UBP14_PANTR
ID UBP14_PANTR Reviewed; 493 AA.
AC P60051;
DT 21-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 130.
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=USP14;
OS Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=14962675; DOI=10.1016/j.ygeno.2003.08.017;
RA Dennehey B.K., Gutches D.G., McConkey E.H., Krauter K.S.;
RT "Inversion, duplication, and changes in gene context are associated with
RT human chromosome 18 evolution.";
RL Genomics 83:493-501(2004).
CC -!- FUNCTION: Proteasome-associated deubiquitinase which releases ubiquitin
CC from the proteasome targeted ubiquitinated proteins. Ensures the
CC regeneration of ubiquitin at the proteasome. Is a reversibly associated
CC subunit of the proteasome and a large fraction of proteasome-free
CC protein exists within the cell. Required for the degradation of the
CC chemokine receptor CXCR4 which is critical for CXCL12-induced cell
CC chemotaxis. Serves also as a physiological inhibitor of endoplasmic
CC reticulum-associated degradation (ERAD) under the non-stressed
CC condition by inhibiting the degradation of unfolded endoplasmic
CC reticulum proteins via interaction with ERN1 (By similarity).
CC Indispensable for synaptic development and function at neuromuscular
CC junctions (NMJs) (By similarity). Plays a role in the innate immune
CC defense against viruses by stabilizing the viral DNA sensor CGAS and
CC thus inhibiting its autophagic degradation (By similarity).
CC {ECO:0000250|UniProtKB:P54578, ECO:0000250|UniProtKB:Q9JMA1}.
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 -!- SUBUNIT: Homodimer (Potential). Associates with the 26S proteasome.
CC Interacts with FANCC, CXCR4 and ERN1. Interacts with TRIM14; this
CC interaction recruits USP14 to cleave ubiquitin chains of CGAS.
CC {ECO:0000250|UniProtKB:P54578}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell membrane
CC {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase C19 family. USP14/UBP6 subfamily.
CC {ECO:0000305}.
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DR EMBL; AY191612; AAP23261.1; -; Genomic_DNA.
DR RefSeq; NP_001038961.1; NM_001045496.1.
DR AlphaFoldDB; P60051; -.
DR BMRB; P60051; -.
DR SMR; P60051; -.
DR STRING; 9598.ENSPTRP00000055013; -.
DR MEROPS; C19.015; -.
DR PaxDb; P60051; -.
DR Ensembl; ENSPTRT00000009757; ENSPTRP00000055013; ENSPTRG00000009815.
DR GeneID; 455325; -.
DR KEGG; ptr:455325; -.
DR CTD; 9097; -.
DR VGNC; VGNC:8873; USP14.
DR eggNOG; KOG1872; Eukaryota.
DR GeneTree; ENSGT00390000009615; -.
DR HOGENOM; CLU_017549_2_1_1; -.
DR InParanoid; P60051; -.
DR OrthoDB; 600543at2759; -.
DR TreeFam; TF314494; -.
DR Proteomes; UP000002277; Chromosome 18.
DR Bgee; ENSPTRG00000009815; Expressed in hindlimb stylopod muscle and 21 other tissues.
DR GO; GO:0009986; C:cell surface; IEA:Ensembl.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000502; C:proteasome complex; IEA:UniProtKB-KW.
DR GO; GO:0045202; C:synapse; IEA:Ensembl.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IBA:GO_Central.
DR GO; GO:0004866; F:endopeptidase inhibitor activity; IEA:Ensembl.
DR GO; GO:0070628; F:proteasome binding; IBA:GO_Central.
DR GO; GO:0007268; P:chemical synaptic transmission; IEA:Ensembl.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:1903070; P:negative regulation of ER-associated ubiquitin-dependent protein catabolic process; IEA:Ensembl.
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:0050920; P:regulation of chemotaxis; IEA:Ensembl.
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; IPR019954; Ubiquitin_CS.
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; PS00299; UBIQUITIN_1; 1.
DR PROSITE; PS50053; UBIQUITIN_2; 1.
DR PROSITE; PS00972; USP_1; 1.
DR PROSITE; PS00973; USP_2; 1.
DR PROSITE; PS50235; USP_3; 1.
PE 3: Inferred from homology;
KW Acetylation; Cell membrane; Cytoplasm; Hydrolase; Immunity;
KW Innate immunity; Membrane; Phosphoprotein; Protease; Proteasome;
KW Reference proteome; Thiol protease; Ubl conjugation pathway.
FT CHAIN 1..493
FT /note="Ubiquitin carboxyl-terminal hydrolase 14"
FT /id="PRO_0000080638"
FT DOMAIN 4..80
FT /note="Ubiquitin-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT DOMAIN 105..483
FT /note="USP"
FT ACT_SITE 114
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
FT ACT_SITE 435
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
FT MOD_RES 52
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P54578"
FT MOD_RES 143
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P54578"
FT MOD_RES 148
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JMA1"
FT MOD_RES 235
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P54578"
FT MOD_RES 237
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P54578"
FT MOD_RES 302
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P54578"
FT MOD_RES 432
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P54578"
FT MOD_RES 449
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P54578"
SQ SEQUENCE 493 AA; 55941 MW; F4679A86E9DF00FF CRC64;
MPLYSVTVKW GKEKFEGVEL NTDEPPMVFK AQLFALTGVQ PARQKVMVKG GTLKDDDWGN
IKIKNGMTLL MMGSADALPE EPSAKTVFVE DMTEEQLASA MELPCGLTNL GNTCYMNATV
QCIRSVPELK DALKRYAGAL RASGEMASAQ YITAALRDLF DSMDKTSSSI PPIILLQFLH
MAFPQFAEKG EQGQYLQQDA NECWIQMMRV LQQKLEAIED DSVKETDSSS ASAATPSKKK
SLIDQFFGVE FETTMKCTES EEEEVTKGKE NQLQLSCFIN QEVKYLFTGL KLRLQEEITK
QSPTLQRNAL YIKSSKISRL PAYLTIQMVR FFYKEKESVN AKVLKDVKFP LMLDMYELCT
PELQEKMVSF RSKFKDLEDK KVNQQPNTSD KKSSPQKEVK YEPFSFADDI GSNNCGYYDL
QAVLTHQGRS SSSGHYVSWV KRKQDEWIKF DDDKVSIVTP EDILRLSGGG DWHIAYVLLY
GPRRVEIMEE ESE
