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Mouse Anti-HUWE1 Recombinant Antibody (AX8D1) (CBMAB-C3560-CN)

This product is a Mouse antibody that recognizes HUWE1. The antibody AX8D1 can be used for immunoassay techniques such as: WB.
See all HUWE1 antibodies

Summary

Host Animal
Mouse
Specificity
Human, Mouse, Rat, Monkey
Clone
AX8D1
Antibody Isotype
IgG1
Application
WB

Basic Information

Specificity
Human, Mouse, Rat, Monkey
Antibody Isotype
IgG1
Clonality
Monoclonal
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.

Target

Full Name
HECT, UBA And WWE Domain Containing 1, E3 Ubiquitin Protein Ligase
Introduction
This gene encodes a protein containing a C-terminal HECT (E6AP type E3 ubiquitin protein ligase) domain that functions as an E3 ubiquitin ligase. The encoded protein is required for the ubiquitination and subsequent degradation of the anti-apoptotic protein Mcl1 (myeloid cell leukemia sequence 1 (BCL2-related)). This protein also ubiquitinates the p53 tumor suppressor, core histones, and DNA polymerase beta. Mutations in this gene are associated with Turner type X-linked syndromic cognitive disability. [provided by RefSeq, Aug 2013]
Entrez Gene ID
Human10075
Mouse59026
Rat501546
Monkey700136
UniProt ID
HumanQ7Z6Z7
MouseQ7TMY8
RatP51593
MonkeyH9ELS9
Alternative Names
HECT, UBA And WWE Domain Containing 1, E3 Ubiquitin Protein Ligase; Homologous To E6AP Carboxyl Terminus Homologous Protein 9; Upstream Regulatory Element-Binding Protein 1; HECT-Type E3 Ubiquitin Transferase HUWE1; Mcl-1 Ubiquitin Ligase E3; Large Structure Of UREB1; ARF-Binding Protein 1; URE-Binding Protein 1; ARF-BP1; HECTH9; URE-B1; LASU1; UREB1; MULE;
Function
E3 ubiquitin-protein ligase which mediates ubiquitination and subsequent proteasomal degradation of target proteins (PubMed:15989957, PubMed:19713937, PubMed:15567145, PubMed:15767685, PubMed:18488021, PubMed:17567951, PubMed:19037095, PubMed:20534529, PubMed:30217973).

Regulates apoptosis by catalyzing the polyubiquitination and degradation of MCL1 (PubMed:15989957).

Mediates monoubiquitination of DNA polymerase beta (POLB) at 'Lys-41', 'Lys-61' and 'Lys-81', thereby playing a role in base-excision repair (PubMed:19713937).

Also ubiquitinates the p53/TP53 tumor suppressor and core histones including H1, H2A, H2B, H3 and H4 (PubMed:15567145, PubMed:15767685, PubMed:15989956).

Ubiquitinates MFN2 to negatively regulate mitochondrial fusion in response to decreased stearoylation of TFRC (PubMed:26214738).

Ubiquitination of MFN2 also takes place following induction of mitophagy; AMBRA1 acts as a cofactor for HUWE1-mediated ubiquitination (PubMed:30217973).

Regulates neural differentiation and proliferation by catalyzing the polyubiquitination and degradation of MYCN (PubMed:18488021).

May regulate abundance of CDC6 after DNA damage by polyubiquitinating and targeting CDC6 to degradation (PubMed:17567951).

Mediates polyubiquitination of isoform 2 of PA2G4 (PubMed:19037095).

Acts in concert with MYCBP2 to regulate the circadian clock gene expression by promoting the lithium-induced ubiquination and degradation of NR1D1 (PubMed:20534529).

