AGAP2
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Official Full Name
ArfGAP with GTPase domain, ankyrin repeat and PH domain 2
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Overview
The protein encoded by this gene belongs to the centaurin gamma-like family. It mediates anti-apoptotic effects of nerve growth factor by activating nuclear phosphoinositide 3-kinase. It is overexpressed in cancer cells, and promotes cancer cell invasion. Alternatively spliced transcript variants encoding different isoforms have been described for this gene. -
Synonyms
AGAP2; ArfGAP with GTPase domain, ankyrin repeat and PH domain 2; centaurin, gamma 1 , CENTG1; arf-GAP with GTPase, ANK repeat and PH domain-containing protein 2; cnt-g1; centaurin, gamma 1; phosphoinositide 3-kinase enhancer; phosphatidylinositol 3-kinas;
- Recombinant Proteins
- Protein Pre-coupled Magnetic Beads
- Human
- Mouse
- Rat
- Rhesus Macaque
- Zebrafish
- HEK293
- In Vitro Cell Free System
- Mammalian Cell
- Wheat Germ
- GST
- His
- His (Fc)
- Avi
- Involved Pathway
- Protein Function
- Interacting Protein
AGAP2 involved in several pathways and played different roles in them. We selected most pathways AGAP2 participated on our site, such as FoxO signaling pathway, Endocytosis, which may be useful for your reference. Also, other proteins which involved in the same pathway with AGAP2 were listed below. Creative BioMart supplied nearly all the proteins listed, you can search them on our site.
| Pathway Name | Pathway Related Protein |
|---|---|
| FoxO signaling pathway | NLK1;MAP2K2A;SMAD2;BNIP4;KLF2A;FOXO1B;PIK3R3A;MAPK9;MAPK3 |
| Endocytosis | LDLRA;VPS4B;SMAD3A;LDLR;MVB12B;EHD1;IL2RGB;BF1;TGFBR1A |
AGAP2 has several biochemical functions, for example, ATP binding, GTP binding, GTPase activator activity. Some of the functions are cooperated with other proteins, some of the functions could acted by AGAP2 itself. We selected most functions AGAP2 had, and list some proteins which have the same functions with AGAP2. You can find most of the proteins on our site.
| Function | Related Protein |
|---|---|
| ATP binding | SEPHS2;SMCHD1;PPP1CA;GLULA;NTRK3;DAPK1;EPHB4B;C22orf28;SMARCAL1 |
| GTP binding | IFT22;RAB7L1;ERAL1;RAB33B;RAB9A;EEF2B;GNAO1A;EEF1A1L2;GBP4 |
| GTPase activator activity | ARHGAP26;LLGL1;ALDH1A1;CHML;GRTP1A;AXIN2;GDI1;ARHGAP6;RGS19 |
| GTPase activity | SRPR;RABL2A;RAB3AA;IRGE4;LRRK2;TUBB2B;EEF1A1L1;GEM;TUBA7L |
| metal ion binding | MICAL2;RORCA;ZNF550;KLF8;ZNF174;PLCH2;ARSK;ZNF238;KLF6 |
| nucleotide binding | RBM27;RAB11AL;TTLL13;NLRP9B;PTBP1B;UBE2G1B;BOLL;ORC4L;PDXK |
| phosphatidylinositol 3-kinase regulator activity | PIK3R1;PIK3R3B;PIK3R3A;KLF4;AGAP2 |
| protein binding | CEP44;C12orf49;HHIPL2;TTC32;IWS1;CERS2;NUP62;GATAD2A;UBAP1 |
| protein kinase activator activity | NCKAP1L;TOM1L1;FAM58A;DAXX;NKX3;MT3;FGF13;WNT11;STK11 |
| protein kinase binding | CDKN2C;AGTR1A;TPRKB;NEFH;TRIB3;ILK;JAK2;CAMK2N1A;NME2 |
AGAP2 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 AGAP2 here. Most of them are supplied by our site. Hope this information will be useful for your research of AGAP2.
Insr; Stat5a; Dcc; Unc5b; Grip1; SNCA; Ywhab
- Q&As
- Reviews
Q&As (20)
Ask a questionAgap2 expression can vary among different cell types and is often regulated by a combination of transcription factors and signaling pathways.
Agap2's involvement in endocytosis can indirectly affect cell signaling by influencing the internalization and processing of cell surface receptors.
Agap2's function in endocytosis is relatively conserved across various species, reflecting its fundamental role in cellular processes.
Researchers often use techniques such as molecular biology, cell imaging, and genetic manipulations to investigate agap2's function, localization, and interactions within cells.
Disruptions in agap2 function have been implicated in certain neurological disorders, potentially affecting cellular communication and signaling.
Agap2 interacts with other proteins to promote the assembly of clathrin-coated pits on the cell membrane, facilitating the invagination and internalization of specific molecules.
Genetic variations in the AGAP2 gene have been linked to certain neurological conditions, suggesting its potential involvement in brain function.
Ongoing research aims to uncover the precise mechanisms of agap2's involvement in endocytosis and its potential implications in various diseases, including neurological disorders.
Agap2 activity can be regulated by cellular signaling pathways and post-translational modifications, affecting its role in endocytic processes.
Agap2 is present in various cells and tissues throughout the body, contributing to the cellular uptake of nutrients and signaling molecules.
Agap2 contains ANK repeat and PH domains, which are crucial for protein-protein interactions and membrane binding, respectively.
Agap2 interacts with various proteins involved in endocytosis, including clathrin and other adaptors, to orchestrate the formation of coated vesicles.
The full name of the protein is "Arf-GAP with GTPase, ANK repeat and PH domain-containing protein 2."
Agap2 can be found in multiple cellular compartments, including the cell membrane and endosomal structures, due to its role in endocytosis.
The role of agap2 in endocytosis suggests it could be a potential target for drugs aimed at modulating cellular uptake processes.
Agap2's ANK repeat and PH domains suggest possible roles in protein-protein interactions and membrane binding, respectively, beyond its role in endocytosis.
Agap2 helps regulate the activity of ADP-ribosylation factor (ARF) GTPases, which are critical for initiating the assembly of clathrin-coated vesicles during endocytosis.
Agap2 helps regulate endocytosis by participating in the formation of clathrin-coated vesicles that transport molecules within cells.
While agap2 is not essential for basic cellular survival, it plays a significant role in maintaining cellular homeostasis and proper functioning.
Agap2 is a protein that plays a role in endocytosis, which is the process by which cells take in molecules from the external environment.
Customer Reviews (5)
Write a reviewProtein’s reliable behavior ensured consistent downstream analyses.
It's quality ensured reliable downstream analysis without interference.
Compatibility across a range of assays expanded our research potential significantly.
The experimental group treated with Protein AGAP2 exhibited accelerated wound healing.
Replicating outcomes across diverse cell lines emphasized the product’s consistent behavior.
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