OTUB1_RAT - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: OTUB1_RAT
• UniProt AC: B2RYG6
• Protein Name: Ubiquitin thioesterase OTUB1 {ECO:0000250|UniProtKB:Q7TQI3}
• Gene Name: Otub1 {ECO:0000312|EMBL:AAI66771.1}
• Organism: Rattus norvegicus (Rat).
• 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 (By similarity).; 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	29779826
18	Phosphorylation	QEPLGSDSEGVNCLA CCCCCCCCCCCCCHH	37.64	27097102
26	Phosphorylation	EGVNCLAYDEAIMAQ CCCCCHHHHHHHHHH	11.02	25403869
71	Ubiquitination	DDNIYQQKIKDLHKK CCCCCHHHHHHHHHH	35.88	-
91	S-nitrosocysteine	KTRPDGNCFYRAFGF CCCCCCCHHHHHCCH	3.76	-
91	S-nitrosylation	KTRPDGNCFYRAFGF CCCCCCCHHHHHCCH	3.76	21278135
109	Acetylation	EALLDDSKELQRFKA HHHHCCCHHHHHHHH	70.23	22902405
109	Ubiquitination	EALLDDSKELQRFKA HHHHCCCHHHHHHHH	70.23	-
188	Acetylation	GYLQRESKFFEHFIE CHHHHHHHHHHHHHH	49.69	22902405
199	Phosphorylation	HFIEGGRTVKEFCQQ HHHHCCHHHHHHHHH	38.92	23984901
201	Ubiquitination	IEGGRTVKEFCQQEV HHCCHHHHHHHHHHH	44.45	-

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

Oops, there are no upstream regulatory protein records of OTUB1_RAT !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of OTUB1_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 OTUB1_RAT !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
PGS2_RAT	Dcn	physical	22279542

Drug and Disease Associations

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