EBP
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Official Full Name
emopamil binding protein (sterol isomerase) -
Overview
The protein encoded by this gene is an integral membrane protein of the endoplasmic reticulum. It is a high affinity binding protein for the antiischemic phenylalkylamine Ca2+ antagonist (3H)emopamil and the photoaffinity label (3H)azidopamil. It is similar to sigma receptors and may be a member of a superfamily of high affinity drug-binding proteins in the endoplasmic reticulum of different tissues. This protein shares structural features with bacterial and eukaryontic drug transporting proteins. It has four putative transmembrane segments and contains two conserved glutamate residues which may be involved in the transport of cationic amphiphilics. Another prominent feature of this protein is its high content of aromatic amino acid residues (>23%) in its transmembrane segments. These aromatic amino acid residues have been suggested to be involved in the drug transport by the P-glycoprotein. Mutations in thisgene cause Chondrodysplasia punctata 2 (CDPX2; also known as Conradi-Hunermann syndrome). -
Synonyms
EBP;emopamil binding protein (sterol isomerase);CDPX2, emopamil binding protein (sterol isomerase);3-beta-hydroxysteroid-Delta(8),Delta(7)-isomerase;3 beta hydroxysteroid delta 8;delta 7 isomerase;CHO2;Chondrodysplasia punctata 2;X linked dominan
Recombinant Proteins
- Rat
- Zebrafish
- Human
- Mouse
- Dictyostelium Discoideum
- Mus musculus
- Guinea pig
- Mammalian Cell
- HEK293
- HEK293T
- Mammalian cells
- E.coli expression system
- His
- Non
- His&Fc&Avi
- Myc&DDK
- Flag
Involved Pathway
EBP involved in several pathways and played different roles in them. We selected most pathways EBP participated on our site, such as Cholesterol biosynthesis,Metabolic pathways,Metabolism, which may be useful for your reference. Also, other proteins which involved in the same pathway with EBP were listed below. Creative BioMart supplied nearly all the proteins listed, you can search them on our site.
| Pathway Name | Pathway Related Protein |
|---|---|
| Cholesterol biosynthesis | LBR,ARV1,SREBF2,CYP51A1,PMVK,DHCR24,DHCR7 |
| Metabolism | HPSE,CYP2R1,SLC25A12,SLC25A1,AGL,OAZ2,SULT1C2,UROC1,HAS3,COQ6 |
| Metabolic pathways | CYP2J5,GAL3ST1A,NDUFA8,CYP2C55,AMPD2,PNPLA2,PDXK,CYP51,PYCR1B,HEXB |
| cholesterol biosynthesis III (via desmosterol) | LBR |
| Metabolism of lipids and lipoproteins | FABP11A,ACOT12,Agmo,MED26,CYP2Y3,ARF3,FABP11B,PTGDSA,APOA4A,APOEA |
| Steroid biosynthesis | CEL.1,SQLEA,FAXDC2,SQLE,Cel,LSS,CELL,CYP51,HSD17B7,SC5D |
| cholesterol biosynthesis I | DHCR7,DHCR24,LBR |
| cholesterol biosynthesis II (via 24,25-dihydrolanosterol) | DHCR24,LBR |
Protein Function
EBP has several biochemical functions, for example, C-8 sterol isomerase activity,cholestenol delta-isomerase activity,drug transmembrane transporter activity. Some of the functions are cooperated with other proteins, some of the functions could acted by EBP itself. We selected most functions EBP had, and list some proteins which have the same functions with EBP. You can find most of the proteins on our site.
| Function | Related Protein |
|---|---|
| drug transmembrane transporter activity | SLC17A3,ABCG2A,ABCG3,SLC22A18,SLC18A1,Abcb1b,SLCO1B2,ABCG2D,SLC47A2,SLC22A5 |
| steroid delta-isomerase activity | HSD3B6,HSD3B2,HSD3B1 |
| transmembrane signaling receptor activity | GLP1R,BAI2,ANTXR1,LILRB3,NRXN1,TLR2-2,NFAM1,FZD9B,CLDN3,TLR2 |
| cholestenol delta-isomerase activity | EBPL |
Interacting Protein
EBP 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 EBP here. Most of them are supplied by our site. Hope this information will be useful for your research of EBP.
MITF;q9wmx2-pro_0000037550;SAP30;HSP90B1;Samm50;Spire2;NCSTN;Tmed2;Mad2l1
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References
- Chen, Y; Lu, RQ; et al. The NFKB1 polymorphism (rs4648068) is associated with the cell proliferation and motility in gastric cancer. BMC GASTROENTEROLOGY 15:-(2015).
- Bil-Lula, I; Sochocka, M; et al. Adenovirus Type 9 Enhances Differentiation and Decreases Cytokine Release from Preadipocytes. JOURNAL OF MEDICAL VIROLOGY 87:230-239(2015).
