ACTN4, actinin alpha 4, 81

N. diseases: 166; N. variants: 10
Disease: Focal glomerulosclerosis ×
Source: ALL
Variant Gene Disease Risk Allele Score vda Association Type Original DB Sentence supporting the association PMID PMID Year
dbSNP: rs121908415
rs121908415
Entrez Id: 81;107985291
Gene Symbol: ACTN4;LOC107985291
ACTN4;LOC107985291
CUI: C0017668
Disease:
Focal glomerulosclerosis 		0.050 GeneticVariation BEFREE A putative kinase target site at Y265 in the actin binding domain was also generated as a phosphomimetic ACTN4 Y265E that demonstrated even greater binding to actin filaments than K255E and the other FSGS mutants. 31664084 2019
dbSNP: rs121908415
rs121908415
Entrez Id: 81;107985291
Gene Symbol: ACTN4;LOC107985291
ACTN4;LOC107985291
CUI: C0017668
Disease:
Focal glomerulosclerosis 		0.050 GeneticVariation BEFREE Transgenic mice that express actinin-4 K256E in podocytes develop podocyte injury, proteinuria, and FSGS in association with glomerular ER stress. 29873512 2018
dbSNP: rs121908415
rs121908415
Entrez Id: 81;107985291
Gene Symbol: ACTN4;LOC107985291
ACTN4;LOC107985291
CUI: C0017668
Disease:
Focal glomerulosclerosis 		0.050 GeneticVariation BEFREE Despite the absence of a familial pattern of inheritance, these similar biological changes caused by the Y265H and K255E amino acid substitutions suggest that this new variant is potentially the cause of FSGS in this patient. 27977723 2016
dbSNP: rs121908415
rs121908415
Entrez Id: 81;107985291
Gene Symbol: ACTN4;LOC107985291
ACTN4;LOC107985291
CUI: C0017668
Disease:
Focal glomerulosclerosis 		0.050 GeneticVariation BEFREE We crossed Col1α1-eGFP-L10a mice with the Actn4(-/-) and Actn4(+/K256E) models of FSGS and analyzed podocyte transcriptional profiles at 2, 6, and 44 weeks of age. 24940801 2014
dbSNP: rs121908415
rs121908415
Entrez Id: 81;107985291
Gene Symbol: ACTN4;LOC107985291
ACTN4;LOC107985291
CUI: C0017668
Disease:
Focal glomerulosclerosis 		0.050 GeneticVariation BEFREE Furthermore, the sedimentation coefficients by analytical ultracentrifugation of wild-type and FSGS mutant ABDs (Lys255Glu, Ser262Pro, and Thr259Ile) are nearly identical (2.50+/-0.03 S) and are in good agreement with the theoretical value calculated from the crystal structure (2.382 S), implying that the compact conformation is retained in solution. 18164029 2008
dbSNP: rs121908416
rs121908416
Entrez Id: 81;107985291
Gene Symbol: ACTN4;LOC107985291
ACTN4;LOC107985291
CUI: C0017668
Disease:
Focal glomerulosclerosis 		0.020 GeneticVariation BEFREE Natural mutations such as lysine 255 to glutamic acid (K to E), threonine 259 to isoleucine (T to I) and serine 262 to proline (S to P) that occur within the actin binding domain of alpha-actinin-4 (ACTN4) cause an autosomal dominant form of focal segmental glomerulosclerosis (FSGS) in affected humans. 31664084 2019
dbSNP: rs121908416
rs121908416
Entrez Id: 81;107985291
Gene Symbol: ACTN4;LOC107985291
ACTN4;LOC107985291
CUI: C0017668
Disease:
Focal glomerulosclerosis 		0.020 GeneticVariation BEFREE Furthermore, the sedimentation coefficients by analytical ultracentrifugation of wild-type and FSGS mutant ABDs (Lys255Glu, Ser262Pro, and Thr259Ile) are nearly identical (2.50+/-0.03 S) and are in good agreement with the theoretical value calculated from the crystal structure (2.382 S), implying that the compact conformation is retained in solution. 18164029 2008
dbSNP: rs121908417
rs121908417
Entrez Id: 81;107985291
Gene Symbol: ACTN4;LOC107985291
ACTN4;LOC107985291
CUI: C0017668
Disease:
Focal glomerulosclerosis 		0.010 GeneticVariation BEFREE Natural mutations such as lysine 255 to glutamic acid (K to E), threonine 259 to isoleucine (T to I) and serine 262 to proline (S to P) that occur within the actin binding domain of alpha-actinin-4 (ACTN4) cause an autosomal dominant form of focal segmental glomerulosclerosis (FSGS) in affected humans. 31664084 2019
dbSNP: rs112545413
rs112545413
Entrez Id: 81;107985291
Gene Symbol: ACTN4;LOC107985291
ACTN4;LOC107985291
CUI: C0017668
Disease:
Focal glomerulosclerosis 		0.010 GeneticVariation BEFREE Additionally, two FSGS-associated α-actinin-4 mutations (R310Q and Q348R) inhibited the complex formation between α-actinin-4 and CLP36. 21680739 2011