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Ubiquitin carboxyl-terminal hydrolase 10 (EC 3.4.19.12) (Deubiquitinating enzyme 10) (Ubiquitin thioesterase 10) (Ubiquitin-specific-processing protease 10)

 UBP10_HUMAN             Reviewed;         798 AA.
Q14694; B2RDJ8; B4DS84; Q9BWG7; Q9NSL7;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
01-NOV-1997, sequence version 2.
22-NOV-2017, entry version 174.
RecName: Full=Ubiquitin carboxyl-terminal hydrolase 10;
EC=3.4.19.12 {ECO:0000269|PubMed:20096447};
AltName: Full=Deubiquitinating enzyme 10;
AltName: Full=Ubiquitin thioesterase 10;
AltName: Full=Ubiquitin-specific-processing protease 10;
Name=USP10; Synonyms=KIAA0190;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY,
INTERACTION WITH G3BP, AND MUTAGENESIS OF CYS-424.
PubMed=11439350; DOI=10.1038/sj.onc.1204553;
Soncini C., Berdo I., Draetta G.;
"Ras-GAP SH3 domain binding protein (G3BP) is a modulator of USP10, a
novel human ubiquitin specific protease.";
Oncogene 20:3869-3879(2001).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Bone marrow;
PubMed=8724849; DOI=10.1093/dnares/3.1.17;
Nagase T., Seki N., Ishikawa K., Tanaka A., Nomura N.;
"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.";
DNA Res. 3:17-24(1996).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
TISSUE=Brain, and Placenta;
PubMed=14702039; DOI=10.1038/ng1285;
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
VAL-200.
TISSUE=Melanoma, and Retina;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
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.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15616553; DOI=10.1038/nature03187;
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.;
"The sequence and analysis of duplication-rich human chromosome 16.";
Nature 432:988-994(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS
PRO-203 AND LEU-204.
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-576, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-365 AND SER-370, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=16964243; DOI=10.1038/nbt1240;
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
"A probability-based approach for high-throughput protein
phosphorylation analysis and site localization.";
Nat. Biotechnol. 24:1285-1292(2006).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-576, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Prostate cancer;
PubMed=17487921; DOI=10.1002/elps.200600782;
Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S.;
"Toward a global characterization of the phosphoproteome in prostate
cancer cells: identification of phosphoproteins in the LNCaP cell
line.";
Electrophoresis 28:2027-2034(2007).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-576, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic kidney;
PubMed=17693683; DOI=10.1074/mcp.M700120-MCP200;
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.;
"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.";
Mol. Cell. Proteomics 6:1952-1967(2007).
[11]
FUNCTION, AND INTERACTION WITH SNX3.
PubMed=18632802; DOI=10.1152/ajprenal.00001.2008;
Boulkroun S., Ruffieux-Daidie D., Vitagliano J.J., Poirot O.,
Charles R.P., Lagnaz D., Firsov D., Kellenberger S., Staub O.;
"Vasopressin-inducible ubiquitin-specific protease 10 increases ENaC
cell surface expression by deubiquitylating and stabilizing sorting
nexin 3.";
Am. J. Physiol. 295:F889-F900(2008).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-100; SER-226 AND
SER-370, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-576, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=18318008; DOI=10.1002/pmic.200700884;
Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,
Zou H., Gu J.;
"Large-scale phosphoproteome analysis of human liver tissue by
enrichment and fractionation of phosphopeptides with strong anion
exchange chromatography.";
Proteomics 8:1346-1361(2008).
[14]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[15]
FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH CFTR, AND MUTAGENESIS
OF CYS-424.
PubMed=19398555; DOI=10.1074/jbc.M109.001685;
Bomberger J.M., Barnaby R.L., Stanton B.A.;
"The deubiquitinating enzyme USP10 regulates the post-endocytic
sorting of cystic fibrosis transmembrane conductance regulator in
airway epithelial cells.";
J. Biol. Chem. 284:18778-18789(2009).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-563 AND SER-576, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[17]
FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, INDUCTION,
INTERACTION WITH TP53, PHOSPHORYLATION AT THR-42 AND SER-337, AND
MUTAGENESIS OF THR-42 AND SER-337.
