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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot O95140: Variant p.Arg707Trp

Mitofusin-2
Gene: MFN2
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Variant information Variant position: help 707 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Type of variant: help LP/P [Disclaimer] The variants are classified into three categories: LP/P, LB/B and US.
  • LP/P: likely pathogenic or pathogenic.
  • LB/B: likely benign or benign.
  • US: uncertain significance
Residue change: help From Arginine (R) to Tryptophan (W) at position 707 (R707W, p.Arg707Trp). Indicates the amino acid change of the variant. The one-letter and three-letter codes for amino acids used in UniProtKB/Swiss-Prot are those adopted by the commission on Biochemical Nomenclature of the IUPAC-IUB.
Physico-chemical properties: help Change from large size and basic (R) to large size and aromatic (W) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help -3 The score within a Blosum matrix for the corresponding wild-type to variant amino acid change. The log-odds score measures the logarithm for the ratio of the likelihood of two amino acids appearing by chance. The Blosum62 substitution matrix is used. This substitution matrix contains scores for all possible exchanges of one amino acid with another:
  • Lowest score: -4 (low probability of substitution).
  • Highest score: 11 (high probability of substitution).
More information can be found on the following page
Variant description: help In CMT2A2A, CMT2A2B and MSL; decreased function in mitochondrial fusion; reduced homo-oligomerization; no effect on hetero-oligomerization with MFN1. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 707 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 757 The length of the canonical sequence.
Location on the sequence: help QVQQELSGTFAHLCQQVDVT R ENLEQEIAAMNKKIEVLDSL 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: help The multiple alignment of the region surrounding the variant against various orthologous sequences. 
Human                         QVQQELSGTFAHLCQQVDVTRENLEQEIAAMNKKIEVLDSL

Mouse                         QVQQELSGTFAHLCQQVDITRDNLEQEIAAMNKKVEALDSL

Rat                           QVQQELSGTFAHLCQQVDITRDNLEQEIAAMNKKVEALDSL
Sequence annotation in neighborhood: help 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.
TypePositionsDescription
Chain 1 – 757 Mitofusin-2
Topological domain 648 – 757 Cytoplasmic
Coiled coil 695 – 738
Alternative sequence 705 – 757 VTRENLEQEIAAMNKKIEVLDSLQSKAKLLRNKAGWLDSELNMFTHQYLQPSR -> GETLSERSMAKSTLMLLTLLFLCSFAGAQDVLTQ. In isoform 2.



Literature citations
Homozygous mutations in MFN2 cause multiple symmetric lipomatosis associated with neuropathy.
Sawyer S.L.; Cheuk-Him Ng A.; Innes A.M.; Wagner J.D.; Dyment D.A.; Tetreault M.; Majewski J.; Boycott K.M.; Screaton R.A.; Nicholson G.;
Hum. Mol. Genet. 24:5109-5114(2015)
Cited for: FUNCTION; SUBUNIT; VARIANT MSL TRP-707; CHARACTERIZATION OF VARIANT HMSN6A TRP-94; CHARACTERIZATION OF VARIANT MSL TRP-707; Human biallelic MFN2 mutations induce mitochondrial dysfunction, upper body adipose hyperplasia, and suppression of leptin expression.
Rocha N.; Bulger D.A.; Frontini A.; Titheradge H.; Gribsholt S.B.; Knox R.; Page M.; Harris J.; Payne F.; Adams C.; Sleigh A.; Crawford J.; Gjesing A.P.; Bork-Jensen J.; Pedersen O.; Barroso I.; Hansen T.; Cox H.; Reilly M.; Rossor A.; Brown R.J.; Taylor S.I.; McHale D.; Armstrong M.; Oral E.A.; Saudek V.; O'Rahilly S.; Maher E.R.; Richelsen B.; Savage D.B.; Semple R.K.;
Elife 6:0-0(2017)
Cited for: INVOLVEMENT IN MSL; VARIANTS MSL ARG-343 DEL AND TRP-707; Severe early-onset axonal neuropathy with homozygous and compound heterozygous MFN2 mutations.
Nicholson G.A.; Magdelaine C.; Zhu D.; Grew S.; Ryan M.M.; Sturtz F.; Vallat J.M.; Ouvrier R.A.;
Neurology 70:1678-1681(2008)
Cited for: VARIANT MSL TRP-707; VARIANTS CMT2A2B VAL-164; ASN-214; MET-362 AND ARG-390; Genotype-phenotype correlations in Charcot-Marie-Tooth disease type 2 caused by mitofusin 2 mutations.
Calvo J.; Funalot B.; Ouvrier R.A.; Lazaro L.; Toutain A.; De Mas P.; Bouche P.; Gilbert-Dussardier B.; Arne-Bes M.C.; Carriere J.P.; Journel H.; Minot-Myhie M.C.; Guillou C.; Ghorab K.; Magy L.; Sturtz F.; Vallat J.M.; Magdelaine C.;
Arch. Neurol. 66:1511-1516(2009)
Cited for: VARIANTS CMT2A2B ARG-108 AND TRP-707; VARIANTS HMSN6A TRP-94; TRP-104 AND ARG-276; VARIANTS CMT2A2A ARG-128; ILE-156; MET-236; MET-244; TYR-277; PRO-364; GLN-364; SER-665; CYS-740; PRO-745 AND THR-747; MFN2 point mutations occur in 3.4% of Charcot-Marie-Tooth families. An investigation of 232 Norwegian CMT families.
Braathen G.J.; Sand J.C.; Lobato A.; Hoeyer H.; Russell M.B.;
BMC Med. Genet. 11:48-48(2010)
Cited for: VARIANT HMSN6A TRP-94; VARIANT CMT2A2B GLN-94; VARIANTS HIS-468; SER-570; ILE-705 AND THR-716; VARIANT CMT2A2A TRP-707;
Disclaimer: 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.