Any feedback?
Information on EC 2.3.2.27 - RING-type E3 ubiquitin transferase and Organism(s) Arabidopsis thaliana and UniProt Accession Q9ZU51
for references in articles please use BRENDA:EC2.3.2.27Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
2.3.2.27 RING-type E3 ubiquitin transferaseIUBMB Comments
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, HECT-type E3 ubiquitin transferase, 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, cullin-RING-type E3 NEDD8 transferase). cf. EC 2.3.2.31, RBR-type E3 ubiquitin transferase.
Specify your search results
Word Map
- 2.3.2.27
- brca2
- ovarian
- women
- proteasome
-
germline
- hereditary
- ligases
- pink1
- tumour
-
mitophagy
- tumorigenesis
-
checkpoint
- adaptor
-
polyubiquitination
- neurodegenerative
- parp
- estrogen
-
counsel
- chromatin
-
high-risk
- histone
-
predisposition
- pten
-
early-onset
- rad51
-
founder
-
ubiquitin-proteasome
- serous
-
dopaminergic
-
prophylactic
- sumo
-
triple-negative
-
ubiquitin-mediated
-
mastectomy
-
proteasome-dependent
-
ubiquitin-dependent
-
basal-like
-
ubiquitin-like
- xiap
-
sumoylation
-
fanconi
-
ubiquitin-conjugating
-
deubiquitinating
- alpha-synuclein
- medicine
-
mammography
-
first-degree
- analysis
-
polycomb
- fork
- centrosome
- chk1
The taxonomic range for the selected organisms is: Arabidopsis thaliana
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
+
=
+
[E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine
+
[acceptor protein]-L-lysine
=
[E2 ubiquitin-conjugating enzyme]-L-cysteine
+
[acceptor protein]-N6-ubiquitinyl-L-lysine
Synonyms
brca1, parkin, e3 ubiquitin ligase, e3 ligase, c-cbl, ciap2, trim5alpha, rnf43, trim25, trim5, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
RING E3 ubiquitin ligase
SDIR1
PATHWAY SOURCE
PATHWAYS
-
-
SYSTEMATIC NAME
IUBMB Comments
[E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine:[acceptor protein] ubiquitin transferase (isopeptide bond-forming; RING-type)
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, HECT-type E3 ubiquitin transferase, 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, cullin-RING-type E3 NEDD8 transferase). cf. EC 2.3.2.31, RBR-type E3 ubiquitin transferase.
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
S-(ubiquitin)n-[UbcH5]-L-cysteine + [STRF1]-L-lysine
[UbcH5]-L-cysteine + N6-(ubiquitin)n-[STRF1]-L-lysine
-
autoubiquitylation reaction leading to polyubiquitylated protein
-
?
S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [ABI5]-L-lysine
[E2 ubiquitin-conjugating enzyme]-L-cysteine + N6-ubiquitinyl-[ABI5]-L-lysine
ABI5 i.e. abscisic acid-responsive transcription factor
-
-
?
S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine
[E2 ubiquitin-conjugating enzyme]-L-cysteine + N6-ubiquitinyl-[acceptor protein]-L-lysine
S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [ACS4]-L-lysine
[E2 ubiquitin-conjugating enzyme]-L-cysteine + N6-ubiquitinyl-[ACS4]-L-lysine
ACS4 i.e. aminocyclopropane-1-carboxylic acid synthase 4
-
-
?
S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [ACS7]-L-lysine
[E2 ubiquitin-conjugating enzyme]-L-cysteine + N6-ubiquitinyl-[ACS7]-L-lysine
ACS4 i.e. aminocyclopropane-1-carboxylic acid synthase 7
-
-
?
S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [SDIRIP1 protein]-L-lysine
[E2 ubiquitin-conjugating enzyme]-L-cysteine + N6-ubiquitinyl-[SDIRIP1 protein]-L-lysine
-
-
-
-
?