PubMed=20096447; DOI=10.1016/j.cell.2009.12.032;
Yuan J., Luo K., Zhang L., Cheville J.C., Lou Z.;
"USP10 regulates p53 localization and stability by deubiquitinating
p53.";
Cell 140:384-396(2010).
[18]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE
SCALE ANALYSIS] AT THR-24; SER-365; SER-370 AND SER-576, CLEAVAGE OF
INITIATOR METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
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.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[19]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[20]
FUNCTION, ENZYME REGULATION, UBIQUITINATION, AND MUTAGENESIS OF
CYS-424.
PubMed=21962518; DOI=10.1016/j.cell.2011.08.037;
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.;
"Beclin1 controls the levels of p53 by regulating the deubiquitination
activity of USP10 and USP13.";
Cell 147:223-234(2011).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-576, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[22]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-370; SER-547 AND
SER-576, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[23]
FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH TBX21, AND
MUTAGENESIS OF CYS-424.
PubMed=24845384; DOI=10.1016/j.bbrc.2014.05.037;
Pan L., Chen Z., Wang L., Chen C., Li D., Wan H., Li B., Shi G.;
"Deubiquitination and stabilization of T-bet by USP10.";
Biochem. Biophys. Res. Commun. 449:289-294(2014).
[24]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-321 AND SER-365, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[25]
FUNCTION, IDENTIFICATION IN A DEUBIQUITINATION COMPLEX WITH TANK AND
ZC3H12A, AND INTERACTION WITH IKBKG; TANK; TRAF6 AND ZC3H12A.
PubMed=25861989; DOI=10.1074/jbc.M115.643767;
Wang W., Huang X., Xin H.B., Fu M., Xue A., Wu Z.H.;
"TRAF family member-associated NF-kappaB activator (TANK) inhibits
genotoxic nuclear factor kappaB activation by facilitating
deubiquitinase USP10-dependent deubiquitination of TRAF6 ligase.";
J. Biol. Chem. 290:13372-13385(2015).
-!- 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. Involved in a TANK-dependent
negative feedback response to attenuate NF-kappaB activation via
deubiquitinating IKBKG or TRAF6 in response to interleukin-1-beta
(IL1B) stimulation or upon DNA damage (PubMed:25861989).
Deubiquitinates TBX21 leading to its stabilization
(PubMed:24845384). {ECO:0000269|PubMed:11439350,
ECO:0000269|PubMed:18632802, ECO:0000269|PubMed:19398555,
ECO:0000269|PubMed:20096447, ECO:0000269|PubMed:21962518,
ECO:0000269|PubMed:24845384, ECO:0000269|PubMed:25861989}.
-!- 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).
{ECO:0000269|PubMed:20096447}.
-!- 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. {ECO:0000269|PubMed:21962518}.
-!- SUBUNIT: Found in a deubiquitination complex with TANK, USP10 and
ZC3H12A; this complex inhibits genotoxic stress- or interleukin-1-
beta (IL1B)-mediated NF-kappaB activation by promoting IKBKG or
TRAF6 deubiquitination (PubMed:25861989). Interacts with IKBKG;
this interaction increases in response to DNA damage
(PubMed:25861989). Interacts with TANK; this interaction increases
in response to DNA damage (PubMed:25861989). Interacts with TRAF6;
this interaction increases in response to DNA damage
(PubMed:25861989). Interacts with ZC3H12A; this interaction
increases in response to DNA damage (PubMed:25861989). Interacts
with G3BP, which may regulate its function (PubMed:11439350).
Interacts with p53/TP53 (PubMed:20096447). Interacts with SNX3
(PubMed:18632802). Interacts with CFTR (PubMed:19398555).
Interacts with TBX21 (PubMed:24845384).
{ECO:0000269|PubMed:11439350, ECO:0000269|PubMed:18632802,
ECO:0000269|PubMed:19398555, ECO:0000269|PubMed:20096447,
ECO:0000269|PubMed:24845384, ECO:0000269|PubMed:25861989}.
