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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot Q9BU89: Variant p.Ile249Thr

Deoxyhypusine hydroxylase
Gene: DOHH
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Variant information Variant position: help 249 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 Isoleucine (I) to Threonine (T) at position 249 (I249T, p.Ile249Thr). 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 hydrophobic (I) to medium size and polar (T) 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 NEDMVIC. Any additional useful information about the variant.


Sequence information Variant position: help 249 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 302 The length of the canonical sequence.
Location on the sequence: help LARCTENPMVRHECAEALGA I ARPACLAALQAHADDPERVV 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                         LARCTENPMVRHECAEALGAIARPACLAALQAHADDPERVV

Mouse                         LARTTESPMVRHECAEALGAIARPACLAALREHIEDPEQVV

Rat                           LARTTESPMVRHECAEALGAIARPACLAALREYITDPERVV

Bovine                        LAQPTENPMVRHECAEALGAIARPACLAALRAHVADPERVV

Chicken                       LRSRAENPMVRHECAEALGSIARPSCLETLRAFAQDEERVV

Xenopus laevis                LERFEENPMVRHECAEALGSIAHEDCLKALRAHVGDGERVV

Zebrafish                     LEKMDENAMVRHECAEALGSIGKEPCVQILERYRKDQERVV

Caenorhabditis elegans        LLLSTENCMVRHECAEALGAIANEECTEILKQYVNDEERVV

Drosophila                    LEDRLENEMVRHECAEALGAIATEDCIQILNRYAEDDKRVV

Slime mold                    VLDESENAMVRHEAAEALGAIASTETIPLLEKLLQDKEPIV

Baker's yeast                 LGRKEEAPMVRHEAAEALGAIASPEVVDVLKSYLNDEVDVV

Fission yeast                 LENTEEVPMVRHEAAEALGGIANDECLPVLKKFSKDDVRVV
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 – 302 Deoxyhypusine hydroxylase
Repeat 238 – 264 HEAT-like PBS-type 5
Binding site 240 – 240
Binding site 241 – 241
Mutagenesis 237 – 237 M -> L. Decreased iron-binding. Loss of iron-binding; when associated with L-86.
Mutagenesis 240 – 240 H -> A. Loss of deoxyhypusine monooxygenase activity. Loss of iron-binding.
Mutagenesis 241 – 241 E -> A. Loss of deoxyhypusine monooxygenase activity. Loss of iron-binding.
Helix 236 – 249



Literature citations
Bi-allelic variants in DOHH, catalyzing the last step of hypusine biosynthesis, are associated with a neurodevelopmental disorder.
Ziegler A.; Steindl K.; Hanner A.S.; Kumar Kar R.; Prouteau C.; Boland A.; Deleuze J.F.; Coubes C.; Bezieau S.; Kuery S.; Maystadt I.; Le Mao M.; Lenaers G.; Navet B.; Faivre L.; Tran Mau-Them F.; Zanoni P.; Chung W.K.; Rauch A.; Bonneau D.; Park M.H.;
Am. J. Hum. Genet. 109:1549-1558(2022)
Cited for: VARIANTS NEDMVIC LEU-152; LYS-184; LEU-223; THR-249 AND 280-TYR--SER-302 DEL; INVOLVEMENT IN NEDMVIC;
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.