PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
24469331-3	2014	They catalyse ubiquitin conjugation by a concerted RING/HECT-like mechanism in which the RING1 domain facilitates E2-discharge to directly form a thioester intermediate with a cysteine in RING2.	Cysteine	176-184	ring finger protein 2	Homo sapiens	188-193	
30446597-6	2018	Further, NMR and mass spectrometry experiments indicate the RING0/RING2 interface is re-modelled, remote from the E2 binding site, and this alters the reactivity of the RING2(Rcat) catalytic cysteine, needed for ubiquitin transfer.	Cysteine	191-199	ring finger protein 2	Homo sapiens	66-71	
30446597-6	2018	Further, NMR and mass spectrometry experiments indicate the RING0/RING2 interface is re-modelled, remote from the E2 binding site, and this alters the reactivity of the RING2(Rcat) catalytic cysteine, needed for ubiquitin transfer.	Cysteine	191-199	ring finger protein 2	Homo sapiens	169-174	
29311602-2	2018	The RBR module comprises three domains, RING1, IBR and RING2 that collaborate to transfer ubiquitin from the E2~Ub conjugate, recognised by RING1, onto a catalytic cysteine in RING2 and finally onto the substrate in a multi-step reaction.	Cysteine	164-172	ring finger protein 2	Homo sapiens	55-60	
29311602-2	2018	The RBR module comprises three domains, RING1, IBR and RING2 that collaborate to transfer ubiquitin from the E2~Ub conjugate, recognised by RING1, onto a catalytic cysteine in RING2 and finally onto the substrate in a multi-step reaction.	Cysteine	164-172	ring finger protein 2	Homo sapiens	176-181	
28827147-3	2017	RING-in-Between-RING (RBR) E3s constitute one of three classes of E3 ligases and are defined by a RING-HECT-hybrid mechanism that utilizes a E2-binding RING domain and a second domain (called RING2) that contains an active site Cys required for the formation of an obligatory E3~Ub intermediate.	Cysteine	228-231	ring finger protein 2	Homo sapiens	192-197	
27312108-1	2016	RING-in-between-RING (RBR) ubiquitin (Ub) ligases are a distinct class of E3s, defined by a RING1 domain that binds E2 Ub-conjugating enzyme and a RING2 domain that contains an active site cysteine similar to HECT-type E3s.	Cysteine	189-197	ring finger protein 2	Homo sapiens	147-152	
24141947-3	2013	RBR family members act as RING/HECT hybrids, employing RING1 to recognize ubiquitin-loaded E2 while a conserved cysteine in RING2 subsequently forms a thioester intermediate with the transferred or "donor" ubiquitin.	Cysteine	112-120	ring finger protein 2	Homo sapiens	124-129	
23770917-5	2013	Several pathogenic mutations in RING2 alter the environment of a single surface-exposed catalytic cysteine to inhibit ubiquitination.	Cysteine	98-106	ring finger protein 2	Homo sapiens	32-37	
17428788-3	2007	The cysteine-rich CXXC domains of MBD1 bound to Ring1b and the chromodomain of hPc2.	Cysteine	4-12	ring finger protein 2	Homo sapiens	48-54