-!- INTERACTION:
Q13283:G3BP1; NbExp=4; IntAct=EBI-2510389, EBI-1047359;
Q9UN86:G3BP2; NbExp=5; IntAct=EBI-2510389, EBI-1044298;
Q5D1E8:ZC3H12A; NbExp=5; IntAct=EBI-2510389, EBI-747793;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:20096447}.
Nucleus {ECO:0000269|PubMed:20096447,
ECO:0000269|PubMed:24845384}. Early endosome
{ECO:0000269|PubMed:19398555}. Note=Cytoplasmic in normal
conditions (PubMed:20096447). After DNA damage, translocates to
the nucleus following phosphorylation by ATM (PubMed:20096447).
{ECO:0000269|PubMed:20096447}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q14694-1; Sequence=Displayed;
Name=2;
IsoId=Q14694-2; Sequence=VSP_038869;
Name=3;
IsoId=Q14694-3; Sequence=VSP_038868;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Widely expressed.
{ECO:0000269|PubMed:11439350}.
-!- INDUCTION: Following DNA damage. Down-regulated in renal cell
carcinomas. {ECO:0000269|PubMed:20096447}.
-!- PTM: Phosphorylated by ATM following DNA damage, leading to
stablization and translocation it to the nucleus.
{ECO:0000269|PubMed:20096447}.
-!- PTM: Ubiquitinated. Deubiquitinated by USP13.
{ECO:0000269|PubMed:21962518}.
-!- SIMILARITY: Belongs to the peptidase C19 family. USP10 subfamily.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=CAD97644.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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EMBL; D80012; BAA11507.1; -; mRNA.
EMBL; AK299618; BAG61546.1; -; mRNA.
EMBL; AK315570; BAG37945.1; -; mRNA.
EMBL; AL162049; CAB82392.2; -; mRNA.
EMBL; BX537402; CAD97644.1; ALT_INIT; mRNA.
EMBL; AC009116; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC025280; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC000263; AAH00263.1; -; mRNA.
CCDS; CCDS45537.1; -. [Q14694-1]
CCDS; CCDS62004.1; -. [Q14694-3]
RefSeq; NP_001259004.1; NM_001272075.1. [Q14694-3]
RefSeq; NP_005144.2; NM_005153.2. [Q14694-1]
UniGene; Hs.136778; -.
ProteinModelPortal; Q14694; -.
BioGrid; 114554; 64.
ELM; Q14694; -.
IntAct; Q14694; 29.
MINT; MINT-3030173; -.
STRING; 9606.ENSP00000219473; -.
BindingDB; Q14694; -.
ChEMBL; CHEMBL3407323; -.
MEROPS; C19.018; -.
iPTMnet; Q14694; -.
PhosphoSitePlus; Q14694; -.
BioMuta; USP10; -.
DMDM; 2501458; -.
EPD; Q14694; -.
MaxQB; Q14694; -.
PaxDb; Q14694; -.
PeptideAtlas; Q14694; -.
PRIDE; Q14694; -.
DNASU; 9100; -.
Ensembl; ENST00000219473; ENSP00000219473; ENSG00000103194. [Q14694-1]
Ensembl; ENST00000570191; ENSP00000457411; ENSG00000103194. [Q14694-3]
GeneID; 9100; -.
KEGG; hsa:9100; -.
UCSC; uc002fii.4; human. [Q14694-1]
CTD; 9100; -.
DisGeNET; 9100; -.
EuPathDB; HostDB:ENSG00000103194.15; -.
GeneCards; USP10; -.
H-InvDB; HIX0173245; -.
HGNC; HGNC:12608; USP10.
HPA; HPA006731; -.
HPA; HPA006749; -.
MIM; 609818; gene.
neXtProt; NX_Q14694; -.
OpenTargets; ENSG00000103194; -.
PharmGKB; PA37234; -.
eggNOG; KOG1871; Eukaryota.
eggNOG; ENOG410XSIH; LUCA.
