ID A0A0D9S8B3_CHLSB Unreviewed; 1035 AA.
AC A0A0D9S8B3;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase 48 {ECO:0000256|ARBA:ARBA00035173};
DE EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
GN Name=USP48 {ECO:0000313|Ensembl:ENSCSAP00000017102.1};
OS Chlorocebus sabaeus (Green monkey) (Cercopithecus sabaeus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Chlorocebus.
OX NCBI_TaxID=60711 {ECO:0000313|Ensembl:ENSCSAP00000017102.1, ECO:0000313|Proteomes:UP000029965};
RN [1] {ECO:0000313|Ensembl:ENSCSAP00000017102.1, ECO:0000313|Proteomes:UP000029965}
RP NUCLEOTIDE SEQUENCE.
RA Warren W., Wilson R.K.;
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSCSAP00000017102.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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:0000256|ARBA:ARBA00000707};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR EMBL; AQIB01141934; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AQIB01141935; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AQIB01141936; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_007978323.1; XM_007980132.1.
DR AlphaFoldDB; A0A0D9S8B3; -.
DR STRING; 60711.ENSCSAP00000017102; -.
DR Ensembl; ENSCSAT00000017628.1; ENSCSAP00000017102.1; ENSCSAG00000000905.1.
DR GeneID; 103225432; -.
DR KEGG; csab:103225432; -.
DR CTD; 84196; -.
DR eggNOG; KOG1863; Eukaryota.
DR GeneTree; ENSGT00940000156015; -.
DR OMA; YLGQEKW; -.
DR OrthoDB; 307371at2759; -.
DR BioGRID-ORCS; 103225432; 1 hit in 9 CRISPR screens.
DR Proteomes; UP000029965; Chromosome 20.
DR Bgee; ENSCSAG00000000905; Expressed in pituitary gland and 7 other cell types or tissues.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd02668; Peptidase_C19L; 1.
DR CDD; cd01795; Ubl_USP48; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR InterPro; IPR035927; DUSP-like_sf.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR006615; Pept_C19_DUSP.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR000626; Ubiquitin-like_dom.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR InterPro; IPR044743; Ubl_USP48.
DR InterPro; IPR033841; USP48.
DR InterPro; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR PANTHER; PTHR24006; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR PANTHER; PTHR24006:SF722; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 48; 1.
DR Pfam; PF06337; DUSP; 1.
DR Pfam; PF00443; UCH; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF143791; DUSP-like; 1.
DR SUPFAM; SSF54236; Ubiquitin-like; 1.
DR PROSITE; PS51283; DUSP; 1.
DR PROSITE; PS50053; UBIQUITIN_2; 1.
DR PROSITE; PS00973; USP_2; 1.
DR PROSITE; PS50235; USP_3; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022807};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000029965};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT DOMAIN 89..421
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT DOMAIN 460..554
FT /note="DUSP"
FT /evidence="ECO:0000259|PROSITE:PS51283"
FT DOMAIN 929..1002
FT /note="Ubiquitin-like"
FT /evidence="ECO:0000259|PROSITE:PS50053"
FT REGION 612..640
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 879..919
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 887..905
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1035 AA; 119043 MW; 8793C78D3AE114F4 CRC64;
MAPRLQLEKA AWRWAETVRP EEVSQEHIET AYRIWLEPCI RGVCRRNCKG NPNCLVGIGE
HIWLGEIDEN SFHNIDDPNC ERRKKNSFVG LTNLGATCYV NTFLQVWFLN LELRQALYLC
PSTCSDYVLG DGIQEEKDYE PQTICEHLQY LFALLQNSNR RYIDPSGFVK ALGLDTGQQQ
DAQEFSKLFM SLLEDTLSKQ KNPDVRNIVQ QQFCGEYAYV TVCNQCGRES KLLSKFYELE
LNIQGHKQLT DCISEFLKEE KLEGDNRYFC ENCQSKQNAT RKIRLLSLPC TLNLQLMRFV
FDRQTGHKKK LNTYIGFSEI LDMEPYVEHK GGSYVYELSA VLIHRGVSAY SGHYIAHVKD
PQSGEWYKFN DEDIEKMEGK KLQLGIEEDL AEPSKSQTRK PKCGKGTHCS RNAYMLVYRL
QTQEKPNTTV QVPAFLQELV DRDNSKFEEW CIEMAEMRKQ SVDKGKAKHE EVKELYQRLP
AGAEPYEFVS LEWLQKWLDE STPTKPIDNH ACLCSHDKLH PDKISIMKRI SEYAADIFYS
RYGGGPRLTV KALCKECVVE RCRVLRLKNQ LNEDYKTVNN LLKAAVKGND GFWVGKSSLR
SWRQLALEQL DEQDGDAEQS NGKMNGSTLN KDESKEERKE EEELNFNEDI LCPHGELCIS
ENERRLVSKE AWSKLQQYFP KAPEFPSYKE CCSQCKILER EGEENEALHK MIANEQKTSL
PNLFQDKNRP CLSNWPEDTD VLYIVSQFFV EEWRKFVRKP TRCSPVSSVG NSALLCPHGG
LMFTFASMTK EDSKLIALIW PSEWQMIQKL FVVDHVIKIM RIEVGDVNPS ETQYISEPKL
CPECREGLLC QQQRDLREYT QATIYVHKVV DNKKVMKDSA PELNVSSSET EEDKEEAKPD
GEKDPDFNQS NGGTKRQKIS HQNYIAYQKQ VIRRSMRHRK VRGEKALLVS ANQTLKELKI
QIMHAFSVAP FDQNLSIDGK ILSDDCATLG TLGVIPESVI LLKADEPIAD YAAMDDVMQV
CMPEEGFKGT GLLGH
//
