OTUB1_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: OTUB1_MOUSE
• UniProt AC: Q7TQI3
• Protein Name: Ubiquitin thioesterase OTUB1
• Gene Name: Otub1
• Organism: Mus musculus (Mouse).
• Sequence Length: 271
• Subcellular Localization: Cytoplasm.
• Protein Description: Hydrolase that can specifically remove compared to 'Lys-48'-linked conjugated ubiquitin from proteins and plays an important regulatory role at the level of protein turnover by preventing degradation. Regulator of T-cell anergy, a phenomenon that occurs when T-cells are rendered unresponsive to antigen rechallenge and no longer respond to their cognate antigen. Acts via its interaction with RNF128/GRAIL. Surprisingly, it regulates RNF128-mediated ubiquitination, but does not deubiquitinate polyubiquitinated RNF128. Deubiquitinates estrogen receptor alpha (ESR1). Mediates deubiquitination of 'Lys-48'-linked polyubiquitin chains, but not 'Lys-63'-linked polyubiquitin chains. Not able to cleave di-ubiquitin. Also capable of removing NEDD8 from NEDD8 conjugates, but with a much lower preference compared to 'Lys-48'-linked ubiquitin.; Plays a key non-catalytic role in DNA repair regulation by inhibiting activity of RNF168, an E3 ubiquitin-protein ligase that promotes accumulation of 'Lys-63'-linked histone H2A and H2AX at DNA damage sites. Inhibits RNF168 independently of ubiquitin thioesterase activity by binding and inhibiting UBE2N/UBC13, the E2 partner of RNF168, thereby limiting spreading of 'Lys-63'-linked histone H2A and H2AX marks. Inhibition occurs by binding to free ubiquitin: free ubiquitin acts as an allosteric regulator that increases affinity for UBE2N/UBC13 and disrupts interaction with UBE2V1. The OTUB1-UBE2N/UBC13-free ubiquitin complex adopts a configuration that mimics a cleaved 'Lys48'-linked di-ubiquitin chain (By similarity)..
• Protein Sequence: MAAEEPQQQKQEPLGSDSEGVNCLAYDEAIMAQQDRIQQEIAVQNPLVSERLELSVLYKEYAEDDNIYQQKIKDLHKKYSYIRKTRPDGNCFYRAFGFSHLEALLDDSKELQRFKAVSAKSKEDLVSQGFTEFTIEDFHNTFMDLIEQVEKQTSVADLLASFNDQSTSDYLVVYLRLLTSGYLQRESKFFEHFIEGGRTVKEFCQQEVEPMCKESDHIHIIALAQALSVSIQVEYMDRGEGGTTNPHVFPEGSEPKVYLLYRPGHYDILYK

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	------MAAEEPQQQ ------CCCCCHHHH	24.47	-
16	Phosphorylation	QKQEPLGSDSEGVNC HCCCCCCCCCCCCCC	45.72	25521595
18	Phosphorylation	QEPLGSDSEGVNCLA CCCCCCCCCCCCCHH	37.64	24925903
26	Phosphorylation	EGVNCLAYDEAIMAQ CCCCCHHHHHHHHHH	11.02	25619855
31	Oxidation	LAYDEAIMAQQDRIQ HHHHHHHHHHHHHHH	3.38	17242355
55	Phosphorylation	VSERLELSVLYKEYA HHHHHHHHHHHHHHH	10.74	26824392
59	Ubiquitination	LELSVLYKEYAEDDN HHHHHHHHHHHCCCC	39.84	22790023
71	Acetylation	DDNIYQQKIKDLHKK CCCCCHHHHHHHHHH	35.88	23954790
71	Ubiquitination	DDNIYQQKIKDLHKK CCCCCHHHHHHHHHH	35.88	22790023
78	Ubiquitination	KIKDLHKKYSYIRKT HHHHHHHHHHHHCCC	28.78	27667366
84	Ubiquitination	KKYSYIRKTRPDGNC HHHHHHCCCCCCCCH	39.05	22790023
91	Glutathionylation	KTRPDGNCFYRAFGF CCCCCCCHHHHHCCH	3.76	24333276
99	Phosphorylation	FYRAFGFSHLEALLD HHHHCCHHHHHHHHC	27.78	23984901
108	Phosphorylation	LEALLDDSKELQRFK HHHHHCCCHHHHHHH	27.91	29899451
109	Ubiquitination	EALLDDSKELQRFKA HHHHCCCHHHHHHHH	70.23	22790023
109	Acetylation	EALLDDSKELQRFKA HHHHCCCHHHHHHHH	70.23	23954790
118	Phosphorylation	LQRFKAVSAKSKEDL HHHHHHHCCCCHHHH	34.53	20139300
121	Phosphorylation	FKAVSAKSKEDLVSQ HHHHCCCCHHHHHHC	40.78	20139300
187	Phosphorylation	SGYLQRESKFFEHFI HCHHHHHHHHHHHHH	36.63	25338131
188	Acetylation	GYLQRESKFFEHFIE CHHHHHHHHHHHHHH	49.69	22826441
188	Ubiquitination	GYLQRESKFFEHFIE CHHHHHHHHHHHHHH	49.69	22790023
201	Ubiquitination	IEGGRTVKEFCQQEV HHCCHHHHHHHHHHH	44.45	22790023
201	Acetylation	IEGGRTVKEFCQQEV HHCCHHHHHHHHHHH	44.45	22826441

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

Oops, there are no upstream regulatory protein records of OTUB1_MOUSE !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of OTUB1_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 OTUB1_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SMAD2_MOUSE	Smad2	physical	24071738
SMAD3_MOUSE	Smad3	physical	24071738

Drug and Disease Associations

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

Related Literatures of Post-Translational Modification

Phosphorylation

"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 SER-16, AND MASSSPECTROMETRY.
PubMed: 17242355