Search Results

Overview

Uniprot IDQ86UV5
Protein NameUbiquitin carboxyl-terminal hydrolase 48
Gene NameUSP48
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
395 EDLAEPSKSQTRKPK
587 NLLKAAVKGSDGFWV
918 NGGTKRQKISHQNYI
929 QNYIAYQKQVIRRSM

Function

Deubiquitinase that recognizes and hydrolyzes the peptide bond at the C-terminal Gly of ubiquitin. Involved in the processing of polyubiquitin precursors as well as that of ubiquitinated proteins (PubMed:16214042, PubMed:34059922). Plays a role in the regulation of NF-kappa-B activation by TNF receptor superfamily via its interactions with RELA and TRAF2. May also play a regulatory role at postsynaptic sites. Plays an important role in cell cycle progression by deubiquitinating Aurora B/AURKB and thereby extending its stability (PubMed:34445214). In the context of H.pylori infection, stabilizes nuclear RELA through deubiquitination, thereby promoting the transcriptional activity of RELA to prolong TNFAIP3 de novo synthesis. Consequently, TNFAIP3 suppresses caspase activity and apoptotic cell death (PubMed:35913642). Also functions in the modulation of the ciliary and synaptic transport as well as cytoskeleton organization, which are key for photoreceptor function and homeostasis. To achieve this, stabilizes the levels of the retinal degeneration-associated proteins ARL3 and UNC119 using distinct mechanisms (PubMed:36293380). Plays a positive role in pyroptosis by stabilizing gasdermin E/GSDME through removal of its 'Lys-48'-linked ubiquitination (PubMed:36607699)

Protein Sequence

10 MAPRLQLEKA 20 AWRWAETVRP 30 EEVSQEHIET 40 AYRIWLEPCI 50 RGVCRRNCKG 60 NPNCLVGIGE 70 HIWLGEIDEN 80 SFHNIDDPNC 90 ERRKKNSFVG 100 LTNLGATCYV 110 NTFLQVWFLN 120 LELRQALYLC 130 PSTCSDYMLG 140 DGIQEEKDYE 150 PQTICEHLQY 160 LFALLQNSNR 170 RYIDPSGFVK 180 ALGLDTGQQQ 190 DAQEFSKLFM 200 SLLEDTLSKQ 210 KNPDVRNIVQ 220 QQFCGEYAYV 230 TVCNQCGRES 240 KLLSKFYELE 250 LNIQGHKQLT 260 DCISEFLKEE 270 KLEGDNRYFC 280 ENCQSKQNAT 290 RKIRLLSLPC 300 TLNLQLMRFV 310 FDRQTGHKKK 320 LNTYIGFSEI 330 LDMEPYVEHK 340 GGSYVYELSA 350 VLIHRGVSAY 360 SGHYIAHVKD 370 PQSGEWYKFN 380 DEDIEKMEGK 390 KLQLGIEEDL 400 AEPSKSQTRK 410 PKCGKGTHCS 420 RNAYMLVYRL 430 QTQEKPNTTV 440 QVPAFLQELV 450 DRDNSKFEEW 460 CIEMAEMRKQ 470 SVDKGKAKHE 480 EVKELYQRLP 490 AGAEPYEFVS 500 LEWLQKWLDE 510 STPTKPIDNH 520 ACLCSHDKLH 530 PDKISIMKRI 540 SEYAADIFYS 550 RYGGGPRLTV 560 KALCKECVVE 570 RCRILRLKNQ 580 LNEDYKTVNN 590 LLKAAVKGSD 600 GFWVGKSSLR 610 SWRQLALEQL 620 DEQDGDAEQS 630 NGKMNGSTLN 640 KDESKEERKE 650 EEELNFNEDI 660 LCPHGELCIS 670 ENERRLVSKE 680 AWSKLQQYFP 690 KAPEFPSYKE 700 CCSQCKILER 710 EGEENEALHK 720 MIANEQKTSL 730 PNLFQDKNRP 740 CLSNWPEDTD 750 VLYIVSQFFV 760 EEWRKFVRKP 770 TRCSPVSSVG 780 NSALLCPHGG 790 LMFTFASMTK 800 EDSKLIALIW 810 PSEWQMIQKL 820 FVVDHVIKIT 830 RIEVGDVNPS 840 ETQYISEPKL 850 CPECREGLLC 860 QQQRDLREYT 870 QATIYVHKVV 880 DNKKVMKDSA 890 PELNVSSSET 900 EEDKEEAKPD 910 GEKDPDFNQS 920 NGGTKRQKIS 930 HQNYIAYQKQ 940 VIRRSMRHRK 950 VRGEKALLVS 960 ANQTLKELKI 970 QIMHAFSVAP 980 FDQNLSIDGK 990 ILSDDCATLG 1000 TLGVIPESVI 1010 LLKADEPIAD 1020 YAAMDDVMQV 1030 CMPEEGFKGT GLLGH

Gene Ontology

Classification GO ID Description
Cellular Component GO:0005929 cilium
Cellular Component GO:0005829 cytosol
Cellular Component GO:0005739 mitochondrion
Cellular Component GO:0005654 nucleoplasm
Cellular Component GO:0005634 nucleus
Molecular Function GO:0004843 cysteine-type deubiquitinase activity
Molecular Function GO:0004197 cysteine-type endopeptidase activity
Molecular Function GO:0101005 deubiquitinase activity
Biological Process GO:0016579 protein deubiquitination
Biological Process GO:0006508 proteolysis
Biological Process GO:0031647 regulation of protein stability

Reference

[1] He C, Zhang J, Bai X, Lu C, Zhang K. Lysine lactylation-based insight to understanding the characterization of cervical cancer.. Biochim Biophys Acta Mol Basis Dis 1870(7):167356. 2024 Oct. PMID: 39025375.

[2] 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.