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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P61457: Variant p.Thr79Ile

Pterin-4-alpha-carbinolamine dehydratase
Gene: PCBD1
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Variant information Variant position: help 79 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 Threonine (T) to Isoleucine (I) at position 79 (T79I, p.Thr79Ile). 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 polar (T) to medium size and hydrophobic (I) 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 HPABH4D; increased proteolytic degradation; reduced interaction with HNF1B; loss of HNF1B-coactivator activity. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 79 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 104 The length of the canonical sequence.
Location on the sequence: help KLDHHPEWFNVYNKVHITLS T HECAGLSERDINLASFIEQV 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                         KLDHHPEWFNVYNKVHITLSTHEC-------AGLSERDINLASFIEQV

Mouse                         KLDHHPEWFNVYNKVHITLSTHEC-------AGLSERDINL

Rat                           KLDHHPEWFNVYNKVHITLSTHEC-------AGLSERDINL

Bovine                        KLDHHPEWFNVYNKVHITLSTHEC-------AGLSERDVNL

Chicken                       KLDHHPEWFNVYNKVHITLSTHEC-------TGLSERDINL

Xenopus laevis                KLDHHPEWFNVYDKVHITLSTHDC-------GGLSERDINL

Caenorhabditis elegans        KMDHHPEWFNVYNKVDITLSTHDC-------GGLSPNDVKL

Drosophila                    KINHHPEWFNCYNKVDVTLSTHDV-------GGLSSQDIRM

Slime mold                    QMNHHPEWFNVYNRVEITLATHDC-------SGLSVNDTKM

Baker's yeast                 LWGHHPLIHTSYTWVKLELHTHDIDPKDGAHSQLSDIDVRM

Fission yeast                 QLNHHPEWTNVYNKVDITLTTHDT-------KGLTEKDLKL
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 2 – 104 Pterin-4-alpha-carbinolamine dehydratase
Binding site 78 – 81



Literature citations
Hyperphenylalaninemia with high levels of 7-biopterin is associated with mutations in the PCBD gene encoding the bifunctional protein pterin-4a-carbinolamine dehydratase and transcriptional coactivator (DCoH).
Thoeny B.; Neuheiser F.; Kierat L.; Blaskovics M.; Arn P.H.; Ferreira P.; Rebrin I.; Ayling J.; Blau N.;
Am. J. Hum. Genet. 62:1302-1311(1998)
Cited for: VARIANTS HPABH4D ILE-79; 87-GLU--THR-104 DEL AND 98-GLN--THR-104 DEL; Mutations in PCBD1 cause hypomagnesemia and renal magnesium wasting.
Ferre S.; de Baaij J.H.; Ferreira P.; Germann R.; de Klerk J.B.; Lavrijsen M.; van Zeeland F.; Venselaar H.; Kluijtmans L.A.; Hoenderop J.G.; Bindels R.J.;
J. Am. Soc. Nephrol. 25:574-586(2014)
Cited for: CHARACTERIZATION OF VARIANTS HPABH4D 27-GLU--THR-104 DEL; ILE-79; ARG-82; 87-GLU--THR-104 DEL; LYS-97 AND 98-GLU--THR-104 DEL; CHARACTERIZATION OF VARIANT GLN-88; FUNCTION; INTERACTION WITH HNF1B; 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.