S-ubiquitinyl-[Ubc8]-L-cysteine + [acceptor protein]-L-lysine
[Ubc8]-L-cysteine + N6-ubiquitinyl-[acceptor protein]-L-lysine
-
the RING domain of Sis3 is sufficient for E3 ligase activity
-
?
S-ubiquitinyl-[UbcH5b]-L-cysteine + [DAF]-L-lysine
[UbcH5b]-L-cysteine + N6-ubiquitinyl-[DAF]-L-lysine
-
-
autoubiquitylation reaction
-
?
S-ubiquitinyl-[UbcH5b]-L-cysteine + [NERF]-L-lysine
[UbcH5b]-L-cysteine + N6-ubiquitinyl-[NERF]-L-lysine
-
autoubiquitylation reaction
-
?
S-ubiquitinyl-[UbcH5c]-L-cysteine + [ERF53]-L-lysine
[UbcH5c]-L-cysteine + N6-ubiquitinyl-[ERF53]-L-lysine
ERF53 i.e. ethylene response factor 53
RING E3 ligase RGLG2 mediates ERF53 ubiquitination for proteasomal degradation
-
?
[ACRE276-RING domain-E3-ubiquitin-carrier protein HubC5B]-S-ubiquitinyl-L-cysteine + [acceptor protein]-L-lysine
[ACRE276-RING domain-E3-ubiquitin-carrier protein]-L-cysteine + [acceptor protein]-N6-ubiquitinyl-L-lysine
enzyme displays ubiquitination activity in the presence of yeast E1 and human E2 HubC5B
-
-
?
[E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine + [MLO12-Myc]-L-lysine
[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor MLO12-Myc]-N6-ubiquitinyl-L-lysine
-
-
-
?
[PUB54-RING domain-ubiquitin-carrier protein Ubc13]-S-ubiquitinyl-L-cysteine + [acceptor protein]-L-lysine
[PUB54-RING domain-ubiquitin-carrier protein Ubc13]-L-cysteine + [acceptor protein]-N6-ubiquitinyl-L-lysine
ubiquitination activity is seen with both family-4/5 UBC enzymes, encoded by At2g16740 and At5g53300 and both family-13 UBC enzymes, encoded by At1g78870 and At16890
-
-
?
[PUB54-RING domain-ubiquitin-carrier protein Ubc4/5]-S-ubiquitinyl-L-cysteine + [acceptor protein]-L-lysine
[PUB54-RING domain-ubiquitin-carrier protein Ubc4/5]-L-cysteine + [acceptor protein]-N6-ubiquitinyl-L-lysine
ubiquitination activity is seen with both family-4/5 UBC enzymes and both family-13 UBC enzymes
-
-
?
S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine
[E2 ubiquitin-conjugating enzyme]-L-cysteine + N6-ubiquitinyl-[acceptor protein]-L-lysine
-
-
-
-
?
S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine
[E2 ubiquitin-conjugating enzyme]-L-cysteine + N6-ubiquitinyl-[acceptor protein]-L-lysine
-
-
-
?
additional information
?
-
isoform ACRE276 is an E3 ubiquitin ligase requiring an intact U-box domain
-
-
?
additional information
?
-
-
isoform ACRE276 is an E3 ubiquitin ligase requiring an intact U-box domain
-
-
?
additional information
?
-
isoform RMA2 exhibits a high degree of E3 activity with E2 enzyme UBC8 and a moderate level with E2 enzyme UBC10 and no activity wih E2 enzymes UBC5 and UBC13
-
-
?
additional information
?
-
isoform RMA2 exhibits a high degree of E3 activity with E2 enzyme UBC8 and a moderate level with E2 enzyme UBC10 and no activity wih E2 enzymes UBC5 and UBC13
-
-
?
additional information
?
-
isoform RMA2 exhibits a high degree of E3 activity with E2 enzyme UBC8 and a moderate level with E2 enzyme UBC10 and no activity wih E2 enzymes UBC5 and UBC13
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine
[E2 ubiquitin-conjugating enzyme]-L-cysteine + N6-ubiquitinyl-[acceptor protein]-L-lysine
S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [SDIRIP1 protein]-L-lysine
[E2 ubiquitin-conjugating enzyme]-L-cysteine + N6-ubiquitinyl-[SDIRIP1 protein]-L-lysine
-
-
-
-
?
