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http://purl.uniprot.org/uniprot/P12235In MTDPS12B; loss of function in ADP transport.
http://purl.uniprot.org/uniprot/P12235In MTDPS12B; loss of function in ADP transport.
http://purl.uniprot.org/uniprot/Q8TD30In MRT49; loss of function mutation.
http://purl.uniprot.org/uniprot/Q13873In PPH1; complete loss of function.
http://purl.uniprot.org/uniprot/Q6ZSZ5In RP78; decreased function in positive regulation of Rho protein signal transduction; loss of function in regulation of actomyosin structure organization.
http://purl.uniprot.org/uniprot/P50993In FHM2; loss of function.
http://purl.uniprot.org/uniprot/P50993In FHM2; loss of function.
http://purl.uniprot.org/uniprot/O00555In SCA6; also found in patients with global developmental delay and congenital ataxia; loss of function observed in the Drosophila homolog.
http://purl.uniprot.org/uniprot/O00555In EA2; loss of function.
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/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/Q01484In LQT4; loss of function.
http://purl.uniprot.org/uniprot/Q01484In LQT4; loss of function.
http://purl.uniprot.org/uniprot/Q01484In LQT4; loss of function.
http://purl.uniprot.org/uniprot/Q01484In LQT4; loss of function.
http://purl.uniprot.org/uniprot/P41181In ANDI; exerts a dominant-negative effect on wild-type-AQP2 in that it interferes with its trafficking to the apical membrane; is a loss of function instead of a gain of function mutation on dominant nephrogenic diabetes insipidus.
http://purl.uniprot.org/uniprot/Q8N100In PHPVAR; loss of function; polypeptide is stable, but does not bind DNA or activate transcription; does not restore retinal ganglion cell development in retinal explants from a mouse Atoh7 null mutant.
http://purl.uniprot.org/uniprot/Q96F25In CMS15; results in a severe reduction in protein expression; loss of function mutation.