UniProtKB/Swiss-Prot Q12840: Variant p.Arg1007Gly

Kinesin heavy chain isoform 5A
Gene: KIF5A
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Variant information Variant position:

1007 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Type of variant:

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:

From Arginine (R) to Glycine (G) at position 1007 (R1007G, p.Arg1007Gly). 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:

Change from large size and basic (R) to glycine (G) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score:

-2 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:

In ALS25. Any additional useful information about the variant.
Other resources:

Links to websites of interest for the variant.

Variant rs1555179087 [ dbSNP | Ensembl ]

Sequence information Variant position:

1007 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length:

1032 The length of the canonical sequence.
Location on the sequence:

LASYQKANMDNGNATDINDN R SDLPCGYEAEDQAKLFPLHQ 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                         LASYQKANMDNGNATDINDNRSDLPCGYEAEDQAKLFPLHQ

Mouse                         LASYQKANMDNGNATDINDNRSDLPCGYEAEDQAKLFPLHQ

Rat                           LASYQKANTDNGNATDINDNRSDLPCGYEAEDPAKLFPLHQ

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
Chain	2 – 1032	Kinesin heavy chain isoform 5A
Region	353 – 1032	Interaction with BICD2
Region	907 – 1032	Globular
Region	978 – 1010	Disordered

Literature citations
Hot-spot KIF5A mutations cause familial ALS.
Brenner D.; Yilmaz R.; Mueller K.; Grehl T.; Petri S.; Meyer T.; Grosskreutz J.; Weydt P.; Ruf W.; Neuwirth C.; Weber M.; Pinto S.; Claeys K.G.; Schrank B.; Jordan B.; Knehr A.; Guenther K.; Huebers A.; Zeller D.; Kubisch C.; Jablonka S.; Sendtner M.; Klopstock T.; de Carvalho M.; Sperfeld A.; Borck G.; Volk A.E.; Dorst J.; Weis J.; Otto M.; Schuster J.; Del Tredici K.; Braak H.; Danzer K.M.; Freischmidt A.; Meitinger T.; Strom T.M.; Ludolph A.C.; Andersen P.M.; Weishaupt J.H.;
Brain 141:688-697(2018)
Cited for: INVOLVEMENT IN ALS25; VARIANTS ALS25 GLY-413; HIS-474; GLY-577; LEU-986 AND GLY-1007; Genome-wide Analyses Identify KIF5A as a Novel ALS Gene.
Nicolas A.; Kenna K.P.; Renton A.E.; Ticozzi N.; Faghri F.; Chia R.; Dominov J.A.; Kenna B.J.; Nalls M.A.; Keagle P.; Rivera A.M.; van Rheenen W.; Murphy N.A.; van Vugt J.J.F.A.; Geiger J.T.; Van der Spek R.A.; Pliner H.A.; Shankaracharya X.; Smith B.N.; Marangi G.; Topp S.D.; Abramzon Y.; Gkazi A.S.; Eicher J.D.; Kenna A.; Mora G.; Calvo A.; Mazzini L.; Riva N.; Mandrioli J.; Caponnetto C.; Battistini S.; Volanti P.; La Bella V.; Conforti F.L.; Borghero G.; Messina S.; Simone I.L.; Trojsi F.; Salvi F.; Logullo F.O.; D'Alfonso S.; Corrado L.; Capasso M.; Ferrucci L.; Moreno C.A.M.; Kamalakaran S.; Goldstein D.B.; Gitler A.D.; Harris T.; Myers R.M.; Phatnani H.; Musunuri R.L.; Evani U.S.; Abhyankar A.; Zody M.C.; Kaye J.; Finkbeiner S.; Wyman S.K.; LeNail A.; Lima L.; Fraenkel E.; Svendsen C.N.; Thompson L.M.; Van Eyk J.E.; Berry J.D.; Miller T.M.; Kolb S.J.; Cudkowicz M.; Baxi E.; Benatar M.; Taylor J.P.; Rampersaud E.; Wu G.; Wuu J.; Lauria G.; Verde F.; Fogh I.; Tiloca C.; Comi G.P.; Soraru G.; Cereda C.; Corcia P.; Laaksovirta H.; Myllykangas L.; Jansson L.; Valori M.; Ealing J.; Hamdalla H.; Rollinson S.; Pickering-Brown S.; Orrell R.W.; Sidle K.C.; Malaspina A.; Hardy J.; Singleton A.B.; Johnson J.O.; Arepalli S.; Sapp P.C.; McKenna-Yasek D.; Polak M.; Asress S.; Al-Sarraj S.; King A.; Troakes C.; Vance C.; de Belleroche J.; Baas F.; Ten Asbroek A.L.M.A.; Munoz-Blanco J.L.; Hernandez D.G.; Ding J.; Gibbs J.R.; Scholz S.W.; Floeter M.K.; Campbell R.H.; Landi F.; Bowser R.; Pulst S.M.; Ravits J.M.; MacGowan D.J.L.; Kirby J.; Pioro E.P.; Pamphlett R.; Broach J.; Gerhard G.; Dunckley T.L.; Brady C.B.; Kowall N.W.; Troncoso J.C.; Le Ber I.; Mouzat K.; Lumbroso S.; Heiman-Patterson T.D.; Kamel F.; Van Den Bosch L.; Baloh R.H.; Strom T.M.; Meitinger T.; Shatunov A.; Van Eijk K.R.; de Carvalho M.; Kooyman M.; Middelkoop B.; Moisse M.; McLaughlin R.L.; Van Es M.A.; Weber M.; Boylan K.B.; Van Blitterswijk M.; Rademakers R.; Morrison K.E.; Basak A.N.; Mora J.S.; Drory V.E.; Shaw P.J.; Turner M.R.; Talbot K.; Hardiman O.; Williams K.L.; Fifita J.A.; Nicholson G.A.; Blair I.P.; Rouleau G.A.; Esteban-Perez J.; Garcia-Redondo A.; Al-Chalabi A.; Rogaeva E.; Zinman L.; Ostrow L.W.; Maragakis N.J.; Rothstein J.D.; Simmons Z.; Cooper-Knock J.; Brice A.; Goutman S.A.; Feldman E.L.; Gibson S.B.; Taroni F.; Ratti A.; Gellera C.; Van Damme P.; Robberecht W.; Fratta P.; Sabatelli M.; Lunetta C.; Ludolph A.C.; Andersen P.M.; Weishaupt J.H.; Camu W.; Trojanowski J.Q.; Van Deerlin V.M.; Brown R.H. Jr.; van den Berg L.H.; Veldink J.H.; Harms M.B.; Glass J.D.; Stone D.J.; Tienari P.; Silani V.; Chio A.; Shaw C.E.; Traynor B.J.; Landers J.E.;
Neuron 97:1268-1283(2018)
Cited for: INVOLVEMENT IN ALS25; VARIANTS ALS25 544-ARG--SER-1032 DEL; LEU-986 AND GLY-1007;

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.