S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine
[E2 ubiquitin-conjugating enzyme]-L-cysteine + N6-ubiquitinyl-[acceptor protein]-L-lysine
-
-
-
-
?
S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine
[E2 ubiquitin-conjugating enzyme]-L-cysteine + N6-ubiquitinyl-[acceptor protein]-L-lysine
-
-
-
?
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
enzyme moves from the plasma membrane to the nucleus under salt stress
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
RING finger E3 ligase RHA2b expression is induced by abscisic acid and overexpression of RHA2b leads to abscisic acid-associated phenotypes such as abscisic acid hypersensitivity in seed germination and seedling growth, enhanced stomatal closure, reduced water loss, and, therefore, increased drought tolerance. T-DNA insertion mutant Rha2b-1 shows abscisic acid-insensitive phenotypes and reduced drought tolerance. A Rha2a Rha2b-1 double mutant generally enhances abscisic acid insensitivity of mutant Rha2b-1 in seed germination, seedling growth, and stomatal closure, suggesting that Rha2b and Rha2a act redundantly in regulating abscisic acid responses
malfunction
physiological function
malfunction
-
enzyme-impaired mutants show reduced sensitivity to low ambient temperature in flowering
malfunction
the atatl80 insertion mutant line exhibits an increased tolerance to cold stress
malfunction
-
the idf1 mutants show increased tolerance to Fe deficiency, resulting from increased IRT1 protein levels
physiological function
transient expression of isoform PUB17 in Cf-9 tobacco silenced for ubiquitin ligase ACRE276 restores hypersensitive response, while mutant PUB17 lacking E3 ligase activity fails to do so. PUB17 ligase activity is crucial for defense signaling. PUB17 knockout plants are compromised in RPM1- and RPS4-mediated resistance against Pseudomonas syringae pv tomato containing avirulence genes AvrB and AvrRPS4, respectively
physiological function
C3H2C3-Type RING E3 ubiquitin ligase AIRP1-overexpressing transgenic plants (35S:AtAIRP1-sGFP) are hypersensitive to exogenous abscisic acid in terms of radicle emergence, cotyledon development, root elongation, and stomatal closure. Overexpressing transgenic plants accumulate higher amounts of hydrogen peroxide in response to exogenous abscisic acid than wild-type and mutant plants. AIRP1 overexpressors are markedly tolerant to severe drought stress, as opposed to mutant plants, which are highly susceptible. The levels of drought stress-related genes and basic leucine zipper transcription factor genes are up-regulated in overexpressing plants relative to wild-type and mutant plants in response to abscisic acid
physiological function
-
C3HC4-type RING E3 ubiquitin ligase AIRP2-overexpressing transgenic and loss-of-function mutant plants exhibit hypersensitive and hyposensitive phenotypes, respectively, to abscisic acid in terms of seed germination, root growth, and stomatal movement. Overexpressing transgenic plants are highly tolerant to severe drought stress, and loss-of-function mutant alleles are more susceptible to water stress than are wild-type plants. Higher levels of drought-induced hydrogen peroxide production are detected in overexpressing mutant as compared with loss-of-function mutant plants. Abscisic acid-inducible drought-related genes are up-regulated in overexpressing and down-regulated in loss-of-function progeny. The positive effects of AIRP2 on abscisic acid-induced stress genes are dependent on SNF1-related protein kinases
physiological function
E3 RING ligase KEG acts as an important factor in plant hormone signaling and a positive regulator of jasmonate zim-domain JAZ12 stability. JAZ12 interacts directly with KEG. Abscisic acid treatment promotes JAZ12 degradation, and KEG knockdown leads to a decrease in JAZ12 protein levels
physiological function
