCTION, INTERACTION WITH TP53, PHOSPHORYLATION AT THR-42 AND SER-337, MUTAGENESIS OF THR-42 AND SER-337.
    18. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-24; SER-365; SER-370 AND SER-576, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    19. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    20. "Beclin1 controls the levels of p53 by regulating the deubiquitination activity of USP10 and USP13."
      Liu J., Xia H., Kim M., Xu L., Li Y., Zhang L., Cai Y., Norberg H.V., Zhang T., Furuya T., Jin M., Zhu Z., Wang H., Yu J., Li Y., Hao Y., Choi A., Ke H., Ma D., Yuan J.
      Cell 147:223-234(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, ENZYME REGULATION, UBIQUITINATION, MUTAGENESIS OF CYS-424.
    21. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-576, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiUBP10_HUMAN
    AccessioniPrimary (citable) accession number: Q14694
    Secondary accession number(s): B2RDJ8
    , B4DS84, Q9BWG7, Q9NSL7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: November 1, 1997
    Last modified: October 1, 2014
    This is version 142 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 16
      Human chromosome 16: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. Peptidase families
      Classification of peptidase families and list of entries
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3