UBP36_MOUSE - dbPTM
UBP36_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID UBP36_MOUSE
UniProt AC B1AQJ2
Protein Name Ubiquitin carboxyl-terminal hydrolase 36
Gene Name Usp36
Organism Mus musculus (Mouse).
Sequence Length 1098
Subcellular Localization Nucleus, nucleolus . Cytoplasm .
Protein Description Deubiquitinase essential for the regulation of nucleolar structure and function. Required for cell and organism viability. 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: 29273634 Function 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 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. In contrast, it does not interact with isoform 1 of FBXW7 (FBW7alpha) in the nucleoplasm. 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. Deubiquitinates SOD2, regulates SOD2 protein stability. Deubiquitinase activity is required to control selective autophagy activation by ubiquitinated proteins (By similarity]
Protein Sequence MPIVDKLKEALKPGRKDSAEDGDLGRLLAASAKKVLLQRIEFEPASKSFSYQLESLKSKYVLLSARAEGASRHRSGDELQARKPGTERVSGSGGDGVPAPQKVLFPVERLSLRWERVFRVGAGLHNLGNTCFLNSTIQCLTYTPPLANYLLSKEHARSCHQGGFCMLCLMQNHMVQAFANSGNAIKPVSFIRDLKKIARHFRFGNQEDAHEFLRYTIDAMQKACLNGYAKLDRQTQATTLVHQIFGGYLRSRVKCSVCKSVSDTYDPYLDIALEIRQAANIVRALELFVKSDVLSGENAYMCAKCKKKVPASKRFTIHRTSNVLTLSLKRFANFSGGKITKDVGYPEFLNIRPYMSQSSGDPVMYGLYAVLVHSGYSCHAGHYYCYVKASNGQWYQMNDSLVHSSNVKVVLNQQAYVLFYLRIPGSKKSPEGPVSRVGATLPSRPKVVPEHSKKSPGNGVVPSPLMAKRQDSVMMRKLPAPEEVGVPVSRNGSLPGLKLQNGCAPAKTPAGSPSPRLTPTPTHMPTILDEPGKKVKKSAPLQSLTTSPTTSQGSPGTGESRSQRPGSWASRDTIFSTSPKLLARAITNGHRLKGEGSGVDLEKGDSSSSSPEHSASSDPAKAPQTAESRAAHACDSQGTNCPTAGHPKALLNGVDAKMVKLKSPALSSTTTEPTSLMSPPPAKKLALSAKKASTLRRATGNDIGSPSPSAFCDLTSPMKATHPVVASTGPVSKTRTAAPAPRPSTHPHSASLSSSSAKPLGTSEPQSCRPSAWTPLPQVNGHFTSHLHQLPEASEALHSPSKKRKKTPNGDPQRLGIDTLLPQCLRGAPAAARRKRKKRCSEGEGATAPKQEGQFQDQSWSSGSQKEEGTQPQVNGHQVSHILDSYHVSSRKRRKRKRSEGLSQEATPSQDLIQHSCSPVDHSEPEARTELQKKKKKKRRKRKPEPQQDEESKHPGDQRSPRPSVTPVPALSVNGHLPSDCLGLGQAPLVTWNRDQEPDVVQALLQDSSDKAYGKKVLTWDGEPSAISQDAIKDSRLARTQTVVDDWDEEFDRGKEKKIKKFKREKKRNFNAFQKLQSRRNFWSVTHPAKVASLSYRR
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
18PhosphorylationLKPGRKDSAEDGDLG
HCCCCCCCCCCCHHH		36.2726824392
31PhosphorylationLGRLLAASAKKVLLQ
HHHHHHHHHHHHHHH		34.7128066266
75PhosphorylationEGASRHRSGDELQAR
CCHHCCCCCCCCCCC		44.4625159016
111PhosphorylationLFPVERLSLRWERVF
EEEEHHHHHCHHHHE		23.3124704852
335PhosphorylationLKRFANFSGGKITKD
EEEHHCCCCCCCCCC		46.5828382018
338UbiquitinationFANFSGGKITKDVGY
HHCCCCCCCCCCCCC		51.2127667366
426PhosphorylationFYLRIPGSKKSPEGP
EEEECCCCCCCCCCC		31.4029514104
429PhosphorylationRIPGSKKSPEGPVSR
ECCCCCCCCCCCCCC		31.7428066266
435PhosphorylationKSPEGPVSRVGATLP
CCCCCCCCCCCCCCC		25.1222668510
463PhosphorylationPGNGVVPSPLMAKRQ
CCCCCCCCCCHHHCC		21.0328059163
508PhosphorylationNGCAPAKTPAGSPSP
CCCCCCCCCCCCCCC		22.0726643407
512PhosphorylationPAKTPAGSPSPRLTP
CCCCCCCCCCCCCCC		25.0626643407
514PhosphorylationKTPAGSPSPRLTPTP
CCCCCCCCCCCCCCC		25.0926643407
518PhosphorylationGSPSPRLTPTPTHMP
CCCCCCCCCCCCCCC		26.7925159016
520PhosphorylationPSPRLTPTPTHMPTI
CCCCCCCCCCCCCCC		35.2726643407
522PhosphorylationPRLTPTPTHMPTILD
CCCCCCCCCCCCCCC		33.0326643407
538PhosphorylationPGKKVKKSAPLQSLT
CCCCCCCCCCCCCEE		29.4223984901
543PhosphorylationKKSAPLQSLTTSPTT
CCCCCCCCEECCCCC		35.0525159016
545PhosphorylationSAPLQSLTTSPTTSQ
CCCCCCEECCCCCCC		30.4025159016
546PhosphorylationAPLQSLTTSPTTSQG