isoform NERF is the cis-natural antisense transcript gene of NFYA5. NERF can produce siRNAs from their overlapping region and affect NFYA5 transcripts by functioning together with miR169. The NERF protein functions as an E3 ligase for ubiquitination. Overexpression of NERF or overlapping region cDNA leads to siRNA-NERF accumulation, miR169 repression, and NFYA5 transcript enhancement. Knockdown of NERF transcripts by an artificial miRNA enhances miR169 abundance and reduces NFYA5 transcripts
physiological function
loss-of-function mutant line shows hyposensitivity to abscisic acid during its germination stage. AIRP3 is idetical to Loss of Gdu2, LOG2, which participates in an amino acid export system. The knockout mutant and RNAi knockdown transgenic plants display impaired abscisic acid-mediated seed germination and stomata closure. Suppression of AIRP3 results in marked hypersensitive phenotypes toward high salinity and water deficit relative to wild-type plants
physiological function
loss-of-function mutant seedlings exhibit accelerated endocytosis in roots, and have altered expression of several genes involved in the membrane trafficking system. Protein trafficking inhibitor, brefeldin A, treatment leads to brefeldin A bodies in the mutant. The mutant also shows increased tolerance to salt, ionic and osmotic stresses, reduced accumulation of reactive oxygen species during salt stress, and increased expression of AtRbohD, which encodes a nicotinamide adenine dinucleotide phosphate oxidase involved in H2O2 production
physiological function
mutant sugar-insensitive3, i.e. Sis3 is resistant to the inhibitory effects of high concentrations of exogenous glucose and sucrose on early seedling development. In contrast to wild-type plants, sis3 mutants develop green, expanded cotyledons and true leaves when sown on medium containing high concentrations (e.g. 270 mM) of sucrose. Mutant Sis3 exhibits wild-type responses to the inhibitory effects of abscisic acid and paclobutrazol, a gibberellic acid biosynthesis inhibitor, on seed germination
physiological function
RING E3 ligase RGLG2 negatively regulates the drought stress response by mediating ERF53 transcriptional activity in Arabidopsis thaliana
physiological function
RING E3 Ligase Xbat32 mutants produce significantly more ethylene than wildtype plants and inhibition of ethylene biosynthesis or perception significantly increases Xbat32 lateral root production. Xbat32 interacts with the ethylene biosynthesis enzymes aminocyclopropane-1-carboxylic acid synthases ACS4 and ACS7 in yeast-two-hybrid assays and may negatively regulate ethylene biosynthesis by modulating the abundance of ACS proteins. Loss of Xbat32 may promote the stabilization of ACSs and lead to increased ethylene synthesis and suppression of lateral root formation. Auxin treatments only partially rescue the lateral root defect of Xbat32 mutants, but they completely restore wild-type levels of Xbat32 lateral root production when coupled with ethylene inhibition. Abscisic acid stimulates rather than inhibits mutant Xbat32 lateral root formation, and abscisic acid acts synergistically with auxin to promote mutant Xbat32 lateral root production
physiological function
RING-type E3 ligase KEG interacts directly with abscisic acid-responsive transcription factor ABI5 via its conserved C3 region. Interactions between KEG and ABI5 are observed in the cytoplasm and trans-Golgi network only when the RING domain of KEG is inactivated or when ABI5 is stabilized via mutations. Deletion of the C-terminal region of ABI5 or substituting lysine 344 for alanine prohibits protein turnover
physiological function
-
suppression of expression of DAF, i.e. DEFECTIVE IN ANTHER DEHISCENCE1 (DAD1)-activating factor, causes non-dehiscence of the anthers, alters pollen development and causes sterility in 35S:DAF RNAi/antisense Arabidopsis plants. Ectopic expression of the dominant-negative C132S or H137Y mutations causes similar indehiscence of anthers and reduction in DAD1 expression in transgenic Arabidopsis thaliana
