ID UBP10_HUMAN Reviewed; 798 AA. AC Q14694; B2RDJ8; B4DS84; Q9BWG7; Q9NSL7; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 2. DT 28-JAN-2026, entry version 224. DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase 10 {ECO:0000305}; DE EC=3.4.19.12 {ECO:0000269|PubMed:20096447, ECO:0000269|PubMed:21962518, ECO:0000269|PubMed:32011234, ECO:0000269|PubMed:34469731}; DE AltName: Full=Deubiquitinating enzyme 10; DE AltName: Full=Ubiquitin thioesterase 10; DE AltName: Full=Ubiquitin-specific-processing protease 10; GN Name=USP10 {ECO:0000303|PubMed:11439350, ECO:0000312|HGNC:HGNC:12608}; GN Synonyms=KIAA0190 {ECO:0000303|PubMed:8724849}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), ACTIVE SITE, TISSUE SPECIFICITY, RP INTERACTION WITH G3BP, AND MUTAGENESIS OF CYS-424. RX PubMed=11439350; DOI=10.1038/sj.onc.1204553; RA Soncini C., Berdo I., Draetta G.; RT "Ras-GAP SH3 domain binding protein (G3BP) is a modulator of USP10, a novel RT human ubiquitin specific protease."; RL Oncogene 20:3869-3879(2001). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Bone marrow; RX PubMed=8724849; DOI=10.1093/dnares/3.1.17; RA Nagase T., Seki N., Ishikawa K., Tanaka A., Nomura N.; RT "Prediction of the coding sequences of unidentified human genes. V. The RT coding sequences of 40 new genes (KIAA0161-KIAA0200) deduced by analysis of RT cDNA clones from human cell line KG-1."; RL DNA Res. 3:17-24(1996). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3). RC TISSUE=Brain, and Placenta; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT VAL-200. RC TISSUE=Melanoma, and Retina; RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., RA Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15616553; DOI=10.1038/nature03187; RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M., RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., RA Myers R.M., Rubin E.M., Pennacchio L.A.; RT "The sequence and analysis of duplication-rich human chromosome 16."; RL Nature 432:988-994(2004). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS PRO-203 RP AND LEU-204. RC TISSUE=Brain; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-576, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026; RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling RT networks."; RL Cell 127:635-648(2006). RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-365 AND SER-370, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=16964243; DOI=10.1038/nbt1240; RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.; RT "A probability-based approach for high-throughput protein phosphorylation RT analysis and site localization."; RL Nat. Biotechnol. 24:1285-1292(2006). RN [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-576, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Prostate cancer; RX PubMed=17487921; DOI=10.1002/elps.200600782; RA Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S.; RT "Toward a global characterization of the phosphoproteome in prostate cancer RT cells: identification of phosphoproteins in the LNCaP cell line."; RL Electrophoresis 28:2027-2034(2007). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-576, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Embryonic kidney; RX PubMed=17693683; DOI=10.1074/mcp.m700120-mcp200; RA Tang L.-Y., Deng N., Wang L.-S., Dai J., Wang Z.-L., Jiang X.-S., Li S.-J., RA Li L., Sheng Q.-H., Wu D.