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2.3.2.26: HECT-type E3 ubiquitin transferase

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

Word Map on EC 2.3.2.26

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

AIP2, AIP4, apoptosis-resistant E3 ligase 1, AREL1, atrophin-1 interacting protein 2, DDB_G0286931, E3 ligase, E3 ubiquitin-protein ligase NEDD4, E3 ubiquitin-protein ligase TOM1, E6-AP, E6AP, ETC-1, HECT domain E3 ubiquitin ligase, HECT ligase, HECT-domain ubiquitin ligase, HECT-type E3 ligase, HECT-type ubiquitin E3 ligase, HECTD3, HectPH1, HECTWWP2, Herc4, Huwe1, Itch, Nedd4, Nedd4 HECT, Nedd4-1, Nedd4L, NEDL1, NleL, RSP5, Smurf1, Smurf2, sog-1, TRIP12, Trp120, UBE3B, Ube3C, ubiquitin-protein ligase E3C, UBR E3 ubiquitin ligase homolog, Ubr-5, UBR1, UBR5, UPL3, UPL5, WW domain-containing E3 Ub–protein ligase 2, WWP1, WWP2

ECTree

     2 Transferases
         2.3 Acyltransferases
             2.3.2 Aminoacyltransferases
                2.3.2.26 HECT-type E3 ubiquitin transferase

Engineering

Engineering on EC 2.3.2.26 - HECT-type E3 ubiquitin transferase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A349P
mutant is defective in thioester formation
A713P
mutant is defective in thioester formation
C1036A
loss of ubiquitylation activity
C2579G
-
mutation in catalytic cysteine, loss of E3 ligase activity
C716A
-
mutation in catalytic cysteine. Cells transfected with C716A fail to accumulate securin with significant reduction in Mad2 level. Cell show a significant increase in cells displaying misaligned chromosomes, lagging chromosomes during mitotic exit, and multinucleation
C922A
-
dominant-negative active site mutant, predicted to result in an end point of 33% activity compared with wild-type. Addition of mutant C922A to the wild-type enzyme at saturating concentration inhibits wild-type NEDD4L to 30% limiting activity
DELTA382-385
HECT domain mutant, capable of forming DTT-sensitive HECT-ubiquitin thioesters, defective in polyubiquitination
DELTA383-385
HECT domain mutant, capable of forming DTT-sensitive HECT-ubiquitin thioesters, defective in polyubiquitination
DELTA384-385
HECT domain mutant, capable of forming DTT-sensitive HECT-ubiquitin thioesters, defective in polyubiquitination
E411Q
slight decrease of affinity to human papilloma virus E6 oncogens
E411Q/E415Q
about 6fold decrease of affinity to human papilloma virus E6 oncogens
E415Q
slight decrease of affinity to human papilloma virus E6 oncogens
E415R
slight decrease of affinity to human papilloma virus E6 oncogens
E646A
-
400fold reduction in kcat value for polyubiquitination
E646D
-
1200fold reduction in kcat value for polyubiquitination
E701A
substitution in the Arel1 HECT domain, substantially increases its autopolyubiquitination and SMAC ubiquitination activity
E748A
mutant produces thioester levels comparable to the wild-type and shows enhanced polyubiquitination activity
F707A
Nedd4 mutant, almost abolished HECTNedd4 binding to Lys 63 ubiquitin. Mutant F707A has defective chain elongation on substrate or shorter free chains
F823A
-
10000fold reduction in kcat value
F823D
-
no detectable free or anchored polyubiquitin chain assembly is observed with the mutant
G383A/L384A
mutant produces thioester levels comparable to the wild-type
K1013Q
mutation increases the formation of E3-Ub thioester intermediate and shows 2fold enhanced ubiquitination activity
L346P
mutation abolishes E2-E3 transthiolation and consequently polyubiquitination activity
L384A
mutant produces thioester levels comparable to the wild-type
L409V
about 30fold decrease of affinity to human papilloma virus E6 oncogens characterised by very fast dissociation rates
L412V
moderate decrease of affinity to human papilloma virus E6 oncogens
L413S
about 40fold decrease of affinity to human papilloma virus E6 oncogens characterised by very fast dissociation rates
L413V
moderate decrease of affinity to human papilloma virus E6 oncogens
medicine
Q410E
no decrease of affinity to human papilloma virus E6 oncogens
Q961A
mutation of residues in the HECT domain, substantial decrease in autoubiquitination activity and in the formation of E3-Ub thioester intermediate
Q961E
mutation substantially reduces the formation of E3-Ub thioester intermediate
Q961E/K1013Q
mutant shows a reduced level of autoubiquitination activity
R604D
-
15fold reduction in kcat value for polyubiquitination
Ser1049
mutation of residues in the HECT domain, substantial decrease in autoubiquitination activity
V747A/E748A
mutant produces thioester levels comparable to the wild-type
Y605A
Nedd4 mutant, almost abolished HECTNedd4 binding to Lys 63 ubiquitin
additional information