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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot Q15904: Variant p.Glu346Lys

V-type proton ATPase subunit S1
Gene: ATP6AP1
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Variant information Variant position: help 346 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 Glutamate (E) to Lysine (K) at position 346 (E346K, p.Glu346Lys). 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 acidic (E) to large size and basic (K) 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 IMD47; probable loss of proton-transporting V-type ATPase complex assembly in yeast; unable to restore V-ATPase-dependent growth in Voa1 mutant yeast. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 346 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 470 The length of the canonical sequence.
Location on the sequence: help ILANRLYPVSARHWFTMERL E VHSNGSVAYFNASQVTGPSI 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                         ILANRLYPVSARHWFTMERLEVHSNGSVAYFNASQVTGPSI----------------

Mouse                         ILASRFYPVSARYWFAMERLEIHSNGSVAHFNVSQVTGPSI

Rat                           ILASRFYPVSARYWFTMERLEIHSNGSVAHFNVSQVTGPSI

Bovine                        ILANSYYSVSARHWFTLENLEIHSNGSVAYFNASQVTGPSI

Caenorhabditis elegans        TFTGDLFGYWALNKASASNLAISGYDP---YKSASVDGSKV

Drosophila                    VYNGGYF--------SLSNLVYDNNN----FRSSGVNAPTT
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 42 – 470 V-type proton ATPase subunit S1
Topological domain 42 – 419 Lumenal
Glycosylation 350 – 350 N-linked (GlcNAc...) asparagine
Glycosylation 357 – 357 N-linked (GlcNAc...) asparagine
Beta strand 337 – 348



Literature citations
ATP6AP1 deficiency causes an immunodeficiency with hepatopathy, cognitive impairment and abnormal protein glycosylation.
Jansen E.J.; Timal S.; Ryan M.; Ashikov A.; van Scherpenzeel M.; Graham L.A.; Mandel H.; Hoischen A.; Iancu T.C.; Raymond K.; Steenbergen G.; Gilissen C.; Huijben K.; van Bakel N.H.; Maeda Y.; Rodenburg R.J.; Adamowicz M.; Crushell E.; Koenen H.; Adams D.; Vodopiutz J.; Greber-Platzer S.; Mueller T.; Dueckers G.; Morava E.; Sykut-Cegielska J.; Martens G.J.; Wevers R.A.; Niehues T.; Huynen M.A.; Veltman J.A.; Stevens T.H.; Lefeber D.J.;
Nat. Commun. 7:11600-11600(2016)
Cited for: INVOLVEMENT IN IMD47; VARIANTS IMD47 PRO-144; CYS-313; LYS-346 AND ILE-428; CHARACTERIZATION OF VARIANTS IMD47 CYS-313; LYS-346 AND ILE-428; SUBCELLULAR LOCATION; TISSUE SPECIFICITY; GLYCOSYLATION; MUTAGENESIS OF VAL-470;
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.