CCCCCEECCCCCCCC		37.6925159016
547PhosphorylationPLQSLTTSPTTSQGS
CCCCEECCCCCCCCC		18.2725159016
549PhosphorylationQSLTTSPTTSQGSPG
CCEECCCCCCCCCCC		38.5625159016
550PhosphorylationSLTTSPTTSQGSPGT
CEECCCCCCCCCCCC		23.5722668510
551PhosphorylationLTTSPTTSQGSPGTG
EECCCCCCCCCCCCC		34.7125159016
554PhosphorylationSPTTSQGSPGTGESR
CCCCCCCCCCCCCCC		16.7225159016
557PhosphorylationTSQGSPGTGESRSQR
CCCCCCCCCCCCCCC		40.9525159016
560PhosphorylationGSPGTGESRSQRPGS
CCCCCCCCCCCCCCC		38.2823984901
567PhosphorylationSRSQRPGSWASRDTI
CCCCCCCCCCCCCCC		23.3525338131
576PhosphorylationASRDTIFSTSPKLLA
CCCCCCCCCCHHHHH		24.9126745281
577PhosphorylationSRDTIFSTSPKLLAR
CCCCCCCCCHHHHHH		38.0024453211
578PhosphorylationRDTIFSTSPKLLARA
CCCCCCCCHHHHHHH		20.8826824392
597PhosphorylationHRLKGEGSGVDLEKG
CCCCCCCCCCCCCCC		31.2025159016
606PhosphorylationVDLEKGDSSSSSPEH
CCCCCCCCCCCCCCC		40.5721149613
607PhosphorylationDLEKGDSSSSSPEHS
CCCCCCCCCCCCCCC		38.6921149613
608PhosphorylationLEKGDSSSSSPEHSA
CCCCCCCCCCCCCCC		38.4921149613
609PhosphorylationEKGDSSSSSPEHSAS
CCCCCCCCCCCCCCC		52.4321149613
610PhosphorylationKGDSSSSSPEHSASS
CCCCCCCCCCCCCCC		35.9321149613
614PhosphorylationSSSSPEHSASSDPAK
CCCCCCCCCCCCCCC		28.3423984901
616PhosphorylationSSPEHSASSDPAKAP
CCCCCCCCCCCCCCC		37.9823984901
617PhosphorylationSPEHSASSDPAKAPQ
CCCCCCCCCCCCCCC		47.5323984901
663PhosphorylationAKMVKLKSPALSSTT
CEEEECCCCCCCCCC		26.33-
667PhosphorylationKLKSPALSSTTTEPT
ECCCCCCCCCCCCCC		27.9528066266
668PhosphorylationLKSPALSSTTTEPTS
CCCCCCCCCCCCCCC		30.5328066266
669PhosphorylationKSPALSSTTTEPTSL
CCCCCCCCCCCCCCC		34.0728066266
670PhosphorylationSPALSSTTTEPTSLM
CCCCCCCCCCCCCCC		30.9828066266
671PhosphorylationPALSSTTTEPTSLMS
CCCCCCCCCCCCCCC		39.8028066266
674PhosphorylationSSTTTEPTSLMSPPP
CCCCCCCCCCCCCCH		28.4128066266
675PhosphorylationSTTTEPTSLMSPPPA
CCCCCCCCCCCCCHH		32.5628066266
678PhosphorylationTEPTSLMSPPPAKKL
CCCCCCCCCCHHHHH		39.2826745281
705PhosphorylationATGNDIGSPSPSAFC
HHCCCCCCCCCCCCC		23.6524453211
707PhosphorylationGNDIGSPSPSAFCDL
CCCCCCCCCCCCCCC		32.9325619855
709PhosphorylationDIGSPSPSAFCDLTS
CCCCCCCCCCCCCCC		38.0125619855
715PhosphorylationPSAFCDLTSPMKATH
CCCCCCCCCCCCCCC		19.9625619855
716PhosphorylationSAFCDLTSPMKATHP
CCCCCCCCCCCCCCC		30.2325619855
841PhosphorylationRKRKKRCSEGEGATA
HHHHHCCCCCCCCCC		53.3125263469
899PhosphorylationKRRKRKRSEGLSQEA
HHHHHHHHHCCCCCC		38.7725159016
903PhosphorylationRKRSEGLSQEATPSQ
HHHHHCCCCCCCCCH		36.5125159016
907PhosphorylationEGLSQEATPSQDLIQ
HCCCCCCCCCHHHHH		23.7923984901
909PhosphorylationLSQEATPSQDLIQHS
CCCCCCCCHHHHHHC		31.7825159016
916PhosphorylationSQDLIQHSCSPVDHS
CHHHHHHCCCCCCCC		10.4221149613
918PhosphorylationDLIQHSCSPVDHSEP
HHHHHCCCCCCCCCH		30.8522942356
923PhosphorylationSCSPVDHSEPEARTE
CCCCCCCCCHHHHHH		50.8421149613
1009PhosphorylationQALLQDSSDKAYGKK
HHHHHCCCCCCCCCE		51.9619854140
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

Oops, there are no upstream regulatory protein records of UBP36_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of UBP36_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 UBP36_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of UBP36_MOUSE !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of UBP36_MOUSE

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Related Literatures of Post-Translational Modification

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