UBP13_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: UBP13_MOUSE
• UniProt AC: Q5BKP2
• Protein Name: Ubiquitin carboxyl-terminal hydrolase 13
• Gene Name: Usp13
• Organism: Mus musculus (Mouse).
• Sequence Length: 858
• Protein Description: Deubiquitinase that mediates deubiquitination of target proteins such as BECN1, MITF, SKP2 and USP10 and is involved in various processes such as autophagy and endoplasmic reticulum-associated degradation (ERAD). 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. Also deubiquitinates USP10, an essential regulator of p53/TP53 stability. In turn, PIK3C3/VPS34-containing complexes regulate USP13 stability, suggesting the existence of a regulatory system by which PIK3C3/VPS34-containing complexes regulate p53/TP53 protein levels via USP10 and USP13. Recruited by nuclear UFD1 and mediates deubiquitination of SKP2, thereby regulating endoplasmic reticulum-associated degradation (ERAD). Also regulates ERAD through the deubiquitination of UBL4A a component of the BAG6/BAT3 complex. Mediates stabilization of SIAH2 independently of deubiquitinase activity: binds ubiquitinated SIAH2 and acts by impairing SIAH2 autoubiquitination. Has a weak deubiquitinase activity in vitro and preferentially cleaves 'Lys-63'-linked polyubiquitin chains. In contrast to USP5, it is not able to mediate unanchored polyubiquitin disassembly. Able to cleave ISG15 in vitro; however, additional experiments are required to confirm such data..
• Protein Sequence: MQRRGALFSVPGGGGKMAAGDLGELLVPHMPTIRVPRSGDRVYKNECAFSYDSPNSEGGLYVCMNTFLAFGREHVERHFRKTGQSVYMHLKRHMREKVRGASGGALPKRRNSKIFLDLDMDDDLNSDDYEYEDEAKLVIFPDHYEIALPNIEELPALVTIACDAVLSSKSPYRKQDPDTWENEVPVSKYANNLVQLDNGVRIPPSGWKCARCDLRENLWLNLTDGSVLCGKWFFDSSGGNGHALEHYRDMGYPLAVKLGTITPDGADVYSFQEEGPVSDPHLAKHLAHFGIDMLHTQGTENGLRDNDIKPRVSEWEVIQESGTKLKPMYGPGYTGLKNLGNSCYLSSVMQAIFSIPEFQRAYVGNLPRIFDYSPLDPTQDFNTQMTKLGHGLLSGQYSKPPVKSELIEQVMKEEHKPQQNGISPRMFKAFVSKSHPEFSSNRQQDAQEFFLHLVNLVERNRIGSENPSDVFRFLVEERIQCCQTRKVRYTERVDYLMQLPVAMEAATNKDELITYELMRREAEANRRPLPELVRAKIPFSACLQAFAEPDNVDDFWSSALQAKSAGVKTSRFASFPEYLVVQIKKFTFGLDWVPRKFDVSIDMPDLLDISHLRARGLQPGEEELPDISPPIVIPDDSKDRLMNQLIDPSDIDESSVMQLAEMGFPLEACRKAVYFTGNTGAEVAFNWIIVHMEEPDFAEPLAIPGYGGAGASVFGATGLDNQPPEEIVAIITSMGFQRNQAVQALQATNHNLERALDWIFSHPEFEEDSDFVIEMENNANANIVSEAKPEGPRVKDGSGMYELFAFISHMGTSTMSGHYVCHIKKEGRWVIYNDHKVCASERPPKDLGYMYFYRRIPS

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
77	Ubiquitination	FGREHVERHFRKTGQ HCHHHHHHHHHHHCH	32.91	27667366
112	Phosphorylation	ALPKRRNSKIFLDLD CCCCCCCCEEEEECC	25.89	-
262	Phosphorylation	AVKLGTITPDGADVY EEEECEECCCCCCEE	18.37	-
324	Ubiquitination	VIQESGTKLKPMYGP HHHCCCCCCCCCCCC	59.02	22790023
326	Ubiquitination	QESGTKLKPMYGPGY HCCCCCCCCCCCCCC	29.33	22790023
563	Acetylation	WSSALQAKSAGVKTS HHHHHHHHHCCCCCC	28.07	19861917
568	Acetylation	QAKSAGVKTSRFASF HHHHCCCCCCCCCCC	39.61	19861925
628	Phosphorylation	EEELPDISPPIVIPD CCCCCCCCCCEECCC	31.81	29899451
638	Ubiquitination	IVIPDDSKDRLMNQL EECCCCCCCHHHHHC	54.59	22790023
813	Phosphorylation	FISHMGTSTMSGHYV HHHCCCCCCCCCEEE	19.18	-

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

Oops, there are no upstream regulatory protein records of UBP13_MOUSE !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of UBP13_MOUSE !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of UBP13_MOUSE !!

Protein-Protein Interaction

Oops, there are no PPI records of UBP13_MOUSE !!

Drug and Disease Associations

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