-Q., Li L., Zeng R.; RT "Quantitative phosphoproteome profiling of Wnt3a-mediated signaling RT network: indicating the involvement of ribonucleoside-diphosphate reductase RT M2 subunit phosphorylation at residue serine 20 in canonical Wnt signal RT transduction."; RL Mol. Cell. Proteomics 6:1952-1967(2007). RN [11] RP FUNCTION. RX PubMed=18632802; DOI=10.1152/ajprenal.00001.2008; RA Boulkroun S., Ruffieux-Daidie D., Vitagliano J.J., Poirot O., Charles R.P., RA Lagnaz D., Firsov D., Kellenberger S., Staub O.; RT "Vasopressin-inducible ubiquitin-specific protease 10 increases ENaC cell RT surface expression by deubiquitylating and stabilizing sorting nexin 3."; RL Am. J. Physiol. 295:F889-F900(2008). RN [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-100; SER-226 AND SER-370, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-576, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=18318008; DOI=10.1002/pmic.200700884; RA Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., RA Zou H., Gu J.; RT "Large-scale phosphoproteome analysis of human liver tissue by enrichment RT and fractionation of phosphopeptides with strong anion exchange RT chromatography."; RL Proteomics 8:1346-1361(2008). RN [14] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [15] RP FUNCTION, ACTIVE SITE, SUBCELLULAR LOCATION, AND MUTAGENESIS OF CYS-424. RX PubMed=19398555; DOI=10.1074/jbc.m109.001685; RA Bomberger J.M., Barnaby R.L., Stanton B.A.; RT "The deubiquitinating enzyme USP10 regulates the post-endocytic sorting of RT cystic fibrosis transmembrane conductance regulator in airway epithelial RT cells."; RL J. Biol. Chem. 284:18778-18789(2009). RN [16] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-563 AND SER-576, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [17] RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, INDUCTION, RP PHOSPHORYLATION AT THR-42 AND SER-337, AND MUTAGENESIS OF THR-42 AND RP SER-337. RX PubMed=20096447; DOI=10.1016/j.cell.2009.12.032; RA Yuan J., Luo K., Zhang L., Cheville J.C., Lou Z.; RT "USP10 regulates p53 localization and stability by deubiquitinating p53."; RL Cell 140:384-396(2010). RN [18] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE RP ANALYSIS] AT THR-24; SER-365; SER-370 AND SER-576, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [19] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [20] RP FUNCTION, CATALYTIC ACTIVITY, ACTIVE SITE, ACTIVITY REGULATION, RP UBIQUITINATION, AND MUTAGENESIS OF CYS-424. RX PubMed=21962518; DOI=10.1016/j.cell.2011.08.037; RA Liu J., Xia H., Kim M., Xu L., Li Y., Zhang L., Cai Y., Norberg H.V., RA Zhang T., Furuya T., Jin M., Zhu Z., Wang H., Yu J., Li Y., Hao Y., RA Choi A., Ke H., Ma D., Yuan J.; RT "Beclin1 controls the levels of p53 by regulating the deubiquitination RT activity of USP10 and USP13."; RL Cell 147:223-234(2011). RN [21] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-576, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [22] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-370; SER-547 AND SER-576, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [23] RP INTERACTION WITH G3BP1 AND G3BP2. RX PubMed=23279204; DOI=10.1111/gtc.12023; RA Matsuki H., Takahashi M., Higuchi M., Makokha G.N., Oie M., Fujii M.; RT "Both G3BP1 and G3BP2 contribute to stress granule formation."; RL Genes Cells 18:135-146(2013). RN [24] RP FUNCTION, ACTIVE SITE, SUBCELLULAR LOCATION, AND MUTAGENESIS OF CYS-424. RX PubMed=24845384; DOI=10.1016/j.bbrc.2014.05.037; RA Pan L., Chen Z., Wang L., Chen C., Li D., Wan H., Li B., Shi G.; RT "Deubiquitination and stabilization of T-bet by USP10."; RL Biochem. Biophys. Res. Commun. 