GeneTree; ENSGT00550000074994; -.
HOGENOM; HOG000285959; -.
HOVERGEN; HBG059823; -.
InParanoid; Q14694; -.
KO; K11841; -.
OMA; PEFILGC; -.
OrthoDB; EOG091G023X; -.
PhylomeDB; Q14694; -.
TreeFam; TF323203; -.
Reactome; R-HSA-5656169; Termination of translesion DNA synthesis.
Reactome; R-HSA-5689880; Ub-specific processing proteases.
ChiTaRS; USP10; human.
GeneWiki; USP10; -.
GenomeRNAi; 9100; -.
PRO; PR:Q14694; -.
Proteomes; UP000005640; Chromosome 16.
Bgee; ENSG00000103194; -.
CleanEx; HS_USP10; -.
ExpressionAtlas; Q14694; baseline and differential.
Genevisible; Q14694; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0005769; C:early endosome; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0043234; C:protein complex; IDA:UniProtKB.
GO; GO:0004197; F:cysteine-type endopeptidase activity; IMP:UniProtKB.
GO; GO:0044325; F:ion channel binding; IDA:UniProtKB.
GO; GO:0002039; F:p53 binding; IPI:UniProtKB.
GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
GO; GO:0004843; F:thiol-dependent ubiquitin-specific protease activity; IDA:UniProtKB.
GO; GO:0036459; F:thiol-dependent ubiquitinyl hydrolase activity; IDA:UniProtKB.
GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
GO; GO:0006974; P:cellular response to DNA damage stimulus; IMP:UniProtKB.
GO; GO:0071347; P:cellular response to interleukin-1; IMP:UniProtKB.
GO; GO:0030330; P:DNA damage response, signal transduction by p53 class mediator; IMP:UniProtKB.
GO; GO:0043124; P:negative regulation of I-kappaB kinase/NF-kappaB signaling; IMP:UniProtKB.
GO; GO:0016579; P:protein deubiquitination; IDA:UniProtKB.
GO; GO:0010506; P:regulation of autophagy; IDA:UniProtKB.
GO; GO:0019985; P:translesion synthesis; TAS:Reactome.
GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
InterPro; IPR009818; Ataxin-2_C.
InterPro; IPR001394; Peptidase_C19_UCH.
InterPro; IPR018200; USP_CS.
InterPro; IPR028889; USP_dom.
Pfam; PF07145; PAM2; 1.
Pfam; PF00443; UCH; 1.
PROSITE; PS00972; USP_1; 1.
PROSITE; PS00973; USP_2; 1.
PROSITE; PS50235; USP_3; 1.
1: Evidence at protein level;
Acetylation; Alternative splicing; Autophagy; Complete proteome;
Cytoplasm; DNA damage; DNA repair; Endosome; Hydrolase; Nucleus;
Phosphoprotein; Polymorphism; Protease; Reference proteome;
Thiol protease; Ubl conjugation; Ubl conjugation pathway.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:20068231}.
CHAIN 2 798 Ubiquitin carboxyl-terminal hydrolase 10.
/FTId=PRO_0000080629.
DOMAIN 415 795 USP.
REGION 2 100 Interaction with p53/TP53.
{ECO:0000269|PubMed:20096447}.
ACT_SITE 424 424 Nucleophile.
ACT_SITE 749 749 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU10092, ECO:0000255|PROSITE-
ProRule:PRU10093}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 24 24 Phosphothreonine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 42 42 Phosphothreonine; by ATM.
{ECO:0000269|PubMed:20096447}.
MOD_RES 100 100 Phosphothreonine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 211 211 Phosphoserine.
{ECO:0000250|UniProtKB:P52479}.
MOD_RES 226 226 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 321 321 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 337 337 Phosphoserine; by ATM.
{ECO:0000269|PubMed:20096447}.
MOD_RES 365 365 Phosphoserine.
{ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:24275569}.
MOD_RES 370 370 Phosphoserine.
{ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 547 547 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 563 563 Phosphoserine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 576 576 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:17487921,
ECO:0000244|PubMed:17693683,
ECO:0000244|PubMed:18318008,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
VAR_SEQ 1 6 MALHSP -> MPWLPSPGIG (in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_038868.
VAR_SEQ 1 1 M -> MCSKDTVLSVCALYWRKGIQSHTPLIGAWRRGKQRE
QPEDRGVPMKRAA (in isoform 2).
{ECO:0000303|PubMed:8724849}.
/FTId=VSP_038869.
VARIANT 200 200 M -> V (in dbSNP:rs1862792).
{ECO:0000269|PubMed:17974005}.
/FTId=VAR_015859.
VARIANT 203 203 S -> P (in dbSNP:rs2326391).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_015860.
VARIANT 204 204 V -> L (in dbSNP:rs1812061).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_015861.
MUTAGEN 42 42 T->A: Abolishes phosphorylation by ATM;
when associated with A-337.
{ECO:0000269|PubMed:20096447}.
MUTAGEN 42 42 T->E: Phospho-mimetic mutant that
translocates to the nucleus in absence of
genotoxic stress; when associated with D-
337. {ECO:0000269|PubMed:20096447}.
MUTAGEN 337 337 S->A: Abolishes phosphorylation by ATM;
when associated with A-42.
{ECO:0000269|PubMed:20096447}.
MUTAGEN 337 337 S->D: Phospho-mimetic mutant that
translocates to the nucleus in absence of
genotoxic stress; when associated with E-
42. {ECO:0000269|PubMed:20096447}.
MUTAGEN 424 424 C->A: Abolishes de-ubiquitinating
activity. {ECO:0000269|PubMed:11439350,
ECO:0000269|PubMed:19398555,
ECO:0000269|PubMed:21962518,
ECO:0000269|PubMed:24845384}.
CONFLICT 108 108 A -> V (in Ref. 3; BAG61546).
{ECO:0000305}.
CONFLICT 263 263 T -> A (in Ref. 3; BAG61546).
{ECO:0000305}.
SEQUENCE 798 AA; 87134 MW; E6BA77E2B5CE2B3F CRC64;
MALHSPQYIF GDFSPDEFNQ FFVTPRSSVE LPPYSGTVLC GTQAVDKLPD GQEYQRIEFG
VDEVIEPSDT LPRTPSYSIS STLNPQAPEF ILGCTASKIT PDGITKEASY GSIDCQYPGS
ALALDGSSNV EAEVLENDGV SGGLGQRERK KKKKRPPGYY SYLKDGGDDS ISTEALVNGH
ANSAVPNSVS AEDAEFMGDM PPSVTPRTCN SPQNSTDSVS DIVPDSPFPG ALGSDTRTAG
QPEGGPGADF GQSCFPAEAG RDTLSRTAGA QPCVGTDTTE NLGVANGQIL ESSGEGTATN
GVELHTTESI DLDPTKPESA SPPADGTGSA SGTLPVSQPK SWASLFHDSK PSSSSPVAYV
ETKYSPPAIS PLVSEKQVEV KEGLVPVSED PVAIKIAELL ENVTLIHKPV SLQPRGLINK
GNWCYINATL QALVACPPMY HLMKFIPLYS KVQRPCTSTP MIDSFVRLMN EFTNMPVPPK
PRQALGDKIV RDIRPGAAFE PTYIYRLLTV NKSSLSEKGR QEDAEEYLGF ILNGLHEEML
NLKKLLSPSN EKLTISNGPK NHSVNEEEQE EQGEGSEDEW EQVGPRNKTS VTRQADFVQT
PITGIFGGHI RSVVYQQSSK ESATLQPFFT LQLDIQSDKI RTVQDALESL VARESVQGYT
TKTKQEVEIS RRVTLEKLPP VLVLHLKRFV YEKTGGCQKL IKNIEYPVDL EISKELLSPG
VKNKNFKCHR TYRLFAVVYH HGNSATGGHY TTDVFQIGLN GWLRIDDQTV KVINQYQVVK
PTAERTAYLL YYRRVDLL


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