Variant position: 706 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 798 The length of the canonical sequence.
Location on the sequence:
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: The multiple alignment of the region surrounding the variant against various orthologous sequences.
Human IDYTLSRLE-RDGIVVFCDVS MDEDLFTGDGDYQFDIYRLMK
Mouse IDYTLSRLE-RDGIVVFCDIS AEEDLFTGEGDYQFEIYRLM
Bovine IDYTLSRLE-RDGIVVFCDIS RDEDLFMGQGDYQFEIYRLM
Drosophila IDYTLSRVT-INDCCYFNDLS RDEELFQATGDYQYDVYRMM
Fission yeast IDFTLARASYSQGIISYNEFN -DPDLFNGVDDYQFDIYRLM
Sequence annotation in neighborhood: 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.
Type Positions Description
1 – 798 Serine/threonine-protein kinase haspin
484 – 798 Protein kinase
315 – 798 Missing. In isoform 2.
707 – 707 D -> L. Markedly reduced affinity for histone H3 and reduced histone H3 phosphorylation.
709 – 709 D -> N. Markedly reduced affinity for histone H3 and reduced histone H3 phosphorylation.
713 – 713 G -> F. Markedly reduced affinity for histone H3 and reduced histone H3 phosphorylation.
716 – 716 D -> L. Markedly reduced histone H3 phosphorylation.
Patterns of somatic mutation in human cancer genomes.
Greenman C.; Stephens P.; Smith R.; Dalgliesh G.L.; Hunter C.; Bignell G.; Davies H.; Teague J.; Butler A.; Stevens C.; Edkins S.; O'Meara S.; Vastrik I.; Schmidt E.E.; Avis T.; Barthorpe S.; Bhamra G.; Buck G.; Choudhury B.; Clements J.; Cole J.; Dicks E.; Forbes S.; Gray K.; Halliday K.; Harrison R.; Hills K.; Hinton J.; Jenkinson A.; Jones D.; Menzies A.; Mironenko T.; Perry J.; Raine K.; Richardson D.; Shepherd R.; Small A.; Tofts C.; Varian J.; Webb T.; West S.; Widaa S.; Yates A.; Cahill D.P.; Louis D.N.; Goldstraw P.; Nicholson A.G.; Brasseur F.; Looijenga L.; Weber B.L.; Chiew Y.-E.; DeFazio A.; Greaves M.F.; Green A.R.; Campbell P.; Birney E.; Easton D.F.; Chenevix-Trench G.; Tan M.-H.; Khoo S.K.; Teh B.T.; Yuen S.T.; Leung S.Y.; Wooster R.; Futreal P.A.; Stratton M.R.;
Cited for: VARIANTS [LARGE SCALE ANALYSIS] GLU-76; CYS-82; HIS-145; ASP-204; SER-283; LEU-301; THR-328; ALA-378 AND VAL-706;
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