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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot Q6N021: Variant p.Cys1396Trp

Methylcytosine dioxygenase TET2
Gene: TET2
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Variant information Variant position: help 1396 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Type of variant: help US 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 Cysteine (C) to Tryptophan (W) at position 1396 (C1396W, p.Cys1396Trp). 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 polar (C) to large size and aromatic (W) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help -2 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 a myelodysplastic syndrome. Any additional useful information about the variant.


Sequence information Variant position: help 1396 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 2002 The length of the canonical sequence.
Location on the sequence: help DFCAHAHRDLHNMQNGSTLV C TLTREDNREFGGKPEDEQLH 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                         DFCAHAHRDLHNMQNGSTLVCTLTREDNREFGGKPEDEQLH

Mouse                         DFSAHSHRDQQNMPNGSTVVVTLNREDNREVGAKPEDEQFH

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 – 2002 Methylcytosine dioxygenase TET2
Binding site 1380 – 1380
Binding site 1382 – 1382
Binding site 1384 – 1384
Binding site 1387 – 1387
Binding site 1416 – 1416
Alternative sequence 1166 – 2002 Missing. In isoform 2.
Alternative sequence 1195 – 2002 Missing. In isoform 3.
Mutagenesis 1382 – 1382 H -> Y. Loss of enzyme activity. Still able to enhance histone H2B GlcNAcylation by OGT; when associated with A-1384. Loss of enzyme activity; when associated with V-1384.
Mutagenesis 1384 – 1384 D -> A. Loss of enzyme activity. Still able to enhance histone H2B GlcNAcylation by OGT; when associated with Y-1382.
Mutagenesis 1384 – 1384 D -> V. Loss of enzyme activity; when associated with Y-1382.
Mutagenesis 1387 – 1387 N -> A. Near loss of enzyme activity.
Beta strand 1393 – 1399



Literature citations
Acquired mutations in TET2 are common in myelodysplastic syndromes.
Langemeijer S.M.C.; Kuiper R.P.; Berends M.; Knops R.; Aslanyan M.G.; Massop M.; Stevens-Linders E.; van Hoogen P.; van Kessel A.G.; Raymakers R.A.P.; Kamping E.J.; Verhoef G.E.; Verburgh E.; Hagemeijer A.; Vandenberghe P.; de Witte T.; van der Reijden B.A.; Jansen J.H.;
Nat. Genet. 41:838-842(2009)
Cited for: INVOLVEMENT IN MDS; FUNCTION; TISSUE SPECIFICITY; VARIANTS ARG-29; PHE-34; HIS-123; MET-218; ASP-355; LEU-363; ARG-429; HIS-867; ARG-924; ARG-949; PRO-1084; TRP-1214; LEU-1261; PHE-1285 DEL; ARG-1291; TRP-1396; ARG-1398; ILE-1701; TRP-1721; SER-1723; VAL-1762; ARG-1778; THR-1873; ARG-1875; GLN-1881; SER-1896; 1911-LYS--LEU-1916 DEL; ASP-1913 AND LEU-1962;
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.