449:289-294(2014). RN [25] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-321 AND SER-365, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [26] RP FUNCTION, IDENTIFICATION IN A DEUBIQUITINATION COMPLEX WITH TANK AND RP ZC3H12A, AND INTERACTION WITH IKBKG; TANK; TRAF6 AND ZC3H12A. RX PubMed=25861989; DOI=10.1074/jbc.m115.643767; RA Wang W., Huang X., Xin H.B., Fu M., Xue A., Wu Z.H.; RT "TRAF family member-associated NF-kappaB activator (TANK) inhibits RT genotoxic nuclear factor kappaB activation by facilitating deubiquitinase RT USP10-dependent deubiquitination of TRAF6 ligase."; RL J. Biol. Chem. 290:13372-13385(2015). RN [27] RP FUNCTION, INTERACTION WITH G3BP1 AND G3BP2, AND MUTAGENESIS OF PHE-10. RX PubMed=27022092; DOI=10.1083/jcb.201508028; RA Kedersha N., Panas M.D., Achorn C.A., Lyons S., Tisdale S., Hickman T., RA Thomas M., Lieberman J., McInerney G.M., Ivanov P., Anderson P.; RT "G3BP-Caprin1-USP10 complexes mediate stress granule condensation and RT associate with 40S subunits."; RL J. Cell Biol. 212:845-860(2016). RN [28] RP FUNCTION, AND INTERACTION WITH G3BP1. RX PubMed=32302570; DOI=10.1016/j.cell.2020.03.050; RA Sanders D.W., Kedersha N., Lee D.S.W., Strom A.R., Drake V., Riback J.A., RA Bracha D., Eeftens J.M., Iwanicki A., Wang A., Wei M.T., Whitney G., RA Lyons S.M., Anderson P., Jacobs W.M., Ivanov P., Brangwynne C.P.; RT "Competing protein-RNA interaction networks control multiphase RT intracellular organization."; RL Cell 181:306-324(2020). RN [29] RP CATALYTIC ACTIVITY, ACTIVE SITE, AND MUTAGENESIS OF CYS-424. RX PubMed=32011234; DOI=10.7554/elife.54023; RA Garshott D.M., Sundaramoorthy E., Leonard M., Bennett E.J.; RT "Distinct regulatory ribosomal ubiquitylation events are reversible and RT hierarchically organized."; RL Elife 9:0-0(2020). RN [30] RP FUNCTION, CATALYTIC ACTIVITY, ACTIVE SITE, INTERACTION WITH G3BP1 AND RP G3BP2, AND MUTAGENESIS OF CYS-424. RX PubMed=31981475; DOI=10.1016/j.molcel.2019.12.024; RA Meyer C., Garzia A., Morozov P., Molina H., Tuschl T.; RT "The G3BP1-family-USP10 deubiquitinase complex rescues ubiquitinated 40S RT subunits of ribosomes stalled in translation from lysosomal degradation."; RL Mol. Cell 77:1193-1205(2020). RN [31] RP FUNCTION. RX PubMed=34348161; DOI=10.1016/j.celrep.2021.109468; RA Garzia A., Meyer C., Tuschl T.; RT "The E3 ubiquitin ligase RNF10 modifies 40S ribosomal subunits of ribosomes RT compromised in translation."; RL Cell Rep. 36:109468-109468(2021). RN [32] RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=34469731; DOI=10.1016/j.celrep.2021.109642; RA Garshott D.M., An H., Sundaramoorthy E., Leonard M., Vicary A., RA Harper J.W., Bennett E.J.; RT "iRQC, a surveillance pathway for 40S ribosomal quality control during mRNA RT translation initiation."; RL Cell Rep. 36:109642-109642(2021). RN [33] RP INTERACTION WITH G3BP1, AND MUTAGENESIS OF PHE-10; GLY-11; ASP-12 AND RP PHE-13. RX PubMed=36183834; DOI=10.1016/j.jbc.2022.102552; RA Sheehan C.T., Hampton T.H., Madden D.R.; RT "Tryptophan mutations in G3BP1 tune the stability of a cellular signaling RT hub by weakening transient interactions with Caprin1 and USP10."; RL J. Biol. Chem. 298:102552-102552(2022). RN [34] RP FUNCTION, MUTAGENESIS OF CYS-424, AND SUBCELLULAR LOCATION. RX PubMed=37582970; DOI=10.1038/s41423-023-01065-2; RA Liu F., Zhuang W., Song B., Yang Y., Liu J., Zheng Y., Liu B., Zheng J., RA Zhao W., Gao C.; RT "MAVS-loaded unanchored Lys63-linked polyubiquitin chains activate the RIG- RT I-MAVS signaling cascade."; RL Cell. Mol. Immunol. 0:0-0(2023). RN [35] RP X-RAY CRYSTALLOGRAPHY (2.46 ANGSTROMS) OF 6-21 IN COMPLEX WITH G3BP1, AND RP INTERACTION WITH G3BP1. RX PubMed=36279435; DOI=10.1073/pnas.2207975119; RA Song D., Kuang L., Yang L., Wang L., Li H., Li X., Zhu Z., Shi C., Zhu H., RA Gong W.; RT "Yin and yang regulation of stress granules by Caprin-1."; RL Proc. Natl. Acad. Sci. U.S.A. 119:e2207975119-e2207975119(2022). CC -!