Search Results

Overview

Uniprot IDP54578
Protein NameUbiquitin carboxyl-terminal hydrolase 14
Gene NameUSP14
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
313 QRNALYIKSSKISRL
336 VRFFYKEKESVNAKV
342 EKESVNAKVLKDVKF
49 ARQKVMVKGGTLKDD

Function

Proteasome-associated deubiquitinase which releases ubiquitin from the proteasome targeted ubiquitinated proteins (PubMed:35145029). Ensures the regeneration of ubiquitin at the proteasome (PubMed:18162577, PubMed:28396413). Is a reversibly associated subunit of the proteasome and a large fraction of proteasome-free protein exists within the cell (PubMed:18162577). Required for the degradation of the chemokine receptor CXCR4 which is critical for CXCL12-induced cell chemotaxis (PubMed:19106094). Also serves as a physiological inhibitor of endoplasmic reticulum-associated degradation (ERAD) under the non-stressed condition by inhibiting the degradation of unfolded endoplasmic reticulum proteins via interaction with ERN1 (PubMed:19135427). Indispensable for synaptic development and function at neuromuscular junctions (NMJs) (By similarity). Plays a role in the innate immune defense against viruses by stabilizing the viral DNA sensor CGAS and thus inhibiting its autophagic degradation (PubMed:27666593). Inhibits OPTN-mediated selective autophagic degradation of KDM4D and thereby negatively regulates H3K9me2 and H3K9me3 (PubMed:35145029)

Protein Sequence

10 MPLYSVTVKW 20 GKEKFEGVEL 30 NTDEPPMVFK 40 AQLFALTGVQ 50 PARQKVMVKG 60 GTLKDDDWGN 70 IKIKNGMTLL 80 MMGSADALPE 90 EPSAKTVFVE 100 DMTEEQLASA 110 MELPCGLTNL 120 GNTCYMNATV 130 QCIRSVPELK 140 DALKRYAGAL 150 RASGEMASAQ 160 YITAALRDLF 170 DSMDKTSSSI 180 PPIILLQFLH 190 MAFPQFAEKG 200 EQGQYLQQDA 210 NECWIQMMRV 220 LQQKLEAIED 230 DSVKETDSSS 240 ASAATPSKKK 250 SLIDQFFGVE 260 FETTMKCTES 270 EEEEVTKGKE 280 NQLQLSCFIN 290 QEVKYLFTGL 300 KLRLQEEITK 310 QSPTLQRNAL 320 YIKSSKISRL 330 PAYLTIQMVR 340 FFYKEKESVN 350 AKVLKDVKFP 360 LMLDMYELCT 370 PELQEKMVSF 380 RSKFKDLEDK 390 KVNQQPNTSD 400 KKSSPQKEVK 410 YEPFSFADDI 420 GSNNCGYYDL 430 QAVLTHQGRS 440 SSSGHYVSWV 450 KRKQDEWIKF 460 DDDKVSIVTP 470 EDILRLSGGG 480 DWHIAYVLLY 490 GPRRVEIMEE ESEQ

Gene Ontology

Classification GO ID Description
Cellular Component GO:0009986 cell surface
Cellular Component GO:0005737 cytoplasm
Cellular Component GO:0031410 cytoplasmic vesicle
Cellular Component GO:0005829 cytosol
Cellular Component GO:0070062 extracellular exosome
Cellular Component GO:0098978 glutamatergic synapse
Cellular Component GO:0005886 plasma membrane
Cellular Component GO:0099523 presynaptic cytosol
Cellular Component GO:0000502 proteasome complex
Molecular Function GO:0004843 cysteine-type deubiquitinase activity
Molecular Function GO:0004197 cysteine-type endopeptidase activity
Molecular Function GO:0101005 deubiquitinase activity
Molecular Function GO:0004866 endopeptidase inhibitor activity
Molecular Function GO:0061578 K63-linked deubiquitinase activity
Molecular Function GO:0070628 proteasome binding
Biological Process GO:0006954 inflammatory response
Biological Process GO:0045087 innate immune response
Biological Process GO:1904293 negative regulation of ERAD pathway
Biological Process GO:2000059 negative regulation of ubiquitin-dependent protein catabolic process
Biological Process GO:0043161 proteasome-mediated ubiquitin-dependent protein catabolic process
Biological Process GO:0071108 protein K48-linked deubiquitination
Biological Process GO:0050920 regulation of chemotaxis
Biological Process GO:0061136 regulation of proteasomal protein catabolic process

Reference

[1] Yang Z, Yan C, Ma J, Peng P, Ren X et al.. Lactylome analysis suggests lactylation-dependent mechanisms of metabolic adaptation in hepatocellular carcinoma.. Nat Metab 5(1):61-79. 2023 Jan. PMID: 36593272.

[2] Hong H, Chen X, Wang H, Gu X, Yuan Y et al.. Global profiling of protein lysine lactylation and potential target modified protein analysis in hepatocellular carcinoma.. Proteomics 23(9):e2200432. 2023 May. PMID: 36625413.

[3] Wu Q, Li Z, Gong T, Zheng X, Zhou X et al.. Porphyromonas gingivalis infection induces lysine lactylation reprogramming in human umbilical vein endothelial cells.. Front Cell Infect Microbiol 16:1706727. 2026. PMID: 41696360.