Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Scott, D.; Rhee, D.; Duda, D.; Kelsall, I.; Olszewski, J.; Paulo, J.; de Jong, A.; Ovaa, H.; Alpi, A.; Harper, J.; Schulman, B.
    Two distinct types of E3 ligases work in unison to regulate substrate ubiquitylation (2016), Cell, 166, 1198-1214 .
No PubMed abstract available

Protein Variants

EC Number Protein Variants Comment Organism
2.3.2.31 additional information mutants in ARIH1's UBA-to-RING1 helix, RING1, RING1-to-IBR helix, and RING2 domains display activity profile signatures corresponding to intrinsic RBR E3 activities of ubiquitin transfer from UBCH7 to ARIH1, alignment of the RING2 active site, and intrinsic ability of RING2 to mediate ligation Homo sapiens

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.3.2.31 [E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine + [acceptor protein]-L-lysine Homo sapiens overall reaction [E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-N6-ubiquitinyl-L-lysine
-
?
2.3.2.31 [E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine + [RBR-type E3 ubiquitin transferase]-L-cysteine Homo sapiens
-
[E2 ubiquitin-conjugating enzyme]-L-cysteine + [RBR-type E3 ubiquitin transferase]-S-ubiquitinyl-L-cysteine
-
?
2.3.2.31 [RBR-type E3 ubiquitin transferase]-S-ubiquitinyl-L-cysteine + [acceptor protein]-L-lysine Homo sapiens
-
[RBR-type E3 ubiquitin transferase]-L-cysteine + [acceptor protein]-N6-ubiquitinyl-L-lysine
-
?

Organism

EC Number Organism UniProt Comment Textmining
2.3.2.31 Homo sapiens
-
-
-
2.3.2.31 Homo sapiens Q9Y4X5
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.3.2.31 additional information the enzyme acts as a monoubiquitin conjugating enzyme for neddylated CUL3KLHL12-RBX1 substrate SEC13-SEC31A Homo sapiens ?
-
?
2.3.2.31 [E2 ubiquitin-conjugating enzyme UBCH7]-S-ubiquitinyl-L-cysteine + [SEC13-SEC31A]-L-lysine
-
Homo sapiens [E2 ubiquitin-conjugating enzyme UBCH7]-L-cysteine + [SEC13-SEC31A]-N6-ubiquitinyl-L-lysine
-
?
2.3.2.31 [E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine + [acceptor protein]-L-lysine overall reaction Homo sapiens [E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-N6-ubiquitinyl-L-lysine
-
?
2.3.2.31 [E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine + [RBR-type E3 ubiquitin transferase]-L-cysteine
-
Homo sapiens [E2 ubiquitin-conjugating enzyme]-L-cysteine + [RBR-type E3 ubiquitin transferase]-S-ubiquitinyl-L-cysteine
-
?
2.3.2.31 [RBR-type E3 ubiquitin transferase]-S-ubiquitinyl-L-cysteine + [acceptor protein]-L-lysine
-
Homo sapiens [RBR-type E3 ubiquitin transferase]-L-cysteine + [acceptor protein]-N6-ubiquitinyl-L-lysine
-
?

Synonyms

EC Number Synonyms Comment Organism
2.3.2.31 ARIH1
-
Homo sapiens
2.3.2.31 RBR-type E3
-
Homo sapiens

General Information

EC Number General Information Comment Organism
2.3.2.31 physiological function ARIH1 predominantly and extensively interacts with activated cullin-RING E3 enzymes and acts as a monoubiquitin conjugating enzyme for neddylated CUL3-RBX1 substrate SEC13-SEC31A. Efficient neddylated cullin-RING E3 substrate polyubiquitylation can be achieved by UBCH7-ARIH1-mediated priming and CDC34-mediated chain elongation Homo sapiens