Variant position: 123 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 323 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 GCFKA-----------IVAGDQNV----EYKGTVW HKDCFTCSNCKQVI----------GTGSFFP
Mouse GCFKA-----------IVAGDQNV----EYKGTVW HKDCFT
Rat GCFKA-----------IVAGDQNV----EYKGTIW HKDCFT
Baker's yeast TCIRKYSTAKGMSLSEIYAGIRELFPYYKYCPDGW QSSVRH
Fission yeast RTLIA-NPNKKMTLGDICEWIANNWSYYRHQPPAW HNSIRH
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.
Type Positions Description
2 – 323 Four and a half LIM domains protein 1
101 – 153 LIM zinc-binding 2
121 – 123
Proteomic identification of FHL1 as the protein mutated in human reducing body myopathy.
Schessl J.; Zou Y.; McGrath M.J.; Cowling B.S.; Maiti B.; Chin S.S.; Sewry C.; Battini R.; Hu Y.; Cottle D.L.; Rosenblatt M.; Spruce L.; Ganguly A.; Kirschner J.; Judkins A.R.; Golden J.A.; Goebel H.-H.; Muntoni F.; Flanigan K.M.; Mitchell C.A.; Boennemann C.G.;
J. Clin. Invest. 118:904-912(2008)
Cited for: INVOLVEMENT IN RBMX1A; INVOLVEMENT IN RBMX1B; VARIANTS RBMX1A TYR-123 AND PHE-132; VARIANTS RBMX1B TYR-153 AND ARG-153;
Clinical, histological and genetic characterization of reducing body myopathy caused by mutations in FHL1.
Schessl J.; Taratuto A.L.; Sewry C.; Battini R.; Chin S.S.; Maiti B.; Dubrovsky A.L.; Erro M.G.; Espada G.; Robertella M.; Saccoliti M.; Olmos P.; Bridges L.R.; Standring P.; Hu Y.; Zou Y.; Swoboda K.J.; Scavina M.; Goebel H.H.; Mitchell C.A.; Flanigan K.M.; Muntoni F.; Boennemann C.G.;
Cited for: VARIANTS RBMX1A GLN-123; LEU-123; TYR-123 AND PHE-132; VARIANTS RBMX1B ARG-153 AND TYR-153;
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