UBP10_MOUSE - dbPTM
UBP10_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID UBP10_MOUSE
UniProt AC P52479
Protein Name Ubiquitin carboxyl-terminal hydrolase 10
Gene Name Usp10
Organism Mus musculus (Mouse).
Sequence Length 792
Subcellular Localization Cytoplasm . Nucleus . Early endosome . Cytoplasmic in normal conditions (By similarity). After DNA damage, translocates to the nucleus following phosphorylation by ATM (By similarity).
Protein Description Hydrolase that can remove conjugated ubiquitin from target proteins such as p53/TP53, BECN1, SNX3 and CFTR. Acts as an essential regulator of p53/TP53 stability: in unstressed cells, specifically deubiquitinates p53/TP53 in the cytoplasm, leading to counteract MDM2 action and stabilize p53/TP53. Following DNA damage, translocates to the nucleus and deubiquitinates p53/TP53, leading to regulate the p53/TP53-dependent DNA damage response. Component of a regulatory loop that controls autophagy and p53/TP53 levels: mediates deubiquitination of BECN1, a key regulator of autophagy, leading to stabilize the PIK3C3/VPS34-containing complexes. In turn, PIK3C3/VPS34-containing complexes regulate USP10 stability, suggesting the existence of a regulatory system by which PIK3C3/VPS34-containing complexes regulate p53/TP53 protein levels via USP10 and USP13. Does not deubiquitinate MDM2. Deubiquitinates CFTR in early endosomes, enhancing its endocytic recycling. Involved in a TANK-dependent negative feedback response to attenuate NF-kappaB activation via deubiquitinating IKBKG or TRAF6 in response to interleukin-1-beta (IL1B) stimulation or upon DNA damage. Deubiquitinates TBX21 leading to its stabilization..
Protein Sequence MALHNPQYIFGDFSPDEFNQFFVTPRSSVELPPYSGTLCSIQAEDELPDGQEHQRIEFGVDEVIEPSEGLPPTPSYSISSTLNPQAPEFILGCTTSKKIPEAVEKDETYSSIDQYPASALALESNSNAEAETLENDSGAGGLGQRERKKKKKRPPGYYSYLKDGGEDSASPATLVNGHATSVGTSGEAVEDAEFMDVLPPVMPRTCDSPQNPVDFISGPVPDSPFPRTLGGDARTAGLCEGCHEADFEQPCLPADSLLRTAGTQPYVGTDTTENFAVANGKILESPGEDTAANGAELHTDEGADLDPAKPESQSPPAESALSASGAIPISQPAKSWASLFHDSKPSASSPMAYVETKCSPPVPSPLASEKQMEVKEGLVPVSEDPVAIKIAELLETVTLIHKPVSLQPRGLINKGNWCYINATLQALVACPPMYHLMKFIPLYSKVQRPCTSTPMIDSFVRLMNEFTNMPVPPKPRQALGDKIVRDIRPGAAFEPTYIYRLLTVIKSSLSEKGRQEDAEEYLGFILNGLHEEMLSLKKLLSPTHEKHSVSNGPRSDLIEDEELEDTGKGSEDEWEQVGPKNKTSITRQADFVQTPITGIFGGHIRSVVYQQSSKESATLQLFFTLQLDIQSDKIRTVQDALESLVARESVQGYTTKTKQEVEVSRRVTLEKLPPVLVLHLKRFVYEKTGGCQKLVKNIDYPVDLEISRELLSPGIKNKNFKCQRTYRLFAVVYHHGNSATGGHYTTDVFQIGLNGWLRIDDQTVKVINQYQVVKPPADRTAYLLYYRRVDLL
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
2Acetylation------MALHNPQYI
------CCCCCCCEE		19.96-
8PhosphorylationMALHNPQYIFGDFSP
CCCCCCCEECCCCCH		10.2426643407
14PhosphorylationQYIFGDFSPDEFNQF
CEECCCCCHHHHHCC		35.8626643407
24PhosphorylationEFNQFFVTPRSSVEL
HHHCCEECCCCCCCC		14.0826643407
27 (in isoform 2)Phosphorylation-39.6829472430
27PhosphorylationQFFVTPRSSVELPPY
CCEECCCCCCCCCCC		39.6830352176
28PhosphorylationFFVTPRSSVELPPYS
CEECCCCCCCCCCCC		22.3830352176
28 (in isoform 2)Phosphorylation-22.3829472430
34 (in isoform 2)Phosphorylation-20.1429472430
