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UniProtKB/Swiss-Prot Q9BY32: Variant p.Pro32Thr

Inosine triphosphate pyrophosphatase
Gene: ITPA
Variant information

Variant position:  32
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Type of variant:  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:  From Proline (P) to Threonine (T) at position 32 (P32T, p.Pro32Thr).
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 medium size and hydrophobic (P) to medium size and polar (T)
The physico-chemical property of the reference and variant residues and the change implicated.

BLOSUM score:  -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:  In ITPAD; complete loss of enzymatic activity at homozygosity; partial loss of activity without ITP accumulation in heterozygous individuals.
Any additional useful information about the variant.

Other resources:  
Links to websites of interest for the variant.



Sequence information

Variant position:  32
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Protein sequence length:  194
The length of the canonical sequence.

Location on the sequence:   FVTGNAKKLEEVVQILGDKF  P CTLVAQKIDLPEYQGEPDEI
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                         FVTGNAKKLEEVVQIL-----GDKFPCTLVAQKIDLPEYQG-EPDEI

Mouse                         FVTGNAKKLEEVIQIL-----GDNFPCTLEAQKIDLPEYQG

Rat                           FVTGNAKKLEEVIQIL-----GDKFPCTLVAQKIDLPEYQG

Bovine                        FVTGNAKKLEEVIQIL-----GDKFPCTLVAQKIDLPEYQG

Chicken                       FVTGNAKKLEEVTQIL-----GDSSPYTLVARKIDLPEYQG

Xenopus laevis                FVTGNAKKLEEVVQIL-----GDKFPCKLVAKKIDLPEYQG

Zebrafish                     FVTGNAKKLEEVVQIL-----GDKFPYKLISKKIDLPEYQG

Caenorhabditis elegans        FVTGNVKKLEEVKAIL------KNF--EVSNVDVDLDEFQG

Drosophila                    FVTGNAKKLEELVAIL-----GPSFPRTIVSKKIDLPELQG

Slime mold                    FVTGNAKKLEEALQIL-----GTSFP--IESKKVDLPELQG

Baker's yeast                 FVTGNANKLKEVQSILTQEVDNNNKTIHLINEALDLEELQD

Fission yeast                 FVTGNKHKLADVKNIL-----GDRF--EIKNHDYDLPEIQG

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 2 – 194 Inosine triphosphate pyrophosphatase
Metal binding 44 – 44 Magnesium
Alternative sequence 23 – 63 Missing. In isoform 3.


Literature citations

Submission
Mao Y.M.; Xie Y.; Zheng Z.H.;
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1); VARIANT ITPAD THR-32;

Genetic basis of inosine triphosphate pyrophosphohydrolase deficiency.
Sumi S.; Marinaki A.M.; Arenas M.; Fairbanks L.; Shobowale-Bakre M.; Rees D.C.; Thein S.L.; Ansari A.; Sanderson J.; De Abreu R.A.; Simmonds H.A.; Duley J.A.;
Hum. Genet. 111:360-367(2002)
Cited for: VARIANT ITPAD THR-32;

DNA polymorphisms in ITPA including basis of inosine triphosphatase deficiency.
Cao H.; Hegele R.A.;
J. Hum. Genet. 47:620-622(2002)
Cited for: VARIANT ITPAD THR-32;

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.