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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot Q5VTY9: Variant p.Gly287Val

Protein-cysteine N-palmitoyltransferase HHAT
Gene: HHAT
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Variant information Variant position: help 287 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 Glycine (G) to Valine (V) at position 287 (G287V, p.Gly287Val). 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 glycine (G) to medium size and hydrophobic (V) 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 NNMS; loss of palmitoyltransferase activity; unable to carry out SHH and DHH palmitoylation; does not affect HHAT protein levels. Any additional useful information about the variant.


Sequence information Variant position: help 287 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 493 The length of the canonical sequence.
Location on the sequence: help MHAIYSSIPLLETVSCWTLG G LALAQVLFFYVKYLVLFGVP 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                         MHAIYSSIPLLETVSC--WTL-GGLALAQVLFFYVKYLVLFGVP

Mouse                         MHALYSSAPLLESVSC--WTL-GGLALAQVLFFYVKYLVLF

Drosophila                    IHYMSRDVRMVEMMDSVFWQHSAGYFMGQ--FFFLYYVVTY
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 – 493 Protein-cysteine N-palmitoyltransferase HHAT
Transmembrane 285 – 314 Helical; Name=alpha8
Alternative sequence 1 – 369 Missing. In isoform 4.
Mutagenesis 306 – 306 V -> LF. Does not affect palmitoyltransferase activity.
Mutagenesis 306 – 306 V -> R. Strongly reduced palmitoyltransferase activity.
Helix 282 – 314



Literature citations
Structure, mechanism, and inhibition of Hedgehog acyltransferase.
Coupland C.E.; Andrei S.A.; Ansell T.B.; Carrique L.; Kumar P.; Sefer L.; Schwab R.A.; Byrne E.F.X.; Pardon E.; Steyaert J.; Magee A.I.; Lanyon-Hogg T.; Sansom M.S.P.; Tate E.W.; Siebold C.;
Mol. Cell 81:5025-5038(2021)
Cited for: STRUCTURE BY ELECTRON MICROSCOPY (2.7 ANGSTROMS) IN COMPLEX WITH HEME; COFACTOR; FUNCTION; CATALYTIC ACTIVITY; ACTIVITY REGULATION; MUTAGENESIS OF PHE-58; GLU-59; GLY-67; TRP-255; VAL-306; CYS-324; VAL-325; TRP-335; ARG-336; ASP-339; HIS-343; HIS-379; 382-TYR--TYR-384; TRP-386 AND TYR-479; CHARACTERIZATION OF VARIANT NNMS VAL-287; CHARACTERIZATION OF VARIANT GLU-448;
Loss of function mutation in the palmitoyl-transferase HHAT leads to syndromic 46,XY disorder of sex development by impeding Hedgehog protein palmitoylation and signaling.
Callier P.; Calvel P.; Matevossian A.; Makrythanasis P.; Bernard P.; Kurosaka H.; Vannier A.; Thauvin-Robinet C.; Borel C.; Mazaud-Guittot S.; Rolland A.; Desdoits-Lethimonier C.; Guipponi M.; Zimmermann C.; Stevant I.; Kuhne F.; Conne B.; Santoni F.; Lambert S.; Huet F.; Mugneret F.; Jaruzelska J.; Faivre L.; Wilhelm D.; Jegou B.; Trainor P.A.; Resh M.D.; Antonarakis S.E.; Nef S.;
PLoS Genet. 10:e1004340-e1004340(2014)
Cited for: VARIANT NNMS VAL-287; INVOLVEMENT IN NNMS; CHARACTERIZATION OF VARIANT NNMS VAL-287; FUNCTION; CATALYTIC ACTIVITY; TISSUE SPECIFICITY;
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.