Any feedback?
Please rate this page
(all_enzymes.php)
(0/150)

BRENDA support

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

Crystallization

Crystallization on EC 2.3.2.27 - RING-type E3 ubiquitin transferase

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
2.9 A crystal structure of the ubiquitin ligase CHIP U-box domain complexed with UbcH5a. CHIP binds to UbcH5 and Ubc13 through similar specificity determinants located on the long loops and central helix of the CHIP U-box, and on the N-terminal helix and loops L4 and L7 of its cognate E2 enzymes including a key S-P-A motif. The determinants make different relative contributions to the overall interactions between CHIP and the two E2 enzymes. CHIP undergoes auto-ubiquitination by UbcH5 but not by Ubc13-Uev1a. Instead, CHIP drives the formation of unanchored polyubiquitin by Ubc13-Uev1a. CHIP also interacts productively with the class III E2 enzyme Ube2e2
crystal structure of ZNRF1 C-terminal domain in complex with Ube2N. The domain binds Ube2N exclusively via its RING domain. The ZNRF1:Ube2N interface contains three salt-bridges/H-bonds involving Glu183 of ZNRF1 and Arg14/Lys10 of Ube2N
crystallization of isoform parkin protein residues 141-465 including RING 0 and RING-between-RING domains. The protein is assembled into two compact domain groups separated by linkers. The catalytic network consists of residues C431 and H433. Parkin functions as a RING/HECT hybrid ubiquitin ligase
hanging drop vapor diffusion method, using either 1.0-1.4 M potassium/sodium tartrate /0.1M CHES pH 9.5 /0.2M LiSO4, or 0.5-0.55 M trisodium citrate/0.1 M citric acid pH 5.2/0.2 M lithium acetate, at room temperature
heterodimeric structure of the complex of Ring1b and Bmi1. Complex formation depends on an N-terminal arm of Ring1b that embraces the Bmi1 Ring-domain. Catalytic activity resides in Ring1b and not in Bmi1
in complex with polycomb group RING finger proteins PCGF5 or PCGF4 and E2 enzyme UbcH5. RING1B binds directly to UbcH5c, with the PCGF partner making no contacts with the E2. The catalytically critical hydrogen bond between RING1B R91 and the backbone carbonyl of UbcH5c Q92 is present in both the structures, consistent with an activated conformation of the E2. Differences between the PCGF4 and PCGF5 ternary complex structures are found at the N termini of the PCGF and RING1B
RNF8(345-485)/Ubc13-Ub complex, hanging drop vapor diffusion method, using
solution structure of the isoform HHARI RING2 domain, the key portion of this E3 ligase required for the RING/HECT hybrid mechanism. The domain possesses two Zn2+-binding sites and a single exposed cysteine used for ubiquitin catalysis. A structural comparison of the RING2 domain with the HECT E3 ligase NEDD4 reveals a near mirror image of the cysteine and histidine residues in the catalytic site. A tandem pair of aromatic residues exists near the C-terminus of the HHARI RING2 domain that is conserved in other RING-in-Between-RING E3 ligases
structure of dimeric Ring finger domain of MEX3C and comparison with the complex structure of MDM2/MDMX-UbcH5b-Ub. The Ring finger domain of MEX3C acts as a ubiquitin E3 ligase in vitro, cooperating with E2 enzymes UbcH5b and UbcH5c to mediate ubiquitination
structure of the RING domain (residues 907-975) at a resolution of 1.8 A. The core RING domain resembles other RING domains, with two zinc ions coordinated in a cross-braced arrangement by one His and seven Cys side chains. Residues in the core RING domain, the N-terminal alpha-helix, and the C-terminal tail comprise the dimer interface
structures of MUL1-RING domain and of its complex with the cognate E2 enzyme UbeD2
structures of the TRIM23 RING domain in isolation and in complex with an E2-ubiquitin conjugate. TRIM23 enzymatic activity requires RING dimerization. The two RING domains have distinct interactions with the E2-ubiquitin conjugate and cooperate in facilitating the ubiquitination reaction
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
isoform Rnf4 trimeric complex with UbcH5a and ubiquitin. E2 enzyme UbcH5a is linked by an isopeptide bond to ubiquitin. UbcH5a contacts a single protomer of the RING, and ubiquitin is folded back onto the UbcH5a by contacts from both RING protomers. The C-terminal tail of ubiquitin is locked into an active site groove on UbcH5a by an intricate network of interactions, resulting in changes at the UbcH5a active site
structure of fragment Prp19(1-133), which contains both the N-terminal U-box and central coiled-coil domain, to 1.38 A resolution. The Prp19 U-box domain exists in a dimeric state in the context of intact Prp19. The hydrophobic character of the dimer interface is due to residues Leu15, Ile22, Val51, and Ile53. All four positions are conserved long-chain hydrophobic residues