CATH Classification
Level | CATH Code | Description |
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2 | Mainly Beta |
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2.30 | Roll |
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2.30.30 | SH3 type barrels. |
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2.30.30.1150 |
Domain Context
CATH Clusters
Superfamily | 2.30.30.1150 |
Functional Family | E3 ubiquitin-protein ligase UHRF2 isoform X1 |
Enzyme Information
2.3.2.27 |
RING-type E3 ubiquitin transferase.
based on mapping to UniProt Q96T88
S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)- ubiquitinyl-[acceptor protein]-L-lysine.
-!- RING E3 ubiquitin transferases serve as mediators bringing the ubiquitin-charged E2 ubiquitin-conjugating enzyme (EC 2.3.2.23) and an acceptor protein together to enable the direct transfer of ubiquitin through the formation of an isopeptide bond between the C-terminal glycine residue of ubiquitin and the epsilon-amino group of an L-lysine residue of the acceptor protein. -!- Unlike EC 2.3.2.26 the RING-E3 domain does not form a catalytic thioester intermediate with ubiquitin. -!- Many members of the RING-type E3 ubiquitin transferase family are not able to bind a substrate directly, and form a complex with a cullin scaffold protein and a substrate recognition module (the complexes are named CRL for Cullin-RING-Ligase). -!- In these complexes, the RING-type E3 ubiquitin transferase provides an additional function, mediating the transfer of a NEDD8 protein from a dedicated E2 carrier to the cullin protein (see EC 2.3.2.32). -!- Cf. EC 2.3.2.31.
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UniProtKB Entries (1)
Q96T88 |
UHRF1_HUMAN
Homo sapiens
E3 ubiquitin-protein ligase UHRF1
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PDB Structure
PDB | 3ASK |
External Links | |
Method | X-RAY DIFFRACTION |
Organism | |
Primary Citation |
Recognition of modification status on a histone H3 tail by linked histone reader modules of the epigenetic regulator UHRF1
Proc.Natl.Acad.Sci.USA
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