Oxygen-dependent asparagine hydroxylation of the ubiquitin-associated (UBA) domain in Cezanne regulates ubiquitin binding.
Amino Acid Sequence
Asparagine
/ metabolism
Consensus Sequence
Endopeptidases
/ chemistry
HEK293 Cells
Humans
Hydroxylation
Mixed Function Oxygenases
/ metabolism
Oxygen
/ metabolism
Polyubiquitin
/ metabolism
Protein Binding
Protein Domains
Repressor Proteins
/ metabolism
Structure-Activity Relationship
Ubiquitin
/ metabolism
Cezanne
FIH1
OTU domain-containing protein 7B (OTUD7B)
UBA domain
deubiquitinase (DUB)
deubiquitylation (deubiquitination)
hydroxylation
nuclear magnetic resonance (NMR)
posttranslational modification (PTM)
protein-protein interaction
ubiquitin
Journal
The Journal of biological chemistry
ISSN: 1083-351X
Titre abrégé: J Biol Chem
Pays: United States
ID NLM: 2985121R
Informations de publication
Date de publication:
21 02 2020
21 02 2020
Historique:
received:
23
07
2019
revised:
27
12
2019
pubmed:
16
1
2020
medline:
21
10
2020
entrez:
16
1
2020
Statut:
ppublish
Résumé
Deubiquitinases (DUBs) are vital for the regulation of ubiquitin signals, and both catalytic activity of and target recruitment by DUBs need to be tightly controlled. Here, we identify asparagine hydroxylation as a novel posttranslational modification involved in the regulation of Cezanne (also known as OTU domain-containing protein 7B (OTUD7B)), a DUB that controls key cellular functions and signaling pathways. We demonstrate that Cezanne is a substrate for factor inhibiting HIF1 (FIH1)- and oxygen-dependent asparagine hydroxylation. We found that FIH1 modifies Asn
Identifiants
pubmed: 31937588
pii: S0021-9258(17)48255-X
doi: 10.1074/jbc.RA119.010315
pmc: PMC7039550
pii:
doi:
Substances chimiques
Repressor Proteins
0
Ubiquitin
0
Polyubiquitin
120904-94-1
Asparagine
7006-34-0
Mixed Function Oxygenases
EC 1.-
HIF1AN protein, human
EC 1.14.11.-
Endopeptidases
EC 3.4.-
OTUD7B protein, human
EC 3.4.-
Oxygen
S88TT14065
Banques de données
PDB
['2L2D', '2W9N']
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
2160-2174Informations de copyright
© 2020 Mader et al.
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