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UniProtKB/Swiss-Prot P54760: Variant p.Pro820Leu

Ephrin type-B receptor 4
Gene: EPHB4
Variant information

Variant position:  820
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Type of variant:  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:  From Proline (P) to Leucine (L) at position 820 (P820L, p.Pro820Leu).
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:  -3
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 CMAVM2; unknown pathological significance.
Any additional useful information about the variant.

Other resources:  
Links to websites of interest for the variant.



Sequence information

Variant position:  820
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Protein sequence length:  987
The length of the canonical sequence.

Location on the sequence:   ASDAWSYGIVMWEVMSFGER  P YWDMSNQDVINAIEQDYRLP
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                         ASDAWSYGIVMWEVMSFGERPYWDMSNQDVINAIEQDYRLP

Mouse                         ASDAWSYGIVMWEVMSFGERPYWDMSNQDVINAIEQDYRLP

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 16 – 987 Ephrin type-B receptor 4
Topological domain 561 – 987 Cytoplasmic
Domain 615 – 899 Protein kinase
Alternative sequence 307 – 987 Missing. In isoform 3.
Alternative sequence 415 – 987 Missing. In isoform 4.
Alternative sequence 517 – 987 Missing. In isoform 2.
Turn 820 – 823


Literature citations

Germline loss-of-function mutations in EPHB4 cause a second form of capillary malformation-arteriovenous malformation (CM-AVM2) deregulating RAS-MAPK signaling.
Amyere M.; Revencu N.; Helaers R.; Pairet E.; Baselga E.; Cordisco M.; Chung W.; Dubois J.; Lacour J.P.; Martorell L.; Mazereeuw-Hautier J.; Pyeritz R.E.; Amor D.J.; Bisdorff A.; Blei F.; Bombei H.; Dompmartin A.; Brooks D.; Dupont J.; Gonzalez-Ensenat M.A.; Frieden I.; Gerard M.; Kvarnung M.; Hanson-Kahn A.K.; Hudgins L.; Leaute-Labreze C.; McCuaig C.; Metry D.; Parent P.; Paul C.; Petit F.; Phan A.; Quere I.; Salhi A.; Turner A.; Vabres P.; Vicente A.; Wargon O.; Watanabe S.; Weibel L.; Wilson A.; Willing M.; Mulliken J.B.; Boon L.M.; Vikkula M.;
Circulation 136:1037-1048(2017)
Cited for: VARIANTS CMAVM2 LYS-59; PRO-74; TYR-115 DEL; 130-TRP--TYR-987 DEL; 161-VAL-LYS-162 DELINS LEU; PRO-187; 244-GLN--TYR-987 DEL; ARG-268; 352-ARG--TYR-987 DEL; 375-GLY--TYR-987 DEL; 431-ARG--TYR-987 DEL; GLY-469; ARG-516; 520-GLN--TYR-987 DEL; 596-TYR--TYR-987 DEL; TRP-656; LYS-664; THR-725; 739-ARG--TYR-987 DEL; ASP-745; ARG-789; SER-789; 806-TYR--TYR-987 DEL; ARG-807; LEU-820; THR-820; TRP-838; ARG-845; TYR-856; TRP-864 AND PRO-874; CHARACTERIZATION OF VARIANTS CMAVM2 LYS-664; TRP-838; ARG-845 AND TRP-864; INVOLVEMENT IN CMAVM2; SUBCELLULAR LOCATION;

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.