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2.3.2.27: RING-type E3 ubiquitin transferase

This is an abbreviated version!
For detailed information about RING-type E3 ubiquitin transferase, go to the full flat file.

Word Map on EC 2.3.2.27

Reaction

[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

ABA-insensitive RING protein3, abscisic acid-insensitive RING protein 4, ACRE276, AIR1, AIR2, AIRP1, AIRP2, AIRP3, AIRP4, AMFR, Arabidopsis ABA-insensitive RING protein 1, Arabidopsis ABA-insensitive RING protein 2, ARIH1, As-induced RING E3 ligase 2, At1g54150, At1g74410, At2g15580, At4g23450, At4g26400, ATL2, ATL80, Avr9/Cf-9 rapidly elicited protein 276, BIG BROTHER, BIRC3, BRCA1, BRE1A, BRE1B, breast cancer susceptibility protein 1, breast cancer type 1 susceptibility protein, c-Cbl, C3HC4-RING finger E3 ubiquitin ligase, CaRING1, CHIP, cIAP2, Cop1, COP1 SUPPRESSOR1, CSU1, CUL4, cullin-4, DAF, DEAR1, DEFECTIVE IN ANTHER DEHISCENCE1 (DAD1)-activating factor, Der3, Dir1, E3 ligase, E3 ubiquitin ligase, E3 ubiquitin ligase Erysiphe necator-induced RING finger protein 1, E3 ubiquitin ligase RING1, E3 ubiquitin-protein ligase Arkadia, E3 ubiquitin-protein ligase Mdm2, E3 ubiquitin-protein ligase MIR1, E3 ubiquitin-protein ligase RNF25, E3-enzyme, EIRP1, EMR, ERAD-associated E3 ubiquitin-protein ligase DOA10, ERAD-associated E3 ubiquitin-protein ligase HRD1, ERAD-mediating RING finger protein, FANCL, gamma rays-induced RING finger protein1, GIRP1, gp78, H2-10, HCI1, HHARI, HIR1, HOS1, HSPC238, HTAS, HUB1, Human Homologue of Drosophila Ariadne, IDF1, IRT1 degradation factor1, KEEP ON GOING, KEG, Kf-1, LOG2, mahogunin ring finger-1, MARCH10, MARCH6, Mdm2, MEX3C, MGRN1, microtubule-associated E3 ubiquitin ligase isoform 1, MIEL1, MUL1, NERF, NFYA5 enhancing RING FINGER, Os05g41795, Os10g30850, Parkin, Parkinson juvenile disease protein 2, PIR1, PIR2, Pirh2, PLANT U-BOX17, PP2CA interacting RING finger protein 1, PP2CA interacting RING finger protein 2, pre-mRNA-splicing factor 19, PRP19, PUB17, PUB54, RanBP-type and C3HC4-type zinc finger-containing protein 1, RBCK1, RBX1, RCHY1, RFP1, RFPH2-10, RGLG2, RHA2b, Rines, Ring, RING E3, RING E3 ubiquitin ligase, ring finger protein 103, Ring finger protein 186, RING finger ubiquitin E3 ligase, RING-CH 10, ring-finer protein 55, RING-finger E3 ligase, RING-finger E3 ubiquitin ligase, RING-finger ubiquitin ligase Ubr1, RING-H2 finger E3 ubiquitin ligase, RING-H2 finger protein ATL63, RING-IBR-RING ubiquitin ligase, RING-type E3 ligase, RING-type E3 ubiquitin ligase, Ring1B, RMA1, RMA2, RMA3, RN181, RNF103, RNF111, RNF180, RNF186, RNF190, RNF2, RNF20, RNF220, RNF4, RNF43, RNF45, RNF8, salt tolerance RING finger 1, SDIR1, SIRP2, Sis3, SSM4, STIP1 homology and U-Box containing protein 1, Strf1, TEB4, TRIM22, Trim23, TRIM25, TRIM3, TRIM5, TRIM5alpha, TRIM62, TRIM69, tripartite motif-containing protein 5, U-box domain-containing protein 17, Ube4A, UBE4B, ubiquitin ligase E3, ubiquitin ligase Ubr1, ubiquitin-protein ligase K3, UBR1, UFD-2, Xbat32, ZNRF1

ECTree

     2 Transferases
         2.3 Acyltransferases
             2.3.2 Aminoacyltransferases
                2.3.2.27 RING-type E3 ubiquitin transferase