- FUNCTION: Hydrolase that can remove conjugated ubiquitin from target CC proteins such as p53/TP53, RPS2/us5, RPS3/us3, RPS10/eS10, BECN1, SNX3 CC and CFTR (PubMed:11439350, PubMed:18632802, PubMed:31981475). Acts as CC an essential regulator of p53/TP53 stability: in unstressed cells, CC specifically deubiquitinates p53/TP53 in the cytoplasm, leading to CC counteract MDM2 action and stabilize p53/TP53 (PubMed:20096447). CC Following DNA damage, translocates to the nucleus and deubiquitinates CC p53/TP53, leading to regulate the p53/TP53-dependent DNA damage CC response (PubMed:20096447). Component of a regulatory loop that CC controls autophagy and p53/TP53 levels: mediates deubiquitination of CC BECN1, a key regulator of autophagy, leading to stabilize the CC PIK3C3/VPS34-containing complexes (PubMed:21962518). In turn, CC PIK3C3/VPS34-containing complexes regulate USP10 stability, suggesting CC the existence of a regulatory system by which PIK3C3/VPS34-containing CC complexes regulate p53/TP53 protein levels via USP10 and USP13 CC (PubMed:21962518). Does not deubiquitinate MDM2 (PubMed:20096447). CC Plays a key role in 40S ribosome subunit recycling when a ribosome has CC stalled during translation: acts both by inhibiting formation of stress CC granules, which store stalled translation pre-initiation complexes, and CC mediating deubiquitination of 40S ribosome subunits (PubMed:27022092, CC PubMed:31981475, PubMed:34348161, PubMed:34469731). Acts as a negative CC regulator of stress granules formation by lowering G3BP1 and G3BP2 CC valence, thereby preventing G3BP1 and G3BP2 ability to undergo liquid- CC liquid phase separation (LLPS) and assembly of stress granules CC (PubMed:11439350, PubMed:27022092, PubMed:32302570). Promotes 40S CC ribosome subunit recycling following ribosome dissociation in response CC to ribosome stalling by mediating deubiquitination of 40S ribosomal CC proteins RPS2/us5, RPS3/us3 and RPS10/eS10, thereby preventing their CC degradation by the proteasome (PubMed:31981475, PubMed:34348161, CC PubMed:34469731). Part of a ribosome quality control that takes place CC when ribosomes have stalled during translation initiation (iRQC): USP10 CC acts by removing monoubiquitination of RPS2/us5 and RPS3/us3, promoting CC 40S ribosomal subunit recycling (PubMed:34469731). Deubiquitinates CFTR CC in early endosomes, enhancing its endocytic recycling CC (PubMed:19398555). Involved in a TANK-dependent negative feedback CC response to attenuate NF-kappa-B activation via deubiquitinating IKBKG CC or TRAF6 in response to interleukin-1-beta (IL1B) stimulation or upon CC DNA damage (PubMed:25861989). Deubiquitinates TBX21 leading to its CC stabilization (PubMed:24845384). Plays a negative role in the RLR CC signaling pathway upon RNA virus infection by blocking the RIGI- CC mediated MAVS activation. Mechanistically, removes the unanchored 'Lys- CC 63'-linked polyubiquitin chains of MAVS to inhibit its aggregation, CC essential for its activation (PubMed:37582970). CC {ECO:0000269|PubMed:11439350, ECO:0000269|PubMed:18632802, CC ECO:0000269|PubMed:19398555, ECO:0000269|PubMed:20096447, CC ECO:0000269|PubMed:21962518, ECO:0000269|PubMed:24845384, CC ECO:0000269|PubMed:25861989, ECO:0000269|PubMed:27022092, CC ECO:0000269|PubMed:31981475, ECO:0000269|PubMed:32302570, CC ECO:0000269|PubMed:34348161, ECO:0000269|PubMed:34469731, CC ECO:0000269|PubMed:37582970}. CC -!- CATALYTIC ACTIVITY: CC Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide CC and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76- CC residue protein attached to proteins as an intracellular targeting CC signal).; EC=3.4.19.12; Evidence={ECO:0000269|PubMed:20096447, CC ECO:0000269|PubMed:21962518, ECO:0000269|PubMed:31981475, CC ECO:0000269|PubMed:32011234}; CC -!