Home  |  Contact

UniProtKB/Swiss-Prot P19525: Variant p.Leu439Val

Interferon-induced, double-stranded RNA-activated protein kinase
Gene: EIF2AK2
Variant information

Variant position:  439
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Type of variant:  Unclassified
The variants are classified into three categories: Disease, Polymorphism and Unclassified.
  • Disease: Variants implicated in disease according to literature reports.
  • Polymorphism: Variants not reported to be implicated in disease.
  • Unclassified: Variants with uncertain implication in disease according to literature reports. Evidence against or in favor of a pathogenic role is limited and/or conflicting.

Residue change:  From Leucine (L) to Valine (V) at position 439 (L439V, p.Leu439Val).
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:  Similar physico-chemical property. Both residues are medium size and hydrophobic.
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

Variant description:  In a lung adenocarcinoma sample; somatic mutation.
Any additional useful information about the variant.



Sequence information

Variant position:  439
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Protein sequence length:  551
The length of the canonical sequence.

Location on the sequence:   NIFLVDTKQVKIGDFGLVTS  L KNDGKRTRSKGTLRYMSPEQ
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                         NIFLV----------------DTKQVK------IGDFGLVTSLKNDGK----------------RTRSKGTLRYMSPE--Q-

Mouse                         NIFLV----------------DERHIK------IGDFGLAT

Rat                           NIFLV----------------DEKHIK------IGDFGLAT

Fission yeast                 NIFLAKSLPEDRGSVPLISYNDKNDLKEYITPKIGDFGLVV

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.

TypePositionsDescription
Chain 2 – 551 Interferon-induced, double-stranded RNA-activated protein kinase
Domain 267 – 538 Protein kinase
Region 266 – 551 Interaction with TRAF5
Modified residue 446 – 446 Phosphothreonine; by autocatalysis
Modified residue 451 – 451 Phosphothreonine; by autocatalysis
Modified residue 456 – 456 Phosphoserine
Mutagenesis 446 – 446 T -> A. Significant loss of activity and impairs autophosphorylation of T-451.
Mutagenesis 451 – 451 T -> A. Loss of activity.
Beta strand 437 – 440


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] GLU-428; VAL-439 AND VAL-506;

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.