Variant position: 154 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 210 The length of the canonical sequence.
Location on the sequence:
The residue change on the sequence. Unless the variant is located at the beginning or at the end of the protein sequence, both residues upstream (20) and downstream (20) of the variant will be shown.
Residue conservation: The multiple alignment of the region surrounding the variant against various orthologous sequences.
Human VKLGGDLGTYVINKQTPNKQ IWLSSPSSGPKRYDW----TGKNWV
Mouse IKLGGDLGTYVINKQTPNKQ IWLSSPSSGPKRYDW----TG
Rat IKLGGDLGTYVINKQTPLLY LWFSGPCSGPKRYDW----TG
Bovine VKLGGDLGTYVINKQTPNKQ IWLSSPSSGPKRYDW----TG
Caenorhabditis elegans VNVSKSVGTYVINKQSPNKQ IWLSSPMSGPKRYDL---EEE
Drosophila VNLGGQHGTYVINRQTPNKQ IWLSSPTSGPKRYDFVGTVAA
Slime mold IIVGNK-GTYVINKQTPNRQ IWWSSPLSGPKRFDY--DSVE
Baker's yeast LEIPAF-GTYVINKQPPNKQ IWLASPLSGPNRFDL----LN
Fission yeast LMLGEK-GTYVINKQPPAHQ IWLSSPVSGPKHYEY--SLKS
Sequence annotation in neighborhood: The regions or sites of interest surrounding the variant. In general the features listed are posttranslational modifications, binding sites, enzyme active sites, local secondary structure or other characteristics reported in the cited references. The "Sequence annotation in neighborhood" lines have a fixed format:
Type: the type of sequence feature. Positions: endpoints of the sequence feature. Description: contains additional information about the feature.
Friedreich's ataxia: autosomal recessive disease caused by an intronic GAA triplet repeat expansion.
Campuzano V.; Montermini L.; Molto M.D.; Pianese L.; Cossee M.; Cavalcanti F.; Monros E.; Rodius F.; Duclos F.; Monticelli A.; Zara F.; Canizares J.; Koutnikova H.; Bidichandani S.; Gellera C.; Brice A.; Trouillas P.; de Michele G.; Filla A.; de Frutos R.; Palau F.; Patel P.I.; di Donato S.; Mandel J.-L.; Cocozza S.; Koenig M.; Pandolfo M.;
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 2); ALTERNATIVE SPLICING; VARIANT PHE-154;
Mitochondrial frataxin interacts with ISD11 of the NFS1/ISCU complex and multiple mitochondrial chaperones.
Shan Y.; Napoli E.; Cortopassi G.;
Hum. Mol. Genet. 16:929-941(2007)
Cited for: INTERACTION WITH LYRM4 AND HSPA9; CHARACTERIZATION OF VARIANTS PHE-154 AND ARG-155;
Atypical Friedreich ataxia caused by compound heterozygosity for a novel missense mutation and the GAA triplet-repeat expansion.
Bidichandani S.I.; Ashizawa T.; Patel P.I.;
Am. J. Hum. Genet. 60:1251-1256(1997)
Cited for: VARIANTS FRDA VAL-130 AND PHE-154;
The first cellular models based on frataxin missense mutations that reproduce spontaneously the defects associated with Friedreich ataxia.
Calmels N.; Schmucker S.; Wattenhofer-Donze M.; Martelli A.; Vaucamps N.; Reutenauer L.; Messaddeq N.; Bouton C.; Koenig M.; Puccio H.;
PLoS ONE 4:E6379-E6379(2009)
Cited for: CHARACTERIZATION OF VARIANT FRDA PHE-154;
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