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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot Q14203: Variant p.Gly59Ser

Dynactin subunit 1
Gene: DCTN1
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Variant information Variant position: help 59 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 Glycine (G) to Serine (S) at position 59 (G59S, p.Gly59Ser). 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 glycine (G) to small size and polar (S) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help 0 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 HMND14; reduced affinity for microtubules which has been suggested to impair axonal transport; the effect is identical to that of complete loss of the CAP-Gly domain; decreased interaction with MAPRE1; no effect on its interaction with TBCB. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 59 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 1278 The length of the canonical sequence.
Location on the sequence: help GHRGTVAYVGATLFATGKWV G VILDEAKGKNDGTVQGRKYF 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                         GHRGTVAYVGATLFATGKWVGVILDEAKGKNDGTVQGRKYF

Mouse                         GHRGTVAYVGATLFATGKWVGVILDEAKGKNDGTVQGRKYF

Rat                           GHRGTVAYVGATLFATGKWVGVILDEAKGKNDGTVQGRKYF

Pig                           GHRGTVAYVGATLFATGKWVGVILDEAKGKNDGTVQGRKYF

Chicken                       GHRGTVAYVGATLXATGKWVGVILDEAKGKNDGTVQGRKYF

Xenopus laevis                GYRGTVAYVGATLFATGKWVGVILDDSKGKNDGTVQGRRYF

Drosophila                    DLLGTVAYVGMTSFAVGKWVGVVLDEPKGKNSGSIKGQQYF

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 – 1278 Dynactin subunit 1
Domain 48 – 90 CAP-Gly
Alternative sequence 1 – 138 MAQSKRHVYSRTPSGSRMSAEASARPLRVGSRVEVIGKGHRGTVAYVGATLFATGKWVGVILDEAKGKNDGTVQGRKYFTCDEGHGIFVRQSQIQVFEDGADTTSPETPDSSASKVLKREGTDTTAKTSKLRGLKPKK -> MMRQ. In isoform p135 and isoform 5.
Mutagenesis 68 – 68 K -> A. Abolishes interaction with CLIP1.
Beta strand 57 – 65



Literature citations
Mutant dynactin in motor neuron disease.
Puls I.; Jonnakuty C.; LaMonte B.H.; Holzbaur E.L.; Tokito M.; Mann E.; Floeter M.K.; Bidus K.; Drayna D.; Oh S.J.; Brown R.H. Jr.; Ludlow C.L.; Fischbeck K.H.;
Nat. Genet. 33:455-456(2003)
Cited for: VARIANT HMND14 SER-59; A motor neuron disease-associated mutation in p150Glued perturbs dynactin function and induces protein aggregation.
Levy J.R.; Sumner C.J.; Caviston J.P.; Tokito M.K.; Ranganathan S.; Ligon L.A.; Wallace K.E.; LaMonte B.H.; Harmison G.G.; Puls I.; Fischbeck K.H.; Holzbaur E.L.F.;
J. Cell Biol. 172:733-745(2006)
Cited for: CHARACTERIZATION OF VARIANT HMND14 SER-59; INTERACTION WITH MAPRE1; DCTN1 mutations in Perry syndrome.
Farrer M.J.; Hulihan M.M.; Kachergus J.M.; Daechsel J.C.; Stoessl A.J.; Grantier L.L.; Calne S.; Calne D.B.; Lechevalier B.; Chapon F.; Tsuboi Y.; Yamada T.; Gutmann L.; Elibol B.; Bhatia K.P.; Wider C.; Vilarino-Gueell C.; Ross O.A.; Brown L.A.; Castanedes-Casey M.; Dickson D.W.; Wszolek Z.K.;
Nat. Genet. 41:163-165(2009)
Cited for: VARIANTS PERRYS ARG-71; GLU-71; ALA-71; PRO-72 AND PRO-74; CHARACTERIZATION OF VARIANTS PERRYS ARG-71 AND PRO-74; CHARACTERIZATION OF VARIANT HMND14 SER-59; Neurodegeneration mutations in dynactin impair dynein-dependent nuclear migration.
Moore J.K.; Sept D.; Cooper J.A.;
Proc. Natl. Acad. Sci. U.S.A. 106:5147-5152(2009)
Cited for: CHARACTERIZATION OF VARIANT HMND14 SER-59; Tubulin-binding cofactor B is a direct interaction partner of the dynactin subunit p150(Glued).
Kuh G.F.; Stockmann M.; Meyer-Ohlendorf M.; Linta L.; Proepper C.; Ludolph A.C.; Bockmann J.; Boeckers T.M.; Liebau S.;
Cell Tissue Res. 350:13-26(2012)
Cited for: CHARACTERIZATION OF VARIANT HMND14 SER-59; CHARACTERIZATION OF VARIANT 196-ILE; INTERACTION WITH TBCB; SUBCELLULAR LOCATION;
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.