UBP11_CANLF
ID UBP11_CANLF Reviewed; 445 AA.
AC Q01988;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase 11;
DE EC=3.4.19.12 {ECO:0000250|UniProtKB:P51784};
DE AltName: Full=Deubiquitinating enzyme 11;
DE AltName: Full=Ubiquitin thioesterase 11;
DE AltName: Full=Ubiquitin-specific-processing protease 11;
DE Flags: Fragment;
GN Name=USP11;
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Trachea;
RX PubMed=1282002; DOI=10.1016/0006-291x(92)92297-b;
RA Shankar V., Tan S., Gilmore M.S., Sachdev G.P.;
RT "Molecular cloning of the carboxy terminus of a canine tracheobronchial
RT mucin.";
RL Biochem. Biophys. Res. Commun. 189:958-964(1992).
CC -!- FUNCTION: Protease that can remove conjugated ubiquitin from target
CC proteins and polyubiquitin chains. Inhibits the degradation of target
CC proteins by the proteasome. Cleaves preferentially 'Lys-6' and 'Lys-
CC 63'-linked ubiquitin chains. Has lower activity with 'Lys-11' and 'Lys-
CC 33'-linked ubiquitin chains, and extremely low activity with 'Lys-27',
CC 'Lys-29' and 'Lys-48'-linked ubiquitin chains (in vitro). Plays a role
CC in the regulation of pathways leading to NF-kappa-B activation. Plays a
CC role in the regulation of DNA repair after double-stranded DNA breaks.
CC Acts as a chromatin regulator via its association with the Polycomb
CC group (PcG) multiprotein PRC1-like complex; may act by deubiquitinating
CC components of the PRC1-like complex. Promotes cell proliferation by
CC deubiquitinating phosphorylated E2F1. {ECO:0000250|UniProtKB:P51784}.
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:P51784};
CC -!- SUBUNIT: Monomer. Interacts with RANBP9/RANBPM. Interacts with BRCA2.
CC Interacts with CHUK/IKKA. Interacts with NFKBIA. Associated component
CC of the Polycomb group (PcG) multiprotein PRC1-like complex.
CC {ECO:0000250|UniProtKB:P51784}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P51784}. Cytoplasm
CC {ECO:0000250|UniProtKB:P51784}. Chromosome
CC {ECO:0000250|UniProtKB:P51784}. Note=Predominantly nuclear. Associates
CC with chromatin. {ECO:0000250|UniProtKB:P51784}.
CC -!- SIMILARITY: Belongs to the peptidase C19 family. {ECO:0000305}.
CC -!- CAUTION: Was originally thought to be apomucin (also known as mucin
CC core protein; CTM-A). {ECO:0000305|PubMed:1282002}.
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; L03387; AAA30875.1; -; mRNA.
DR PIR; PC1174; I46225.
DR AlphaFoldDB; Q01988; -.
DR SMR; Q01988; -.
DR STRING; 9615.ENSCAFP00000058620; -.
DR MEROPS; C19.014; -.
DR PRIDE; Q01988; -.
DR eggNOG; KOG1870; Eukaryota.
DR InParanoid; Q01988; -.
DR Proteomes; UP000002254; Unplaced.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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:0016579; P:protein deubiquitination; 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; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR Pfam; PF00443; UCH; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
DR PROSITE; PS00973; USP_2; 1.
DR PROSITE; PS50235; USP_3; 1.
PE 2: Evidence at transcript level;
KW Chromosome; Cytoplasm; Hydrolase; Nucleus; Phosphoprotein; Protease;
KW Reference proteome; Thiol protease; Ubl conjugation pathway.
FT CHAIN <1..445
FT /note="Ubiquitin carboxyl-terminal hydrolase 11"
FT /id="PRO_0000080631"
FT DOMAIN 1..412
FT /note="USP"
FT REGION 127..194
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 416..445
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 362
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
FT ACT_SITE 370
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
FT MOD_RES 130
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P51784"
FT MOD_RES 430
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P51784"
FT NON_TER 1
SQ SEQUENCE 445 AA; 50892 MW; FE921DD1EEAF7C9E CRC64;
NSARADLCVA LAKHTGMSPE RMMVADVFSH RFYKIYQLEE SLSSILDRDD IFIYEVSGRS
AIGENSREDV VLPIYLRERT PARDYNNSYY GLMLFGHPLL VSVPRDRLSW DALYHILLYR
LSRYVTRPSS DDEDDGDEKD IEDKDNIPKP GHVAGASSQD SGAGSGGAQL WSRRRKPAPV
DNSPGPSHWP QRARRKHLFT LQTVNSNGTS DRSTFNEDTH AQPYIAIDWE PEMKKRYYDE
VEAEGYVKHD CVGYVLKKAP VRLQECIELF TTVETLEKEN PWFCPTCKQH QLATKKLDLW
MLPETLIIHL KRFSYTKFSR EKLDTLVEFP IRDLDFSEFV IKPQNESAPE LYKYDLIAVS
NHYGGLRDGH YTTFACNKDS GQSDYFDDNS VSPVTENQIE SKAAYVLFYQ RQDVARRLQP
QPSSSDPPAS PACGSPPNSE FMDVN
