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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P12931: Variant p.Glu527Lys

Proto-oncogene tyrosine-protein kinase Src
Gene: SRC
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Variant information Variant position: help 527 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 527 (E527K, p.Glu527Lys). 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 THC6; increased protein tyrosine kinase activity; increased autophosphorylation at Y-419; causes defective megakaryopoiesis associated with increased overall tyrosine phosphorylation in megakaryocytes. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 527 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 536 The length of the canonical sequence.
Location on the sequence: help EERPTFEYLQAFLEDYFTST E PQYQPGENL 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                         EERPTFEYLQAFLEDYFTSTEPQYQPGENL

Mouse                         EERPTFEYLQAFLEDYFTSTEPQYQPGENL

Rat                           EERPTFEYLQAFLEDYFTSTEPQYQPGENL

Chicken                       EERPTFEYLQAFLEDYFTSTEPQYQPGENL

Zebrafish                     EERPTFEYLQGFLEDYFTSTEPQYQPGENL
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 2 – 536 Proto-oncogene tyrosine-protein kinase Src
Modified residue 530 – 530 Phosphotyrosine; by CSK



Literature citations
A dominant gain-of-function mutation in universal tyrosine kinase SRC causes thrombocytopenia, myelofibrosis, bleeding, and bone pathologies.
Turro E.; Greene D.; Wijgaerts A.; Thys C.; Lentaigne C.; Bariana T.K.; Westbury S.K.; Kelly A.M.; Selleslag D.; Stephens J.C.; Papadia S.; Simeoni I.; Penkett C.J.; Ashford S.; Attwood A.; Austin S.; Bakchoul T.; Collins P.; Deevi S.V.; Favier R.; Kostadima M.; Lambert M.P.; Mathias M.; Millar C.M.; Peerlinck K.; Perry D.J.; Schulman S.; Whitehorn D.; Wittevrongel C.; De Maeyer M.; Rendon A.; Gomez K.; Erber W.N.; Mumford A.D.; Nurden P.; Stirrups K.; Bradley J.R.; Raymond F.L.; Laffan M.A.; Van Geet C.; Richardson S.; Freson K.; Ouwehand W.H.;
Sci. Transl. Med. 8:328RA30-328RA30(2016)
Cited for: PHOSPHORYLATION AT TYR-419 AND TYR-530; INVOLVEMENT IN THC6; VARIANT THC6 LYS-527; CHARACTERIZATION OF VARIANT THC6 LYS-527;
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.