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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P47712: Variant p.Arg485His

Cytosolic phospholipase A2
Gene: PLA2G4A
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Variant information Variant position: help 485 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 Arginine (R) to Histidine (H) at position 485 (R485H, p.Arg485His). 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 large size and basic (R) to medium size and polar (H) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help 0 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 GURDP; uncertain significance. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 485 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 749 The length of the canonical sequence.
Location on the sequence: help IHRMIMALVSDSALFNTREG R AGKVHNFMLGLNLNTSYPLS 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                         IHRMIMALVSDSALFNTREGRAGKVHNFMLGLNLNTSYPLS

Mouse                         VHRMLMALVSDSALFNTREGRAGKVHNFMLGLNLNTSYPLS

Rat                           VHRMLMALVSDSALFNTREGRAGKEHNFMLGLNLNTSYPLS

Bovine                        VQRMLMALVSDSALFNTREGRAGKVHNFMLGLNLNTSYPMS

Rabbit                        VHRMLMALVSDSALFNTREGRAGKVHNFMLGLNLNTSYPLS

Horse                         VHRMLMALVSDSALFNTREGRAGKVHNFMLGLNLNTSYPLS

Chicken                       VQRMLMALVGDSALFNTREGRAGKVHNFMLGLNLNSCYPLS

Xenopus laevis                VQRMLMAILGDSAIFNTREGRAGKVHNFMLGLNLNTSYPYS

Xenopus tropicalis            VQRMLMALLGDSALFNTREGRAGKVHNFMLGLNLNTSYPYS

Zebrafish                     VQRMLTSIMGDTTLFTTREGRAGKVHNFMLGLNLNSTLPFS

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 – 749 Cytosolic phospholipase A2
Domain 140 – 740 PLA2c
Modified residue 505 – 505 Phosphoserine; by MAPK
Mutagenesis 488 – 488 K -> E. Impairs phosphoinositide-stimulated phospholipase A2 activity.
Mutagenesis 505 – 505 S -> A. Decreases agonist-stimulated release of arachidonic acid. Reduces phospholipase A2 activity; when associated with A-437; A-454 and A-727.



Literature citations
Inherited human cPLA(2alpha) deficiency is associated with impaired eicosanoid biosynthesis, small intestinal ulceration, and platelet dysfunction.
Adler D.H.; Cogan J.D.; Phillips J.A.; Schnetz-Boutaud N.; Milne G.L.; Iverson T.; Stein J.A.; Brenner D.A.; Morrow J.D.; Boutaud O.; Oates J.A.;
J. Clin. Invest. 118:2121-2131(2008)
Cited for: INVOLVEMENT IN GURDP; VARIANTS GURDP PRO-111 AND HIS-485; VARIANT LYS-651; FUNCTION; CATALYTIC ACTIVITY; PATHWAY;
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.