ARL2BP
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Official Full Name
ADP-ribosylation factor-like 2 binding protein
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Overview
ADP-ribosylation factor (ARF)-like proteins (ARLs) comprise a functionally distinct group of the ARF family of RAS-related GTPases. The protein encoded by this gene binds to ARL2.GTP with high affinity but does not interact with ARL2.GDP, activated ARF, or RHO proteins. The lack of detectable membrane association of this protein or ARL2 upon activation of ARL2 is suggestive of actions distinct from those of the ARFs. This protein is considered to be the first ARL2-specific effector identified, due to its interaction with ARL2.GTP but lack of ARL2 GTPase-activating protein activity. -
Synonyms
ARL2BP; ADP-ribosylation factor-like 2 binding protein; ADP-ribosylation factor-like protein 2-binding protein; BART; BART1; binder of Arl2; ADP ribosylation factor like 2 binding protein; Arf like 2 binding protein BART1; ARL2BP protein; Binder of Arl Two; binder of ARF2 protein 1; ARF-like 2-binding protein; Arf-like 2 binding protein BART1;
- Recombinant Proteins
- Cell & Tissue Lysates
- Protein Pre-coupled Magnetic Beads
- Chicken
- Cynomolgus Monkey
- Human
- Mouse
- Rat
- Rhesus Macaque
- Zebrafish
- E.coli
- HEK293
- In Vitro Cell Free System
- Mammalian Cell
- Wheat Germ
- Fc|His
- GST
- His
- His (Fc)
- Avi
- N/A
- Involved Pathway
- Protein Function
- Interacting Protein
- ARL2BP Related Articles
ARL2BP involved in several pathways and played different roles in them. We selected most pathways ARL2BP participated on our site, such as Integration of energy metabolism, Metabolism, Regulation of insulin secretion, which may be useful for your reference. Also, other proteins which involved in the same pathway with ARL2BP were listed below. Creative BioMart supplied nearly all the proteins listed, you can search them on our site.
| Pathway Name | Pathway Related Protein |
|---|---|
| Integration of energy metabolism | KCNS3A;KCNS3;MARCKSA;ARL2BP;GNB5A;RAPGEF4;KCNJ11;GNG13B;MARCKSB |
| Metabolism | COQ7;ALOX5B.2;ATP5S;SULT1B1;LYVE1;DHCR24;TYMP;TPH2;SLC25A32 |
| Regulation of insulin secretion | KCNC2;ARL2;KCNS3A;SYT5;MARCKSB;MARCKSA;KCNB1;KCNS3;ARL2BP |
ARL2BP has several biochemical functions, for example, GTPase regulator activity, protein binding, transcription coactivator activity. Some of the functions are cooperated with other proteins, some of the functions could acted by ARL2BP itself. We selected most functions ARL2BP had, and list some proteins which have the same functions with ARL2BP. You can find most of the proteins on our site.
| Function | Related Protein |
|---|---|
| GTPase regulator activity | KRIT1;RGS12;WASL;ARL2BP;TSC1A;RIMS1;RGS12B;TSC1B;RALGDS |
| protein binding | CCNA1;TBX5;AGO3;SETDB2;SRPK1;FYB;PRPF6;TPSB2;IL36RN |
| transcription coactivator activity | TAF9;AIP;RNF20;SUB1;ECD;TFDP1B;RARA;CDK7;TAF12 |
ARL2BP 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 ARL2BP here. Most of them are supplied by our site. Hope this information will be useful for your research of ARL2BP.
ARL2; RAC1; MPP3; CAMK2D
- Q&As
- Reviews
Q&As (7)
Ask a questionYes, genetic variations in the ARL2BP gene have been reported. For example, single nucleotide polymorphisms (SNPs) in the ARL2BP gene have been identified in some population studies. However, the functional consequences of these variants remain to be fully understood.
While the exact role of ARL2BP in human diseases is not well-established, there is emerging evidence suggesting its involvement in certain pathologies. For example, ARL2BP dysregulation has been observed in some cancer types, indicating its potential significance in tumorigenesis.
Yes, ARL2BP has been found to interact with additional proteins. For example, it can bind to BART (beta-amyloid precursor protein (APP)-binding protein), which is involved in the regulation of APP processing and Alzheimer's disease.
Currently, there is limited research on targeting ARL2BP for therapeutic purposes. However, further exploration into its functional roles and potential disease associations may reveal its suitability as a therapeutic target in the future.
Yes, ARL2BP can undergo post-translational modifications, including phosphorylation and ubiquitination. These modifications may regulate its stability, subcellular localization, or interaction with other proteins.
ARL2BP deficiency has been associated with certain cellular dysfunctions. Studies have suggested that decreased levels of ARL2BP can lead to impaired mitochondrial fusion and fission dynamics, as well as disruptions in Golgi morphology and protein trafficking.
ARL2BP is mainly localized to the cytoplasm but can also be found associated with specific cellular membranes, including the Golgi apparatus and the endoplasmic reticulum (ER).
Customer Reviews (8)
Write a reviewResearchers can confidently rely on its capabilities to generate precise and significant results, enhancing the understanding of protein function and dynamics.
It has demonstrated exceptional effectiveness in WB experiments, showcasing its reliability and precision in detecting and quantifying specific targets.
With ARL2BP protein, researchers can visualize protein complexes and their interactions with remarkable clarity, unraveling important insights into their functional mechanisms.
Its exceptional purity and stability make it an ideal choice for a wide range of applications, ensuring reliable and reproducible results.
Its unique characteristics contribute to obtaining clear and detailed structural information, allowing researchers to gain insights into protein interactions and conformational changes.
ARL2BP protein has proven to be instrumental in protein electron microscopy structure analysis.
This protein demonstrates exceptional performance in ELISA, delivering accurate and reliable results in the detection and quantification of specific antigens.
ARL2BP protein is highly recommended for scientific research applications, especially in ELISA assays and protein electron microscopy structure analysis.
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