Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q14694 (UBP10_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 136. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:USP10
Synonyms:KIAA0190
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length798 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.1 Ref.11 Ref.15 Ref.17 Ref.20

Catalytic activity

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). Ref.17

Enzyme regulation

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. Ref.20

Subunit structure

Interacts with G3BP, which may regulate its function. Interacts with p53/TP53, SNX3 and CFTR. Ref.1 Ref.11 Ref.15 Ref.17

Subcellular location

Cytoplasm. Nucleus. Early endosome. Note: Cytoplasmic in normal conditions. After DNA damage, translocates to the nucleus following phosphorylation by ATM. Ref.15 Ref.17

Tissue specificity

Widely expressed. Ref.1

Induction

Following DNA damage. Down-regulated in renal cell carcinomas. Ref.17 Ref.20

Post-translational modification

Phosphorylated by ATM following DNA damage, leading to stablization and translocation it to the nucleus. Ref.17

Ubiquitinated. Deubiquitinated by USP13. Ref.20

Sequence similarities

Belongs to the peptidase C19 family. USP10 subfamily.

Contains 1 USP domain.

Sequence caution

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

Ontologies

Keywords
   Biological processAutophagy
DNA damage
DNA repair
Ubl conjugation pathway
   Cellular componentCytoplasm
Endosome
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   Molecular functionHydrolase
Protease
Thiol protease
   PTMAcetylation
Phosphoprotein
Ubl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processDNA damage response, signal transduction by p53 class mediator

Inferred from mutant phenotype Ref.17. Source: UniProtKB

DNA repair

Inferred from electronic annotation. Source: UniProtKB-KW

autophagy

Inferred from electronic annotation. Source: UniProtKB-KW

protein deubiquitination

Inferred from direct assay Ref.17. Source: UniProtKB

regulation of autophagy

Inferred from direct assay Ref.20. Source: UniProtKB

ubiquitin-dependent protein catabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular_componentearly endosome

Inferred from direct assay Ref.15. Source: UniProtKB

intermediate filament cytoskeleton

Inferred from direct assay. Source: HPA

nucleus

Inferred from direct assay Ref.17. Source: UniProtKB

   Molecular_functioncysteine-type endopeptidase activity

Inferred from mutant phenotype Ref.20. Source: UniProtKB

ion channel binding

Inferred from direct assay Ref.15. Source: UniProtKB

ubiquitin thiolesterase activity

Inferred from direct assay Ref.20. Source: UniProtKB

ubiquitin-specific protease activity

Inferred from direct assay Ref.17Ref.20. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q14694-1)

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.
Isoform 2 (identifier: Q14694-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MCSKDTVLSVCALYWRKGIQSHTPLIGAWRRGKQREQPEDRGVPMKRAA
Isoform 3 (identifier: Q14694-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-6: MALHSP → MPWLPSPGIG
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.18
Chain2 – 798797Ubiquitin carboxyl-terminal hydrolase 10
PRO_0000080629

Regions

Domain415 – 795381USP
Region2 – 10099Interaction with p53/TP53

Sites

Active site4241Nucleophile
Active site7491Proton acceptor By similarity

Amino acid modifications

Modified residue21N-acetylalanine Ref.18
Modified residue241Phosphothreonine Ref.18
Modified residue421Phosphothreonine; by ATM Ref.17
Modified residue1001Phosphothreonine Ref.12
Modified residue2261Phosphoserine Ref.12
Modified residue3371Phosphoserine; by ATM Ref.17
Modified residue3651Phosphoserine Ref.8 Ref.18
Modified residue3701Phosphoserine Ref.8 Ref.12 Ref.18
Modified residue5631Phosphoserine Ref.16
Modified residue5761Phosphoserine Ref.7 Ref.9 Ref.10 Ref.13 Ref.16 Ref.18 Ref.21

Natural variations

Alternative sequence1 – 66MALHSP → MPWLPSPGIG in isoform 3.
VSP_038868
Alternative sequence11M → MCSKDTVLSVCALYWRKGIQ SHTPLIGAWRRGKQREQPED RGVPMKRAA in isoform 2.
VSP_038869
Natural variant2001M → V. Ref.4
Corresponds to variant rs1862792 [ dbSNP | Ensembl ].
VAR_015859
Natural variant2031S → P. Ref.6
Corresponds to variant rs2326391 [ dbSNP | Ensembl ].
VAR_015860
Natural variant2041V → L. Ref.6
Corresponds to variant rs1812061 [ dbSNP | Ensembl ].
VAR_015861

Experimental info

Mutagenesis421T → A: Abolishes phosphorylation by ATM; when associated with A-337. Ref.17
Mutagenesis421T → E: Phospho-mimetic mutant that translocates to the nucleus in absence of genotoxic stress; when associated with D-337. Ref.17
Mutagenesis3371S → A: Abolishes phosphorylation by ATM; when associated with A-42. Ref.17
Mutagenesis3371S → D: Phospho-mimetic mutant that translocates to the nucleus in absence of genotoxic stress; when associated with E-42. Ref.17
Mutagenesis4241C → A: Abolishes de-ubiquitinating activity. Ref.1 Ref.15 Ref.20
Sequence conflict1081A → V in BAG61546. Ref.3
Sequence conflict2631T → A in BAG61546. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 1, 1997. Version 2.
Checksum: E6BA77E2B5CE2B3F