- ACTIVITY REGULATION: Specifically inhibited by spautin-1 (specific and CC potent autophagy inhibitor-1), a derivative of MBCQ that binds to USP10 CC and inhibits deubiquitinase activity. Regulated by PIK3C3/VPS34- CC containing complexes. {ECO:0000269|PubMed:21962518}. CC -!- SUBUNIT: Found in a deubiquitination complex with TANK, USP10 and CC ZC3H12A; this complex inhibits genotoxic stress- or interleukin-1-beta CC (IL1B)-mediated NF-kappa-B activation by promoting IKBKG or TRAF6 CC deubiquitination (PubMed:25861989). Interacts with IKBKG; this CC interaction increases in response to DNA damage (PubMed:25861989). CC Interacts with TANK; this interaction increases in response to DNA CC damage (PubMed:25861989). Interacts with TRAF6; this interaction CC increases in response to DNA damage (PubMed:25861989). Interacts with CC ZC3H12A; this interaction increases in response to DNA damage CC (PubMed:25861989). Interacts with G3BP1 (via NTF2 domain) and G3BP2 CC (via NTF2 domain); inhibiting stress granule formation CC (PubMed:11439350, PubMed:23279204, PubMed:27022092, PubMed:31981475, CC PubMed:32302570, PubMed:36183834, PubMed:36279435). CC {ECO:0000269|PubMed:11439350, ECO:0000269|PubMed:23279204, CC ECO:0000269|PubMed:25861989, ECO:0000269|PubMed:27022092, CC ECO:0000269|PubMed:31981475, ECO:0000269|PubMed:32302570, CC ECO:0000269|PubMed:36183834, ECO:0000269|PubMed:36279435}. CC -!- INTERACTION: CC Q14694; P13569: CFTR; NbExp=7; IntAct=EBI-2510389, EBI-349854; CC Q14694; Q13283: G3BP1; NbExp=17; IntAct=EBI-2510389, EBI-1047359; CC Q14694; Q9UN86: G3BP2; NbExp=14; IntAct=EBI-2510389, EBI-1044298; CC Q14694; Q9UN86-2: G3BP2; NbExp=3; IntAct=EBI-2510389, EBI-11035716; CC Q14694; P14136: GFAP; NbExp=3; IntAct=EBI-2510389, EBI-744302; CC Q14694; Q8WXH2: JPH3; NbExp=3; IntAct=EBI-2510389, EBI-1055254; CC Q14694; P63244: RACK1; NbExp=4; IntAct=EBI-2510389, EBI-296739; CC Q14694; Q5D1E8: ZC3H12A; NbExp=5; IntAct=EBI-2510389, EBI-747793; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:20096447, CC ECO:0000269|PubMed:37582970}. Nucleus {ECO:0000269|PubMed:20096447, CC ECO:0000269|PubMed:24845384}. Early endosome CC {ECO:0000269|PubMed:19398555}. Note=Cytoplasmic in normal conditions CC (PubMed:20096447). After DNA damage, translocates to the nucleus CC following phosphorylation by ATM (PubMed:20096447). CC {ECO:0000269|PubMed:20096447}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=Q14694-1; Sequence=Displayed; CC Name=2; CC IsoId=Q14694-2; Sequence=VSP_038869; CC Name=3; CC IsoId=Q14694-3; Sequence=VSP_038868; CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:11439350}. CC -!- INDUCTION: Following DNA damage. Down-regulated in renal cell CC carcinomas. {ECO:0000269|PubMed:20096447}. CC -!- PTM: Phosphorylated by ATM following DNA damage, leading to CC stabilization and translocation it to the nucleus. CC {ECO:0000269|PubMed:20096447}. CC -!- PTM: Ubiquitinated. Deubiquitinated by USP13. CC {ECO:0000269|PubMed:21962518}. CC -!- SIMILARITY: Belongs to the peptidase C19 family. USP10 subfamily. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=CAD97644.