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UniProtKB/Swiss-Prot Q8WTS1: Variant p.Glu260Lys

1-acylglycerol-3-phosphate O-acyltransferase ABHD5
Gene: ABHD5
Variant information

Variant position:  260
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 Glutamate (E) to Lysine (K) at position 260 (E260K, p.Glu260Lys).
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 acidic (E) to large size and basic (K)
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 CDS; loss of PNPLA2-dependent triacylclycerol hydrolysis but no effect on LPA acyltransferase activity.
Any additional useful information about the variant.

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



Sequence information

Variant position:  260
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Protein sequence length:  349
The length of the canonical sequence.

Location on the sequence:   FEDDTVTEYIYHCNVQTPSG  E TAFKNMTIPYGWAKRPMLQR
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                         FEDDTVTEYIYHCNVQTPSGETAFKNMTIPYGWAKRPMLQR

Mouse                         FEDDTVTEYIYHCNVQTPSGETAFKNMTIPYGWAKRPMLQR

Rat                           FEDDTVTEYIYHCNVQTPSGETAFKNMTIPYGWAKRPMLQR

Pig                           FEDDTVTEYIYHCNVQTPSGETAFKNMTIPYGWAKRPMLHR

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 – 349 1-acylglycerol-3-phosphate O-acyltransferase ABHD5


Literature citations

Mutations in CGI-58, the gene encoding a new protein of the esterase/lipase/thioesterase subfamily, in Chanarin-Dorfman syndrome.
Lefevre C.; Jobard F.; Caux F.; Bouadjar B.; Karaduman A.; Heilig R.; Lakhdar H.; Wollenberg A.; Verret J.-L.; Weissenbach J.; Oezguec M.; Lathrop M.; Prud'homme J.-F.; Fischer J.;
Am. J. Hum. Genet. 69:1002-1012(2001)
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]; TISSUE SPECIFICITY; VARIANTS CDS LYS-7; PRO-130 AND LYS-260;

Adipose triglyceride lipase-mediated lipolysis of cellular fat stores is activated by CGI-58 and defective in Chanarin-Dorfman Syndrome.
Lass A.; Zimmermann R.; Haemmerle G.; Riederer M.; Schoiswohl G.; Schweiger M.; Kienesberger P.; Strauss J.G.; Gorkiewicz G.; Zechner R.;
Cell Metab. 3:309-319(2006)
Cited for: FUNCTION; CHARACTERIZATION OF VARIANTS CDS PRO-130 AND LYS-260;

CGI-58, the causative gene for Chanarin-Dorfman syndrome, mediates acylation of lysophosphatidic acid.
Ghosh A.K.; Ramakrishnan G.; Chandramohan C.; Rajasekharan R.;
J. Biol. Chem. 283:24525-24533(2008)
Cited for: FUNCTION; CATALYTIC ACTIVITY; CHARACTERIZATION OF VARIANTS CDS PRO-130 AND LYS-260;

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.