Variant position: 36 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 736 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 NTVGADIIQLPQIVVVGTQS SGKSSVLESLVGRDLLPRGTG
Mouse NTVGADIIQLPQIVVVGTQS SGKSSVLESLVGRDLLPRGTG
Rat NTVGADIIQLPQIVVVGTQS SGKSSVLESLVGRDLLPRGTG
Bovine NTVGADIIQLPQIVVVGTQS SGKSSVLESLVGRDLLPRGTG
Zebrafish NTVGADIIQLPQIAVVGTQS SGKSSVLESLVGRDLLPRGTG
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
1 – 736 Dynamin-1-like protein
22 – 302 Dynamin-type G
32 – 40 GTP
32 – 39 G1 motif
1 – 43 MEALIPVINKLQDVFNTVGADIIQLPQIVVVGTQSSGKSSVLE -> MFHKKINGKQQEKKMTLLHGKTQDTFLKGWKQKNGVNFFTPKI. In isoform 7.
34 – 34 Q -> A. Abolishes GTP hydrolysis.
38 – 38 K -> A. Loss of GTPase activity. Impairs mitochondrial division and induces changes in peroxisome morphology. No effect on oligomerization. Increase in sumoylation by SUMO3.
38 – 38 K -> E. Overexpression delays protein secretion.
39 – 39 S -> A. Abolishes GTP hydrolysis.
39 – 39 S -> I. Decreased localization to the perinuclear region.
39 – 39 S -> N. Reduces peroxisomal abundance.
41 – 41 V -> F. Temperature-sensitive. Impairs mitochondrial division.
34 – 36
Biallelic Mutations in DNM1L are Associated with a Slowly Progressive Infantile Encephalopathy.
Nasca A.; Legati A.; Baruffini E.; Nolli C.; Moroni I.; Ardissone A.; Goffrini P.; Ghezzi D.;
Hum. Mutat. 37:898-903(2016)
Cited for: VARIANT EMPF1 GLY-36; CHARACTERIZATION OF VARIANT EMPF1 GLY-36; FUNCTION;
Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. They are not in any way intended to be used as a substitute for professional medical advice, diagnostic, treatment or care.