Ubiquitin carboxyl-terminal hydrolase 10 (EC 3.4.19.12) (Deubiquitinating enzyme 10) (Ubiquitin thioesterase 10) (Ubiquitin-specific-processing protease 10)
1_MALHS 6_ PQYIF 11_ GDFSP 16_ DEFNQ 21_ FFVTP 26_ RSSVE 31_ LPPYS 36_ GTVLC 41_ GTQAV 46_ DKLPD 51_ GQEYQ 56_ RIEFG 61_ VDEVI 66_ EPSDT 71_ LPRTP 76_ SYSIS 81_ STLNP 86_ QAPEF 91_ ILGCT 96_ ASKIT 101_ PDGIT 106_ KEASY 111_ GSIDC 116_ QYPGS 121_ ALALD 126_ GSSNV 131_ EAEVL 136_ ENDGV 141_ SGGLG 146_ QRERK 151_ KKKKR 156_ PPGYY 161_ SYLKD 166_ GGDDS 171_ ISTEA 176_ LVNGH 181_ ANSAV 186_ PNSVS 191_ AEDAE 196_ FMGDM 201_ PPSVT 206_ PRTCN 211_ SPQNS 216_ TDSVS 221_ DIVPD 226_ SPFPG 231_ ALGSD 236_ TRTAG 241_ QPEGG 246_ PGADF 251_ GQSCF 256_ PAEAG 261_ RDTLS 266_ RTAGA 271_ QPCVG 276_ TDTTE 281_ NLGVA 286_ NGQIL 291_ ESSGE 296_ GTATN 301_ GVELH 306_ TTESI 311_ DLDPT 316_ KPESA 321_ SPPAD 326_ GTGSA 331_ SGTLP 336_ VSQPK 341_ SWASL 346_ FHDSK 351_ PSSSS 356_ PVAYV 361_ ETKYS 366_ PPAIS 371_ PLVSE 376_ KQVEV 381_ KEGLV 386_ PVSED 391_ PVAIK 396_ IAELL 401_ ENVTL 406_ IHKPV 411_ SLQPR 416_ GLINK 421_ GNWCY 426_ INATL 431_ QALVA 436_ CPPMY 441_ HLMKF 446_ IPLYS 451_ KVQRP 456_ CTSTP 461_ MIDSF 466_ VRLMN 471_ EFTNM 476_ PVPPK 481_ PRQAL 486_ GDKIV 491_ RDIRP 496_ GAAFE 501_ PTYIY 506_ RLLTV 511_ NKSSL 516_ SEKGR 521_ QEDAE 526_ EYLGF 531_ ILNGL 536_ HEEML 541_ NLKKL 546_ LSPSN 551_ EKLTI 556_ SNGPK 561_ NHSVN 566_ EEEQE 571_ EQGEG 576_ SEDEW 581_ EQVGP 586_ RNKTS 591_ VTRQA 596_ DFVQT 601_ PITGI 606_ FGGHI 611_ RSVVY 616_ QQSSK 621_ ESATL 626_ QPFFT 631_ LQLDI 636_ QSDKI 641_ RTVQD 646_ ALESL 651_ VARES 656_ VQGYT 661_ TKTKQ 666_ EVEIS 671_ RRVTL 676_ EKLPP 681_ VLVLH 686_ LKRFV 691_ YEKTG 696_ GCQKL 701_ IKNIE 706_ YPVDL 711_ EISKE 716_ LLSPG 721_ VKNKN 726_ FKCHR 731_ TYRLF 736_ AVVYH 741_ HGNSA 746_ TGGHY 751_ TTDVF 756_ QIGLN 761_ GWLRI 766_ DDQTV 771_ KVINQ 776_ YQVVK 781_ PTAER 786_ TAYLL 791_YYRRV
1: Hydrolase that can remove conjugated ubiquitin from target proteins such as p53/TP53, RPS2/us5, RPS3/us3, RPS10/eS10, BECN1, SNX3 and CFTR (PubMed:11439350, PubMed:18632802, PubMed:31981475). 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 (PubMed:20096447). Following DNA damage, translocates to the nucleus and deubiquitinates p53/TP53, leading to regulate the p53/TP53-dependent DNA damage response (PubMed:20096447). 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 (PubMed:21962518). 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 (PubMed:21962518). Does not deubiquitinate MDM2 (PubMed:20096447). Plays a key role in 40S ribosome subunit recycling when a ribosome has stalled during translation: acts both by inhibiting formation of stress granules, which store stalled translation pre-initiation complexes, and mediating deubiquitination of 40S ribosome subunits (PubMed:27022092, PubMed:31981475, PubMed:34348161, PubMed:34469731). Acts as a negative regulator of stress granules formation by lowering G3BP1 and G3BP2 valence, thereby preventing G3BP1 and G3BP2 ability to undergo liquid-liquid phase separation (LLPS) and assembly of stress granules (PubMed:11439350, PubMed:27022092, PubMed:32302570). Promotes 40S ribosome subunit recycling following ribosome dissociation in response to ribosome stalling by mediating deubiquitination of 40S ribosomal proteins RPS2/us5, RPS3/us3 and RPS10/eS10, thereby preventing their degradation by the proteasome (PubMed:31981475, PubMed:34348161, PubMed:34469731). Part of a ribosome quality control that takes place when ribosomes have stalled during translation initiation (iRQC): USP10 acts by removing monoubiquitination of RPS2/us5 and RPS3/us3, promoting 40S ribosomal subunit recycling (PubMed:34469731). Deubiquitinates CFTR in early endosomes, enhancing its endocytic recycling (PubMed:19398555). Involved in a TANK-dependent negative feedback response to attenuate NF-kappa-B 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). Plays a negative role in the RLR signaling pathway upon RNA virus infection by blocking the RIGI-mediated MAVS activation. Mechanistically, removes the unanchored 'Lys-63'-linked polyubiquitin chains of MAVS to inhibit its aggregation, essential for its activation (PubMed:37582970)