physiological function
-
the enzyme acts as a positive regulator of absisic acid-mediated drought avoidance and a negative regulator of salt tolerance in Arabidopsis. Enzyme overexpression plants are hypersensitive to salt and osmotic stresses during seed germination, and show drought avoidance
physiological function
the enzyme is negatively correlated not only with phosphorus content and phosphorus utilization efficiency, but also with biomass and seed yield in Arabidopsis. Enzyme overexpression results in the delayed flowering time and decrease in seed yield in sufficient phosphate condition
physiological function
-
the enzyme negatively regulates COP1 and SPA1 protein accumulation in darkness
physiological function
-
the enzyme regulates the degradation of iron-regulated transporter1 in Arabidopsis
physiological function
-
the enzyme regulates thermosensory flowering by triggering gigantea protein degradation
physiological function
-
the enzyme targets SDIR1-interacting protein1 for degradation to modulate the salt stress response and abscisic acid signaling
physiological function
enzyme belongs to a family of E3 ligases with a RING-H2 domain related in sequence to the ATL and BTL RING-H2 domains. This family, named CTL, carries a motif YEELL that expands 21 amino acids next to the RING-H2 domain. E3 ubiquitin ligase BIG BROTHER is a plant CTL that regulates organ size
physiological function
-
RING E3 ligase PIR2 interacts with protein phosphatase PP2CA. A PIR2 knockout mutant does not display altered response to abscisic acid, the PIR1-1/PIR2 double mutant becomes more insensitive to abscisic acid than the wild-type or PIR1-1 and PIR2 single mutants
physiological function
-
splicing isoform PIR1.2 exhibits E3 ligase activity and determines protein phosphatase PP2CA's stability in the presence of abscisic acid. The PIR1 knockout mutant displays an abscisic acid-hyposensitive phenotype. A PIR1-1/PIR2 double mutant becomes more insensitive to abscisic acid than the wild-type or PIR1-1 and PIR2 single mutants
physiological function
tobacco leaf-produced EMR mediates mildew resistance locus O-12 degradation in a proteasome-dependent manner. EMR forms a complex with ubiquitin-conjugating enzyme UBC32. Mutation of EMR and RNAi increase the tolerance of plants to endoplasmic reticulum stress. EMR RNAi in a brassinosteroid signaling mutant protein background, leads to partial recovery of the brassinosteroid insensitive phenotypes as compared with the original mutant plants and increased ER stress tolerance
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). RHA2B_ARATH
147
0
16241
Swiss-Prot
other Location (Reliability: 5)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
protein PRL1, for Pleiotropic Regulatory Locus 1, a DWD protein containig a DDB1 binding WD40 motif may act as part of a CUL4-based E3 ligase. PRL1 directly interacts with adaptor protein DDB1, and prl1 and cul4cs mutants exhibit similar phenotypes, including altered responses to a variety of stimuli. Protein AKIN10, Arabidopsis SNF1 Kinase Homolog 10, is degraded more slowly in cell extracts of prl1 and cul4cs than in cell extracts of the wild type
additional information
-
protein PRL1, for Pleiotropic Regulatory Locus 1, a DWD protein containig a DDB1 binding WD40 motif may act as part of a CUL4-based E3 ligase. PRL1 directly interacts with adaptor protein DDB1, and prl1 and cul4cs mutants exhibit similar phenotypes, including altered responses to a variety of stimuli. Protein AKIN10, Arabidopsis SNF1 Kinase Homolog 10, is degraded more slowly in cell extracts of prl1 and cul4cs than in cell extracts of the wild type
additional information
proteins containing DWD motifs, for DDB1 binding WD40, function as substrate receptors for CUL4-based E3 ligases in plants. DDB1 functions as adaptor protein that links ligase CUL4 to substrate receptors 11 Arabidopsis DWD proteins directly interact with DDB1 and may serve as substrate receptors for the DDB1CUL4 machinery
