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http://purl.uniprot.org/uniprot/Q96C12In AIMAH2; loss of function in promoting apoptosis.
http://purl.uniprot.org/uniprot/Q96C12In AIMAH2; loss of function in promoting apoptosis.
http://purl.uniprot.org/uniprot/Q96C12In AIMAH2; loss of function in promoting apoptosis.
http://purl.uniprot.org/uniprot/Q96C12In AIMAH2; loss of function in promoting apoptosis.
http://purl.uniprot.org/uniprot/Q96C12In AIMAH2; loss of function in promoting apoptosis.
http://purl.uniprot.org/uniprot/Q8TD30In MRT49; loss of function mutation.
http://purl.uniprot.org/uniprot/Q96F25In CMS15; results in a severe reduction in protein expression; loss of function mutation.
http://purl.uniprot.org/uniprot/Q9H165In IDPFH, de novo mutation, loss of function in transactivation of transcription, reduces the interaction between isoform 2 and isoform 3, disrupts the nuclear paraspeckle distribution of isoform 2 and isoform 3.
http://purl.uniprot.org/uniprot/Q9H165In IDPFH; de novo mutation; loss of function in transactivation of transcription; reduces the interaction between isoform 2 and isoform 3; disrupts the nuclear paraspeckle distribution of isoform 2 and isoform 3.
http://purl.uniprot.org/uniprot/Q9H165In IDPFH, de novo mutation, loss of function in transactivation of transcription, reduces the interaction between isoform 2 and isoform 3, disrupts the nuclear paraspeckle distribution of isoform 2 and isoform 3.
http://purl.uniprot.org/uniprot/Q9H165In IDPFH, de novo mutation, loss of function transactivation of transcription, reduces the interaction between isoform 2 and isoform 3, disrupts the nuclear paraspeckle distribution of isoform 2 and isoform 3.
http://purl.uniprot.org/uniprot/Q9H165In IDPFH, de novo mutation, loss of function in transactivation of transcription, reduces the interaction between isoform 2 and isoform 3, disrupts the nuclear paraspeckle distribution of isoform 2 and isoform 3.
http://purl.uniprot.org/uniprot/Q9H165In IDPFH, de novo mutation, loss of function in transactivation of transcription, reduces the interaction between isoform 2 and isoform 3, disrupts the nuclear paraspeckle distribution of isoform 2 and isoform 3.
http://purl.uniprot.org/uniprot/Q9H165In IDPFH; de novo mutation; loss of function in transactivation of transcription; reduces the interaction between isoform 2 and isoform 3; disrupts the nuclear paraspeckle distribution of isoform 2 and isoform 3.
http://purl.uniprot.org/uniprot/Q9H165In IDPFH, de novo mutation, loss of function in transactivation of transcription, reduces the interaction between isoform 2 and isoform 3, disrupts the nuclear paraspeckle distribution of isoform 2 and isoform 3.
http://purl.uniprot.org/uniprot/Q9H165In IDPFH; de novo mutation; loss of function in transactivation of transcription; reduces the interaction between isoform 2 and isoform 3; disrupts the nuclear paraspeckle distribution of isoform 2 and isoform 3.
http://purl.uniprot.org/uniprot/P51788In LKPAT; loss of function mutation; the mutant protein is restricted to the endoplasmic reticulum and hardly reached the plasma membrane; lower amounts of the mutant protein compared to wild-type.
http://purl.uniprot.org/uniprot/P51788In LKPAT; loss of function mutation; the mutant protein is restricted to the endoplasmic reticulum and hardly reaches the plasma membrane; lower amounts of the mutant protein compared to wild-type.
http://purl.uniprot.org/uniprot/P51795In NPHL2; causes retention in the endoplasmic reticulum and alters protein stability; total loss of function.
http://purl.uniprot.org/uniprot/P51795In NPHL2; abolishes the chloride currents; total loss of function.
http://purl.uniprot.org/uniprot/P51795In NPHL2; causes retention in the endoplasmic reticulum and alters protein stability; total loss of function.
http://purl.uniprot.org/uniprot/P51795In LMWPHN; causes retention in the endoplasmic reticulum and alters protein stability; total loss of function.
http://purl.uniprot.org/uniprot/P48165In CTRCT1; incomplete penetrance; results in loss of function.
http://purl.uniprot.org/uniprot/P51530In PEOA6; the mutant protein has decreased nuclease activity (30% of wild-type) and enhanced helicase activity; consistent with a loss of function mutation.
http://purl.uniprot.org/uniprot/P51530In PEOA6; the mutant protein has significantly reduced nuclease and helicase activity; consistent with a loss of function mutation.