UniProtKB/Swiss-Prot Q9UKB3: Variant p.Arg72Pro

DnaJ homolog subfamily C member 12
Gene: DNAJC12
Chromosomal location: 10q22.1
Variant information

Variant position:  72
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Type of variant:  Disease [Disclaimer]
The variants are classified into three categories: Disease, Polymorphism and Unclassified.
  • Disease: Variants implicated in disease according to literature reports.
  • Polymorphism: Variants not reported to be implicated in disease.
  • Unclassified: Variants with uncertain implication in disease according to literature reports. Evidence against or in favor of a pathogenic role is limited and/or conflicting.

Residue change:  From Arginine (R) to Proline (P) at position 72 (R72P, p.Arg72Pro).
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 medium size and hydrophobic (P)
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

Involvement in disease:  Hyperphenylalaninemia, mild, non-BH4-deficient (HPANBH4) [MIM:617384]: An autosomal recessive disorder characterized by increased serum phenylalanine, normal BH4 metabolism, and highly variable neurologic defects, including movement abnormalities and intellectual disability. {ECO:0000269|PubMed:28132689}. Note=The disease is caused by mutations affecting the gene represented in this entry.
The name and a short description of the disease associated with the variant. For more information about the disease, the user can refer to OMIM, following the link provided after the disease acronym.

Variant description:  In HPANBH4; decreased protein levels in patient cells.
Any additional useful information about the variant.



Sequence information

Variant position:  72
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Protein sequence length:  198
The length of the canonical sequence.

Location on the sequence:   AVETFQKLQKAKEILTNEES  R ARYDHWRRSQMSMPFQQWEA
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                         AVETFQKLQKAKEILTNEESRARYDHWRRSQMSMPFQQWEA

Mouse                         AVETFQKLQKAKEILCNAESRARYDHWRRSQMSMPFEQWEA

Rat                           AVETFQKLQKAKEILSNAESRARYDHWRRSQMSMSFEQWEA

Bovine                        AVETFQKLQKAKDILTNEASRARYDHWRRSQMSMSFQQWEA

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.

TypePositionsDescription
Chain 1 – 198 DnaJ homolog subfamily C member 12
Domain 14 – 79 J
Helix 69 – 81


Literature citations

Biallelic mutations in DNAJC12 cause hyperphenylalaninemia, dystonia, and intellectual disability.
Anikster Y.; Haack T.B.; Vilboux T.; Pode-Shakked B.; Thoeny B.; Shen N.; Guarani V.; Meissner T.; Mayatepek E.; Trefz F.K.; Marek-Yagel D.; Martinez A.; Huttlin E.L.; Paulo J.A.; Berutti R.; Benoist J.F.; Imbard A.; Dorboz I.; Heimer G.; Landau Y.; Ziv-Strasser L.; Malicdan M.C.; Gemperle-Britschgi C.; Cremer K.; Engels H.; Meili D.; Keller I.; Bruggmann R.; Strom T.M.; Meitinger T.; Mullikin J.C.; Schwartz G.; Ben-Zeev B.; Gahl W.A.; Harper J.W.; Blau N.; Hoffmann G.F.; Prokisch H.; Opladen T.; Schiff M.;
Am. J. Hum. Genet. 100:257-266(2017)
Cited for: INVOLVEMENT IN HPANBH4; VARIANT HPANBH4 PRO-72; CHARACTERIZATION OF VARIANT HPANBH4 PRO-72;

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.