additional information
-
proteins containing DWD motifs, for DDB1 binding WD40, function as substrate receptors for CUL4-based E3 ligases in plants. DDB1 functions as adaptor protein that links ligase CUL4 to substrate receptors 11 Arabidopsis DWD proteins directly interact with DDB1 and may serve as substrate receptors for the DDB1CUL4 machinery
additional information
AIRP3 harbors a single C3HC4-type RING motif in its C-terminal region, a putative myristoylation site in the N-terminal region, and a domain associated with RING2 domain in the central region
additional information
Sis3 sequence is predicted to have a RING domain located between amino acids 235 and 275
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C132S
-
mutation in the RING domain, loss of E3 ubiquitin ligase activity
C367S
mutation within RING finger domain, mutant protein does not display significant ubiquitin ligase activity
C36S
mutation in conserved residue of RING motif. Ser substitution strongly diminishes the ubiquitin ligase activity
C59S
mutation of conserved residue of RING motif. Ser substitution strongly diminishes the ubiquitin ligase activity
C63S
mutation of conserved residue of RING motif. Ser substitution strongly diminishes the ubiquitin ligase activity
H137Y
-
mutation in the RING domain, loss of E3 ubiquitin ligase activity
H348Y
mutation within RING finger domain, mutant protein does not display significant ubiquitin ligase activity
W266H
mutation results in loss of activity with family 13 Ubc enzymes
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
EMR is significantly upregulated under endoplasmic reticulum stress conditions
expression is markedly induced by abscisic acid and dehydration stress
-
expression is significantly induced by abscisic acid and drought stress
the enzyme is upregulated by 10 days low phosphate (0-02 mM KH2PO4) conditions
the transcription level can be induced by absisic acid (0.1 mM), heat (37°C), osmotic (300 mM mannitol) and oxidative stresses (20 mM H2O2)
-
transcript levels of AIRP3 are up-regulated by drought, high salinity, and abscisic acid
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Yang, C.W.; Gonzalez-Lamothe, R.; Ewan, R.A.; Rowland, O.; Yoshioka, H.; Shenton, M.; Ye, H.; ODonnell, E.; Jones, J.D.; Sadanandom, A.
The E3 ubiquitin ligase activity of Arabidopsis PLANT U-BOX17 and its functional tobacco homolog ACRE276 are required for cell death and defense
Plant Cell
18
1084-1098
2006
Solanum lycopersicum, Nicotiana tabacum (Q84QD7), Nicotiana tabacum, Arabidopsis thaliana (Q9C7R6), Arabidopsis thaliana
Wiborg, J.; OShea, C.; Skriver, K.
Biochemical function of typical and variant Arabidopsis thaliana U-box E3 ubiquitin-protein ligases
Biochem. J.
413
447-457
2008
Arabidopsis thaliana (Q9LQ92)
Lee, J.H.; Terzaghi, W.; Gusmaroli, G.; Charron, J.B.; Yoon, H.J.; Chen, H.; He, Y.J.; Xiong, Y.; Deng, X.W.
Characterization of Arabidopsis and rice DWD proteins and their roles as substrate receptors for CUL4-RING E3 ubiquitin ligases
Plant Cell
20
152-167
2008
Arabidopsis thaliana (Q8LGH4), Arabidopsis thaliana
Son, O.; Cho, S.K.; Kim, E.Y.; Kim, W.T.
Characterization of three Arabidopsis homologs of human RING membrane anchor E3 ubiquitin ligase
Plant Cell Rep.
28
561-569
2009
Arabidopsis thaliana (O64425), Arabidopsis thaliana (P93030), Arabidopsis thaliana (Q8GUK7)
Huang, F.; Xiao, H.; Sun, B.L.; Yang, R.G.
Characterization of TRIM62 as a RING finger E3 ubiquitin ligase and its subcellular localization
Biochem. Biophys. Res. Commun.
432
208-213
2013
Arabidopsis thaliana (Q8GYT9), Homo sapiens (Q9BVG3)
Liu, H.; Stone, S.L.
Cytoplasmic degradation of the Arabidopsis transcription factor abscisic acid insensitive 5 is mediated by the RING-type E3 ligase KEEP ON GOING
J. Biol. Chem.
288
20267-20279
2013
Arabidopsis thaliana (Q9FY48), Arabidopsis thaliana
Gao, W.; Liu, W.; Zhao, M.; Li, W.X.