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; D80012; BAA11507.1; -; mRNA. DR EMBL; AK299618; BAG61546.1; -; mRNA. DR EMBL; AK315570; BAG37945.1; -; mRNA. DR EMBL; AL162049; CAB82392.2; -; mRNA. DR EMBL; BX537402; CAD97644.1; ALT_INIT; mRNA. DR EMBL; AC009116; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC025280; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC000263; AAH00263.1; -; mRNA. DR CCDS; CCDS45537.1; -. [Q14694-1] DR CCDS; CCDS62004.1; -. [Q14694-3] DR RefSeq; NP_001259004.1; NM_001272075.2. [Q14694-3] DR RefSeq; NP_005144.2; NM_005153.3. [Q14694-1] DR PDB; 7XHF; X-ray; 2.68 A; C/D=6-21. DR PDB; 8TH6; X-ray; 2.34 A; E/F/G/H=2-24. DR PDBsum; 7XHF; -. DR PDBsum; 8TH6; -. DR AlphaFoldDB; Q14694; -. DR SMR; Q14694; -. DR BioGRID; 114554; 344. DR CORUM; Q14694; -. DR ELM; Q14694; -. DR FunCoup; Q14694; 2569. DR IntAct; Q14694; 88. DR MINT; Q14694; -. DR STRING; 9606.ENSP00000457411; -. DR BindingDB; Q14694; -. DR ChEMBL; CHEMBL3407323; -. DR MEROPS; C19.018; -. DR GlyGen; Q14694; 3 sites, 1 O-linked glycan (2 sites). DR iPTMnet; Q14694; -. DR PhosphoSitePlus; Q14694; -. DR SwissPalm; Q14694; -. DR BioMuta; USP10; -. DR DMDM; 2501458; -. DR jPOST; Q14694; -. DR MassIVE; Q14694; -. DR PaxDb; 9606-ENSP00000457411; -. DR PeptideAtlas; Q14694; -. DR ProteomicsDB; 60132; -. [Q14694-1] DR ProteomicsDB; 60133; -. [Q14694-2] DR ProteomicsDB; 60134; -. [Q14694-3] DR Pumba; Q14694; -. DR Antibodypedia; 1716; 397 antibodies from 40 providers. DR DNASU; 9100; -. DR Ensembl; ENST00000219473.12; ENSP00000219473.7; ENSG00000103194.17. [Q14694-1] DR Ensembl; ENST00000570191.5; ENSP00000457411.1; ENSG00000103194.17. [Q14694-3] DR GeneID; 9100; -. DR KEGG; hsa:9100; -. DR MANE-Select; ENST00000219473.12; ENSP00000219473.7; NM_005153.3; NP_005144.2. DR UCSC; uc002fii.4; human. [Q14694-1] DR AGR; HGNC:12608; -. DR ClinPGx; PA37234; -. DR CTD; 9100; -. DR DisGeNET; 9100; -. DR GeneCards; USP10; -. DR HGNC; HGNC:12608; USP10. DR HPA; ENSG00000103194; Low tissue specificity. DR MIM; 609818; gene. DR OpenTargets; ENSG00000103194; -. DR VEuPathDB; HostDB:ENSG00000103194; -. DR eggNOG; KOG1871; Eukaryota. DR GeneTree; ENSGT00550000074994; -. DR HOGENOM; CLU_008279_4_1_1; -. DR InParanoid; Q14694; -. DR OMA; RTCGSPQ; -. DR OrthoDB; 429671at2759; -. DR PAN-GO; Q14694; 8 GO annotations based on evolutionary models. DR PhylomeDB; Q14694; -. DR PathwayCommons; Q14694; -. DR Reactome; R-HSA-5656169; Termination of translesion DNA synthesis. DR Reactome; R-HSA-5689880; Ub-specific processing proteases. DR SignaLink; Q14694; -. DR SIGNOR; Q14694; -. DR Agora; ENSG00000103194; -. DR BioGRID-ORCS; 9100; 473 hits in 1183 CRISPR screens. DR CD-CODE; 232F8A39; P-body. DR CD-CODE; DEE660B4; Stress granule. DR ChiTaRS; USP10; human. DR GeneWiki; USP10; -. DR GenomeRNAi; 9100; -. DR Pharos; Q14694; Tchem. DR PRO; PR:Q14694; -. DR Proteomes; UP000005640; Chromosome 16. DR RNAct; Q14694; protein. DR Bgee; ENSG00000103194; Expressed in ventricular zone and 200 other cell types or tissues. DR ExpressionAtlas; Q14694; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0022626; C:cytosolic ribosome; IDA:UniProt. DR GO; GO:0005769; C:early endosome; IDA:UniProtKB. DR GO; GO:0045111; C:intermediate filament cytoskeleton; IDA:HPA. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB. DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IDA:UniProtKB. DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IMP:UniProtKB. DR GO; GO:0140678; F:molecular function inhibitor activity; IDA:UniProt. DR GO; GO:0002039; F:p53 binding; IPI:UniProtKB. DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB. DR GO; GO:0044325; F:transmembrane transporter binding; IDA:UniProtKB. DR GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW. DR GO; GO:0071347; P:cellular response to interleukin-1; IMP:UniProtKB. DR GO; GO:0006974; P:DNA damage response; IMP:UniProtKB. DR GO; GO:0030330; P:DNA damage response, signal transduction by p53 class mediator; IMP:UniProtKB. DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW. DR GO; GO:0045087; P:innate immune