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Information on EC 2.3.2.25 - N-terminal E2 ubiquitin-conjugating enzyme
for references in articles please use BRENDA:EC2.3.2.25
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EC Tree 2 Transferases
2.3 Acyltransferases
2.3.2 Aminoacyltransferases
2.3.2.25 N-terminal E2 ubiquitin-conjugating enzyme
IUBMB Comments
The enzyme ubiquitinylates the N-terminus of the acceptor protein. It is not reactive towards free lysine.
The enzyme appears in viruses and cellular organisms
Reaction Schemes
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S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine
+
[acceptor protein]-N-terminal-amino acid
=
[E1 ubiquitin-activating enzyme]-L-cysteine
+
N-terminal-ubiquitinyl-[acceptor protein]
Synonyms
ubiquitin conjugating enzyme, ubiquitin conjugating enzyme e2, e2 ube2w, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
E2 ubiquitin-conjugating enzyme
UBE2W
ubiquitin conjugating enzyme
ubiquitin conjugating enzyme E2
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [acceptor protein]-N-terminal-amino acid = [E1 ubiquitin-activating enzyme]-L-cysteine + N-terminal-ubiquitinyl-[acceptor protein]
S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [N-terminal E2 ubiquitin-conjugating enzyme]-L-cysteine = [E1 ubiquitin-activating enzyme]-L-cysteine + S-ubiquitinyl-[N-terminal ubiquitin-conjugating enzyme]-L-cysteine
(1a)
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S-ubiquitinyl-[N-terminal E2 ubiquitin-conjugating E2 enzyme]-L-cysteine + [acceptor protein]-N-terminal-amino acid = [N-terminal E2 ubiquitin-conjugating enzyme]-L-cysteine + N-ubiquitinyl-[acceptor protein]-N-terminal amino acid
(1b)
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S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [acceptor protein]-N-terminal-amino acid = [E1 ubiquitin-activating enzyme]-L-cysteine + N-terminal-ubiquitinyl-[acceptor protein]
in contrast to other ubiquitin-conjugating enzymes which form an isopeptide bond, this enzyme catalyzes the formation of a peptide bond at the N-terminus of the acceptor protein
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S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [acceptor protein]-N-terminal-amino acid = [E1 ubiquitin-activating enzyme]-L-cysteine + N-terminal-ubiquitinyl-[acceptor protein]
overall reaction
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SYSTEMATIC NAME
IUBMB Comments
S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine:acceptor protein ubiquitin ligase (peptide bond-forming)
The enzyme ubiquitinylates the N-terminus of the acceptor protein. It is not reactive towards free lysine.
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [acceptor protein]-N-terminal-amino acid
[E1 ubiquitin-activating enzyme]-L-cysteine + N-terminal-ubiquitinyl-[acceptor protein]
S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [alpha-synuclein]-N-terminal-amino acid
[E1 ubiquitin-activating enzyme]-L-cysteine + N-terminal-ubiquitinyl-[alpha-synuclein]
Substrates: full-length alpha-synuclein
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S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [ATXN3]-N-terminal-amino acid
[E1 ubiquitin-activating enzyme]-L-cysteine + N-terminal-ubiquitinyl-[ATXN3]
Substrates: Ube2w ubiquitinates the alpha-amino-terminus of ATXN3 and lysine-less ATXN3, in presence and absence of ligase CHIP
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S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [huntingtin]-N-terminal-amino acid
[E1 ubiquitin-activating enzyme]-L-cysteine + N-terminal-ubiquitinyl-[huntingtin]
S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [NLRP1B]-N-terminal-amino acid
[E1 ubiquitin-activating enzyme]-L-cysteine + N-terminal-ubiquitinyl-[NLRP1B]
Substrates: NLRP1B inflammasome is ubiquitinylated at the N-terminal Leu248
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S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [NLRP1B]-N-terminal-leucine248
[E1 ubiquitin-activating enzyme]-L-cysteine + N-terminal-ubiquitinyl-[NLRP1B]
Substrates: NLRP1B inflammasome
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S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [Rnf4]-N-terminal-amino acid
[E1 ubiquitin-activating enzyme]-L-cysteine + N-terminal-ubiquitinyl-[Rnf4]
S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [SUMO-2]-N-terminal-amino acid
[E1 ubiquitin-activating enzyme]-L-cysteine + N-terminal-ubiquitinyl-[SUMO-2]
Substrates: -
Products: N-terminal mono-ubiquitylation of SUMO-2 primes it for poly-ubiquitylation by the Ubc13-UEV1 (ubiquitin-conjugating enzyme E2 variant 1) heterodimer
Products: N-terminal mono-ubiquitylation of SUMO-2 primes it for poly-ubiquitylation by the Ubc13-UEV1 (ubiquitin-conjugating enzyme E2 variant 1) heterodimer
?
S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [tau tetra-repeat domain]-N-terminal-Lys18
[E1 ubiquitin-activating enzyme]-L-cysteine + N-terminal-ubiquitinyl-[tau tetra-repeat domain]
Substrates: -
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S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [Ube2W]-N-terminal-amino acid
[E1 ubiquitin-activating enzyme]-L-cysteine + N-terminal-ubiquitinyl-[Ube2W]
Substrates: -
Products: isoform Ube2W ubiquitylates its own N-terminus
Products: isoform Ube2W ubiquitylates its own N-terminus
?
