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A new class EC 7, Translocases, has been added to the EC list. It will be part of ENZYME from release 2018_10. Read more about EC 7 here.

ENZYME entry: EC 2.3.2.31

Accepted Name
RBR-type E3 ubiquitin transferase.
Reaction catalysed
[E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine + [acceptor protein]-L-lysine <=> [E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-N(6)-ubiquitinyl-L-lysine
Comment(s)
  • RBR-type E3 ubiquitin transferases have two RING fingers separated by an internal motif (IBR, for In Between RING).
  • The enzyme interacts with the CRL (Cullin-RING ubiquitin Ligase) complexes formed by certain RING-type E3 ubiquitin transferase (see EC 2.3.2.27), which include a neddylated cullin scaffold protein and a substrate recognition module.
  • The RING1 domain binds an EC 2.3.2.23, and transfers the ubiquitin that is bound to it to an internal cysteine residue in the RING2 domain, followed by the transfer of the ubiquitin from RING2 to the substrate.
  • Once the substrate has been ubiquitinated by the RBR-type ligase, it can be ubiqutylated further using ubiquitin carried directly on E2 enzymes, in a reaction catalyzed by EC 2.3.2.27.
  • Activity of the RBR-type enzyme is dependent on neddylation of the cullin protein in the CRL complex.
  • Cf. EC 2.3.2.26, EC 2.3.2.27, and EC 2.3.2.32.
Cross-references
BRENDA2.3.2.31
EC2PDB2.3.2.31
ExplorEnz2.3.2.31
PRIAM enzyme-specific profiles2.3.2.31
KEGG Ligand Database for Enzyme Nomenclature2.3.2.31
IUBMB Enzyme Nomenclature2.3.2.31
IntEnz2.3.2.31
MEDLINEFind literature relating to 2.3.2.31
MetaCyc2.3.2.31
UniProtKB/Swiss-Prot
Q1L8G6, AKIB1_DANRE;  Q9P2G1, AKIB1_HUMAN;  Q6ZPS6, AKIB1_MOUSE;  
Q9SKC4, ARI10_ARATH;  Q9SKC2, ARI11_ARATH;  Q84RQ9, ARI12_ARATH;  
Q9FFN9, ARI13_ARATH;  Q9FFP1, ARI14_ARATH;  Q84RQ8, ARI15_ARATH;  
Q9C5A4, ARI16_ARATH;  Q6NW85, ARI1L_DANRE;  Q949V6, ARI1_ARATH;  
A2VEA3, ARI1_BOVIN;  Q6PFJ9, ARI1_DANRE;  Q94981, ARI1_DROME;  
Q9Y4X5, ARI1_HUMAN;  Q9Z1K5, ARI1_MOUSE;  Q32NS4, ARI1_XENLA;  
B1H1E4, ARI1_XENTR;  Q84RR2, ARI2_ARATH;  Q22431, ARI2_CAEEL;  
O76924, ARI2_DROME;  O95376, ARI2_HUMAN;  Q9Z1K6, ARI2_MOUSE;  
Q9LVX0, ARI3_ARATH;  Q9LVW9, ARI4_ARATH;  Q8L829, ARI5_ARATH;  
P0C8K8, ARI6_ARATH;  Q84RR0, ARI7_ARATH;  Q8W468, ARI8_ARATH;  
Q9SKC3, ARI9_ARATH;  Q9P3U4, HEL1_SCHPO;  P36113, HEL1_YEAST;  
A9JTG5, HOIL1_DANRE;  E6ZIJ1, HOIL1_DICLA;  Q9BYM8, HOIL1_HUMAN;  
Q9WUB0, HOIL1_MOUSE;  Q62921, HOIL1_RAT;  Q9US46, ITT1_SCHPO;  
Q04638, ITT1_YEAST;  O60260, PRKN_HUMAN;  Q9WVS6, PRKN_MOUSE;  
Q9JK66, PRKN_RAT;  Q5RFV4, R1441_DANRE;  Q6DH94, R1442_DANRE;  
P50876, R144A_HUMAN;  Q925F3, R144A_MOUSE;  A4IIY1, R144A_XENTR;  
A5PK27, R144B_BOVIN;  Q7Z419, R144B_HUMAN;  Q8BKD6, R144B_MOUSE;  
Q6T486, RBRA_DICDI;  Q9NV58, RN19A_HUMAN;  P50636, RN19A_MOUSE;  
Q2VJ60, RN19A_PIG;  Q1L8L6, RN19B_DANRE;  Q6ZMZ0, RN19B_HUMAN;  
A2A7Q9, RN19B_MOUSE;  Q08B84, RN19B_XENLA;  Q8TC41, RN217_HUMAN;  
D3YYI7, RN217_MOUSE;  Q4KLT0, RN217_XENLA;  Q9UBS8, RNF14_HUMAN;  
Q9JI90, RNF14_MOUSE;  Q96EP0, RNF31_HUMAN;  Q924T7, RNF31_MOUSE;  

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All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 2.3.2.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 2.3.-.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 2.-.-.-