Variant position: 399 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 616 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 LLFGPPGNGKTMLAKAVAAE SNATFFNISAASLTSKYVGEG
Mouse LLFGPPGNGKTMLAKAVAAE SNATFFNISAASLTSKYVGEG
Rat LLFGPPGNGKTMLAKAVAAE SNATFFNISAASLTSKYVGEG
Pig LLFGPPGNGKTMLAKAVAAE SNATFFNISAASLTSKYVGEG
Bovine LLFGPPGNGKTMLAKAVAAE SNATFFNISAASLTSKYVGEG
Chicken LLFGPPGNGKTMLAKAVAAE SNATFFNISAASLTSKYVGEG
Xenopus laevis LLFGPPGNGKTMLAKAVAAE SNATFFNISAASLTSKYVGEG
Xenopus tropicalis LLFGPPGNGKTMLAKAVAAE SNATFFNISAASLTSKYVGEG
Zebrafish LLFGPPGNGKTMLAKAVAME SNATFFNISAATLTSKYVGEG
Caenorhabditis elegans LLFGPPGNGKTLLAKAVAGE SKQMFFNISASSLTSKWVGDS
Drosophila LLFGPPGNGKTLLARAVATE CSATFLNISAASLTSKYVGDG
Slime mold LLFGPPGNGKTMIAKAVAYE SKVTFFSISSSSLTSKYVGDG
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 – 616 Spastin
78 – 616 Cytoplasmic
228 – 616 Sufficient for microtubule severing
388 – 388 K -> A. Abrogates ATPase activity and abolishes microtubule severing.
415 – 415 Y -> A. Abrogates binding to the tail of alpha-tubulin and beta-3-tubulin, impairs ATPase activity and abolishes microtubule severing.
Spectrum of SPG4 mutations in a large collection of North American families with hereditary spastic paraplegia.
Meijer I.A.; Hand C.K.; Cossette P.; Figlewicz D.A.; Rouleau G.A.;
Arch. Neurol. 59:281-286(2002)
Cited for: VARIANTS SPG4 LEU-399; VAL-426; LEU-489; ASP-559 AND GLN-562;
Novel and recurrent spastin mutations in a large series of SPG4 Italian families.
Nanetti L.; Baratta S.; Panzeri M.; Tomasello C.; Lovati C.; Azzollini J.; Gellera C.; Di Bella D.; Taroni F.; Mariotti C.;
Neurosci. Lett. 528:42-45(2012)
Cited for: VARIANTS SPG4 THR-95; 112-GLU--VAL-616 DEL; 135-GLU--VAL-616 DEL; LEU-399; ARG-406; THR-409; VAL-426; 431-ARG--VAL-616 DEL; CYS-460; TRP-503; ARG-559 AND 562-ARG--VAL-616 DEL;
Mutation analysis of SPAST, ATL1, and REEP1 in Korean Patients with Hereditary Spastic Paraplegia.
Kim T.H.; Lee J.H.; Park Y.E.; Shin J.H.; Nam T.S.; Kim H.S.; Jang H.J.; Semenov A.; Kim S.J.; Kim D.S.;
J. Clin. Neurol. 10:257-261(2014)
Cited for: VARIANTS SPG4 44-SER--VAL-616 DEL; 245-SER--VAL-616 DEL; 254-LYS--VAL-616 DEL; GLY-372; LEU-399; ARG-451 DEL; ARG-458; HIS-499 AND 581-ARG--VAL-616 DEL;
Spastin mutation screening in Chinese patients with pure hereditary spastic paraplegia.
Wei Q.Q.; Chen Y.; Zheng Z.Z.; Chen X.; Huang R.; Yang Y.; Burgunder J.; Shang H.F.;
Parkinsonism Relat. Disord. 20:845-849(2014)
Cited for: VARIANTS SPG4 PRO-363; LEU-399; VAL-441 AND ARG-595;
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