UBP15_RAT - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: UBP15_RAT
• UniProt AC: Q9R085
• Protein Name: Ubiquitin carboxyl-terminal hydrolase 15
• Gene Name: Usp15
• Organism: Rattus norvegicus (Rat).
• Sequence Length: 952
• 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: MAEGGAADLDTQRSDIATLLKTSLRKGDTWYLVDSRWFKQWKKYVGFDSWDKYQMGDQNVYPGPIDNSGLLKDGDAQSLKEHLIDELDYILLPTEGWNKLVSWYTLMEGQEPIARKVVEQGMFVKHCKVEVYLTELKLCENGNMNNVVTRRFSKADTIDTIEKEIRKIFNIPDEKEARLWNKYMSNTFEPLNKPDSTIQDAGLYQGQVLVIEQKNEDGTWPRGPSAPNVKNSNYCLPSYTAYKNYDYSEPGRNNEQPGLCGLSNLGNTCFMNSAIQCLSNTPPLTEYFLNDKYQEELNFDNPLGMRGEIAKSYAELIKQMWSGKFSYVTPRAFKTQVGRFAPQFSGYQQQDCQELLAFLLDGLHEDLNRIRKKPYIQLKDADGRPDKVVAEEAWENHLKRNDSIIVDIFHGLFKSTLVCPECAKISVTFDPFCYLTLPLPMKKERSLEVYLVRMDPLAKPMQYKVIVPKIGNILDLCTALSALSGVPADKMIVTDIYNHRFHRIFAMDENLSSIMERDDIYVFEININRTEDTEHVVIPVCLREKFRHSSYTHHTGSSLFGQPFLMAVPRNNTEDKLYNLLLLRMCRYVKMSTETEETDGPLRCCEDQNINGNGPNGIHEEGSPSEMETDEPDDESSQDQELPSENENSQSEDSVGGDNDSENGLCTEETCKGRLTGHKKRLFTFQFNNLGNTDINYIKDDTRHIRFDDRQLRLDERSFLALDWDPDLKKRYFDENAAEDFEKHESVEYKPPKRPFVKLKDCIELFTTKEKLGAEDPWYCPNCKEHQQATKKLDLWSLPPVLVVHLKRFSYSRYMRDKLDTLVDFPISDLDMSEFLINPNAGPCRYNLIAVSNHYGGMGGGHYTAFAKNKDDGKWYYFDDSSVSSASEDQIVSKAAYVLFYQRQDTFSGTGFFPLDRETKGASAATGVPLESDEDSNDNDNDLENENCMHTN

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
2	Acetylation	------MAEGGAADL ------CCCCCCCCC		-
13	Methylation	AADLDTQRSDIATLL CCCCCCCHHHHHHHH		26494699
44	Phosphorylation	WFKQWKKYVGFDSWD HHHHHHHHCCCCCCC		30181290
49	Phosphorylation	KKYVGFDSWDKYQMG HHHCCCCCCCCCCCC		30181290
232	Phosphorylation	SAPNVKNSNYCLPSY CCCCCCCCCCCCCCC		30181290
234	Phosphorylation	PNVKNSNYCLPSYTA CCCCCCCCCCCCCCE		22276854
245	Phosphorylation	SYTAYKNYDYSEPGR CCCEECCCCCCCCCC		21940666
573	Phosphorylation	MAVPRNNTEDKLYNL EEECCCCCHHHHHHH		-
852	Phosphorylation	RYNLIAVSNHYGGMG EEEEEEEECCCCCCC		28689409
855	Phosphorylation	LIAVSNHYGGMGGGH EEEEECCCCCCCCCC		28689409
863	Phosphorylation	GGMGGGHYTAFAKNK CCCCCCCEEEEEEEC		28689409
864	Phosphorylation	GMGGGHYTAFAKNKD CCCCCCEEEEEEECC		28689409
923	Phosphorylation	DRETKGASAATGVPL CCCCCCCCCCCCCCC		28689409
926	Phosphorylation	TKGASAATGVPLESD CCCCCCCCCCCCCCC		22673903
932	Phosphorylation	ATGVPLESDEDSNDN CCCCCCCCCCCCCCC		27097102
936	Phosphorylation	PLESDEDSNDNDNDL CCCCCCCCCCCCCCC		27097102
951	Phosphorylation	ENENCMHTN------ CCCCCCCCC------		28689409

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of UBP15_RAT !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of UBP15_RAT !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of UBP15_RAT !!

Protein-Protein Interaction

Oops, there are no PPI records of UBP15_RAT !!

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.