Expasy logo

UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot Q9H4E7: Variant p.Glu331Lys

Differentially expressed in FDCP 6 homolog
Gene: DEF6
Feedback?
Variant information Variant position: help 331 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 331 (E331K, p.Glu331Lys). 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 IMD87; affects function in vesicle-mediated protein transport as shown by impaired CTLA4 trafficking to cell surface in homozygous patient T cells; decreased interaction with RAB11A. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 331 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 631 The length of the canonical sequence.
Location on the sequence: help IRLQAEGKTSLHKDLKQKRR E QREQRERRRAAKEEELLRLQ 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                         IRLQAEGKTSLHKDLKQKRREQREQRERRRAAKEEELLRLQ

Mouse                         IRLQAEGKTSLHKDLKQKRREQREQRERRRAAKEEELLRLQ

Xenopus laevis                IRLQQSGSLSLHRELQKRRREQRELREQRRAARELEMQRLA

Zebrafish                     IRLYVEGKTSLHKDLKLKRRDQREQREKRREAKEQELQRLR
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 – 631 Differentially expressed in FDCP 6 homolog
Region 318 – 341 Disordered
Compositional bias 331 – 341 Basic and acidic residues



Literature citations
Human DEF6 deficiency underlies an immunodeficiency syndrome with systemic autoimmunity and aberrant CTLA-4 homeostasis.
Serwas N.K.; Hoeger B.; Ardy R.C.; Stulz S.V.; Sui Z.; Memaran N.; Meeths M.; Krolo A.; Yuece Petronczki O.; Pfajfer L.; Hou T.Z.; Halliday N.; Santos-Valente E.; Kalinichenko A.; Kennedy A.; Mace E.M.; Mukherjee M.; Tesi B.; Schrempf A.; Pickl W.F.; Loizou J.I.; Kain R.; Bidmon-Fliegenschnee B.; Schickel J.N.; Glauzy S.; Huemer J.; Garncarz W.; Salzer E.; Pierides I.; Bilic I.; Thiel J.; Priftakis P.; Banerjee P.P.; Foerster-Waldl E.; Medgyesi D.; Huber W.D.; Orange J.S.; Meffre E.; Sansom D.M.; Bryceson Y.T.; Altman A.; Boztug K.;
Nat. Commun. 10:3106-3106(2019)
Cited for: VARIANTS IMD87 ASP-210 AND LYS-331; INVOLVEMENT IN IMD87; FUNCTION; INTERACTION WITH RAB11A; TISSUE SPECIFICITY; CHARACTERIZATION OF VARIANTS IMD87 ASP-210 AND LYS-331;
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.