N-acetyl-D-glucosamine kinase (NAGK)
The protein contains 344 amino acids for an estimated molecular weight of 37376 Da.
Converts endogenous N-acetylglucosamine (GlcNAc), a major component of complex carbohydrates, from lysosomal degradation or nutritional sources into GlcNAc 6-phosphate. Involved in the N-glycolylneuraminic acid (Neu5Gc) degradation pathway: although human is not able to catalyze formation of Neu5Gc due to the inactive CMAHP enzyme, Neu5Gc is present in food and must be degraded. Also has ManNAc kinase activity. (updated: March 4, 2015)
Protein identification was indicated in the following studies:
- Goodman and co-workers. (2013) The proteomics and interactomics of human erythrocytes. Exp Biol Med (Maywood) 238(5), 509-518.
- Lange and co-workers. (2014) Annotating N termini for the human proteome project: N termini and Nα-acetylation status differentiate stable cleaved protein species from degradation remnants in the human erythrocyte proteome. J Proteome Res. 13(4), 2028-2044.
- Hegedűs and co-workers. (2015) Inconsistencies in the red blood cell membrane proteome analysis: generation of a database for research and diagnostic applications. Database (Oxford) 1-8.
- D'Alessandro and co-workers. (2017) Red blood cell proteomics update: is there more to discover? Blood Transfus. 15(2), 182-187.
Methods
The following articles were analysed to gather the proteome content of erythrocytes.
The gene or protein list provided in the studies were processed using the ID mapping API of Uniprot in September 2018. The number of proteins identified and mapped without ambiguity in these studies is indicated below.
Only Swiss-Prot entries (reviewed) were considered for protein evidence assignation.
| Publication | Identification 1 | Uniprot mapping 2 | Not mapped / Obsolete | TrEMBL | Swiss-Prot |
|---|---|---|---|---|---|
| Goodman (2013) | 2289 (gene list) | 2278 | 53 | 20599 | 2269 |
| Lange (2014) | 1234 | 1234 | 7 | 28 | 1224 |
| Hegedus (2015) | 2638 | 2622 | 0 | 235 | 2387 |
| Wilson (2016) | 1658 | 1528 | 170 | 291 | 1068 |
| d'Alessandro (2017) | 1826 | 1817 | 2 | 0 | 1815 |
| Bryk (2017) | 2090 | 2060 | 10 | 108 | 1942 |
| Chu (2018) | 1853 | 1804 | 55 | 362 | 1387 |
1 as available in the article and/or in supplementary material
2 uniprot mapping returns all protein isoforms as one entry
The compilation of older studies can be retrieved from the Red Blood Cell Collection database.
The data and differentiation stages presented below come from the proteomic study and analysis performed by our partners of the GReX consortium, more details are available in their published work.
(right-click above to access to more options from the contextual menu)
| Variant | Description |
|---|---|
| dbSNP:rs17856147 | |
| dbSNP:rs17849984 |
Biological Process
Carbohydrate phosphorylation
N-acetylglucosamine metabolic process
N-acetylmannosamine metabolic process
N-acetylneuraminate catabolic process
UDP-N-acetylglucosamine biosynthetic process
Molecular Function
ATP binding
N-acetylglucosamine kinase activity
N-acylmannosamine kinase activity
The reference OMIM entry for this protein is 606828
N-acetylglucosamine kinase; nagk
Glcnac kinase; gnk
DESCRIPTION
N-acetylglucosamine kinase (NAGK; EC 2.7.1.59) converts endogenous N-acetylglucosamine (GlcNAc), a major component of complex carbohydrates, from lysosomal degradation or nutritional sources into GlcNAc 6-phosphate. NAGK belongs to the group of N-acetylhexosamine kinases and is a prominent salvage enzyme of amino sugar metabolism in mammals.CLONING
Using the mouse Nagk sequence to search the human EST database, Hinderlich et al. (2000) obtained a complete cDNA encoding NAGK. The predicted 344-amino acid NAGK protein contains the 5 sequence motifs necessary for the binding of ATP by sugar kinases. NAGK shares 91.6% amino acid similarity with mouse Nagk. Using Northern blot analysis, Hinderlich et al. (2000) detected a 1.35-kb NAGK transcript in all tissues and cancer cell lines tested. They detected enzyme activity in all mouse tissues examined, with highest enzymatic activity in testis.GENE FUNCTION
Hinderlich et al. (2000) functionally expressed murine Nagk in E. coli and detected GlcNAc kinase activity as well as ManNAc kinase activity. They hypothesized that NAGK has a general role in the catabolic pathways of GlcNAc as well as of ManNAc.MAPPING
The International Radiation Hybrid Mapping Consortium mapped the NAGK gene to chromosome 2 (TMAP A006G04). ... More on the omim web site
Feb. 2, 2018: Protein entry updated
Automatic update: Uniprot description updated
Dec. 19, 2017: Protein entry updated
Automatic update: Uniprot description updated
Nov. 23, 2017: Protein entry updated
Automatic update: Uniprot description updated
March 16, 2016: Protein entry updated
Automatic update: OMIM entry 606828 was added.
Jan. 28, 2016: Protein entry updated
Automatic update: model status changed
Jan. 24, 2016: Protein entry updated
Automatic update: model status changed