S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [UCHL1]-N-terminal-amino acid
[E1 ubiquitin-activating enzyme]-L-cysteine + N-terminal-ubiquitinyl-[UCHL1]
Substrates: -
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S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [UCHL5]-N-terminal-amino acid
[E1 ubiquitin-activating enzyme]-L-cysteine + N-terminal-ubiquitinyl-[UCHL5]
Substrates: -
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S-ubiquitinyl-[N-terminal E2 ubiquitin-conjugating E2 enzyme]-L-cysteine + [CARP2 protein]-N-terminal-amino acid
[N-terminal E2 ubiquitin-conjugating enzyme]-L-cysteine + N-ubiquitinyl-[ CARP2 protein]-N-terminal amino acid
Substrates: -
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S-ubiquitinyl-[N-terminal E2 ubiquitin-conjugating E2 enzyme]-L-cysteine + [cIAP2 protein]-N-terminal-amino acid
[N-terminal E2 ubiquitin-conjugating enzyme]-L-cysteine + N-ubiquitinyl-[ cIAP2 protein]-N-terminal amino acid
Substrates: -
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S-ubiquitinyl-[N-terminal E2 ubiquitin-conjugating E2 enzyme]-L-cysteine + [MDM2 protein]-N-terminal-amino acid
[N-terminal E2 ubiquitin-conjugating enzyme]-L-cysteine + N-ubiquitinyl-[ MDM2 protein]-N-terminal amino acid
Substrates: -
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?
[ubiquitin-carrier protein E2]-S-ubiquitinyl-L-cysteine + [ataxin-3]-NH2
[ubiquitin-carrier protein E2]-L-cysteine + N-terminal-ubiquitinyl-[ataxin-3]
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Substrates: -
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[ubiquitin-carrier protein E2]-S-ubiquitinyl-L-cysteine + [protein-tau]-NH2
[ubiquitin-carrier protein E2]-L-cysteine + N-terminal-ubiquitinyl-[protein-tau]
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Substrates: -
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[ubiquitin-carrier protein Ubc16]-S-ubiquitinyl-L-cysteine + [CHIP]-NH2
[ubiquitin-carrier protein Ubc16]-L-cysteine + N-terminal-ubiquitinyl-[CHIP]
Substrates: CHIP is a U-box E3 ubiquitin ligase known to interact productively with many E2 enzymes
Products: isoform Ubc16 N-terminally mono-ubiquitinates the ubiquitin E3 ligase CHIP
Products: isoform Ubc16 N-terminally mono-ubiquitinates the ubiquitin E3 ligase CHIP
?
[ubiquitin-carrier protein Ubc16]-S-ubiquitinyl-L-cysteine + [SUMO-2]-NH2
[ubiquitin-carrier protein Ubc16]-L-cysteine + N-terminal-ubiquitinyl-[SUMO-2]
Substrates: -
Products: isoform Ubc16 shows specific protein N-terminal monoubiquitylation activity. Ubc16 conjugates ubiquitin not only to its own N-terminus, but also to that of the small ubiquitin-like modifier SUMO in a manner dependent on the SUMO-targeted ubiquitin ligase RNF4, i.e. RING finger protein 4. N-terminal mono-ubiquitylation of SUMO-2 primes it for poly-ubiquitylation by the Ubc13-UEV1 ubiquitin-conjugating enzyme E2 variant 1 heterodimer
Products: isoform Ubc16 shows specific protein N-terminal monoubiquitylation activity. Ubc16 conjugates ubiquitin not only to its own N-terminus, but also to that of the small ubiquitin-like modifier SUMO in a manner dependent on the SUMO-targeted ubiquitin ligase RNF4, i.e. RING finger protein 4. N-terminal mono-ubiquitylation of SUMO-2 primes it for poly-ubiquitylation by the Ubc13-UEV1 ubiquitin-conjugating enzyme E2 variant 1 heterodimer
?
S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [acceptor protein]-N-terminal-amino acid
[E1 ubiquitin-activating enzyme]-L-cysteine + N-terminal-ubiquitinyl-[acceptor protein]
Substrates: -
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S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [acceptor protein]-N-terminal-amino acid
[E1 ubiquitin-activating enzyme]-L-cysteine + N-terminal-ubiquitinyl-[acceptor protein]
Substrates: -
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S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [acceptor protein]-N-terminal-amino acid
[E1 ubiquitin-activating enzyme]-L-cysteine + N-terminal-ubiquitinyl-[acceptor protein]
Substrates: -
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S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [acceptor protein]-N-terminal-amino acid
[E1 ubiquitin-activating enzyme]-L-cysteine + N-terminal-ubiquitinyl-[acceptor protein]
Substrates: -
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S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [acceptor protein]-N-terminal-amino acid
[E1 ubiquitin-activating enzyme]-L-cysteine + N-terminal-ubiquitinyl-[acceptor protein]
Substrates: -
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S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [acceptor protein]-N-terminal-amino acid
[E1 ubiquitin-activating enzyme]-L-cysteine + N-terminal-ubiquitinyl-[acceptor protein]
Substrates: -
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S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [huntingtin]-N-terminal-amino acid
[E1 ubiquitin-activating enzyme]-L-cysteine + N-terminal-ubiquitinyl-[huntingtin]
Substrates: -
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S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [huntingtin]-N-terminal-amino acid
[E1 ubiquitin-activating enzyme]-L-cysteine + N-terminal-ubiquitinyl-[huntingtin]
Substrates: the relatively disordered nature of the N-terminal domain of HTT predicts it to be a potential candidate target for Ube2W
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S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [huntingtin]-N-terminal-amino acid
[E1 ubiquitin-activating enzyme]-L-cysteine + N-terminal-ubiquitinyl-[huntingtin]
Substrates: -
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S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [huntingtin]-N-terminal-amino acid
[E1 ubiquitin-activating enzyme]-L-cysteine + N-terminal-ubiquitinyl-[huntingtin]
Substrates: the relatively disordered nature of the N-terminal domain of HTT predicts it to be a potential candidate target for Ube2W
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S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [Rnf4]-N-terminal-amino acid
[E1 ubiquitin-activating enzyme]-L-cysteine + N-terminal-ubiquitinyl-[Rnf4]
Substrates: -
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S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [Rnf4]-N-terminal-amino acid
[E1 ubiquitin-activating enzyme]-L-cysteine + N-terminal-ubiquitinyl-[Rnf4]
Substrates: -
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additional information
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Substrates: Ube2w is not reactive toward free lysine and contains novel residues in its active site that are important for activity
