UBP10_XENTR
ID UBP10_XENTR Reviewed; 805 AA.
AC Q6DIJ4;
DT 23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase 10;
DE EC=3.4.19.12 {ECO:0000250|UniProtKB:Q14694};
DE AltName: Full=Deubiquitinating enzyme 10;
DE AltName: Full=Ubiquitin thioesterase 10;
DE AltName: Full=Ubiquitin-specific-processing protease 10;
GN Name=usp10; ORFNames=TGas137m11.1;
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Gastrula;
RG Sanger Xenopus tropicalis EST/cDNA project;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Hydrolase that can remove conjugated ubiquitin from target
CC proteins such as p53/tp53. Acts as an essential regulator of p53/tp53
CC stability: in unstressed cells, specifically deubiquitinates p53/tp53
CC in the cytoplasm, leading to counteracts MDM2 action and stabilize
CC p53/tp53. Following DNA damage, translocates to the nucleus and
CC deubiquitinates p53/tp53, leading to regulate the p53/TP53-dependent
CC DNA damage response. Component of a regulatory loop that controls
CC autophagy and p53/tp53 levels (By similarity).
CC {ECO:0000250|UniProtKB:Q14694}.
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:0000250|UniProtKB:Q14694};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q14694}. Nucleus
CC {ECO:0000250|UniProtKB:Q14694}.
CC -!- SIMILARITY: Belongs to the peptidase C19 family. USP10 subfamily.
CC {ECO:0000305}.
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DR EMBL; CR855702; CAJ83514.1; -; mRNA.
DR EMBL; BC075544; AAH75544.1; -; mRNA.
DR RefSeq; NP_001006761.1; NM_001006760.1.
DR AlphaFoldDB; Q6DIJ4; -.
DR SMR; Q6DIJ4; -.
DR MEROPS; C19.018; -.
DR DNASU; 448441; -.
DR GeneID; 448441; -.
DR KEGG; xtr:448441; -.
DR CTD; 9100; -.
DR Xenbase; XB-GENE-966184; usp10.
DR InParanoid; Q6DIJ4; -.
DR OrthoDB; 1078977at2759; -.
DR Reactome; R-XTR-5656169; Termination of translesion DNA synthesis.
DR Reactome; R-XTR-5689880; Ub-specific processing proteases.
DR Proteomes; UP000008143; Chromosome 4.
DR Proteomes; UP000790000; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005769; C:early endosome; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; ISS:UniProtKB.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; ISS:UniProtKB.
DR GO; GO:0002039; F:p53 binding; ISS:UniProtKB.
DR GO; GO:0044325; F:transmembrane transporter binding; ISS:UniProtKB.
DR GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; ISS:UniProtKB.
DR GO; GO:0071347; P:cellular response to interleukin-1; ISS:UniProtKB.
DR GO; GO:0030330; P:DNA damage response, signal transduction by p53 class mediator; ISS:UniProtKB.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0043124; P:negative regulation of I-kappaB kinase/NF-kappaB signaling; ISS:UniProtKB.
DR GO; GO:0016579; P:protein deubiquitination; ISS:UniProtKB.
DR GO; GO:0010506; P:regulation of autophagy; ISS:UniProtKB.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR028767; USP10.
DR InterPro; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR PANTHER; PTHR13328:SF5; PTHR13328:SF5; 1.
DR Pfam; PF00443; UCH; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
DR PROSITE; PS00972; USP_1; 1.
DR PROSITE; PS00973; USP_2; 1.
DR PROSITE; PS50235; USP_3; 1.
PE 2: Evidence at transcript level;
KW Autophagy; Cytoplasm; DNA damage; DNA repair; Hydrolase; Nucleus; Protease;
KW Reference proteome; Thiol protease; Ubl conjugation pathway.
FT CHAIN 1..805
FT /note="Ubiquitin carboxyl-terminal hydrolase 10"
FT /id="PRO_0000393004"
FT DOMAIN 422..802
FT /note="USP"
FT REGION 139..170
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 561..593
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 431
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
FT ACT_SITE 756
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
SQ SEQUENCE 805 AA; 88936 MW; F95A8A2A4FB60DD1 CRC64;
MASPSGQYIF GEFSDDEFKQ FFVTARCTVE LPPYNEHFFP CGPQSSGDFQ DDMHLKFSEV
IHGISGEDCP RIEFGIEEVI DHSTALPNNT DYSISSNLNP QAPEFILTCS SSPKTSNNVL
HENNFDAINC QFSECAIPDG SGNADSDGTS GTGQRERKKK KKRPPGYYSY LEGVGDVPSE
TLVNGHANST GLNSISTDDP DLAEDIPIST TSPRTCNSPD NFVDLNNEAL SNDASMHNAL
DNARTAGQPE ECSVTSSEQS CIPSDNGRES PVRTAVVQPF AGTDTTENLG VTNGQTLESS
EEGTASNGVV LLPEVSSLSE EAKPEETSTA QAVVHLPGSA SANPPAKSWA SLFHNSKPSS
TTQVAYVETK NATPVTSPQV TEKQVEIKEG PVPVSEDPVA IKIAELLEEV KLVHKPVSLQ
PRGLINKGNW CYINATLQAL VACPPMYHLM KSIPVYTKAQ RPCTSTPMID SFVRLMNEFT
NMPILPKAKQ ASGEKVIRDI RPGAPFEPAY IYRLLTVFKS SLSEKGRQED AEEYLGFILN
GLHEEMLSLK KLLLPQNDKI HINNGPDPVS EKEEINKDEQ EGSDEEWEQV GPRHKSSVTR
QADFVQTPIT DIFGGHMRSV VYQQSSKESA TLQPFFTLQL DIQSEKIRTV QDALESLVAR
ESVQGYTTKT KQEVEICRRV TLEELPPVLV LHLKRFVFEK TGGCQKLIKN IEYPVDLEIS
KDLLSPGVKS KIFKGQRTYR LFAVVYHHGN SATGGHYTTD VFQIGLNGWL RIDDQTVKVI
NQYQVVKQTV ERTAYLLYYR RVDLL
