Literature summary for 2.3.2.27 extracted from

Dodd, R.; Allen, M.; Brown, S.; Sanderson, C.; Duncan, L.; Lehner, P.; Bycroft, M.; Read, R.
Solution structure of the Kaposis sarcoma-associated herpesvirus K3 N-terminal domain reveals a novel E2-binding C4HC3-type RING domain (2004), J. Biol. Chem., 279, 53840-53847.

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Crystallization (Commentary)

Crystallization (Comment)	Organism
the K3 N-terminal domain is a variant member of the RING domain family and not a plant homeodomain. The domain interacts with the cellular ubiquitin-conjugating enzymes UbcH5A to -C and UbcH13, which dock to the equivalent surface as on classical cellular RING domains. May be involved in catalyzing Lys63-linked ubiquitination	Human gammaherpesvirus 8

Organism

Organism	UniProt	Comment	Textmining
Human gammaherpesvirus 8	P90495	-	-
Human gammaherpesvirus 8 GK18	P90495	-	-

Synonyms

Synonyms	Comment	Organism
E3 ubiquitin-protein ligase MIR1	-	Human gammaherpesvirus 8
ubiquitin-protein ligase K3	-	Human gammaherpesvirus 8

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Release 2023.1 (January 2023)