Products: to confirm N-terminal ubiquitination lysine-less and N-terminally blocked substrates are generated. The lysine-less substrate is ubiquinated, but not the N-terminally blocked one
Products: to confirm N-terminal ubiquitination lysine-less and N-terminally blocked substrates are generated. The lysine-less substrate is ubiquinated, but not the N-terminally blocked one
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additional information
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Substrates: in vitro, UBE2W can modify the N-terminus of both alpha-synuclein and a tau tetra-repeat domain with a single ubiquitin. The reaction does not continue beyond monoubiquitination as UBE2W specifically recognizes disordered sequences at the N-terminus of the substrate
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additional information
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Substrates: the enzyme UBE2W is specific for N-terminal amine group, it interacts with E3 ligase of type RING, HECT, and RBR. Ube2W exhibits no intrinsic activity towards free lysine. Instead, Ube2W attaches Ub to the N-terminal alpha-amino group of proteins to form a Ub-fusion protein product.While still an aminolysis reaction and therefore not fundamentally different from the reaction with lysine, intrinsic reactivity assays revealed that Ube2W can transfer Ub to the alpha-amino group of small lysine-less peptides but not to free lysine. The preference for N-terminal modification by Ube2W may not be absolute, as the retroviral restriction RING E3 TRIM5alpha is monoubiquitylated by Ube2W despite being acetylated on its N-terminus. Ube2W may also facilitate isopeptide bond formation, possibly if an N-terminus is blocked. Nevertheless, the preference of Ube2W for disordered N-termini gives it a (so far) unique target selection mechanism for a primary modification event that can subsequently be exploited by other E2 enzymes to form Ub chains. The E2 Ube2W shows unique ability to monoubiquitylate proteins on their N-termini. Ube2W appears to monoubiquitylate the RING E3 ligases TRIM5alpha and TRIM21, a prerequisite for their K63 polyubiquitylation by Ube2N/Ube2V2
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [acceptor protein]-N-terminal-amino acid
[E1 ubiquitin-activating enzyme]-L-cysteine + N-terminal-ubiquitinyl-[acceptor protein]
S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [huntingtin]-N-terminal-amino acid
[E1 ubiquitin-activating enzyme]-L-cysteine + N-terminal-ubiquitinyl-[huntingtin]
S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [NLRP1B]-N-terminal-amino acid
[E1 ubiquitin-activating enzyme]-L-cysteine + N-terminal-ubiquitinyl-[NLRP1B]
Substrates: NLRP1B inflammasome is ubiquitinylated at the N-terminal Leu248
Products: -
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S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [acceptor protein]-N-terminal-amino acid
[E1 ubiquitin-activating enzyme]-L-cysteine + N-terminal-ubiquitinyl-[acceptor protein]
Substrates: -
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S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [acceptor protein]-N-terminal-amino acid
[E1 ubiquitin-activating enzyme]-L-cysteine + N-terminal-ubiquitinyl-[acceptor protein]
Substrates: -
Products: -
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S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [acceptor protein]-N-terminal-amino acid
[E1 ubiquitin-activating enzyme]-L-cysteine + N-terminal-ubiquitinyl-[acceptor protein]
Substrates: -
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S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [acceptor protein]-N-terminal-amino acid
[E1 ubiquitin-activating enzyme]-L-cysteine + N-terminal-ubiquitinyl-[acceptor protein]
Substrates: -
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S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [acceptor protein]-N-terminal-amino acid
[E1 ubiquitin-activating enzyme]-L-cysteine + N-terminal-ubiquitinyl-[acceptor protein]
Substrates: -
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S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [acceptor protein]-N-terminal-amino acid
[E1 ubiquitin-activating enzyme]-L-cysteine + N-terminal-ubiquitinyl-[acceptor protein]
Substrates: -
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S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [huntingtin]-N-terminal-amino acid
[E1 ubiquitin-activating enzyme]-L-cysteine + N-terminal-ubiquitinyl-[huntingtin]
Substrates: -
Products: -
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S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [huntingtin]-N-terminal-amino acid
[E1 ubiquitin-activating enzyme]-L-cysteine + N-terminal-ubiquitinyl-[huntingtin]
Substrates: -
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Adenocarcinoma of Lung
Expression of UBE2C in lung adenocarcinoma based on database analysis and its clinical significance.
Adenocarcinoma of Lung
High ubiquitin conjugating enzyme E2 T mRNA expression and its prognostic significance in lung adenocarcinoma: A study based on the TCGA database.
Adenocarcinoma of Lung
Ubiquitin Conjugating Enzyme E2 H (UBE2H) Is Linked to Poor Outcomes and Metastasis in Lung Adenocarcinoma.
African Swine Fever
An ARID family protein binds to the African swine fever virus encoded ubiquitin conjugating enzyme, UBCv1.
Alzheimer Disease
A human ubiquitin conjugating enzyme, L-UBC, maps in the Alzheimer's disease locus on chromosome 14q24.3.
Alzheimer Disease
Deficiency in the Ubiquitin Conjugating Enzyme UBE2A in Alzheimer's Disease (AD) is Linked to Deficits in a Natural Circular miRNA-7 Sponge (circRNA; ciRS-7).
Autoimmune Diseases
The haplotype of UBE2L3 gene is associated with Hashimoto's thyroiditis in a Chinese Han population.
Breast Neoplasms
Identifying breast cancer subtypes associated modules and biomarkers by integrated bioinformatics analysis.
Breast Neoplasms
Inhibition of ubiquitin conjugating enzyme UBE2C reduces proliferation and sensitizes breast cancer cells to radiation, doxorubicin, tamoxifen and letrozole.
Breast Neoplasms
Prognostic value of ubiquitin E2 UBE2W and its correlation with tumor-infiltrating immune cells in breast cancer.
Breast Neoplasms
Stromal cell extracellular vesicular cargo mediated regulation of breast cancer cell metastasis via ubiquitin conjugating enzyme E2 N pathway.
Carcinogenesis
BIR repeat-containing ubiquitin conjugating enzyme (BRUCE) regulation of ?-catenin signaling in the progression of drug-induced hepatic fibrosis and carcinogenesis.