FASTA79887,134
        10         20         30         40         50         60 
MALHSPQYIF GDFSPDEFNQ FFVTPRSSVE LPPYSGTVLC GTQAVDKLPD GQEYQRIEFG 

        70         80         90        100        110        120 
VDEVIEPSDT LPRTPSYSIS STLNPQAPEF ILGCTASKIT PDGITKEASY GSIDCQYPGS 

       130        140        150        160        170        180 
ALALDGSSNV EAEVLENDGV SGGLGQRERK KKKKRPPGYY SYLKDGGDDS ISTEALVNGH 

       190        200        210        220        230        240 
ANSAVPNSVS AEDAEFMGDM PPSVTPRTCN SPQNSTDSVS DIVPDSPFPG ALGSDTRTAG 

       250        260        270        280        290        300 
QPEGGPGADF GQSCFPAEAG RDTLSRTAGA QPCVGTDTTE NLGVANGQIL ESSGEGTATN 

       310        320        330        340        350        360 
GVELHTTESI DLDPTKPESA SPPADGTGSA SGTLPVSQPK SWASLFHDSK PSSSSPVAYV 

       370        380        390        400        410        420 
ETKYSPPAIS PLVSEKQVEV KEGLVPVSED PVAIKIAELL ENVTLIHKPV SLQPRGLINK 

       430        440        450        460        470        480 
GNWCYINATL QALVACPPMY HLMKFIPLYS KVQRPCTSTP MIDSFVRLMN EFTNMPVPPK 

       490        500        510        520        530        540 
PRQALGDKIV RDIRPGAAFE PTYIYRLLTV NKSSLSEKGR QEDAEEYLGF ILNGLHEEML 

       550        560        570        580        590        600 
NLKKLLSPSN EKLTISNGPK NHSVNEEEQE EQGEGSEDEW EQVGPRNKTS VTRQADFVQT 

       610        620        630        640        650        660 
PITGIFGGHI RSVVYQQSSK ESATLQPFFT LQLDIQSDKI RTVQDALESL VARESVQGYT 

       670        680        690        700        710        720 
TKTKQEVEIS RRVTLEKLPP VLVLHLKRFV YEKTGGCQKL IKNIEYPVDL EISKELLSPG 

       730        740        750        760        770        780 
VKNKNFKCHR TYRLFAVVYH HGNSATGGHY TTDVFQIGLN GWLRIDDQTV KVINQYQVVK 

       790 
PTAERTAYLL YYRRVDLL 

« Hide

Isoform 2 [UniParc].

Checksum: 01C2CD6FC3709AE4
Show »

FASTA84692,597
Isoform 3 [UniParc].

Checksum: CBA33D0F268AEF5A
Show »

FASTA80287,533

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_001259004.1. NM_001272075.1.
NP_005144.2. NM_005153.2.
UniGeneHs.136778.

3D structure databases

ProteinModelPortalQ14694.
SMRQ14694. Positions 416-796.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114554. 29 interactions.
IntActQ14694. 14 interactions.
MINTMINT-3030173.
STRING9606.ENSP00000219473.

Protein family/group databases

MEROPSC19.018.

PTM databases

PhosphoSiteQ14694.

Polymorphism databases

DMDM2501458.

Proteomic databases

PaxDbQ14694.
PRIDEQ14694.

Protocols and materials databases

DNASU9100.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000219473; ENSP00000219473; ENSG00000103194. [Q14694-1]
ENST00000570191; ENSP00000457411; ENSG00000103194. [Q14694-3]
GeneID9100.
KEGGhsa:9100.
UCSCuc002fii.3. human. [Q14694-1]
uc010voe.2. human. [Q14694-3]

Organism-specific databases

CTD9100.
GeneCardsGC16P084734.
H-InvDBHIX0173245.
HGNCHGNC:12608. USP10.
HPAHPA006731.
HPA006749.
MIM609818. gene.
neXtProtNX_Q14694.
PharmGKBPA37234.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5533.
HOGENOMHOG000285959.
HOVERGENHBG059823.
InParanoidQ14694.
KOK11841.
OMAGQEYQRI.
OrthoDBEOG7Z69BX.
TreeFamTF323203.

Gene expression databases

ArrayExpressQ14694.
BgeeQ14694.
CleanExHS_USP10.
GenevestigatorQ14694.

Family and domain databases

InterProIPR018200. Pept_C19ubi-hydrolase_C_CS.
IPR001394. Peptidase_C19_UCH.
IPR028889. UCH/PAN2.
IPR028767. USP10.
[Graphical view]
PANTHERPTHR24006:SF69. PTHR24006:SF69. 1 hit.
PfamPF00443. UCH. 1 hit.
[Graphical view]
PROSITEPS00972. USP_1. 1 hit.
PS00973. USP_2. 1 hit.
PS50235. USP_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSUSP10. human.
GeneWikiUSP10.
GenomeRNAi9100.
NextBio34113.
PROQ14694.
SOURCESearch...

Entry information

Entry nameUBP10_HUMAN
AccessionPrimary (citable) accession number: Q14694
Secondary accession number(s): B2RDJ8 expand/collapse secondary AC list , B4DS84, Q9BWG7, Q9NSL7
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: March 19, 2014
This is version 136 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 16

Human chromosome 16: entries, gene names and cross-references to MIM