APOBEC3C
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Official Full Name
apolipoprotein B mRNA editing enzyme, catalytic polypeptide-like 3C
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Overview
This gene is a member of the cytidine deaminase gene family. It is one of seven related genes or pseudogenes found in a cluster thought to result from gene duplication, on chromosome 22. Members of the cluster encode proteins that are structurally and functionally related to the C to U RNA-editing cytidine deaminase APOBEC1. It is thought that the proteins may be RNA editing enzymes and have roles in growth or cell cycle control. -
Synonyms
APOBEC3C; apolipoprotein B mRNA editing enzyme, catalytic polypeptide-like 3C; probable DNA dC-> dU-editing enzyme APOBEC-3C; APOBEC1L; ARDC2; ARDC4; ARP5; bK150C2.3; PBI; Phorbolin I protein; APOBEC1 like; Apolipoprotein B mRNA editing enzyme catalytic polypeptide like 3C; MGC19485; Probable DNA dC dU editing enzyme APOBEC 3C; phorbolin I; A3C;
- Recombinant Proteins
- Cell & Tissue Lysates
- Protein Pre-coupled Magnetic Beads
- Human
- Rhesus Macaque
- E.coli
- HEK293
- HEK293T
- In Vitro Cell Free System
- Mammalian Cell
- Mammalian cells
- Wheat Germ
- Flag
- GST
- His
- His (Fc)
- Avi
- Myc
- DDK
- N/A
- Involved Pathway
- Protein Function
- Interacting Protein
- APOBEC3C Related Articles
APOBEC3C involved in several pathways and played different roles in them. We selected most pathways APOBEC3C participated on our site, such as , which may be useful for your reference. Also, other proteins which involved in the same pathway with APOBEC3C were listed below. Creative BioMart supplied nearly all the proteins listed, you can search them on our site.
Pathway Name | Pathway Related Protein |
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APOBEC3C has several biochemical functions, for example, hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amidines, poly(A) RNA binding, protein binding. Some of the functions are cooperated with other proteins, some of the functions could acted by APOBEC3C itself. We selected most functions APOBEC3C had, and list some proteins which have the same functions with APOBEC3C. You can find most of the proteins on our site.
Function | Related Protein |
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hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amidines | APOBEC3C;APOBEC4;APOBEC2A;APOBEC3D;APOBEC2B |
poly(A) RNA binding | EIF4A1;KIAA1324;DCN;RBM47;RBMS2;RPL5A;DHX57;RPL10A;MYO5A |
protein binding | NCF1;KPNA2;ERN1;CSRNP1;ATP6V0D1;MED4;ZNF224;SART3;MAP1S |
zinc ion binding | ADH6;PHC2;ADH1C;TRIM28;CALB1;PHF8;BSPRY;ESRRB;RORA |
APOBEC3C has direct interactions with proteins and molecules. Those interactions were detected by several methods such as yeast two hybrid, co-IP, pull-down and so on. We selected proteins and molecules interacted with APOBEC3C here. Most of them are supplied by our site. Hope this information will be useful for your research of APOBEC3C.
RBMY1A1; RBMX; RBMY1F; SRPK2; CNBP; TRAF3; hscA; ssdna_dcdgm; FN1; RPL10; Eif3i
- Q&As
- Reviews
Q&As (16)
Ask a questionResearch on APOBEC3C involves techniques such as gene expression analysis, protein assays, next-generation sequencing, immunohistochemistry, and cell-based assays. These techniques help understand its expression, protein-protein interactions, and functional consequences.
There is limited evidence suggesting that APOBEC3C can induce DNA mutations in human cells. However, its mutational activity may be weaker compared to other APOBEC3 proteins.
APOBEC3C shares structural similarities with other APOBEC3 proteins but has distinct functional characteristics. It has been found to have weaker antiviral activity than some other members, such as APOBEC3A and APOBEC3G.
APOBEC3C has been shown to have activity against retroviruses like HIV-1 and other related viruses. However, its antiviral activity against other viruses is not well-characterized.
Currently, there is no direct evidence linking APOBEC3C to any specific human diseases. However, it is possible that dysregulation or mutations in APOBEC3C could play a role in virus-related diseases or cancer development.
The regulation of APOBEC3C expression is not well-studied. However, similar to other APOBEC3 family members, it is likely regulated at the transcriptional level by various factors and signaling pathways.
APOBEC3C has been reported to interact with certain proteins involved in antiviral defense and DNA repair pathways, such as APOBEC3G, A3G mRNA-binding protein, and RAD52. These interactions suggest possible functional crosstalk between different proteins in these pathways.
APOBEC3C, like other APOBEC3 proteins, acts as a host innate immune defense against viral infections. By deaminating viral DNA or RNA, it disrupts viral replication or leads to the degradation of viral genetic material.
There is limited information available regarding APOBEC3C's role in drug resistance. Further research is needed to understand its potential involvement in this process.
As of now, there are no specific inhibitors or activators known for APOBEC3C. Further research is needed to identify molecules that can modulate its activity.
Currently, there are no specific ongoing research studies or clinical trials focused solely on APOBEC3C. However, as more is understood about its functions and relevance in human diseases, it may become a subject of future investigations.
Although not extensively studied, APOBEC3C mutations or dysregulation could potentially contribute to cancer development or progression. Some studies have shown an association between elevated APOBEC3C expression and certain types of cancer.
Targeting APOBEC3C for therapeutic interventions is still an area of active research. Modulation of its activity or expression could potentially be explored as a strategy against specific viral infections or virus-associated diseases.
APOBEC3C is expressed at low levels in various normal tissues, such as testis, lung, and liver. However, its expression pattern and physiological functions in normal tissues are not well-characterized.
Currently, there is limited evidence suggesting APOBEC3C as a potential biomarker for certain cancers. However, further research is needed to validate its diagnostic or prognostic value.
Studies have identified genetic variations or single-nucleotide polymorphisms (SNPs) in the APOBEC3C gene. However, their functional implications and potential association with diseases are still not well-understood.
Customer Reviews (4)
Write a reviewI highly recommend the APOBEC3C protein for a wide range of research applications.
The APOBEC3C protein's robustness and stability have contributed significantly to the success of my experiments, enabling precise and reproducible measurements.
Its ability to preserve structural integrity and facilitate high-resolution imaging has greatly enhanced my understanding of protein complexes and their interactions.
Furthermore, the APOBEC3C protein has demonstrated great utility in protein electron microscopy structure analysis.
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