Engineering

Engineering on EC 2.3.2.27 - RING-type E3 ubiquitin transferase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
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
C194S
mutation in highly conserved residue, loss of ubiqitin ligase activity
C197S
mutation in highly conserved residue, loss of ubiqitin ligase activity
A46P
-
the mutant shows barely detectable autoubiquitination activity compared to the wild type
C11A
mutation introduced to reduce the stability of the RING domain, poor activity
C15A
mutation in the conserved RING-finger domain, loss of autoubiquitination ability
C431A
mutation eliminates parkin-catalyzed degradation of mitochondria
C431S
C53A
mutation in Zn2+ coordination site of BARD1, increases E3 ligase activity
C608S/C611S
mutation in Zn2+ coordination site, almost complete loss ofactivity
C61A/C64A
mutation of two adjacent cysteine residues at the conserved zinc-binding position, mutant shows weak activity
C632S
mutation in Zn2+ coordination site, almost complete loss of activity
C71A
mutation in Zn2+ coordination site of BARD1, increases E3 ligase activity
C9A
mutation within the RING domain of TEB4, strongly impairs its own degradation
D67E
-
mutation identified in Thai familial breast cancer patients. The mutation is located in the vicinity of Zn2+ binding site II. The D67E BRCA1 RING protein assumes a preformed structure in the absence of Zn2+. The Zn2+-bound mutant protein is more folded than wild-type, resulting in enhanced proteolytic resistance and dimerization. The mutation retains Zn2+ binding, and barely perturbs the native global structure of the BRCA1 RING domain. The D67E mutation might be a neutral or mild cancer-risk modifier of other defective mechanisms underlying BRCA1-mutation-related breast cancer
I26A/L63A/K65A
mutations in BRCA1, complete elimination of BRCA1 activity without disrupting its structure
I53A
the Ring1b/Bmi1 complex with an I53A mutation in Ring1b has almost no catalytic activity
I610A
mutation abolishes selfubiquitination activity. Residue may play key role to interact with E2 and stabilize ubiquitin in the closed active E2-Ub conformation
I636A
mutation abolishes selfubiquitination activity
K27N
-
the mutant shows barely detectable autoubiquitination activity compared to the wild type
K48A
-
the mutant has higher autoubiquitination activity than the wild type
K639A
mutation reduces selfubiquitination activity
K65R
activating mutation in BRCA1
L451D
the mutation causes a drastic decrease in the ability of the enzyme to stimulate Ubc13
L51W
activating mutation in BRCA1
L51W/K65R
mutant of BRCA1, much more active than either of the individual activating mutants
P645A
mutation abolishes selfubiquitination activity
Q648A
mutation abolishes selfubiquitination activity. Residue may play key role to interact with E2 and stabilize ubiquitin in the closed active E2-Ub conformation
R33Q
-
the mutant shows barely detectable autoubiquitination activity compared to the wild type
R42P
-
the mutant has higher autoubiquitination activity than the wild type
R441A
the mutation has little effect on the enzyme activity
S17D
phosphomimetic mutation, stimulates MDM2-mediated polyubiquitination of p53. The stimulation is independent of p53 substrate. Mutation alters the conformation of the isolated N-terminus, it induces increased thermostability of the isolated N-terminal domain, it stimulates the allosteric interaction of MDM2 with the DNA-binding domain of p53 and it stimulates a protein-protein interaction with the E2-ubiquitin complex in the absence of substrate p53 that, in turn, increases hydrolysis of the E2-ubiquitin thioester bond
T240R
-
the mutant shows barely detectable autoubiquitination activity compared to the wild type
V609A
mutation reduces selfubiquitination activity
V609E
mutation abolishes selfubiquitination activity
V646E
mutation abolishes selfubiquitination activity
Y268E
no increased activity compared to unphosphorylated wild-type
Y268F
residue Y268 is not required for phosphorylation-induced activation
Y274E
slightly increased activity compared to unphosphorylated wild-type
Y291E
no increased activity compared to unphosphorylated wild-type
Y307E
strongly increased activity compared to unphosphorylated wild-type
Y337E
strongly increased activity compared to unphosphorylated wild-type
Y371E
C149A
-
mutation in RING domain, inactive
C172A
mutation in the RING domain, mutant does not show autoubiquitylation
C196A
-
amino acid substitution of the RING domain, complete loss of E3 ligase activity
K118R
residue Lys118 is required for Ubc7 activity. Mutant is very poor in assembly of polyubiquitin chains. Lys118 is both essential and sufficient for Doa10-mediated degradation of substrates
L15E
mutant in U-box domain interface, abrogates U-box dimer formation and is lethal in vivo
additional information