UniProtKB/Swiss-Prot Q8NB16: Variant p.Thr364Met

Mixed lineage kinase domain-like protein
Gene: MLKL
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Variant information Variant position:

364 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Type of variant:

LB/B 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:

From Threonine (T) to Methionine (M) at position 364 (T364M, p.Thr364Met). 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:

Change from medium size and polar (T) to medium size and hydrophobic (M) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score:

-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
Other resources:

Links to websites of interest for the variant.

Variant rs34389205 [ dbSNP | Ensembl ]

Sequence information Variant position:

364 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length:

471 The length of the canonical sequence.
Location on the sequence:

QVKLAGFELRKTQTSMSLGT T REKTDRVKSTAYLSPQELED 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                         QVKLAGFELRKTQTSMSLGTTREKTDRVKSTAYLSPQELED

Mouse                         QVKLAGFELSKTQNSISRTAKSTKAERSSSTIYVSPERLKN

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
Chain	1 – 471	Mixed lineage kinase domain-like protein
Domain	194 – 469	Protein kinase
Modified residue	357 – 357	Phosphothreonine; by RIPK3
Modified residue	358 – 358	Phosphoserine; by RIPK3
Modified residue	360 – 360	Phosphoserine; by RIPK3
Alternative sequence	206 – 413	Missing. In isoform 2.
Mutagenesis	351 – 351	E -> K. Binds ATP with an enhanced affinity.
Mutagenesis	357 – 357	T -> A. No effect. Abolishes ability to mediate necroptosis; when associated with A-358.
Mutagenesis	358 – 358	S -> A. No effect. Abolishes ability to mediate necroptosis; when associated with A-357.

Literature citations
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.;
Nature 446:153-158(2007)
Cited for: VARIANTS [LARGE SCALE ANALYSIS] THR-52; GLU-100; PRO-132; GLN-146; LEU-169; PRO-291; MET-364; ILE-398 AND HIS-421;

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.