Carcinogenesis
Combined elevation of AURKB and UBE2C predicts severe outcomes and therapy resistance in glioma.
Carcinogenesis
Identification of key candidate genes and pathways in endometrial cancer: Evidence from bioinformatics analysis.
Carcinogenesis
Inhibiting ubiquitin conjugating enzyme E2 N by microRNA-590-3p reduced cell growth of cervical carcinoma.
Carcinogenesis
[Selecting functional siRNA target sites of hUBE2W based on H1-U6 dual promoter RNAi plasmid]
Carcinoma
Inhibiting ubiquitin conjugating enzyme E2 N by microRNA-590-3p reduced cell growth of cervical carcinoma.
Carcinoma
Overexpression of UBE2C in esophageal squamous cell carcinoma tissues and molecular analysis.
Carcinoma, Hepatocellular
The ménage à trois of autophagy, lipid droplets and liver disease.
Colitis
RNF186 regulates EFNB1 (ephrin B1)-EPHB2-induced autophagy in the colonic epithelial cells for the maintenance of intestinal homeostasis.
Colitis, Ulcerative
RNF186 regulates EFNB1 (ephrin B1)-EPHB2-induced autophagy in the colonic epithelial cells for the maintenance of intestinal homeostasis.
Crohn Disease
RNF186 regulates EFNB1 (ephrin B1)-EPHB2-induced autophagy in the colonic epithelial cells for the maintenance of intestinal homeostasis.
Endometrial Neoplasms
MLN4924 inhibits cell proliferation by targeting the activated neddylation pathway in endometrial carcinoma.
Esophageal Squamous Cell Carcinoma
Overexpression of UBE2C in esophageal squamous cell carcinoma tissues and molecular analysis.
Fanconi Anemia
UBE2W interacts with FANCL and regulates the monoubiquitination of Fanconi anemia protein FANCD2.
Glioma
Combined elevation of AURKB and UBE2C predicts severe outcomes and therapy resistance in glioma.
Huntington Disease
The ubiquitin conjugating enzyme Ube2W regulates solubility of the Huntington's disease protein, huntingtin.
Hypersensitivity
Loss of ubiquitin E2 Ube2w rescues hypersensitivity of Rnf4 mutant cells to DNA damage.
Inflammatory Bowel Diseases
RNF186 regulates EFNB1 (ephrin B1)-EPHB2-induced autophagy in the colonic epithelial cells for the maintenance of intestinal homeostasis.
Leukemia
Identification of novel lipid droplet factors that regulate lipophagy and cholesterol efflux in macrophage foam cells.
Leukemia, T-Cell
Identification of novel lipid droplet factors that regulate lipophagy and cholesterol efflux in macrophage foam cells.
Liver Diseases
BIR repeat-containing ubiquitin conjugating enzyme (BRUCE) regulation of ?-catenin signaling in the progression of drug-induced hepatic fibrosis and carcinogenesis.
Neoplasm Metastasis
Identification of hub genes associated with esophageal cancer progression using bioinformatics analysis.
Neoplasm Metastasis
Long non-coding RNA UBE2CP3 enhances HCC cell secretion of VEGFA and promotes angiogenesis by activating ERK1/2/HIF-1?/VEGFA signalling in hepatocellular carcinoma.
Neoplasm Metastasis
Stromal cell extracellular vesicular cargo mediated regulation of breast cancer cell metastasis via ubiquitin conjugating enzyme E2 N pathway.
Neoplasm Metastasis
Ubiquitin Conjugating Enzyme E2 H (UBE2H) Is Linked to Poor Outcomes and Metastasis in Lung Adenocarcinoma.
Neoplasms
BIR repeat-containing ubiquitin conjugating enzyme (BRUCE) regulation of ?-catenin signaling in the progression of drug-induced hepatic fibrosis and carcinogenesis.
Neoplasms
Combined elevation of AURKB and UBE2C predicts severe outcomes and therapy resistance in glioma.
Neoplasms
High ubiquitin conjugating enzyme E2 T mRNA expression and its prognostic significance in lung adenocarcinoma: A study based on the TCGA database.
Neoplasms
Inhibiting ubiquitin conjugating enzyme E2 N by microRNA-590-3p reduced cell growth of cervical carcinoma.
Neoplasms
Long non-coding RNA UBE2CP3 enhances HCC cell secretion of VEGFA and promotes angiogenesis by activating ERK1/2/HIF-1?/VEGFA signalling in hepatocellular carcinoma.
Neoplasms
Manipulation of the ubiquitin-proteasome pathway in cachexia: pentoxifylline suppresses the activation of 20S and 26S proteasomes in muscles from tumor-bearing rats.
Neoplasms
miRNA?101?3p.1 as an independent diagnostic biomarker aggravates chronic obstructive pulmonary disease via activation of the EGFR/PI3K/AKT signaling pathway.
Neoplasms
Oncogene UBE2I enhances cellular invasion, migration and proliferation abilities via autophagy-related pathway resulting in poor prognosis in hepatocellular carcinoma.
Neoplasms
RNF186 regulates EFNB1 (ephrin B1)-EPHB2-induced autophagy in the colonic epithelial cells for the maintenance of intestinal homeostasis.
Neoplasms
Sumoylation of transcription factor ETV1 modulates its oncogenic potential in prostate cancer.
Neoplasms
The Positive Correlations between the Expression of Histopathological Ubiquitin-Conjugating Enzyme 2O Staining and Prostate Cancer Advancement.
Neoplasms
UBE2C Drives Human Cervical Cancer Progression and Is Positively Modulated by mTOR.
Neoplasms
UBE2C is involved in the functions of ECRG4 on esophageal squamous cell carcinoma.
Neoplasms
UBE2C mRNA expression controlled by miR-300 and HuR determines its oncogenic role in gastric cancer.
Neoplasms
Ube2S regulates Wnt/?-catenin signaling and promotes the progression of non-small cell lung cancer.
