ID   2.3.2.31
DE   RBR-type E3 ubiquitin transferase.
CA   [E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine + [acceptor
CA   protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine +
CA   [acceptor protein]-N(6)-ubiquitinyl-L-lysine.
CC   -!- RBR-type E3 ubiquitin transferases have two RING fingers separated by
CC       an internal motif (IBR, for In Between RING).
CC   -!- The enzyme interacts with the CRL (Cullin-RING ubiquitin Ligase)
CC       complexes formed by certain RING-type E3 ubiquitin transferase (see
CC       EC 2.3.2.27), which include a neddylated cullin scaffold protein and
CC       a substrate recognition module.
CC   -!- The RING1 domain binds an EC 2.3.2.23, and transfers the ubiquitin
CC       that is bound to it to an internal cysteine residue in the RING2
CC       domain, followed by the transfer of the ubiquitin from RING2 to the
CC       substrate.
CC   -!- Once the substrate has been ubiquitinated by the RBR-type ligase,
CC       it can be ubiqutylated further using ubiquitin carried directly on E2
CC       enzymes, in a reaction catalyzed by EC 2.3.2.27.
CC   -!- Activity of the RBR-type enzyme is dependent on neddylation of the
CC       cullin protein in the CRL complex. cf. EC 2.3.2.26, EC 2.3.2.27,
CC       and EC 2.3.2.32.
DR   Q1L8G6, AKIB1_DANRE;  Q9P2G1, AKIB1_HUMAN;  Q6ZPS6, AKIB1_MOUSE;
DR   Q9SKC4, ARI10_ARATH;  Q9SKC2, ARI11_ARATH;  O01965, ARI11_CAEEL;
DR   Q84RQ9, ARI12_ARATH;  Q9FFN9, ARI13_ARATH;  Q9FFP1, ARI14_ARATH;
DR   Q84RQ8, ARI15_ARATH;  Q9C5A4, ARI16_ARATH;  Q6NW85, ARI1L_DANRE;
DR   Q949V6, ARI1_ARATH ;  A2VEA3, ARI1_BOVIN ;  Q6PFJ9, ARI1_DANRE ;
DR   Q94981, ARI1_DROME ;  Q9Y4X5, ARI1_HUMAN ;  Q9Z1K5, ARI1_MOUSE ;
DR   Q32NS4, ARI1_XENLA ;  B1H1E4, ARI1_XENTR ;  Q84RR2, ARI2_ARATH ;
DR   Q22431, ARI2_CAEEL ;  O76924, ARI2_DROME ;  O95376, ARI2_HUMAN ;
DR   Q9Z1K6, ARI2_MOUSE ;  Q9LVX0, ARI3_ARATH ;  Q9LVW9, ARI4_ARATH ;
DR   Q8L829, ARI5_ARATH ;  P0C8K8, ARI6_ARATH ;  Q84RR0, ARI7_ARATH ;
DR   Q8W468, ARI8_ARATH ;  Q9SKC3, ARI9_ARATH ;  Q9P3U4, HEL1_SCHPO ;
DR   P36113, HEL1_YEAST ;  A9JTG5, HOIL1_DANRE;  E6ZIJ1, HOIL1_DICLA;
DR   Q9BYM8, HOIL1_HUMAN;  Q9WUB0, HOIL1_MOUSE;  Q62921, HOIL1_RAT  ;
DR   Q9US46, ITT1_SCHPO ;  Q04638, ITT1_YEAST ;  Q8IPJ3, LUBEL_DROME;
DR   Q7KTX7, PRKN_DROME ;  O60260, PRKN_HUMAN ;  Q9WVS6, PRKN_MOUSE ;
DR   E0VIU9, PRKN_PEDHC ;  Q9JK66, PRKN_RAT   ;  Q5RFV4, R1441_DANRE;
DR   Q6DH94, R1442_DANRE;  P50876, R144A_HUMAN;  Q925F3, R144A_MOUSE;
DR   A4IIY1, R144A_XENTR;  A5PK27, R144B_BOVIN;  Q7Z419, R144B_HUMAN;
DR   Q8BKD6, R144B_MOUSE;  Q6T486, RBRA_DICDI ;  F4ITM1, RGSL1_ARATH;
DR   Q9NV58, RN19A_HUMAN;  P50636, RN19A_MOUSE;  Q2VJ60, RN19A_PIG  ;
DR   Q1L8L6, RN19B_DANRE;  Q6ZMZ0, RN19B_HUMAN;  A2A7Q9, RN19B_MOUSE;
DR   Q08B84, RN19B_XENLA;  Q8TC41, RN217_HUMAN;  D3YYI7, RN217_MOUSE;
DR   Q4KLT0, RN217_XENLA;  F1RB95, RNF14_DANRE;  Q9UBS8, RNF14_HUMAN;
DR   Q9JI90, RNF14_MOUSE;  Q96EP0, RNF31_HUMAN;  Q924T7, RNF31_MOUSE;
DR   Q54CX4, Y5521_DICDI;
//