NERF encodes a RING E3 ligase important for drought resistance and enhances the expression of its antisense gene NFYA5 in Arabidopsis
Nucleic Acids Res.
43
607-617
2015
Arabidopsis thaliana (Q9SYH3)
Peng, Y.J.; Shih, C.F.; Yang, J.Y.; Tan, C.M.; Hsu, W.H.; Huang, Y.P.; Liao, P.C.; Yang, C.H.
A RING-type E3 ligase controls anther dehiscence by activating the jasmonate biosynthetic pathway gene DEFECTIVE IN ANTHER DEHISCENCE1 in Arabidopsis
Plant J.
74
310-327
2013
Arabidopsis thaliana
Tian, M.; Lou, L.; Liu, L.; Yu, F.; Zhao, Q.; Zhang, H.; Wu, Y.; Tang, S.; Xia, R.; Zhu, B.; Serino, G.; Xie, Q.
The RING finger E3 ligase STRF1 is involved in membrane trafficking and modulates salt-stress response in Arabidopsis thaliana
Plant J.
82
81-92
2015
Arabidopsis thaliana (Q9LUZ9), Arabidopsis thaliana
Prasad, M.E.; Schofield, A.; Lyzenga, W.; Liu, H.; Stone, S.L.
Arabidopsis RING E3 ligase XBAT32 regulates lateral root production through its role in ethylene biosynthesis
Plant Physiol.
153
1587-1596
2010
Arabidopsis thaliana (Q6NLQ8)
Ryu, M.Y.; Cho, S.K.; Kim, W.T.
The Arabidopsis C3H2C3-type RING E3 ubiquitin ligase AtAIRP1 is a positive regulator of an abscisic acid-dependent response to drought stress
Plant Physiol.
154
1983-1997
2010
Arabidopsis thaliana (Q93ZF6)
Li, H.; Jiang, H.; Bu, Q.; Zhao, Q.; Sun, J.; Xie, Q.; Li, C.
The Arabidopsis RING finger E3 ligase RHA2b acts additively with RHA2a in regulating abscisic acid signaling and drought response
Plant Physiol.
156
550-563
2011
Arabidopsis thaliana (Q9ZU51)
Cho, S.K.; Ryu, M.Y.; Seo, D.H.; Kang, B.G.; Kim, W.T.
The Arabidopsis RING E3 ubiquitin ligase AtAIRP2 plays combinatory roles with AtAIRP1 in abscisic acid-mediated drought stress responses
Plant Physiol.
157
2240-2257
2011
Arabidopsis thaliana
Cheng, M.C.; Hsieh, E.J.; Chen, J.H.; Chen, H.Y.; Lin, T.P.
Arabidopsis RGLG2, functioning as a RING E3 ligase, interacts with AtERF53 and negatively regulates the plant drought stress response
Plant Physiol.
158
363-375
2012
Arabidopsis thaliana (Q9LY87)
Kim, J.H.; Kim, W.T.
The Arabidopsis RING E3 ubiquitin ligase AtAIRP3/LOG2 participates in positive regulation of high-salt and drought stress responses
Plant Physiol.
162
1733-1749
2013
Arabidopsis thaliana (Q9S752)
Pauwels, L.; Ritter, A.; Goossens, J.; Nagels Durand, A.; Liu, H.X.; Gu, Y.; Geerinck, J.; Boter, M.; Vanden Bossche, R.; De Clercq, R.; Van Leene, J.; Gevaert, K.; De Jaeger, G.; Solano, R.; Stone, S.L.; Innes, R.W.; Callis, J.; Goossens, A.
The RING E3 ligase KEEP ON GOING modulates JAZ12 stability
Plant Physiol.
169
1405-1417
2015
Arabidopsis thaliana (Q9FY48)
Suh, J.Y.; Kim, W.T.
Arabidopsis RING E3 ubiquitin ligase AtATL80 is negatively involved inphosphate mobilization and cold stress response in sufficient phosphate growth conditions
Biochem. Biophys. Res. Commun.