Neoplasms
Ubiquitin Conjugating Enzyme E2 H (UBE2H) Is Linked to Poor Outcomes and Metastasis in Lung Adenocarcinoma.
Neoplasms
Ubiquitin conjugating enzyme E2 L3 promoted tumor growth of NSCLC through accelerating p27kip1 ubiquitination and degradation.
Neoplasms
Uev1A-Ubc13 promotes colorectal cancer metastasis through regulating CXCL1 expression via NF-?B activation.
Non-alcoholic Fatty Liver Disease
The ménage à trois of autophagy, lipid droplets and liver disease.
Osteoarthritis
Ubiquitin conjugating enzyme E2 M promotes apoptosis in osteoarthritis chondrocytes via Wnt/?-catenin signaling.
Prostatic Neoplasms
miR-499a inhibits the proliferation and apoptosis of prostate cancer via targeting UBE2V2.
Prostatic Neoplasms
Sumoylation of transcription factor ETV1 modulates its oncogenic potential in prostate cancer.
Retinoblastoma
An ARID family protein binds to the African swine fever virus encoded ubiquitin conjugating enzyme, UBCv1.
Retinoblastoma
Identification of novel lipid droplet factors that regulate lipophagy and cholesterol efflux in macrophage foam cells.
Sarcoma
Identification of novel lipid droplet factors that regulate lipophagy and cholesterol efflux in macrophage foam cells.
Sarcoma
Using mRNA deep sequencing to analyze differentially expressed genes during Panax notoginseng saponin treatment of ischemic stroke.
Sepsis
Muscle wasting in a rat model of long-lasting sepsis results from the activation of lysosomal, Ca2+ -activated, and ubiquitin-proteasome proteolytic pathways.
Stomach Neoplasms
UBE2C mRNA expression controlled by miR-300 and HuR determines its oncogenic role in gastric cancer.
Triple Negative Breast Neoplasms
Targeting ubiquitin conjugating enzyme UbcH5b by a triterpenoid PC3-15 from Schisandra plants sensitizes triple-negative breast cancer cells to lapatinib.
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
the expression levels of UBE2W in mouse testes are gradually elevated from 2 to 10 weeks, but they are significantly deceased in the testes with hypospermatogenesis
brenda
the expression levels of UBE2W in mouse testes gradually increase from 2 to 10 weeks age
brenda
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the expression levels of UBE2W in mouse testes are gradually elevated from 2 to 10 weeks, but they are significantly deceased in the testes with hypospermatogenesis
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brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Highest Expressing Human Cell Lines
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
humans have about 40 E2s that are involved in the transfer of Ub or Ub-like (Ubl) proteins (e.g. SUMO and NEDD8). Common functional and structural features that define unifying themes among E2s, overview. Highly specific chain builders such as Ube2N, Ube2S, and Ube2R1 can only transfer their conjugated Ub to another Ub molecule. This leads to a division of labor among E2s in which one E2 initiates or primes chain synthesis and a second E2 builds and extends the polyUb chain. Ube2W is fundamentally different in its reactivity (and therefore, its substrates) from all other characterized E2s. Along with its unique reactivity profile, Ube2W has an unusual UBC domain
malfunction
metabolism
physiological function
additional information
malfunction
the expression levels of UBE2W in mouse testes are significantly deceased in the testes with hypospermatogenesis. When UBE2W expression is successfully downregulated in spermatogenic cells, the rate of apoptosis is significantly increased and the P53/Bcl-2/caspase 6/caspase 9 signal pathways are activated. UBE2W downregulation promotes cell apoptosis and correlates with hypospermatogenesis
malfunction
knockdown of two E2s, Ube2o or Ube2t (EC 2.3.2.23), appears to be capable of suppressing LT-stimulated caspase-1 activation. siRNA knockdown of Ube2o expression in the engineered RAW-RA cells efficiently blocks RFP-ASC specks formation as well as release of cellular EGFP in response to LT stimulation
malfunction
the absence of Ube2W in HdhQ200 KI mice significantly increases levels of soluble monomeric mHTT while reducing insoluble oligomeric species. Ube2W null mice show an incompletely penetrant multi-organ defect and post-natal lethality. Mutational analysis reveals that neither wild-type Ube2W nor enzyme mutants alter cell viability. Ube2W deficiency results in decreased mHTT inclusion formation and reduced neurotoxicity, overview. Ube2W deficiency does not alter transcript levels of Htt or striatal markers in HdhQ200 mice
malfunction
-
the absence of Ube2W in HdhQ200 KI mice significantly increases levels of soluble monomeric mHTT while reducing insoluble oligomeric species. Ube2W null mice show an incompletely penetrant multi-organ defect and post-natal lethality. Mutational analysis reveals that neither wild-type Ube2W nor enzyme mutants alter cell viability. Ube2W deficiency results in decreased mHTT inclusion formation and reduced neurotoxicity, overview. Ube2W deficiency does not alter transcript levels of Htt or striatal markers in HdhQ200 mice
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malfunction
-
the expression levels of UBE2W in mouse testes are significantly deceased in the testes with hypospermatogenesis. When UBE2W expression is successfully downregulated in spermatogenic cells, the rate of apoptosis is significantly increased and the P53/Bcl-2/caspase 6/caspase 9 signal pathways are activated. UBE2W downregulation promotes cell apoptosis and correlates with hypospermatogenesis
-
metabolism
UBE2W expression correlates with testis development and hypospermatogenesis. UBE2W expression affects cell apoptosis by P53/Bcl-2/caspase 6/caspase 9 signal pathways, quantitative RT-PCR expression analysis, overview
metabolism
the N-end rule E3 ligase UBR2 is required for LT-induced NLRP1B inflammasome activation. LT is known to cleave NLRP1B after Lys44. The cleaved NLRP1B, bearing an N-terminal leucine, is targeted by UBR2-mediated ubiquitination and degradation. UBR2 partners with the E2 ubiquitin-conjugating enzyme UBE2O in this process. NLRP1B undergoes constitutive autocleavage before the C-terminal CARD domain. UBR2-mediated degradation of LT-cleaved NLRP1B thus triggers release of the noncovalent-bound CARD domain for subsequent caspase-1 activation. Metabolic pathway, overview
