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IUBMB Comments This relatively rare subpopulation of RING-type E3 ubiquitin transferases (cf . EC 2.3.2.27 ), found in mammals and herpes viruses, can transfer ubiquitin to a cysteine residue in target proteins. Additional ubiquitin molecules are polymerized on top of the initial ubiquitin molecule by formation of an isopeptide linkage with lysine48
Reaction Schemes
[E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine
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[acceptor protein]-L-cysteine
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[E2 ubiquitin-conjugating enzyme]-L-cysteine
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[acceptor protein]-S-ubiquitinyl-L-cysteine
Synonyms
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ATL2
Arabidopsis Toxicos en Levadura 2
CHYR1
CHY zinc-finger and ring protein1
E3 ubiquitin ligase MIR1
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RING E3 ligase
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misleading
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RING finger ubiquitin E3 ligase
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SymRK-interacting E3 ubiquitin ligase
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[E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine + [acceptor protein]-L-cysteine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-S-ubiquitinyl-L-cysteine
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[E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine:[acceptor protein] ubiquitin transferase (thioester bond-froming; RING-type)
This relatively rare subpopulation of RING-type E3 ubiquitin transferases (cf. EC 2.3.2.27), found in mammals and herpes viruses, can transfer ubiquitin to a cysteine residue in target proteins. Additional ubiquitin molecules are polymerized on top of the initial ubiquitin molecule by formation of an isopeptide linkage with lysine48 in the pre-attached ubiquitin [2].
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[E2 ubiquitin-conjugating enzyme UBC8]-S-ubiquitinyl-L-cysteine + [SIP1]-L-cysteine
[E2 ubiquitin-conjugating enzyme UBC8]-L-cysteine + [SIP1]-S-ubiquitinyl-L-cysteine
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Substrates: -
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[E2 ubiquitin-conjugating enzyme UBC8]-S-ubiquitinyl-L-cysteine + [symbiosis receptor kinase]-L-cysteine
[E2 ubiquitin-conjugating enzyme UBC8]-L-cysteine + [symbiosis receptor kinase]-S-ubiquitinyl-L-cysteine
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Substrates: -
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[E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine + [acceptor protein]-L-cysteine
[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-S-ubiquitinyl-L-cysteine
[E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine + [ATAF1 protein]-L-cysteine
[E2 ubiquitin-conjugating enzyme]-L-cysteine + [ATAF1 protein]-S-ubiquitinyl-L-cysteine
Substrates: -
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additional information
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Substrates: the enzyme has self-ubiquitination activity
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[E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine + [acceptor protein]-L-cysteine
[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-S-ubiquitinyl-L-cysteine
Substrates: -
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[E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine + [acceptor protein]-L-cysteine
[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-S-ubiquitinyl-L-cysteine
Substrates: -
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[E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine + [acceptor protein]-L-cysteine
[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-S-ubiquitinyl-L-cysteine
Substrates: -
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[E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine + [acceptor protein]-L-cysteine
[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-S-ubiquitinyl-L-cysteine
Substrates: this form of ubiquitination requires a cysteine residue in the intracytoplasmic tail of histocompatibility complex class I (MHC I) molecules. An MHC I molecule containing a single cysteine residue in an artificial glycine and alanine intracytoplasmic domain was endocytosed and degraded in the presence of MIR1. Thus, ubiquitination can occur on proteins lacking accessible lysines or an accessible N terminus
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[E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine + [acceptor protein]-L-cysteine
[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-S-ubiquitinyl-L-cysteine
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Substrates: -
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[E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine + [acceptor protein]-L-cysteine
[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-S-ubiquitinyl-L-cysteine
[E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine + [acceptor protein]-L-cysteine
[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-S-ubiquitinyl-L-cysteine
Substrates: -
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[E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine + [acceptor protein]-L-cysteine
[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-S-ubiquitinyl-L-cysteine
Substrates: -
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[E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine + [acceptor protein]-L-cysteine
[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-S-ubiquitinyl-L-cysteine
Substrates: -
?