Binds to an upstream initiator-like sequence in the preprodynorphin gene (By similarity).
Biological Process
Base-excision repair Source: UniProtKB
Cell differentiation Source: UniProtKB-KW
Circadian regulation of gene expression Source: UniProtKB
Golgi organization Source: GO_Central
Histone ubiquitination Source: UniProtKB
Membrane fusion Source: GO_Central
Negative regulation of mitochondrial fusion Source: UniProtKB
Positive regulation of mitophagy in response to mitochondrial depolarization Source: CACAO
Positive regulation of protein catabolic process Source: GO_Central
Positive regulation of protein targeting to mitochondrion Source: ParkinsonsUK-UCL
Positive regulation of protein ubiquitination Source: UniProtKB
Proteasome-mediated ubiquitin-dependent protein catabolic process Source: GO_Central
Protein monoubiquitination Source: UniProtKB
Protein polyubiquitination Source: UniProtKB
Protein ubiquitination Source: GO_Central
Cellular Location
Cytoplasm; Mitochondrion; Nucleus. Mainly expressed in the cytoplasm of most tissues, except in the nucleus of spermatogonia, primary spermatocytes and neuronal cells (By similarity). Recruited to mitochondria following interaction with AMBRA1 (PubMed:30217973).
Involvement in disease
Intellectual developmental disorder, X-linked, syndromic, Turner type (MRXST):
An X-linked neurodevelopmental disorder with highly variable clinical manifestations. Common features consist of moderate to profound intellectual disability, delayed or absent speech, short stature with small hands and feet, and non-specific but recurrent dysmorphic facial features such as macrocephaly, microcephaly, a broad nasal tip, deep set eyes, epicanthic folds, short palpebral fissures and a short philtrum. Patients may manifest other features, such as hypotonia, seizures and delayed bone age.
PTM
Phosphorylated on tyrosine; phosphorylation is probably required for its ability to inhibit TP53 transactivation.

Yin, J., Xu, J., Chen, C., Ma, X., Zhu, H., Xie, L., ... & Zheng, L. (2023). HECT, UBA and WWE domain containing 1 represses cholesterol efflux during CD4+ T cell activation in Sjögren’s syndrome. Frontiers in Pharmacology, 14.

Yuan, Y., Wang, L. H., Zhao, X. X., Wang, J., Zhang, M. S., Ma, Q. H., ... & Bian, X. W. (2022). The E3 ubiquitin ligase HUWE1 acts through the N‐Myc‐DLL1‐NOTCH1 signaling axis to suppress glioblastoma progression. Cancer Communications, 42(9), 868-886.

Lee, J., Kim, J., Shin, J., Kang, Y., Choi, J., & Cheong, H. (2021). ATG101 degradation by HUWE1-mediated ubiquitination impairs autophagy and reduces survival in cancer cells. International Journal of Molecular Sciences, 22(17), 9182.

Gong, X., Du, D., Deng, Y., Zhou, Y., Sun, L., & Yuan, S. (2020). The structure and regulation of the E3 ubiquitin ligase HUWE1 and its biological functions in cancer. Investigational New Drugs, 38, 515-524.

Guo, Z., Wang, S., Xie, Y., Han, Y., Hu, S., Guan, H., ... & Ma, T. (2020). HUWE1-dependent DNA-PKcs neddylation modulates its autophosphorylation in DNA damage response. Cell Death & Disease, 11(5), 400.

He, G. Q., Chen, Y., Liao, H. J., Xu, W. M., Zhang, W., & He, G. L. (2020). Associations between Huwe1 and autophagy in rat cerebral neuron oxygen‑glucose deprivation and reperfusion injury. Molecular Medicine Reports, 22(6), 5083-5094.

Zhang, Z. Y., Guo, Z., Li, H. L., He, Y. T., Duan, X. L., Suo, Z. W., ... & Hu, X. D. (2019). Ubiquitination and inhibition of glycine receptor by HUWE1 in spinal cord dorsal horn. Neuropharmacology, 148, 358-365.

Qu, H., Liu, H., Jin, Y., Cui, Z., & Han, G. (2018). HUWE1 upregulation has tumor suppressive effect in human prostate cancer cell lines through c-Myc. Biomedicine & Pharmacotherapy, 106, 309-315.

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For research use only. Not intended for any clinical use.

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