UBP15_MOUSE - dbPTM
UBP15_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID UBP15_MOUSE
UniProt AC Q8R5H1
Protein Name Ubiquitin carboxyl-terminal hydrolase 15
Gene Name Usp15
Organism Mus musculus (Mouse).
Sequence Length 981
Subcellular Localization Cytoplasm . Nucleus . Mitochondrion .
Protein Description Hydrolase that removes conjugated ubiquitin from target proteins and regulates various pathways such as the TGF-beta receptor signaling, NF-kappa-B and RNF41/NRDP1-PRKN pathways. Acts as a key regulator of TGF-beta receptor signaling pathway, but the precise mechanism is still unclear: according to a report, acts by promoting deubiquitination of monoubiquitinated R-SMADs (SMAD1, SMAD2 and/or SMAD3), thereby alleviating inhibition of R-SMADs and promoting activation of TGF-beta target genes. According to another reports, regulates the TGF-beta receptor signaling pathway by mediating deubiquitination and stabilization of TGFBR1, leading to an enhanced TGF-beta signal. Able to mediate deubiquitination of monoubiquitinated substrates as well as 'Lys-48'-linked polyubiquitin chains, protecting them against proteasomal degradation. May also regulate gene expression and/or DNA repair through the deubiquitination of histone H2B. Acts as an inhibitor of mitophagy by counteracting the action of parkin (PRKN): hydrolyzes cleavage of 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains attached by parkin on target proteins such as MFN2, thereby reducing parkin's ability to drive mitophagy. Acts as an associated component of COP9 signalosome complex (CSN) and regulates different pathways via this association: regulates NF-kappa-B by mediating deubiquitination of NFKBIA and deubiquitinates substrates bound to VCP. Involved in endosome organization by mediating deubiquitination of SQSTM1: ubiquitinated SQSTM1 forms a molecular bridge that restrains cognate vesicles in the perinuclear region and its deubiquitination releases target vesicles for fast transport into the cell periphery..
Protein Sequence MAEGGAADLDTQRSDIATLLKTSLRKGDTWYLVDSRWFKQWKKYVGFDSWDKYQMGDQNVYPGPIDNSGLLKDGDAQSLKEHLIDELDYILLPTEGWNKLVSWYTLMEGQEPIARKVVEQGMFVKHCKVEVYLTELKLCENGNMNNVVTRRFSKADTIDTIEKEIRKIFNIPDEKEARLWNKYMSNTFEPLNKPDSTIQDAGLYQGQVLVIEQKNEDGTWPRGPSTPKSPGASNFSTLPKISPSSLSNNYNNINNRNVKNSNYCLPSYTAYKNYDYSEPGRNNEQPGLCGLSNLGNTCFMNSAIQCLSNTPPLTEYFLNDKYQEELNFDNPLGMRGEIAKSYAELIKQMWSGKFSYVTPRAFKTQVGRFAPQFSGYQQQDCQELLAFLLDGLHEDLNRIRKKPYIQLKDADGRPDKVVAEEAWENHLKRNDSIIVDIFHGLFKSTLVCPECAKISVTFDPFCYLTLPLPMKKERSLEVYLVRMDPLAKPMQYKVIVPKIGNILDLCTALSALSGVPADKMIVTDIYNHRFHRIFAVDENLSSIMERDDIYVFEININRAEDTEHVVIPVCLREKFRHSSYTHHTGSSLFGQPFLMAIPRNNTEDKLYNLLLLRMCRYVKMSTETEETDGHLRCCEDQNINGNGPNGLHEEGSPSEMETDEPDDESSQDQELPSENENSQSEDSVGGDNDSENGLCTEETCKGQLTGHKKRLFTFQFNNLGNNDINYIKDDTSHIRFDDRQLRLDERSFLALDWDPDLKKRYFDENAAEDFEKHESVEYKPPKRPFVKLKDCIELFTTKEKLGAEDPWYCPNCKEHQQATKKLDLWSLPPVLVVHLKRFSYSRYMRDKLDTLVDFPISDLDMSEFLINPNAGPCRYNLIAVSNHYGGMGGGHYTAFAKNKDDGKWYYFDDSSVSTASEDQIVSKAAYVLFYQRQDTFSGTGFFPLDRETKGASAATGIPLESDEDSNDNDNDLENENCMHTN
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------MAEGGAADL
------CCCCCCCCC
24.92-
154UbiquitinationVVTRRFSKADTIDTI
CEEECCCCCCCHHHH
47.7922790023
193UbiquitinationNTFEPLNKPDSTIQD
CCCCCCCCCCCCCCC
58.8622790023
219PhosphorylationEQKNEDGTWPRGPST