[E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine + [acceptor protein]-L-cysteine
[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-S-ubiquitinyl-L-cysteine
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Substrates: -
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Mg2+
5 mM used in assay conditions
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Breast Neoplasms
Novel RING E3 ubiquitin ligases in breast cancer.
Carcinogenesis
Cullin-4B promotes cell proliferation and invasion through inactivation of p53 signaling pathway in colorectal cancer.
Hypertension
ROMK expression remains unaltered in a mouse model of familial hyperkalemic hypertension caused by the CUL3?403-459 mutation.
Neoplasms
Cullin-4B promotes cell proliferation and invasion through inactivation of p53 signaling pathway in colorectal cancer.
Neoplasms
Novel RING E3 ubiquitin ligases in breast cancer.
Neoplasms
TRIM13 regulates ubiquitination and turnover of NEMO to suppress TNF induced NF-?B activation.
Neoplasms
Von Hippel-Lindau (VHL) small-molecule inhibitor binding increases stability and intracellular levels of VHL protein.
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ecotype Columbia
SwissProt
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UniProt
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UniProt
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Highest Expressing Human Cell Lines
Filter by:
Cell Line Links
Gene Links
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malfunction
an enzyme null mutant exhibits higher susceptibility to Alternaria brassicicola while plants overexpressing the enzyme display increased resistance
physiological function
the enzyme is necessary to successfully defend against the Alternaria brassicicola fungal pathogen
physiological function
the enzyme targets ATAF1 for degradation to modulate the drought stress response of cucumber through the abscisic acid-dependent pathway. The enzyme positively regulates the drought tolerance
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C180A
the mutant cannot transport ubiquitin from E2 to the substrate
C180S
the mutant cannot transport ubiquitin from E2 to the substrate
C266S
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the mutant enzyme is unable to dimerize. The mutation abolishes the ubiquitination of SIP1 in vitro
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enzyme protein stability is markedly increased via chitin treatment, and its degradation is prolonged when 26S proteasomal function is inhibited
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expressed in enzyme-deficient Arabidopsis thaliana mutants
expressed in Escherichia coli BL21(DE3) cells
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the enzyme expression is rapidly and significantly induced by exogenous chitin
the expression level of the enzyme is increased by 4fold after abscisic acid treatment at 9 h
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Cadwell, K.; Coscoy, L.
Biochemistry Ubiquitination on nonlysine residues by a viral E3 ubiquitin ligase
Science
309
127-130
2005
Human gammaherpesvirus 8 (P90495)
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Kim, D.; Jeon, S.J.; Hong, J.K.; Kim, M.G.; Kim, S.H.; Kadam, U.S.; Kim, W.Y.; Chung, W.S.; Stacey, G.; Hong, J.C.
The auto-regulation of ATL2 E3 ubiquitin ligase plays an important role in the immune response against Alternaria brassicicola in Arabidopsis thaliana
Int. J. Mol. Sci.
25
2388
2024
Arabidopsis thaliana (Q8L9T5)
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Guo, L.; Cao, M.; Li, Y.; Wang, J.; He, L.; Li, P.; Lin, X.; Li, X.; Yuan, X.; Zhao, B.; Zhang, N.; Guo, Y.D.
RING finger ubiquitin E3 ligase CsCHYR1 targets CsATAF1 for degradation to modulate the drought stress response of cucumber through the ABA-dependent pathway
Plant Physiol. Biochem.
202
107928
2023
Cucumis sativus (A0A0A0KGJ6)
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Wu, P.; Feng, Y.; Zou, Z.; Cao, Y.; Yuan, S.
Critical role of cysteine-266 of SIE3 in regulating the ubiquitination and degradationof SIP1 transcription factor in Lotus japonicus
Planta
253
126
2021
Lotus japonicus
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