UB10B_XENLA
ID UB10B_XENLA Reviewed; 805 AA.
AC Q7ZXR7;
DT 23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase 10-B;
DE EC=3.4.19.12 {ECO:0000250|UniProtKB:Q14694};
DE AltName: Full=Deubiquitinating enzyme 10-B;
DE AltName: Full=Ubiquitin thioesterase 10-B;
DE AltName: Full=Ubiquitin-specific-processing protease 10-B;
GN Name=usp10-b;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JAN-2003) 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). {ECO:0000250}.
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; BC044285; AAH44285.1; -; mRNA.
DR RefSeq; NP_001080643.1; NM_001087174.1.
DR RefSeq; XP_018111988.1; XM_018256499.1.
DR AlphaFoldDB; Q7ZXR7; -.
DR SMR; Q7ZXR7; -.
DR IntAct; Q7ZXR7; 1.
DR MEROPS; C19.018; -.
DR DNASU; 380335; -.
DR GeneID; 380335; -.
DR KEGG; xla:380335; -.
DR CTD; 380335; -.
DR Xenbase; XB-GENE-17339212; usp10.L.
DR OMA; WLMNEFT; -.
DR OrthoDB; 1078977at2759; -.
DR Proteomes; UP000186698; Chromosome 4L.
DR Bgee; 380335; Expressed in neurula embryo and 19 other tissues.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
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-B"
FT /id="PRO_0000393003"
FT DOMAIN 422..802
FT /note="USP"
FT REGION 136..173
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 284..305
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 573..600
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 136..150
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 284..303
FT /note="Polar residues"
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; 89197 MW; FEC173B9A8021C2E CRC64;
MASPSGQYIF GEFSDDEFKQ FFVTARCTVE LPPYNEHFFP CGPQSSVDFQ DDMHLKFSEV
IHGISGEECP RIEFGIEQVV DRDTALNNNT DYSISSNLNP QAPEFILTCS SFPKTSNNVL
HENNFDAINC QFSESAIPDG SGNADSDGTS GTGQRERKKK KKRPPGYYSY LEGVGDVPSE
TLVNGHANST GLDSISTDDP DLADDIPIST TSPRTCTSPD NFVDLINEAL SDEASMHNVL
DNARTAGQPE ECSVTSSEQS CIPSDNGSES PVRTAVVQPF AGTDTTENLG VTNGQTLESP
EEDTVSNGVV LHPEVSSFSE EVKTEETSTA QALIHLSGSA SSNPPAKSWA SLFHTSKPSS
SPQVAYVETK NAPTVVSPQV PEKQVEIKEE PVPVSDDPVA IEFAELLEEV KLVHKPVSLQ
PRGLINKGNW CYINATLQAL VACPPMYHLM KSIPVYTKAQ RPCTSTPMID SFVRLMNEFT
NMPILPKAKQ APGEKVIKDI RPGAPFEPTY IYRLLTVFKS SLSEKGRQED AEEYLGFILN
GLHEEMLALK KLLLPQNDQI HINNCPNPVS GVEEVNKEEQ EGSDEEWEQV GPRNKSSVTR
QADFVQTPIT DIFGGHMRSV VYQQSSKESA TLQPFFTLQL DIQSEKIRTV QDALESLVAR
ESVQGYTTKT KQEVEICRRV TLEELPPVLV LHLKRFVFEK TGGCQKLIKN IEYPVDLEVS
KDLLSPGVKS KIFKGQRTYR LFAVVYHHGN SATGGHYTTD VFQIGLNGWL RIDDQSVKVI
NQYQVVKQTV ERTAYLLYYR RVDLL
