Literature summary for 2.3.2.27 extracted from

Tatematsu, K.; Yoshimoto, N.; Okajima, T.; Tanizawa, K.; Kuroda, S.
Identification of ubiquitin ligase activity of RBCK1 and its inhibition by splice variant RBCK2 and protein kinase Cbeta (2008), J. Biol. Chem., 283, 11575-11585.

Search for more literature for 2.3.2.27

Inhibitors

Inhibitors	Comment	Organism	Structure
additional information	E3 ubiquitin ligase activity of isoform RBCK1 is inhibited by interaction with splice variant RBCK2	Rattus norvegicus

Organism

Organism	UniProt	Comment	Textmining
Rattus norvegicus	Q62921	isoform RBCK1	-

Posttranslational Modification

Posttranslational Modification	Comment	Organism
phosphoprotein	isoform RBCK1 undergoes efficient phosphorylation by protein kinase Cbeta. The phosphorylated RBCK1 shows no self-ubiquitination activity in vitro. Overexpression of protein kinase Cbeta leads to significant increases in the amounts of intracellular RBCK1, presumably suppressing the proteasomal degradation of RBCK1 through self-ubiquitination	Rattus norvegicus

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
[BRCK1-ubiquitin-carrier protein]-S-ubiquitinyl-L-cysteine + [BRCK1]-L-lysine	the RING1 finger plays an important role in the self-ubiquitination of RBCK1, leading to mono- and slightly diubiquitinated products. Self-ubiquitinated RBCK1 is processed by the proteasomal degradation	Rattus norvegicus	[BRCK1-ubiquitin-carrier protein]-L-cysteine + [BRCK1]-N6-ubiquitinyl-L-lysine	-	?

Synonyms

Synonyms	Comment	Organism
RanBP-type and C3HC4-type zinc finger-containing protein 1	-	Rattus norvegicus
RBCK1	-	Rattus norvegicus

General Information

General Information	Comment	Organism
metabolism	isoform RBCK1 undergoes efficient phosphorylation by protein kinase Cbeta. The phosphorylated RBCK1 shows no self-ubiquitination activity in vitro. Overexpression of protein kinase Cbeta leads to significant increases in the amounts of intracellular RBCK1, presumably suppressing the proteasomal degradation of RBCK1 through self-ubiquitination	Rattus norvegicus

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)