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UniProtKB/Swiss-Prot Q8N371: Variant p.Glu302Asp

Bifunctional peptidase and arginyl-hydroxylase JMJD5
Gene: KDM8
Variant information

Variant position:  302
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 Glutamate (E) to Aspartate (D) at position 302 (E302D, p.Glu302Asp).
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 acidic.
The physico-chemical property of the reference and variant residues and the change implicated.

BLOSUM score:  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

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

Sequence information

Variant position:  302
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Protein sequence length:  416
The length of the canonical sequence.

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.







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.

Chain 1 – 416 Bifunctional peptidase and arginyl-hydroxylase JMJD5
Domain 271 – 416 JmjC
Metal binding 321 – 321 Iron; catalytic
Binding site 318 – 318 2-oxoglutarate
Binding site 318 – 318 N(omega)-methyl-L-arginine and symmetrical N(omega),N'(omega)-dimethyl-L-arginine binding; via carbonyl oxygen
Binding site 321 – 321 2-oxoglutarate
Alternative sequence 167 – 362 Missing. In isoform 2.
Mutagenesis 310 – 310 W -> A. Loss of L-arginyl 3-hydroxylase activity toward RPS6.
Mutagenesis 321 – 321 H -> A. Loss of H3K36me2 demethylase activity.
Mutagenesis 321 – 321 H -> A. Loss of L-arginyl 3-hydroxylase activity toward RPS6. Loss of peptidase activity toward methylated histones; when associated with A-323 and A-400. No effect on its regulatory function on the circadian clock or CRY1 stability.
Helix 302 – 304

Literature citations

No reference for the current variant in UniProtKB/Swiss-Prot.

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.