response; IDA:UniProt. DR GO; GO:0035520; P:monoubiquitinated protein deubiquitination; IDA:UniProt. DR GO; GO:0043124; P:negative regulation of canonical NF-kappaB signal transduction; IMP:UniProtKB. DR GO; GO:0062030; P:negative regulation of stress granule assembly; IDA:UniProtKB. DR GO; GO:0016579; P:protein deubiquitination; IDA:UniProtKB. DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW. DR GO; GO:0010506; P:regulation of autophagy; IDA:UniProtKB. DR GO; GO:0031647; P:regulation of protein stability; IBA:GO_Central. DR GO; GO:0072344; P:rescue of stalled ribosome; IDA:UniProtKB. DR GO; GO:0019985; P:translesion synthesis; TAS:Reactome. DR CDD; cd02257; Peptidase_C19; 1. DR FunFam; 3.90.70.10:FF:000015; Ubiquitin specific peptidase 10; 1. DR Gene3D; 3.90.70.10; Cysteine proteinases; 1. DR InterPro; IPR009818; PAM2_motif. DR InterPro; IPR038765; Papain-like_cys_pep_sf. DR InterPro; IPR050164; Peptidase_C19. DR InterPro; IPR001394; Peptidase_C19_UCH. DR InterPro; IPR028889; USP. DR InterPro; IPR018200; USP_CS. DR PANTHER; PTHR24006; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1. DR PANTHER; PTHR24006:SF687; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 10; 1. DR Pfam; PF07145; PAM2; 1. DR Pfam; PF00443; UCH; 1. DR SUPFAM; SSF54001; Cysteine proteinases; 1. DR PROSITE; PS00972; USP_1; 1. DR PROSITE; PS00973; USP_2; 1. DR PROSITE; PS50235; USP_3; 1. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; Autophagy; Cytoplasm; KW DNA damage; DNA repair; Endosome; Hydrolase; Nucleus; Phosphoprotein; KW Protease; Proteomics identification; Reference proteome; Thiol protease; KW Ubl conjugation; Ubl conjugation pathway. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0007744|PubMed:20068231" FT CHAIN 2..798 FT /note="Ubiquitin carboxyl-terminal hydrolase 10" FT /id="PRO_0000080629" FT DOMAIN 415..795 FT /note="USP" FT REGION 2..100 FT /note="Interaction with p53/TP53" FT /evidence="ECO:0000269|PubMed:20096447" FT REGION 6..21 FT /note="G3BP1-binding" FT /evidence="ECO:0000269|PubMed:27022092, FT ECO:0000269|PubMed:36279435" FT REGION 139..166 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 194..257 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 307..337 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 551..594 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 205..219 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 307..316 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 328..337 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 551..562 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 566..581 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 424 FT /note="Nucleophile" FT /evidence="ECO:0000305|PubMed:11439350, FT ECO:0000305|PubMed:19398555, ECO:0000305|PubMed:21962518, FT ECO:0000305|PubMed:24845384, ECO:0000305|PubMed:31981475, FT ECO:0000305|PubMed:32011234" FT ACT_SITE 749 FT /note="Proton acceptor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092, FT ECO:0000255|PROSITE-ProRule:PRU10093" FT MOD_RES 2 FT /note="N-acetylalanine" FT /evidence="ECO:0007744|PubMed:20068231" FT MOD_RES 24 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:20068231" FT MOD_RES 42 FT /note="Phosphothreonine; by ATM" FT /evidence="ECO:0000269|PubMed:20096447" FT MOD_RES 100 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 211 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P52479" FT MOD_RES 226 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 321 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 337 FT /note="Phosphoserine; by ATM" FT /evidence="ECO:0000269|PubMed:20096447" FT MOD_RES 365 