EPB41 Antibody

• Six single nucleotide polymorphisms (SNPs) within the EPB41 gene have been significantly associated with Mandibular Prognathism (rs2762686, rs2788888, rs4654388, rs502393, rs11581096, and rs488113). Notably, the G-allele of SNP rs4654388 demonstrated the strongest link to an increased risk of Mandibular Prognathism in the Chinese population. PMID: 28570402
• Utilizing Next-Generation sequencing, researchers identified causative genetic mutations in fifteen patients with clinically suspected hereditary elliptocytosis and hereditary pyropoikilocytosis. These identified mutations were correlated with the clinical phenotype and ektacytometry profile. PMID: 27667160
• A study revealed that alternative polyadenylation serves as an additional mechanism for generating 4.1 protein diversity within the already complex EPB41-related genes. Understanding the intricacies of EPB41 RNA processing is essential for a comprehensive comprehension of the numerous 4.1 proteins expressed in both normal and pathological tissues. PMID: 27981895
• Research has identified EPB41 as a hepatocellular carcinoma susceptibility gene both in vitro and in vivo. Notably, EPB41 expression is significantly reduced in HCC tissue specimens, particularly in portal vein metastasis or intrahepatic metastasis, compared to normal tissues. PMID: 27453575
• The 4.1R, 4.1N, and 4.1B proteins are all expressed at the lateral membrane as well as the cytoplasm of epithelial cells, suggesting a potentially redundant role for these proteins. PMID: 24912669
• Calcium mediates the conformation-based 4.1R FERM domain binding to membrane proteins via calmodulin. PMID: 24081810
• Findings suggest a previously unknown role for the scaffolding protein 4.1R in locally regulating CLASP2 behavior, CLASP2 cortical platform turnover, and GSK3 activity, enabling proper MT organization and dynamics essential for cell polarity. PMID: 23943871
• Research indicates that PIP2 may play a significant role as a modulator of apo-CaM binding to 4.1R(80) throughout evolution. PMID: 24607279
• Plasmodium falciparum PF3D7_0402000 has been identified as a novel binding partner for the major erythrocyte cytoskeletal protein, 4.1R. PMID: 23663475
• A novel gene region, EPB41, has been associated with smoking cessation, alongside gene regions in CNR1 that may be targeted to further elucidate the etiology of gender differences in smoking behaviors. PMID: 21808284
• 4.1R regulates NHE1 activity through a direct protein-protein interaction that can be modulated by intracellular pH and Na(+) and Ca(2+) concentrations. PMID: 22731252
• Further studies involving siRNA-mediated knockdowns of spectrin, adducin, or p4.1 revealed that these proteins are essential for efficient docking of enterohaemorrhagic Escherichia coli to host cells. PMID: 22197999
• This study elucidates the mechanism by which RBFOX2 regulates protein 4.1R exon 16 splicing through the downstream intronic element UGCAUG. PMID: 22083953
• Apo-calmodulin stabilizes the 4.1R N-terminal domain through interaction with its beta-strand-rich C-lobe, thus providing a novel function for calmodulin: structural stabilization of 4.1R. PMID: 21848512
• Data demonstrate that protein 4.1R is crucial for the localization of IQGAP1 to the leading edge of cells migrating into a wound, while IQGAP1 is not required for protein 4.1R localization. PMID: 21750196
• 4.1R plays a role in the phosphatidylserine exposure signaling pathway, which is fundamental to red cell turnover. PMID: 19794081
• Proteins belonging to the membrane skeleton protein 4.1 family exhibit weak expression in non-small cell lung cancer and are associated with tumor cell differentiation. PMID: 19624891
• In addition to two known minor shortened and stable spliceoforms, a 4.1R splicing mutation activates an intronic cryptic splice site, resulting in a nonsense mRNA major isoform, targeted for degradation in intact cells by Nonsense-mediated mRNA decay. PMID: 20863723
• Four EPB41 SNPs displayed allelic and genotypic associations with MP in the first stage. In the second stage, the allele rs4654388 exhibited the strongest significant association with MP. The rs4654388 G-allele was linked to a significantly increased risk of MP. PMID: 20797695
• Data suggest that one or both of proteins 4.1 and 4.2 cause a portion of band 3 to localize near the spectrin-actin junctions, providing another point of attachment between the membrane skeleton and the lipid bilayer. PMID: 20007969
• The EPB4.1 gene has been reassigned to 1p36 and its involvement in neuroblastomas is under investigation. PMID: 11737230
