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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot Q14203: Variant p.Gly71Arg

Dynactin subunit 1
Gene: DCTN1
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Variant information Variant position: help 71 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 Arginine (R) at position 71 (G71R, p.Gly71Arg). 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 large size and basic (R) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help -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: help In PERRYS; reduced microtubule binding; results in the accumulation of intracytoplasmic inclusions; loss of interaction with CLIP1; significant decrease in motility of dynein-dynactin complex along microtubules. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 71 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 LFATGKWVGVILDEAKGKND G TVQGRKYFTCDEGHGIFVRQ 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                         LFATGKWVGVILDEAKGKNDGTVQGRKYFTCDEGHGIFVRQ

Mouse                         LFATGKWVGVILDEAKGKNDGTVQGRKYFTCDEGHGIFVRQ

Rat                           LFATGKWVGVILDEAKGKNDGTVQGRKYFTCDEGHGIFVRQ

Pig                           LFATGKWVGVILDEAKGKNDGTVQGRKYFTCDEGHGIFVRQ

Chicken                       LXATGKWVGVILDEAKGKNDGTVQGRKYFTCEENHGIFVRQ

Xenopus laevis                LFATGKWVGVILDDSKGKNDGTVQGRRYFTCEENHGIFVRQ

Drosophila                    SFAVGKWVGVVLDEPKGKNSGSIKGQQYFQCDENCGMFVRP
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.
Mutagenesis 90 – 90 R -> E. Abolishes interaction with CLIP1.
Beta strand 67 – 73



Literature citations
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; Dynactin functions as both a dynamic tether and brake during dynein-driven motility.
Ayloo S.; Lazarus J.E.; Dodda A.; Tokito M.; Ostap E.M.; Holzbaur E.L.;
Nat. Commun. 5:4807-4807(2014)
Cited for: CHARACTERIZATION OF VARIANTS PERRYS ARG-71 AND PRO-74; FUNCTION; INTERACTION WITH DYNEIN INTERMEDIATE CHAIN AND DYNEIN HEAVY CHAIN; DOMAIN CAP-GLY; Three families with Perry syndrome from distinct parts of the world.
Tacik P.; Fiesel F.C.; Fujioka S.; Ross O.A.; Pretelt F.; Castaneda Cardona C.; Kidd A.; Hlavac M.; Raizis A.; Okun M.S.; Traynor S.; Strongosky A.J.; Springer W.; Wszolek Z.K.;
Parkinsonism Relat. Disord. 20:884-888(2014)
Cited for: VARIANTS PERRYS ARG-71 AND CYS-78; CHARACTERIZATION OF VARIANTS PERRYS ARG-71 AND CYS-78; Alpha-tubulin tyrosination and CLIP-170 phosphorylation regulate the initiation of dynein-driven transport in neurons.
Nirschl J.J.; Magiera M.M.; Lazarus J.E.; Janke C.; Holzbaur E.L.;
Cell Rep. 14:2637-2652(2016)
Cited for: CHARACTERIZATION OF VARIANT PERRYS ARG-71; SUBCELLULAR LOCATION; DOMAIN CAP-GLY; INTERACTION WITH CLIP1; ASSOCIATION WITH MICROTUBULES;
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.