metabolism
the proteasome can target soluble oligomers assembled from ubiquitin-modified proteins independently of its peptidase activity, consistent with our recently reported fibril-fragmenting activity. Proteasomes are able to target oligomers assembled from N-terminally ubiquitinated proteins. The results suggest a possible disassembly mechanism by which N-terminal ubiquitination and the proteasome may together impede aggregate formation
metabolism
ubiquitin (Ub) conjugation requires the sequential action of enzymes to target ubiquitin to substrates: Ub activating enzyme (E1), Ub conjugating enzyme (E2) and Ub ligase (E3). Given the diversity in Ub-chain lengths, linkages and substrate attachment sites, dramatically different kinds of ubiquitination can occur. Ube2W can function with various ubiquitin ligases including the C-terminus of Hsc-70-interacting protein (CHIP) and the BRCA1/BARD1 complex to mono-ubiquitinate select substrates at their N-termini
metabolism
ubiquitin-conjugating enzymes (E2s) are the central players in the trio of enzymes responsible for the attachment of ubiquitin (Ub) to cellular proteins. E2 regulation mechanisms, overview
metabolism
-
ubiquitin (Ub) conjugation requires the sequential action of enzymes to target ubiquitin to substrates: Ub activating enzyme (E1), Ub conjugating enzyme (E2) and Ub ligase (E3). Given the diversity in Ub-chain lengths, linkages and substrate attachment sites, dramatically different kinds of ubiquitination can occur. Ube2W can function with various ubiquitin ligases including the C-terminus of Hsc-70-interacting protein (CHIP) and the BRCA1/BARD1 complex to mono-ubiquitinate select substrates at their N-termini
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metabolism
-
UBE2W expression correlates with testis development and hypospermatogenesis. UBE2W expression affects cell apoptosis by P53/Bcl-2/caspase 6/caspase 9 signal pathways, quantitative RT-PCR expression analysis, overview
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physiological function
Ube2W is an E2 ubiquitin-conjugating enzyme with specific protein N-terminal monoubiquitylation activity. Ube2W conjugates ubiquitin to its own N-terminus, but also to that of the small ubiquitin-like modifier SUMO in a manner dependent on the SUMO-targeted ubiquitin ligase RNF4, i.e.RING finger protein 4
physiological function
ubiquitin conjugating enzyme (E2) is crucial for mediating N-terminal ubiquitination. Enzyme UBE2W is involved in male infertility, correlation between UBE2W expression and hypospermatogenesis, overview. UBE2W promotes ubiquitin chain formation in response to DNA damage by interacting with Rnf4
physiological function
UBE2O can mediate the ubiquitination of many different substrates. It is involved in cancer. UBE2O may also regulate other biological processes through UBR2-dependent or UBR2-independent N-end rule pathways. The E2 ubiquitin-conjugating enzyme UBE2O partners with UBR2, an E3 ubiquitin ligase of the N-end rule degradation pathway. UBR2 functions together with UBE2O mediating NLRP1B inflammasome activation. UBE2O is the bona fide E2 enzyme controlling LT-induced NLRP1B inflammasome activation. UBR2-UBE2O ubiquitination pathway mediates degradation of LT-cleaved NLRP1B, which releases its C-terminal CARD domain for subsequent caspase-1 activation
physiological function
UBE2W can modify the N-terminus of proteins with ubiquitin. An engineered N-terminal ubiquitin modification changes the aggregation process of both proteins, resulting in the formation of structurally distinct aggregates. The mammalian proteasome holoenzyme can target oligomers assembled from ubiquitinated tau aggregation domain (tauK18) and alpha-synuclein (alphaS), both tauK18 and alphaS may become ubiquitinated on the N-terminus by UBE2W enabling the proteasomes to target and remove oligomers assembled from these modified proteins. The reaction does not continue beyond monoubiquitination as UBE2W specifically recognizes disordered sequences at the N-terminus of the substrate
physiological function
the ubiquitin conjugating enzyme Ube2W regulates solubility of the Huntington's disease protein, huntingtin (HTT). Potential function of the non-canonical ubiquitin-conjugating enzyme, Ube2W, in the polyQ neurodegenerative disease, Huntington's Disease (HD). Ube2W increases HTT inclusion formation in cultured cells. The effect of Ube2W on HTT most likely occurs post-translationally. But as an E2 that ubiquitinates N-termini, Ube2W can act cotranslationally by interacting with the nascent N-terminal polypeptide as it exits the ribosome and thus alter the rate of HTT protein synthesis itself
physiological function
humans have about 40 E2s that are involved in the transfer of Ub or Ub-like (Ubl) proteins (e.g. SUMO and NEDD8). Although the majority of E2s are only twice the size of Ub, this remarkable family of enzymes performs a variety of functional roles. Ube2W exhibits no intrinsic activity towards free lysine. Instead, Ube2W attaches Ub to the N-terminal alpha-amino group of proteins to form a Ub-fusion protein product. While still an aminolysis reaction and therefore not fundamentally differ not from the reaction with lysine, intrinsic reactivity assays revealed that Ube2W can transfer Ub to the alpha-amino group of small lysine-less peptides but not to free lysine. This feature distinguishes Ube2W as fundamentally different in its reactivity (and therefore, its substrates) from all other characterized E2s. Along with its unique reactivity profile, Ube2W has an unusual UBC domain. Ube2W recognizes and modifies disordered N-termini independently of substrate sequence through interactions between its own disordered C-terminal region and the substrate backbone. The requirement of a disordered N-terminus on its substrate explains the strict monoubiquitylating activity of Ube2W, as the N-terminus of Ub is highly structured and is therefore not a good substrate for Ube2W. The preference for N-terminal modification by Ube2W may not be absolute, as the retroviral restriction RING E3 TRIM5alpha is monoubiquitylated by Ube2W despite being acetylated on its N-terminus. Ube2W may also facilitate isopeptide bond formation, possibly if an N-terminus is blocked. Nevertheless, the preference of Ube2W for disordered N-termini gives it a (so far) unique target selection mechanism for a primary modification event that can subsequently be exploited by other E2 enzymes to form Ub chains. Ube2W may work as a chain-initiating E2 in the innate immune response where K63-linked chains play a critical role