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:16964243, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:24275569" FT MOD_RES 370 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:16964243, FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:23186163" FT MOD_RES 547 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 563 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19690332" FT MOD_RES 576 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:17487921, ECO:0007744|PubMed:17693683, FT ECO:0007744|PubMed:18318008, ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163" FT VAR_SEQ 1..6 FT /note="MALHSP -> MPWLPSPGIG (in isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_038868" FT VAR_SEQ 1 FT /note="M -> MCSKDTVLSVCALYWRKGIQSHTPLIGAWRRGKQREQPEDRGVPMKR FT AA (in isoform 2)" FT /evidence="ECO:0000303|PubMed:8724849" FT /id="VSP_038869" FT VARIANT 200 FT /note="M -> V (in dbSNP:rs1862792)" FT /evidence="ECO:0000269|PubMed:17974005" FT /id="VAR_015859" FT VARIANT 203 FT /note="S -> P (in dbSNP:rs2326391)" FT /evidence="ECO:0000269|PubMed:15489334" FT /id="VAR_015860" FT VARIANT 204 FT /note="V -> L (in dbSNP:rs1812061)" FT /evidence="ECO:0000269|PubMed:15489334" FT /id="VAR_015861" FT MUTAGEN 10 FT /note="F->A,G,P,W,D,E,R,H,K,S,T,C,M,N,Q: Abolished FT interaction with G3BP1 and ability to inhibit stress FT granule formation." FT /evidence="ECO:0000269|PubMed:27022092, FT ECO:0000269|PubMed:36183834" FT MUTAGEN 10 FT /note="F->Y: Decreased but not abolished interaction with FT G3BP1." FT /evidence="ECO:0000269|PubMed:36183834" FT MUTAGEN 11 FT /note="G->A: Decreased but not abolished interaction with FT G3BP1." FT /evidence="ECO:0000269|PubMed:36183834" FT MUTAGEN 11 FT /note="G->I,L,P,V,F,W,Y,D,E,R,H,K,S,T,C,M,N,Q: Abolished FT interaction with G3BP1." FT /evidence="ECO:0000269|PubMed:36183834" FT MUTAGEN 12 FT /note="D->A,G,I,L,V,F,W,Y,E,R,H,K,S,T,C,M,N,Q: Decreased FT but not abolished interaction with G3BP1." FT /evidence="ECO:0000269|PubMed:36183834" FT MUTAGEN 12 FT /note="D->P: Abolished interaction with G3BP1." FT /evidence="ECO:0000269|PubMed:36183834" FT MUTAGEN 13 FT /note="F->A,G,P,W,D,E,R,H,K,S,T,C,M,N,Q: Abolished FT interaction with G3BP1." FT /evidence="ECO:0000269|PubMed:36183834" FT MUTAGEN 13 FT /note="F->Y,V,L,I: Decreased but not abolished interaction FT with G3BP1." FT /evidence="ECO:0000269|PubMed:36183834" FT MUTAGEN 42 FT /note="T->A: Abolishes phosphorylation by ATM; when FT associated with A-337." FT /evidence="ECO:0000269|PubMed:20096447" FT MUTAGEN 42 FT /note="T->E: Phospho-mimetic mutant that translocates to FT the nucleus in absence of genotoxic stress; when associated FT with D-337." FT /evidence="ECO:0000269|PubMed:20096447" FT MUTAGEN 337 FT /note="S->A: Abolishes phosphorylation by ATM; when FT associated with A-42." FT /evidence="ECO:0000269|PubMed:20096447" FT MUTAGEN 337 FT /note="S->D: Phospho-mimetic mutant that translocates to FT the nucleus in absence of genotoxic stress; when associated FT with E-42." FT /evidence="ECO:0000269|PubMed:20096447" FT MUTAGEN 424 FT /note="C->A,S: Abolishes deubiquitinating activity and FT ability to deubiquitinate 40S ribosomal proteins." FT /evidence="ECO:0000269|PubMed:11439350, FT ECO:0000269|PubMed:19398555, ECO:0000269|PubMed:21962518, FT ECO:0000269|PubMed:24845384, ECO:0000269|PubMed:31981475, FT ECO:0000269|PubMed:37582970" FT CONFLICT 108 FT /note="A -> V (in Ref. 3; BAG61546)" FT /evidence="ECO:0000305" FT CONFLICT 263 FT /note="T -> A (in Ref. 3; BAG61546)" FT /evidence="ECO:0000305" FT STRAND 8..12 FT /evidence="ECO:0007829|PDB:8TH6" FT HELIX 15..21 FT /evidence="ECO:0007829|PDB:8TH6" SQ 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 //