CMAH R310P - GET-Evidence

Note: This variant has not been sufficiently evaluated by a GET-Evidence editor.

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Curation:
Currentness:

CMAH R310P

(CMAH Arg310Pro)


Short summary

This is a pseudogene; variants are of no consequence.

Variant evidence
Computational -
Functional -
Case/Control -
Familial -
 
Clinical importance
Severity -
Treatability -
Penetrance -
 

Impact

Insufficiently evaluated not reviewed

(The "insufficiently evaluated" qualifier is assigned automatically based on the above evidence and importance scores.)

Inheritance pattern

unknown

Summary of published research, and additional commentary

 

Allele frequency

  • G @ chr6:25205276: 7.8% (10/128) in GET-Evidence
  • Frequency shown in summary reports: 7.8% (10/128)

Publications
 

Irie A, Koyama S, Kozutsumi Y, Kawasaki T, Suzuki A. The molecular basis for the absence of N-glycolylneuraminic acid in humans. J Biol Chem. 1998 Jun 19;273(25):15866-71. PubMed PMID: 9624188.

N-Glycolylneuraminic acid (NeuGc) is abundantly expressed in most mammals, but it is not detectable in humans. The expression of NeuGc is controlled by cytidine monophospho-N-acetylneuraminic acid (CMP-NeuAc) hydroxylase activity. We previously cloned a cDNA for mouse CMP-NeuAc hydroxylase and found that the human genome contains a homologue. We report here the molecular basis for the absence of NeuGc in humans. We cloned a cDNA for human CMP-NeuAc hydroxylase from a HeLa cell cDNA library. The cDNA encodes a 486-amino acid protein, and its deduced amino acid sequence lacks a domain corresponding to the N-terminal 104 amino acids of the mouse CMP-NeuAc hydroxylase protein, although the human protein is highly identical (93%) to the rest of the mouse hydroxylase protein. The N-terminal truncation of the human hydroxylase is caused by deletion of a 92-base pair-long exon in human genomic DNA. The human hydroxylase expressed in COS-7 cells exhibited no enzymatic activity, and a mouse hydroxylase mutant, which lacks the N-terminal domain, was also inactive. A chimera composed of the human hydroxylase and the N-terminal domain of the mouse hydroxylase displayed the enzyme activity. These results indicate that the human homologue of CMP-NeuAc hydroxylase is inactive because it lacks an N-terminal domain that is essential for enzyme activity. The absence of NeuGc in human glycoconjugates is due to a partial deletion in the gene that encodes CMP-NeuAc hydroxylase.

Genomes
 

 

 

 

 

 

 

hu604D39 - CGI sample GS00253-DNA_B02_200_37
het G @ chr6:25097298

 

 

 

huAE6220 - CGI sample GS00253-DNA_H01_200_37
het G @ chr6:25097298

 

GS06985 - var-GS06985-1100-36-ASM
het G @ chr6:25205277

 

GS18502 - var-GS18502-1100-36-ASM
het G @ chr6:25205277

 

GS18505 - var-GS18505-1100-36-ASM
het G @ chr6:25205277

 

GS18508 - var-GS18508-1100-36-ASM
het G @ chr6:25205277

 

GS19669 - var-GS19669-1100-36-ASM
het G @ chr6:25205277

 

GS19670 - var-GS19670-1100-36-ASM
het G @ chr6:25205277

 

GS19700 - var-GS19700-1100-36-ASM
het G @ chr6:25205277

 

Other external references
 

    dbSNP
  • rs1128827
    www.ncbi.nlm.nih.gov/projects/SNP/snp_ref.cgi

Other in silico analyses
 

  • NBLOSUM100 score = 5
  • GET-Evidence autoscore = 0

Edit history
 

Gene search

"GENE" or "GENE A123C":

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