physiological function
UBE2W downregulation promotes cell apoptosis and correlates with hypospermatogenesis
physiological function
-
the ubiquitin conjugating enzyme Ube2W regulates solubility of the Huntington's disease protein, huntingtin (HTT). Potential function of the non-canonical ubiquitin-conjugating enzyme, Ube2W, in the polyQ neurodegenerative disease, Huntington's Disease (HD). Ube2W increases HTT inclusion formation in cultured cells. The effect of Ube2W on HTT most likely occurs post-translationally. But as an E2 that ubiquitinates N-termini, Ube2W can act cotranslationally by interacting with the nascent N-terminal polypeptide as it exits the ribosome and thus alter the rate of HTT protein synthesis itself
-
physiological function
-
ubiquitin conjugating enzyme (E2) is crucial for mediating N-terminal ubiquitination. Enzyme UBE2W is involved in male infertility, correlation between UBE2W expression and hypospermatogenesis, overview. UBE2W promotes ubiquitin chain formation in response to DNA damage by interacting with Rnf4
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physiological function
-
UBE2W downregulation promotes cell apoptosis and correlates with hypospermatogenesis
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additional information
amino acid W144 near the C-terminus of Ube2W is critically important for substrate binding
additional information
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amino acid W144 near the C-terminus of Ube2W is critically important for substrate binding
additional information
E2 structure-function analysis, overview. Ube2W recognizes and modifies disordered N-termini independently of substrate sequence through interactions between its own disordered C-terminal region and the substrate backbone. The requirement of a disordered N-terminus on its substrate explains the strict monoubiquitylating activity of Ube2W, as the N-terminus of Ub is highly structured and is therefore not a good substrate for Ube2W
additional information
UbcH5 selects substrate lysine residues independent of the E3 ubiquitin ligase C-terminus of Hsc70 interacting protein CHIP. CHIP participates in lysine selection by fine-tuning the subset of substrate lysines that are ubiquitinated. Residue lysine 128 near the C-terminus of UbcH5 is critical for the efficient ubiquitin transfer by UbcH5 in both the presence and absence of CHIP
additional information
-
amino acid W144 near the C-terminus of Ube2W is critically important for substrate binding
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Show AA Sequence and Transmembrane Helices (1654 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C91A
site-directed mutagenesis of an active site residue, the mutation eliminates the ability of Ube2W to transfer ubiquitin (Ub) to substrates while still allowing Ube2W to bind substrates, it disrupts Ube2W-mediated ubiquitination
W144E
site-directed mutagenesis, the mutation eliminates substrate binding and disrupts Ube2W-mediated ubiquitination
C91A
-
site-directed mutagenesis of an active site residue, the mutation eliminates the ability of Ube2W to transfer ubiquitin (Ub) to substrates while still allowing Ube2W to bind substrates, it disrupts Ube2W-mediated ubiquitination
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W144E
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site-directed mutagenesis, the mutation eliminates substrate binding and disrupts Ube2W-mediated ubiquitination
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additional information
additional information
to obtain homogenous and pure ubiquitin (Ub)-modified alphasynuclein (alphaS) and tauK18, engineered constructs that expressed fusion proteins with a single Ub moiety immediately before the first residue of alphaS or tauK18 (Ub-alphaS and Ub-tauK18) are genetically engineered. These engineered N-terminal Ub-fusion proteins are protected from deubiquitination by a Gly76Ser substitution of the C-terminal residue of Ub. No filamentous aggregates from Ub-alphaS are detected under TEM, thus, the morphology of filamentous aggregates is affected by N-terminal Ub modification. Meanwhile, oligomers from both tauK18 and Ub-tauK18 are reproducibly detected early in the aggregation process. An apparent reduction of the fraction of soluble oligomers with time is detected in both unmodified and Ub-modified tauK18 beyond 50 and 70 h, respectively. Comparisons of modified and unmodified proteins' aggregation behaviour, overview. Proteasomes are able to target Ub-modified aggregates
additional information
specific downregulation of enzyme UBE2W in spermatogenic cells by murine UBE2W-specific shRNA. UBE2W downregulation promotes cell apoptosis and correlates with hypospermatogenesis. UBE2W upregulation is performed by a recombinant lentivirus containing murine UBE2W
additional information
-
specific downregulation of enzyme UBE2W in spermatogenic cells by murine UBE2W-specific shRNA. UBE2W downregulation promotes cell apoptosis and correlates with hypospermatogenesis. UBE2W upregulation is performed by a recombinant lentivirus containing murine UBE2W
additional information
generation of E2-knockdown macrophages, siRNA knockdown of Ube2o expression in engineered RAW-RA cells, Ube2o knockdown efficiency is measured by quantitative PCR