35 (in isoform 2)Phosphorylation-30.9529472430
37 (in isoform 2)Phosphorylation-20.7429472430
40 (in isoform 2)Phosphorylation-22.3529472430
110PhosphorylationVEKDETYSSIDQYPA
HHCCCCCCCHHHCCH		28.3925338131
118PhosphorylationSIDQYPASALALESN
CHHHCCHHHHHHHCC		21.2225338131
124PhosphorylationASALALESNSNAEAE
HHHHHHHCCCCHHCE		46.5425338131
126PhosphorylationALALESNSNAEAETL
HHHHHCCCCHHCEEC		46.8527087446
132PhosphorylationNSNAEAETLENDSGA
CCCHHCEECCCCCCC		46.5527087446
152MalonylationRERKKKKKRPPGYYS
HHHHCCCCCCCCCHH		78.1326320211
205PhosphorylationLPPVMPRTCDSPQNP
CCCCCCCCCCCCCCC		18.1324925903
208PhosphorylationVMPRTCDSPQNPVDF
CCCCCCCCCCCCCCC		30.4524925903
209PhosphorylationMPRTCDSPQNPVDFI
CCCCCCCCCCCCCCC		25.3924719451
217PhosphorylationQNPVDFISGPVPDSP
CCCCCCCCCCCCCCC		36.7225619855
223PhosphorylationISGPVPDSPFPRTLG
CCCCCCCCCCCCCCC		23.5224925903
228PhosphorylationPDSPFPRTLGGDART
CCCCCCCCCCCCCCC		29.9623984901
285PhosphorylationANGKILESPGEDTAA
ECCEECCCCCCCCCC		34.4620469934
290PhosphorylationLESPGEDTAANGAEL
CCCCCCCCCCCCCCC		24.3023649490
299PhosphorylationANGAELHTDEGADLD
CCCCCCCCCCCCCCC		48.6623140645
312PhosphorylationLDPAKPESQSPPAES
CCCCCCHHCCCCHHH		44.4823140645
314PhosphorylationPAKPESQSPPAESAL
CCCCHHCCCCHHHHH		41.9724453211
319PhosphorylationSQSPPAESALSASGA
HCCCCHHHHHHCCCC		36.2923649490
322PhosphorylationPPAESALSASGAIPI
CCHHHHHHCCCCCCC		21.8024453211
324PhosphorylationAESALSASGAIPISQ
HHHHHHCCCCCCCCC		25.9423140645
330PhosphorylationASGAIPISQPAKSWA
CCCCCCCCCCCCHHH		25.4220469934
335PhosphorylationPISQPAKSWASLFHD
CCCCCCCHHHHHHCC		29.9523984901
338PhosphorylationQPAKSWASLFHDSKP
CCCCHHHHHHCCCCC		25.8823984901
343PhosphorylationWASLFHDSKPSASSP
HHHHHCCCCCCCCCC		37.5923984901
344AcetylationASLFHDSKPSASSPM
HHHHCCCCCCCCCCC		49.3923954790
346PhosphorylationLFHDSKPSASSPMAY
HHCCCCCCCCCCCEE		44.5123984901
348PhosphorylationHDSKPSASSPMAYVE
CCCCCCCCCCCEEEE		39.0326643407
349PhosphorylationDSKPSASSPMAYVET
CCCCCCCCCCEEEEE		20.5723984901
353PhosphorylationSASSPMAYVETKCSP
CCCCCCEEEEECCCC		7.8026643407
356PhosphorylationSPMAYVETKCSPPVP
CCCEEEEECCCCCCC		27.5726643407
359PhosphorylationAYVETKCSPPVPSPL
EEEEECCCCCCCCCC		33.5225521595
360PhosphorylationYVETKCSPPVPSPLA
EEEECCCCCCCCCCC		43.2924719451
364PhosphorylationKCSPPVPSPLASEKQ
CCCCCCCCCCCCHHH		32.5522942356
368PhosphorylationPVPSPLASEKQMEVK
CCCCCCCCHHHCEEC		53.6725619855
402 (in isoform 2)Ubiquitination-39.8722790023
402UbiquitinationETVTLIHKPVSLQPR
HHEEEECCCCCCCCC		39.8722790023
403 (in isoform 2)Ubiquitination-13.53-
445UbiquitinationKFIPLYSKVQRPCTS
HHHHHHHHCCCCCCC		28.9122790023
445 (in isoform 2)Ubiquitination-28.9122790023
446 (in isoform 2)Ubiquitination-4.86-
482AcetylationPRQALGDKIVRDIRP
CCCCCCCHHHHCCCC		41.106571721
541PhosphorylationLSLKKLLSPTHEKHS
HHHHHHHCCCCHHCC		37.8825521595
543PhosphorylationLKKLLSPTHEKHSVS
HHHHHCCCCHHCCCC		39.0126745281
555PhosphorylationSVSNGPRSDLIEDEE
CCCCCCHHHCCCCCH		39.6425619855
566PhosphorylationEDEELEDTGKGSEDE
CCCHHHHCCCCCHHH		31.2725521595
570PhosphorylationLEDTGKGSEDEWEQV
HHHCCCCCHHHHHHC		45.4124925903
