CMAH V478A - GET-Evidence

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

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Curation:
Currentness:

CMAH V478A

(CMAH Val478Ala)


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 @ chr6:25192696: 83.6% (107/128) in GET-Evidence
  • Frequency shown in summary reports: 83.6% (107/128)

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
 

 

 

hu034DB1 - CGI sample GS00253-DNA_A02_200_37
hom G @ chr6:25084718

 

hu04FD18 - CGI sample GS00253-DNA_F01_200_37
hom G @ chr6:25084718

 

hu0D879F - CGI sample GS00253-DNA_G01_200_37
hom G @ chr6:25084718

 

 

 

 

 

 

 

 

 

 

 

 

 

hu43860C - CGI sample GS00253-DNA_A01_200_37
hom G @ chr6:25084718

 

 

 

hu604D39 - CGI sample GS00253-DNA_B02_200_37
het G @ chr6:25084718

 

 

hu728FFF - hu728FFF build 36 substitution variants
hom G @ chr6:25192697

 

 

 

 

 

 

hu9385BA - CGI sample GS00253-DNA_E01_200_37
hom G @ chr6:25084718

 

 

 

 

huAE6220 - CGI sample GS00253-DNA_H01_200_37
het G @ chr6:25084718

 

 

 

huBEDA0B - CGI sample GS00253-DNA_C01_200_37
hom G @ chr6:25084718

 

huC30901 - CGI sample GS00253-DNA_B01_200_37
hom G @ chr6:25084718

 

 

 

 

huE80E3D - CGI sample GS00253-DNA_D01_200_37
hom G @ chr6:25084718

 

 

 

GS06985 - var-GS06985-1100-36-ASM
hom G @ chr6:25192697

 

GS06994 - var-GS06994-1100-36-ASM
het G @ chr6:25192697

 

GS07357 - var-GS07357-1100-36-ASM
hom G @ chr6:25192697

 

GS10851 - var-GS10851-1100-36-ASM
hom G @ chr6:25192697

 

GS12004 - var-GS12004-1100-36-ASM
het G @ chr6:25192697

 

GS18501 - var-GS18501-1100-36-ASM
hom G @ chr6:25192697

 

GS18502 - var-GS18502-1100-36-ASM
het G @ chr6:25192697

 

GS18504 - var-GS18504-1100-36-ASM
het G @ chr6:25192697

 

GS18505 - var-GS18505-1100-36-ASM
het G @ chr6:25192697

 

GS18508 - var-GS18508-1100-36-ASM
hom G @ chr6:25192697

 

GS18517 - var-GS18517-1100-36-ASM
het G @ chr6:25192697

 

GS18526 - var-GS18526-1100-36-ASM
hom G @ chr6:25192697

 

GS18537 - var-GS18537-1100-36-ASM
het G @ chr6:25192697

 

GS18555 - var-GS18555-1100-36-ASM
hom G @ chr6:25192697

 

GS18558 - var-GS18558-1100-36-ASM
hom G @ chr6:25192697

 

GS18940 - var-GS18940-1100-36-ASM
hom G @ chr6:25192697

 

GS18942 - var-GS18942-1100-36-ASM
hom G @ chr6:25192697

 

GS18947 - var-GS18947-1100-36-ASM
hom G @ chr6:25192697

 

GS18956 - var-GS18956-1100-36-ASM
hom G @ chr6:25192697

 

GS19017 - var-GS19017-1100-36-ASM
het G @ chr6:25192697

 

GS19020 - var-GS19020-1100-36-ASM
hom G @ chr6:25192697

 

GS19025 - var-GS19025-1100-36-ASM
hom G @ chr6:25192697

 

GS19026 - var-GS19026-1100-36-ASM
hom G @ chr6:25192697

 

GS19238 - var-GS19238-1100-36-ASM
het G @ chr6:25192697

 

GS19239 - var-GS19239-1100-36-ASM
het G @ chr6:25192697

 

GS19240 - var-GS19240-1100-36-ASM
hom G @ chr6:25192697

 

GS19648 - var-GS19648-1100-36-ASM
hom G @ chr6:25192697

 

GS19649 - var-GS19649-1100-36-ASM
hom G @ chr6:25192697

 

GS19669 - var-GS19669-1100-36-ASM
het G @ chr6:25192697

 

GS19670 - var-GS19670-1100-36-ASM
hom G @ chr6:25192697

 

GS19700 - var-GS19700-1100-36-ASM
hom G @ chr6:25192697

 

GS19701 - var-GS19701-1100-36-ASM
hom G @ chr6:25192697

 

GS19703 - var-GS19703-1100-36-ASM
het G @ chr6:25192697

 

GS19704 - var-GS19704-1100-36-ASM
hom G @ chr6:25192697

 

GS19735 - var-GS19735-1100-36-ASM
hom G @ chr6:25192697

 

GS19834 - var-GS19834-1100-36-ASM
het G @ chr6:25192697

 

GS20502 - var-GS20502-1100-36-ASM
hom G @ chr6:25192697

 

GS20509 - var-GS20509-1100-36-ASM
het G @ chr6:25192697

 

GS21767 - var-GS21767-1100-36-ASM
hom G @ chr6:25192697

 

Other external references
 

    dbSNP
  • rs303006
    www.ncbi.nlm.nih.gov/projects/SNP/snp_ref.cgi

Other in silico analyses
 

  • NBLOSUM100 score = 2
  • GET-Evidence autoscore = 0

Edit history
 

Gene search

"GENE" or "GENE A123C":

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