EEECCCCCCCCCCCC
44.62-
225PhosphorylationGTWPRGPSTPKSPGA
CCCCCCCCCCCCCCC
61.2322942356
225 (in isoform 5)Phosphorylation-61.2323375375
226 (in isoform 5)Phosphorylation-37.5625263469
226 (in isoform 2)Phosphorylation-37.5623375375
226PhosphorylationTWPRGPSTPKSPGAS
CCCCCCCCCCCCCCC
37.5626824392
227 (in isoform 2)Phosphorylation-39.1925263469
228UbiquitinationPRGPSTPKSPGASNF
CCCCCCCCCCCCCCC
70.1722790023
229PhosphorylationRGPSTPKSPGASNFS
CCCCCCCCCCCCCCC
29.7526824392
231 (in isoform 2)Ubiquitination-49.05-
233PhosphorylationTPKSPGASNFSTLPK
CCCCCCCCCCCCCCC
44.3025521595
234 (in isoform 5)Phosphorylation-34.0629514104
235 (in isoform 2)Phosphorylation-5.6729514104
236PhosphorylationSPGASNFSTLPKISP
CCCCCCCCCCCCCCH
33.0325619855
237PhosphorylationPGASNFSTLPKISPS
CCCCCCCCCCCCCHH
42.8325619855
242PhosphorylationFSTLPKISPSSLSNN
CCCCCCCCHHHCCCC
25.5126824392
244PhosphorylationTLPKISPSSLSNNYN
CCCCCCHHHCCCCCC
36.8025168779
245PhosphorylationLPKISPSSLSNNYNN
CCCCCHHHCCCCCCC
38.9225619855
247PhosphorylationKISPSSLSNNYNNIN
CCCHHHCCCCCCCCC
25.6125619855
250PhosphorylationPSSLSNNYNNINNRN
HHHCCCCCCCCCCCC
17.5225619855
259UbiquitinationNINNRNVKNSNYCLP
CCCCCCCCCCCCCCC
59.2022790023
263PhosphorylationRNVKNSNYCLPSYTA
CCCCCCCCCCCCCCE
8.6629514104
274PhosphorylationSYTAYKNYDYSEPGR
CCCEECCCCCCCCCC
16.4725367039
276PhosphorylationTAYKNYDYSEPGRNN
CEECCCCCCCCCCCC
12.4625367039
363UbiquitinationYVTPRAFKTQVGRFA
EECCHHHHHCCCCCC
36.7422790023
541PhosphorylationFAVDENLSSIMERDD
EEECCCHHHHHHHCC
29.4223984901
542PhosphorylationAVDENLSSIMERDDI
EECCCHHHHHHHCCE
29.1723984901
562PhosphorylationNINRAEDTEHVVIPV
EEECCCCCCCEEEEE
21.35-
602PhosphorylationMAIPRNNTEDKLYNL
EEECCCCCHHHHHHH
49.4622817900
605UbiquitinationPRNNTEDKLYNLLLL
CCCCCHHHHHHHHHH
46.7922790023
607PhosphorylationNNTEDKLYNLLLLRM
CCCHHHHHHHHHHHH
14.9825168779
621PhosphorylationMCRYVKMSTETEETD
HHHHHCCCCCCCCCC
19.8522817900
622PhosphorylationCRYVKMSTETEETDG
HHHHCCCCCCCCCCC
43.3520415495
624PhosphorylationYVKMSTETEETDGHL
HHCCCCCCCCCCCCE
38.9320415495
627PhosphorylationMSTETEETDGHLRCC
CCCCCCCCCCCEEEC
40.8420415495
696PhosphorylationDSENGLCTEETCKGQ
CCCCCCCCCHHHCCC
41.73-
699PhosphorylationNGLCTEETCKGQLTG
CCCCCCHHHCCCCCC
17.18-
705PhosphorylationETCKGQLTGHKKRLF
HHHCCCCCCCCCEEE
29.38-
758UbiquitinationLDWDPDLKKRYFDEN
CCCCHHHHHHHCCCC
42.4522790023
847UbiquitinationYSRYMRDKLDTLVDF
HHHHHHHHHCCCCCC
37.59-
881PhosphorylationRYNLIAVSNHYGGMG
EEEEEEEECCCCCCC
14.63-
952PhosphorylationDRETKGASAATGIPL
CCCCCCCCCCCCCCC
27.4025159016
955PhosphorylationTKGASAATGIPLESD
CCCCCCCCCCCCCCC
35.0525521595
961PhosphorylationATGIPLESDEDSNDN
CCCCCCCCCCCCCCC
54.7225521595
965PhosphorylationPLESDEDSNDNDNDL
CCCCCCCCCCCCCCC
43.9925521595
980PhosphorylationENENCMHTN------
CCCCCCCCC------
0.0025159016

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
678SPhosphorylationKinaseATMQ62388
PSP

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of UBP15_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 UBP15_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SART3_HUMANSART3physical
24984263

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of UBP15_MOUSE

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Related Literatures of Post-Translational Modification

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