571PhosphorylationEDTGKGSEDEWEQVG
HHCCCCCHHHHHHCC		69.4924719451
616PhosphorylationYQQSSKESATLQLFF
EECCCCCCEEEEEEE		30.2327357545
618PhosphorylationQSSKESATLQLFFTL
CCCCCCEEEEEEEEE		25.0627357545
624PhosphorylationATLQLFFTLQLDIQS
EEEEEEEEEECHHCC		13.2727357545
631PhosphorylationTLQLDIQSDKIRTVQ
EEECHHCCCHHHHHH		41.0027357545
636PhosphorylationIQSDKIRTVQDALES
HCCCHHHHHHHHHHH		26.4522345495
643PhosphorylationTVQDALESLVARESV
HHHHHHHHHHHHHHH		29.0622345495
649PhosphorylationESLVARESVQGYTTK
HHHHHHHHHCCCCCC		17.7530635358
653PhosphorylationARESVQGYTTKTKQE
HHHHHCCCCCCCCCE		8.3130635358
654PhosphorylationRESVQGYTTKTKQEV
HHHHCCCCCCCCCEE		28.7430635358
655PhosphorylationESVQGYTTKTKQEVE
HHHCCCCCCCCCEEE		28.3830635358
656UbiquitinationSVQGYTTKTKQEVEV
HHCCCCCCCCCEEEE		46.0227667366
657PhosphorylationVQGYTTKTKQEVEVS
HCCCCCCCCCEEEEE		35.5530635358
657UbiquitinationVQGYTTKTKQEVEVS
HCCCCCCCCCEEEEE		35.5527667366
664PhosphorylationTKQEVEVSRRVTLEK
CCCEEEEECCCCHHH		10.8130635358
671UbiquitinationSRRVTLEKLPPVLVL
ECCCCHHHCCCEEEE		70.2122790023
671 (in isoform 2)Ubiquitination-70.2122790023
672 (in isoform 2)Ubiquitination-4.18-
681UbiquitinationPVLVLHLKRFVYEKT
CEEEEEEEHHHHHHC		32.8027667366
682UbiquitinationVLVLHLKRFVYEKTG
EEEEEEEHHHHHHCC		32.4027667366
687MalonylationLKRFVYEKTGGCQKL
EEHHHHHHCCCCHHH		34.4826320211
696UbiquitinationGGCQKLVKNIDYPVD
CCCHHHHHCCCCCCC		59.6322790023
696 (in isoform 2)Ubiquitination-59.6322790023
697 (in isoform 2)Ubiquitination-25.53-
700PhosphorylationKLVKNIDYPVDLEIS
HHHHCCCCCCCHHHH		11.0223984901
707PhosphorylationYPVDLEISRELLSPG
CCCCHHHHHHHHCCC		15.4423984901
712PhosphorylationEISRELLSPGIKNKN
HHHHHHHCCCCCCCC		33.4326745281
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources
330SPhosphorylationKinaseATMQ62388
Uniprot
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of UBP10_MOUSE !!
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of UBP10_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PABP1_HUMANPABPC1physical
23230274
G3BP1_HUMANG3BP1physical
23230274
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of UBP10_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,Thibault P.;
Immunity 30:143-154(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-570, AND MASSSPECTROMETRY.
"Specific phosphopeptide enrichment with immobilized titanium ionaffinity chromatography adsorbent for phosphoproteome analysis.";
Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
J. Proteome Res. 7:3957-3967(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-570, AND MASSSPECTROMETRY.
"Large-scale phosphorylation analysis of mouse liver.";
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-205 AND SER-570, ANDMASS SPECTROMETRY.
"Protein phosphorylation and expression profiling by Yin-yangmultidimensional liquid chromatography (Yin-yang MDLC) massspectrometry.";
Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
J. Proteome Res. 6:250-262(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-570, AND MASSSPECTROMETRY.

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