463
793-799
2015
Arabidopsis thaliana (Q9LM69)
Ramadan, A.; Nemoto, K.; Seki, M.; Shinozaki, K.; Takeda, H.; Takahashi, H.; Sawasaki, T.
Wheat germ-based protein libraries for the functional characterisation of the Arabidopsis E2 ubiquitin conjugating enzymes and the RING-type E3 ubiquitin ligase enzymes
BMC Plant Biol.
15
275
2015
Arabidopsis thaliana
Yang, L.; Liu, Q.; Liu, Z.; Yang, H.; Wang, J.; Li, X.; Yang, Y.
Arabidopsis C3HC4-RING finger E3 ubiquitin ligase AtAIRP4 positively regulates stress-responsive abscisic acid signaling
J. Integr. Plant Biol.
58
67-80
2016
Arabidopsis thaliana
Shin, L.J.; Lo, J.C.; Chen, G.H.; Callis, J.; Fu, H.; Yeh, K.C.
IRT1 degradation factor1, a RING E3 ubiquitin ligase, regulates the degradation of iron-regulated transporter1 in Arabidopsis
Plant Cell
25
3039-3051
2013
Arabidopsis thaliana
Xu, D.; Lin, F.; Jiang, Y.; Huang, X.; Li, J.; Ling, J.; Hettiarachchi, C.; Tellgren-Roth, C.; Holm, M.; Deng, X.W.
The RING-finger E3 ubiquitin ligase COP1 SUPPRESSOR1 negatively regulates COP1 abundance in maintaining COP1 homeostasis in dark-grown Arabidopsis Sseedlings
Plant Cell
26
1981-1991
2014
Arabidopsis thaliana
Zhang, H.; Cui, F.; Wu, Y.; Lou, L.; Liu, L.; Tian, M.; Ning, Y.; Shu, K.; Tang, S.; Xie, Q.
The RING finger ubiquitin E3 ligase SDIR1 targets SDIR1-INTERACTING PROTEIN1 for degradation to modulate the salt stress response and ABA signaling in Arabidopsis
Plant Cell
27
214-227
2015
Arabidopsis thaliana
Jang, K.; Lee, H.G.; Jung, S.J.; Paek, N.C.; Seo, P.J.
The E3 ubiquitin ligase COP1 regulates thermosensory flowering by triggering GI degradation in Arabidopsis
Sci. Rep.
5
12071
2015
Arabidopsis thaliana
Park, J.H.; Kang, C.H.; Nawkar, G.M.; Lee, E.S.; Paeng, S.K.; Chae, H.B.; Chi, Y.H.; Kim, W.Y.; Yun, D.J.; Lee, S.Y.
EMR, a cytosolic-abundant ring finger E3 ligase, mediates ER-associated protein degradation in Arabidopsis
New Phytol.
220
163-177
2018
Arabidopsis thaliana (A0A178UZG1)
Baek, W.; Lim, C.; Luan, S.; Lee, S.
The RING finger E3 ligases PIR1 and PIR2 mediate PP2CA degradation to enhance abscisic acid response in Arabidopsis
Plant J.
100
473-486
2019
Arabidopsis thaliana
Jimenez-Lopez, D.; Aguilar-Henonin, L.; Gonzalez-Prieto, J.M.; Aguilar-Hernandez, V.; Guzman, P.
CTLs, a new class of RING-H2 ubiquitin ligases uncovered by YEELL, a motif close to the RING domain that is present across eukaryotes
PLoS ONE
13
e0190969
2018
Homo sapiens (Q6ZNA4), Arabidopsis thaliana (Q8L649)
EXTERNAL LINKS (specific for EC-Number 2.3.2.27)
Transporter Classification Database (TCDB): 3.A.16.1.2, 3.A.16.1.5, 8.A.159.1.1, 8.A.159.1.3, 8.A.159.1.9, 3.A.16.1.4, 8.A.133.1.1, 8.A.133.1.2, 8.A.112.1.6, 8.A.159.1.10, 1.A.87.4.1, 3.A.16.1.3
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)
Legal
Curated at
Member of