• With deletions or mutations, the ability of the 8 amino acid motif (LKKNFMES) of the spectrin-actin-binding domain of erythrocyte protein 4.1 recombinant peptides to form ternary complexes with spectrin and actin is significantly diminished. PMID: 12044158
• Falcipain-2-mediated cleavage of protein 4.1 occurs immediately after lysine 437, which resides within a region of the spectrin-actin-binding domain critical for erythrocyte membrane stability. PMID: 12130521
• A splicing alteration of pre-mRNA generates two protein isoforms with distinct assembly to spindle poles in mitotic cells. PMID: 12239178
• A 4.1R isoform expressing the leucine-rich sequence binds to the export receptor CRM1 in a RanGTP-dependent manner, while this interaction does not occur in a mutant where two conserved hydrophobic residues are substituted. PMID: 12427749
• The synthesis of structurally distinct 4.1R protein isoforms in various cell types is regulated by a novel mechanism requiring coordination between upstream transcription initiation events and downstream alternative splicing events. PMID: 12522012
• A novel member of the protein 4.1 family has been cloned and exhibits focal expression in the ovary. PMID: 12601556
• Protein 4.1R plays a role in recruiting hDlg to the lateral membrane in epithelial cells. PMID: 12807908
• Protein 4.1R functions as a significant tumor suppressor in the molecular pathogenesis of meningioma. PMID: 12901833
• Protein 4.1R interacts with nuclear actin during nuclear assembly in vitro. PMID: 12960380
• Alpha-spectrin ubiquitination at repeats 20 and 21 enhances the dissociation of the spectrin-protein-4.1-actin ternary complex, thereby regulating protein 4.1's ability to stimulate the spectrin-actin interaction. PMID: 15040429
• The 135-kDa non-erythroid 4.1R has a role in cell division. PMID: 15184364
• The mitotic regulation of protein 4.1R involves phosphorylation by cdc2 kinase. PMID: 15525677
• 4.1R plays a key role at the centrosome, contributing to the maintenance of a radial microtubule organization. PMID: 15564380
• Protein 4.1 phosphorylation modulates erythrocyte membrane mechanical function. PMID: 15611095
• Alternative splicing isoforms are present in muscular dystrophy skeletal muscle. PMID: 15714879
• Loss of expression of 4.1R was statistically more common in ependymomas. PMID: 15731777
• It is speculated that over the repetitive cycles of heart muscle contraction and relaxation, 4.1s are likely to locate, support, and coordinate the functioning of key membrane-bound macromolecular assemblies. PMID: 15834631
• 4.1R binds to the separate calponin homology CH1 and CH2 domains of beta I spectrin. PMID: 16060676
• EPB41 gene expression remained unchanged in all analyzed meningiomas. This suggests that the involvement of the EPB41 gene (4.1R protein) in meningioma pathogenesis should be reconsidered. PMID: 16157202
• The interaction of protein 4.1 with TRPC4 is required for the activation of the endothelial ISOC channel. PMID: 16254212
• Protein 4.1R interactions with membrane proteins are regulated by Ca2+ and calmodulin [review]. PMID: 16368534
• Fox-1 and Fox-2 splicing factors play roles in the alternative splicing of protein 4.1R. PMID: 16537540
• 4.1R60 isoforms exhibit constitutive self-association, while 4.1R80 and 4.1R135 self-association is prevented by intramolecular interactions. PMID: 16881872
• The interaction of Plasmodium falciparum EBA-181 with the highly conserved 10 kDa domain of 4.1R provides new insight into the molecular mechanisms employed by P. falciparum during erythrocyte entry. PMID: 17087826
• A decreased expression pattern of the 4.1R protein was observed in the erythrocytes of patients with atypical NA. PMID: 17298666
• A regulated splicing event in protein 4.1R pre-mRNA, involving the inclusion of exon 16, which encodes peptides for spectrin-actin binding, occurs during late erythroid differentiation. PMID: 17715393
• A deficit in protein 4.1R is recurrent in myeloid malignancies and should be investigated particularly when deletion del(20q) is present, as this chromosomal abnormality was found in four out of six patients. PMID: 17994571
• In the 4.1R gene, intrasplicing ultimately determines N-terminal protein structure and function. PMID: 18079699
• 4.1R plays crucial roles in the structural integrity of centrosomes and mitotic spindles, which normally enable mitosis and anaphase to proceed with coordinated precision. PMID: 18212055

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HGNC: 3377

OMIM: 130500

KEGG: hsa:2035

STRING: 9606.ENSP00000345259

UniGene: Hs.175437