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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P55157: Variant p.Leu435His

Microsomal triglyceride transfer protein large subunit
Gene: MTTP
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Variant information Variant position: help 435 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 Leucine (L) to Histidine (H) at position 435 (L435H, p.Leu435His). 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 (L) to medium size and polar (H) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help -3 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 ABL; no loss on localization to the endoplasmic reticulum; inhibits triglyceride transfer activity. Any additional useful information about the variant.


Sequence information Variant position: help 435 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 894 The length of the canonical sequence.
Location on the sequence: help FKGSIGSSDIRETVMIITGT L VRKLCQNEGCKLKAVVEAKK 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                         FKGSI--GSSDIRETVMIITGTLVRKLCQNEGCKLKAVVEAKK

Mouse                         FKGSF--ASNDIRESVMIIIGALVRKLCQNEGCKLKAVVEA

Rat                           FKGSF--ASNDIRESVMIIIGALVRKLCQNEGCKLKAVVEA

Pig                           FKGSF--GSNDIRESVMIIIGALVRKLCQNEGCKLKAVVDA

Zebrafish                     SQGKI--GSTEIKESVVIIMGALLRKLCLKGACDLPAVLKV

Caenorhabditis elegans        WLGSLDKKSEEYWKVANTIATVLNKR-CEASTSSLNSCNKG

Drosophila                    LEQESIKKHLKLRESVIQTVATLTRQSGLD--VEDPLLKEV

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 19 – 894 Microsomal triglyceride transfer protein large subunit
Domain 28 – 659 Vitellogenin
Alternative sequence 152 – 894 Missing. In isoform 2.
Mutagenesis 435 – 435 L -> E. No loss on localization to the endoplasmic reticulum. Inhibits triglyceride transfer activity.
Mutagenesis 435 – 435 L -> V. No loss on localization to the endoplasmic reticulum. Does not inhibit triglyceride transfer activity.
Helix 422 – 440



Literature citations
Molecular and functional analysis of two new MTTP gene mutations in an atypical case of abetalipoproteinemia.
Di Filippo M.; Crehalet H.; Samson-Bouma M.E.; Bonnet V.; Aggerbeck L.P.; Rabes J.P.; Gottrand F.; Luc G.; Bozon D.; Sassolas A.;
J. Lipid Res. 53:548-555(2012)
Cited for: VARIANT ABL HIS-435; CHARACTERIZATION OF VARIANT ABL HIS-435; FUNCTION; SUBCELLULAR LOCATION; MUTAGENESIS OF LEU-435;
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.