Overview
| Uniprot ID | Q9P275 |
|---|
| Protein Name | Ubiquitin carboxyl-terminal hydrolase 36 |
|---|
| Gene Name | USP36 |
|---|
| Organism | Homo sapiens |
|---|
Kla Sites from experimental identification
| Position |
Flanking peptide |
| 688 |
MSPPPAKKLALSAKK |
| 694 |
KKLALSAKKASTLWR |
| 918 |
SSRKRRRKGAEGLGE |
Function
Deubiquitinase essential for the regulation of nucleolar structure and function (PubMed:19208757, PubMed:22902402, PubMed:29273634). Required for cell and organism viability (PubMed:19208757, PubMed:22902402, PubMed:29273634). Plays an important role in ribosomal RNA processing and protein synthesis, which is mediated, at least in part, through deubiquitination of DHX33, NPM1 and FBL, regulating their protein stability (PubMed:19208757, PubMed:22902402, PubMed:29273634, PubMed:36912080). Functions as a transcriptional repressor by deubiquiting histone H2B at the promoters of genes critical for cellular differentiation, such as CDKN1A, thereby preventing histone H3 'Lys-4' trimethylation (H3K4) (PubMed:29274341). Specifically deubiquitinates MYC in the nucleolus, leading to prevent MYC degradation by the proteasome: acts by specifically interacting with isoform 3 of FBXW7 (FBW7gamma) in the nucleolus and counteracting ubiquitination of MYC by the SCF(FBW7) complex (PubMed:25775507). In contrast, it does not interact with isoform 1 of FBXW7 (FBW7alpha) in the nucleoplasm (PubMed:25775507). Interacts to and regulates the actions of E3 ubiquitin-protein ligase NEDD4L over substrates such as NTRK1, KCNQ2 and KCNQ3, affecting their expression an functions (PubMed:27445338). Deubiquitinates SOD2, regulates SOD2 protein stability (PubMed:21268071). Deubiquitinase activity is required to control selective autophagy activation by ubiquitinated proteins (PubMed:22622177). Promotes CEP63 stabilization through 'Lys-48'-linked deubiquitination leading to increased stability (PubMed:35989368). Acts as a SUMO ligase to promote EXOSC10 sumoylation critical for the nucleolar RNA exosome function in rRNA processing (PubMed:36912080). Binds to pre-rRNAs (PubMed:36912080)
Protein Sequence
10
MPIVDKLKEA
20
LKPGRKDSAD
30
DGELGKLLAS
40
SAKKVLLQKI
50
EFEPASKSFS
60
YQLEALKSKY
70
VLLNPKTEGA
80
SRHKSGDDPP
90
ARRQGSEHTY
100
ESCGDGVPAP
110
QKVLFPTERL
120
SLRWERVFRV
130
GAGLHNLGNT
140
CFLNATIQCL
150
TYTPPLANYL
160
LSKEHARSCH
170
QGSFCMLCVM
180
QNHIVQAFAN
190
SGNAIKPVSF
200
IRDLKKIARH
210
FRFGNQEDAH
220
EFLRYTIDAM
230
QKACLNGCAK
240
LDRQTQATTL
250
VHQIFGGYLR
260
SRVKCSVCKS
270
VSDTYDPYLD
280
VALEIRQAAN
290
IVRALELFVK
300
ADVLSGENAY
310
MCAKCKKKVP
320
ASKRFTIHRT
330
SNVLTLSLKR
340
FANFSGGKIT
350
KDVGYPEFLN
360
IRPYMSQNNG
370
DPVMYGLYAV
380
LVHSGYSCHA
390
GHYYCYVKAS
400
NGQWYQMNDS
410
LVHSSNVKVV
420
LNQQAYVLFY
430
LRIPGSKKSP
440
EGLISRTGSS
450
SLPGRPSVIP
460
DHSKKNIGNG
470
IISSPLTGKR
480
QDSGTMKKPH
490
TTEEIGVPIS
500
RNGSTLGLKS
510
QNGCIPPKLP
520
SGSPSPKLSQ
530
TPTHMPTILD
540
DPGKKVKKPA
550
PPQHFSPRTA
560
QGLPGTSNSN
570
SSRSGSQRQG
580
SWDSRDVVLS
590
TSPKLLATAT
600
ANGHGLKGND
610
ESAGLDRRGS
620
SSSSPEHSAS
630
SDSTKAPQTP
640
RSGAAHLCDS
650
QETNCSTAGH
660
SKTPPSGADS
670
KTVKLKSPVL
680
SNTTTEPAST
690
MSPPPAKKLA
700
LSAKKASTLW
710
RATGNDLRPP
720
PPSPSSDLTH
730
PMKTSHPVVA
740
STWPVHRARA
750
VSPAPQSSSR
760
LQPPFSPHPT
770
LLSSTPKPPG
780
TSEPRSCSSI
790
STALPQVNED
800
LVSLPHQLPE
810
ASEPPQSPSE
820
KRKKTFVGEP
830
QRLGSETRLP
840
QHIREATAAP
850
HGKRKRKKKK
860
RPEDTAASAL
870
QEGQTQRQPG
880
SPMYRREGQA
890
QLPAVRRQED
900
GTQPQVNGQQ
910
VGCVTDGHHA
920
SSRKRRRKGA
930
EGLGEEGGLH
940
QDPLRHSCSP
950
MGDGDPEAME
960
ESPRKKKKKK
970
RKQETQRAVE
980
EDGHLKCPRS
990
AKPQDAVVPE
1000
SSSCAPSANG
1010
WCPGDRMGLS
1020
QAPPVSWNGE
1030
RESDVVQELL
1040
KYSSDKAYGR
1050
KVLTWDGKMS
1060
AVSQDAIEDS
1070
RQARTETVVD
1080
DWDEEFDRGK
1090
EKKIKKFKRE
1100
KRRNFNAFQK
1110
LQTRRNFWSV
1120
THPAKAASLS
YRR
Gene Ontology
| Classification |
GO ID |
Description |
| Cellular Component |
GO:0005737 |
cytoplasm |
| Cellular Component |
GO:0005829 |
cytosol |
| Cellular Component |
GO:0016607 |
nuclear speck |
| Cellular Component |
GO:0005730 |
nucleolus |
| Cellular Component |
GO:0005634 |
nucleus |
| Molecular Function |
GO:0004843 |
cysteine-type deubiquitinase activity |
| Molecular Function |
GO:0140936 |
histone H2B deubiquitinase activity |
| Molecular Function |
GO:1990380 |
K48-linked deubiquitinase activity |
| Molecular Function |
GO:0003723 |
RNA binding |
| Molecular Function |
GO:0016740 |
transferase activity |
| Biological Process |
GO:0006325 |
chromatin organization |
| Biological Process |
GO:0016242 |
negative regulation of macroautophagy |
| Biological Process |
GO:0007000 |
nucleolus organization |
| Biological Process |
GO:1903955 |
positive regulation of protein targeting to mitochondrion |
| Biological Process |
GO:0016579 |
protein deubiquitination |
| Biological Process |
GO:0050821 |
protein stabilization |
| Biological Process |
GO:0006508 |
proteolysis |
| Biological Process |
GO:0042981 |
regulation of apoptotic process |
| Biological Process |
GO:1901524 |
regulation of mitophagy |
| Biological Process |
GO:0031647 |
regulation of protein stability |
| Biological Process |
GO:2000232 |
regulation of rRNA processing |
Reference
[1] 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.