additional information
absence of Ube2W increases soluble, monomeric mutant huntingtin (HTT) in a knock-in mouse model of Huntington's disease. The absence of Ube2W in HdhQ200 KI mice significantly increases levels of soluble monomeric mHTT while reducing insoluble oligomeric species
additional information
-
absence of Ube2W increases soluble, monomeric mutant huntingtin (HTT) in a knock-in mouse model of Huntington's disease. The absence of Ube2W in HdhQ200 KI mice significantly increases levels of soluble monomeric mHTT while reducing insoluble oligomeric species
additional information
-
specific downregulation of enzyme UBE2W in spermatogenic cells by murine UBE2W-specific shRNA. UBE2W downregulation promotes cell apoptosis and correlates with hypospermatogenesis. UBE2W upregulation is performed by a recombinant lentivirus containing murine UBE2W
-
additional information
-
absence of Ube2W increases soluble, monomeric mutant huntingtin (HTT) in a knock-in mouse model of Huntington's disease. The absence of Ube2W in HdhQ200 KI mice significantly increases levels of soluble monomeric mHTT while reducing insoluble oligomeric species
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant biotin-tagged enzyme from HEK-293T cells by NeutrAvidin affinity chromatography, release from the coloumn by TEV protease cleavage
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene UBE2O, recombinant coexpression of Myc-tagged UBE2O and Flag-tagged UBR2 in HEK-293T cells
gene UBE2W, recombinant expression in HEK-293 cells. When wild-type Ube2W is coexpressed with Httex1Q103, inclusion number and size significantly increases, whereas coexpression of either Ube2W mutant markedly decreases Httex1Q103 inclusion number and average size
gene Ube2w, recombinant expression of a recombinant lentivirus containing murine UBE2W
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
expression levels are significantly deceased in the testes with hypospermatogenesis
expression levels are significantly deceased in the testes with hypospermatogenesis
expression levels are significantly deceased in the testes with hypospermatogenesis
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
mapping of N-terminal ubiquitination sites on endogenous substrates of UBE2W by antibodies that selectively recognize to sites of N-terminal ubiquitination (tryptic peptides with an N-terminal diglycine remnant) but not isopeptide-linked diglycine (ubiquitin) modifications on lysine
diagnostics
medicine
diagnostics
UBE2W downregulation promotes cell apoptosis and correlates with hypospermatogenesis, which may be helpful for the diagnosis of male infertility
diagnostics
-
UBE2W downregulation promotes cell apoptosis and correlates with hypospermatogenesis, which may be helpful for the diagnosis of male infertility
-
medicine
in mice with hypospermatogenesis, expression levels are significantly deceased in the testes. Concommitantly, the rate of apoptosis is significantly increased and the P53/Bcl?2/caspase 6/caspase 9 signal pathways are activated
medicine
-
in mice with hypospermatogenesis, expression levels are significantly deceased in the testes. Concommitantly, the rate of apoptosis is significantly increased and the P53/Bcl?2/caspase 6/caspase 9 signal pathways are activated
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Tatham, M.H.; Geoffroy, M.C.; Shen, L.; Plechanovova, A.; Hattersley, N.; Jaffray, E.G.; Palvimo, J.J.; Hay, R.T.
RNF4 is a poly-SUMO-specific E3 ubiquitin ligase required for arsenic-induced PML degradation
Nat. Cell Biol.
10
538-546
2008
Homo sapiens (Q96B02)
brenda
Scaglione, K.M.; Basrur, V.; Ashraf, N.S.; Konen, J.R.; Elenitoba-Johnson, K.S.; Todi, S.V.; Paulson, H.L.
The ubiquitin-conjugating enzyme (E2) Ube2w ubiquitinates the N terminus of substrates
J. Biol. Chem.
288
18784-18788
2013
Homo sapiens
brenda
Tatham, M.H.; Plechanovova, A.; Jaffray, E.G.; Salmen, H.; Hay, R.T.
Ube2W conjugates ubiquitin to alpha-amino groups of protein N-termini
Biochem. J.
453
137-145
2013
Homo sapiens (Q96B02)
brenda
Schumacher, F.R.; Wilson, G.; Day, C.L.
The N-terminal extension of UBE2E ubiquitin-conjugating enzymes limits chain assembly
J. Mol. Biol.
425
4099-4111
2013
Homo sapiens (P51965)
brenda
Lei, B.; Xie, L.; Zhang, S.; Lv, D.; Shu, F.; Deng, Y.
UBE2W down-regulation promotes cell apoptosis and correlates with hypospermatogenesis
Andrologia
52
e13474
2020
Mus musculus (Q8VDW4), Mus musculus, Mus musculus C57 (Q8VDW4)
brenda
Stewart, M.D.; Ritterhoff, T.; Klevit, R.E.; Brzovic, P.S.
E2 enzymes more than just middle men
Cell Res.
26
423-440
2016
Homo sapiens (Q96B02)
brenda
Xu, H.; Shi, J.; Gao, H.; Liu, Y.; Yang, Z.; Shao, F.; Dong, N.
The N-end rule ubiquitin ligase UBR2 mediates NLRP1B inflammasome activation by anthrax lethal toxin
EMBO J.
38
e101996
2019
Mus musculus (Q6ZPJ3)
brenda
Ye, Y.; Klenerman, D.; Finley, D.
N-terminal ubiquitination of amyloidogenic proteins triggers removal of their oligomers by the proteasome holoenzyme
J. Mol. Biol.
432
585-596
2020
Homo sapiens (Q96B02)
brenda
Wang, B.; Zeng, L.; Merillat, S.A.; Fischer, S.; Ochaba, J.; Thompson, L.M.; Barmada, S.J.; Scaglione, K.M.; Paulson, H.L.
The ubiquitin conjugating enzyme Ube2W regulates solubility of the Huntingtons disease protein, huntingtin
Neurobiol. Dis.
109
127-136
2018
Mus musculus (Q8VDW4), Mus musculus, Mus musculus C57BL/6 (Q8VDW4)
brenda
Kanack, A.; Vittal, V.; Haver, H.; Keppel, T.; Gundry, R.L.; Klevit, R.E.; Scaglione, K.M.
UbcH5 interacts with substrates to participate in lysine selection with the E3 ubiquitin ligase CHIP
Biochemistry
59
2078-2088
2020
Homo sapiens (Q96B02)
brenda
Davies, C.W.; Vidal, S.E.; Phu, L.; Sudhamsu, J.; Hinkle, T.B.; Chan Rosenberg, S.; Schumacher, F.R.; Zeng, Y.J.; Schwerdtfeger, C.; Peterson, A.S.; Lill, J.R.; Rose, C.M.; Shaw, A.S.; Wertz, I.E.; Kirkpatrick, D.S.; Koerber, J.T.
Antibody toolkit reveals N-terminally ubiquitinated substrates of UBE2W
Nat. Commun.
12
4608
2021
Homo sapiens (Q96B02)
brenda
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