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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot Q86TP1: Variant p.Asp30Asn

Exopolyphosphatase PRUNE1
Gene: PRUNE1
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Variant information Variant position: help 30 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 Aspartate (D) to Asparagine (N) at position 30 (D30N, p.Asp30Asn). 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 medium size and acidic (D) to medium size and polar (N) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help 1 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 NMIHBA; loss of function in regulation of cell proliferation and migration; loss of function in neurogenesis; impaired regulation of microtubule polymerization; increased phosphatase activity; no effect on interaction with tubulin beta. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 30 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 453 The length of the canonical sequence.
Location on the sequence: help AALQESRPLHVVLGNEACDL D STVSALALAFYLAKTTEAEE 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                         AALQESRPLHVVLGNEACDLDSTVSALALAFYLAKTTEAEE

Mouse                         AALQDSRPLHVVLGNEACDLDSMVSALALAFYLTKTSEAED

Rat                           AALQESRPLHVVLGNEACDLDSMVSALALAFYLTKTSEAED

Bovine                        AALQESRPIHVVLGNEACDLDSMVSALALAFYLAKTTEAEE
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 – 453 Exopolyphosphatase PRUNE1
Binding site 28 – 28
Binding site 30 – 30
Alternative sequence 1 – 232 Missing. In isoform 6 and isoform 7.
Alternative sequence 1 – 182 Missing. In isoform 3 and isoform 5.
Alternative sequence 15 – 174 Missing. In isoform 4.
Mutagenesis 28 – 28 D -> A. Partial loss of cAMP PDE activity. Partial loss of cAMP PDE activity; when associated with D-106. Partial loss of cAMP PDE activity; when associated with D-106 and D-179.



Literature citations
PRUNE is crucial for normal brain development and mutated in microcephaly with neurodevelopmental impairment.
Zollo M.; Ahmed M.; Ferrucci V.; Salpietro V.; Asadzadeh F.; Carotenuto M.; Maroofian R.; Al-Amri A.; Singh R.; Scognamiglio I.; Mojarrad M.; Musella L.; Duilio A.; Di Somma A.; Karaca E.; Rajab A.; Al-Khayat A.; Mohan Mohapatra T.; Eslahi A.; Ashrafzadeh F.; Rawlins L.E.; Prasad R.; Gupta R.; Kumari P.; Srivastava M.; Cozzolino F.; Kumar Rai S.; Monti M.; Harlalka G.V.; Simpson M.A.; Rich P.; Al-Salmi F.; Patton M.A.; Chioza B.A.; Efthymiou S.; Granata F.; Di Rosa G.; Wiethoff S.; Borgione E.; Scuderi C.; Mankad K.; Hanna M.G.; Pucci P.; Houlden H.; Lupski J.R.; Crosby A.H.; Baple E.L.;
Brain 140:940-952(2017)
Cited for: FUNCTION; INTERACTION WITH TUBULIN; INVOLVEMENT IN NMIHBA; VARIANTS NMIHBA ASN-30; THR-54; ASN-106 AND TRP-297; CHARACTERIZATION OF VARIANTS NMIHBA ASN-30 AND TRP-297; Genes that affect brain structure and function identified by rare variant analyses of mendelian neurologic disease.
Karaca E.; Harel T.; Pehlivan D.; Jhangiani S.N.; Gambin T.; Coban Akdemir Z.; Gonzaga-Jauregui C.; Erdin S.; Bayram Y.; Campbell I.M.; Hunter J.V.; Atik M.M.; Van Esch H.; Yuan B.; Wiszniewski W.; Isikay S.; Yesil G.; Yuregir O.O.; Tug Bozdogan S.; Aslan H.; Aydin H.; Tos T.; Aksoy A.; De Vivo D.C.; Jain P.; Geckinli B.B.; Sezer O.; Gul D.; Durmaz B.; Cogulu O.; Ozkinay F.; Topcu V.; Candan S.; Cebi A.H.; Ikbal M.; Yilmaz Gulec E.; Gezdirici A.; Koparir E.; Ekici F.; Coskun S.; Cicek S.; Karaer K.; Koparir A.; Duz M.B.; Kirat E.; Fenercioglu E.; Ulucan H.; Seven M.; Guran T.; Elcioglu N.; Yildirim M.S.; Aktas D.; Alikasifoglu M.; Ture M.; Yakut T.; Overton J.D.; Yuksel A.; Ozen M.; Muzny D.M.; Adams D.R.; Boerwinkle E.; Chung W.K.; Gibbs R.A.; Lupski J.R.;
Neuron 88:499-513(2015)
Cited for: VARIANTS NMIHBA ASN-30; ASN-106; GLN-128 AND 174-GLY--LYS-453 DEL;
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.