Variant position: 2 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 2564 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 M KQLQPQ-PPPKMGDFYDPEHPT
Mouse M KPLPSQQPPPKMGDFYDPEHP
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 – 2564 Histone-lysine N-methyltransferase SETD2
Mutations in epigenetic regulators including SETD2 are gained during relapse in paediatric acute lymphoblastic leukaemia.
Mar B.G.; Bullinger L.B.; McLean K.M.; Grauman P.V.; Harris M.H.; Stevenson K.; Neuberg D.S.; Sinha A.U.; Sallan S.E.; Silverman L.B.; Kung A.L.; Lo Nigro L.; Ebert B.L.; Armstrong S.A.;
Nat. Commun. 5:3469-3469(2014)
Cited for: INVOLVEMENT IN ALL; VARIANTS ALL ARG-2; GLY-19; ILE-267; PRO-470; ALA-499; 794-TYR--GLU-2564 DEL; PRO-1076; GLY-1093; ALA-1171; GLY-1351; GLU-1365; 1416-GLU--GLU-2564 DEL; ASN-1453; PRO-1609; MET-1663; PRO-1821; ALA-1915; VAL-1920; SER-2361 AND 2546-LYS--GLU-2564 DEL;
Solution structure of the Set2-Rpb1 interacting domain of human Set2 and its interaction with the hyperphosphorylated C-terminal domain of Rpb1.
Li M.; Phatnani H.P.; Guan Z.; Sage H.; Greenleaf A.L.; Zhou P.;
Proc. Natl. Acad. Sci. U.S.A. 102:17636-17641(2005)
Cited for: STRUCTURE BY NMR OF 2457-2564; INTERACTION WITH POLR2A; MUTAGENESIS OF ARG-2475; LYS-2476; GLN-2480; PHE-2481; VAL-2483; LYS-2506; ARG-2510; HIS-2514; GLY-2515; GLU-2528 AND GLU-2531; CHARACTERIZATION OF VARIANT AML LEU-2505;
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