UBP14_CAEEL
ID UBP14_CAEEL Reviewed; 489 AA.
AC Q17361; O45248;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2002, sequence version 2.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase 14;
DE EC=3.4.19.12;
DE AltName: Full=Deubiquitinating enzyme 14;
DE AltName: Full=Ubiquitin thioesterase 14;
DE AltName: Full=Ubiquitin-specific-processing protease 14;
GN Name=usp-14; Synonyms=tgt-1; ORFNames=C13B4.2;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Bristol N2;
RA Deshpande K.L., Katze J.R.;
RL Submitted (AUG-1995) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
CC -!- FUNCTION: Proteasome-associated deubiquitinase which releases ubiquitin
CC from the proteasome targeted ubiquitinated proteins. Ensures the
CC regeneration of ubiquitin at the proteasome (By similarity).
CC {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;
CC -!- SIMILARITY: Belongs to the peptidase C19 family. USP14/UBP6 subfamily.
CC {ECO:0000305}.
CC -!- CAUTION: Was originally (Ref.1) thought to be a queuine tRNA-
CC ribosyltransferase. {ECO:0000305}.
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DR EMBL; U32223; AAA74956.1; -; mRNA.
DR EMBL; Z81468; CAB03876.1; -; Genomic_DNA.
DR EMBL; Z83236; CAB03876.1; JOINED; Genomic_DNA.
DR PIR; T19227; T19227.
DR RefSeq; NP_497006.1; NM_064605.8.
DR AlphaFoldDB; Q17361; -.
DR SMR; Q17361; -.
DR BioGRID; 40386; 20.
DR STRING; 6239.C13B4.2; -.
DR MEROPS; C19.A36; -.
DR EPD; Q17361; -.
DR PaxDb; Q17361; -.
DR PeptideAtlas; Q17361; -.
DR EnsemblMetazoa; C13B4.2.1; C13B4.2.1; WBGene00006856.
DR GeneID; 175105; -.
DR KEGG; cel:CELE_C13B4.2; -.
DR UCSC; C13B4.2.1; c. elegans.
DR CTD; 175105; -.
DR WormBase; C13B4.2; CE15615; WBGene00006856; usp-14.
DR eggNOG; KOG1872; Eukaryota.
DR GeneTree; ENSGT00390000009615; -.
DR HOGENOM; CLU_017549_2_1_1; -.
DR InParanoid; Q17361; -.
DR OMA; MCKGGIL; -.
DR OrthoDB; 600543at2759; -.
DR PhylomeDB; Q17361; -.
DR Reactome; R-CEL-5689880; Ub-specific processing proteases.
DR PRO; PR:Q17361; -.
DR Proteomes; UP000001940; Chromosome II.
DR Bgee; WBGene00006856; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0000502; C:proteasome complex; IEA:UniProtKB-KW.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IBA:GO_Central.
DR GO; GO:0070628; F:proteasome binding; IBA:GO_Central.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR GO; GO:0016579; P:protein deubiquitination; IBA:GO_Central.
DR GO; GO:0061136; P:regulation of proteasomal protein catabolic process; IBA:GO_Central.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR000626; Ubiquitin-like_dom.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR InterPro; IPR044635; UBP14-like.
DR InterPro; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR PANTHER; PTHR43982; PTHR43982; 1.
DR Pfam; PF00443; UCH; 1.
DR SMART; SM00213; UBQ; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
DR SUPFAM; SSF54236; SSF54236; 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 Hydrolase; Protease; Proteasome; Reference proteome; Thiol protease;
KW Ubl conjugation pathway.
FT CHAIN 1..489
FT /note="Ubiquitin carboxyl-terminal hydrolase 14"
FT /id="PRO_0000080640"
FT DOMAIN 102..458
FT /note="USP"
FT REGION 467..489
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 111
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
FT ACT_SITE 409
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
FT CONFLICT 398
FT /note="I -> M (in Ref. 1; AAA74956)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 489 AA; 55878 MW; 4433F2CC59703A9B CRC64;
MPIVNVKWQK EKYVVEVDTS APPMVFKAQL FALTQVVPER QKVVIMGRTL GDDDWEGITI
KENMTIMMMG SVGEIPKPPT VLEKKQANRD KQAEEISALY PCGLANLGNT CYFNSCVQML
KEVNELVLKP AEEMRIREHN DRLCHNLATL FNSLRDKDRA LRSKGEPIKP FAAILTLSDS
FPQFEKFKQQ DANECLVSIM SNVTRIYGLS GWNIESLFRI QTETTMKCLE SDEVSEKKVE
RNNQLTCYVN QDVRFLQTGI KAGFEEEMTR NSEELNRDAK WQKNTQISRL PKYLTVNINR
FFYKESTKTN AKILKSVQFP MQLDTYDLCS QELKDKLVAR RADIKLEEDA KLERELRKKV
LDKEQGDKIF DDGVALPTAF EDDAGSNNSG FYDLKGIITH KGRSSQDGHY VAWMRSSEDG
KWRLFDDEHV TVVDEEAILK TSGGGDWHSA YVLLYEARVI KQFPELPPAP VPTEVAADTA
EPMEVSEKQ
