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Information on EC 2.7.1.60 - N-acylmannosamine kinase and Organism(s) Homo sapiens and UniProt Accession Q9Y223
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2.7.1.60 N-acylmannosamine kinaseIUBMB Comments
Acts on the acetyl and glycolyl derivatives.
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Word Map
- 2.7.1.60
-
sialic
- myopathy
-
n-acetylneuraminic
-
2.7.1.59
-
sialylation
- glycoconjugates
-
rimmed
-
n-acetylmannosamine-6-phosphate
- n-acetyl-d-glucosamine
- glucokinase
-
nanks
-
aminosugars
- neu5ac
- medicine
- molecular biology
The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Synonyms
n-acetylmannosamine kinase, udp-n-acetylglucosamine-2-epimerase/n-acetylmannosamine-kinase, udp-glcnac 2-epimerase/mannac 6-kinase, n-acyl-d-mannosamine kinase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
acetylamidodeoxymannokinase
-
-
-
-
acetylmannosamine kinase
-
-
-
-
acylaminodeoxymannokinase
-
-
-
-
acylmannosamine kinase
-
-
-
-
acylmannosamine kinase (phosphorylating)
-
-
-
-
ATP:N-acetylmannosamine 6-phosphotransferase
-
-
-
-
GNE
MNK
N-acetylmannosamine kinase
N-acyl-D-mannosamine kinase
-
-
-
-
UDP-GlcNAc 2-epimerase/ManNAc kinase
UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase
GNE
bifunctional enzyme with UDP-N-acetylglucosamine 2-epimerase and N-acetylmannosamine kinase activities
N-acetylmannosamine kinase
-
-
-
-
N-acetylmannosamine kinase
bifunctional enzyme: UDP-N-acetylglucosamine 2-epimerase /N-acetylmannosamine kinase
UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase
-
two different enzyme activities combined in a single bifunctional enzyme
UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase
-
UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase
two different enzyme activities combined in a single bifunctional enzyme
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phospho group transfer
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -
SYSTEMATIC NAME
IUBMB Comments
ATP:N-acyl-D-mannosamine 6-phosphotransferase
Acts on the acetyl and glycolyl derivatives.
CAS REGISTRY NUMBER
COMMENTARY
9027-53-6
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + N-acetyl-D-mannosamine
ADP + N-acetyl-D-mannosamine-6-phosphate
-
-
-
?
ATP + N-acetyl-D-mannosamine
ADP + N-acetyl-D-mannosamine 6-phosphate
-
-
-
?
ATP + N-acetyl-D-mannosamine
ADP + N-acetyl-D-mannosamine 6-phosphate
-
-
-
-
?
ATP + N-acetyl-D-mannosamine
ADP + N-acetyl-D-mannosamine 6-phosphate
-
-
-
?
ATP + N-acyl-D-mannosamine
ADP + N-acyl-D-mannosamine 6-phosphate
-
-
-
-
?
ATP + N-acyl-D-mannosamine
ADP + N-acyl-D-mannosamine 6-phosphate
-
-
-
?
ATP + N-acyl-D-mannosamine
ADP + N-acyl-D-mannosamine 6-phosphate
-
-
-
?
ATP + N-acyl-D-mannosamine
ADP + N-acyl-D-mannosamine 6-phosphate
-
key and rate limiting enzyme in the synthesis of N-acetylneuraminic acid and therefore of nearly all other sialic acids, enzyme mutations can cause hereditary inclusion body myopathy
-
-
?
ATP + N-acyl-D-mannosamine
ADP + N-acyl-D-mannosamine 6-phosphate
-
key enzyme in the synthesis of N-acetylneuraminic acid and therefore of nearly all other sialic acids, essential for early embryonic development, enzyme involved in several genetic disorders such as sialuria, hereditary inclusion body myopathy, and Nonaka myopathy
-
-
?
ATP + N-acyl-D-mannosamine
ADP + N-acyl-D-mannosamine 6-phosphate
key enzyme in the synthesis of N-acetylneuraminic acid and therefore of nearly all other sialic acids, mutations in the enzyme causes hereditary inclusion body myopathy
-
-
?
ATP + N-acyl-D-mannosamine
ADP + N-acyl-D-mannosamine 6-phosphate
-
key enzyme in the synthesis of N-acetylneuraminic acid and therefore of nearly all other sialic acids, reduced activity causes distal myopathy with rimmed vacuoles
-
-
?
additional information
?
-
UDP-GlcNAc 2-epimerase and ManNAc kinase are parts of one bifunctional enzyme, catalyzes the first 2 steps in N-acetylneuraminic acid biosynthesis
-
-
?
additional information
?
-
isoform GNE2 displays an extended N-terminus compared with isoform GNE, which is linked directly to the epimerase domain. Recombinant GNE2 still possesses both enzymatic activities of GNE
-
-
?
additional information
?
-
isoform GNE3 displays an deleted N-terminus compared with isoform GNE. Recombinant GNE3 shows a total loss of the epimerase activity
-
-
?
additional information
?
-
the enzyme is a bifunctional enzyme uridine diphosphate 1-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase, i.e. UDP-GlcNAc 2-epimerase/ManNAc kinase or GNE. The N-terminal domain carries out UDP-GlcNAc epimerase function, whereas the C-terminal domain is responsible for ManNAc kinase activity
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + N-acetyl-D-mannosamine
ADP + N-acetyl-D-mannosamine 6-phosphate
-
-
-
?
additional information
?
-
the enzyme is a bifunctional enzyme uridine diphosphate 1-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase, i.e. UDP-GlcNAc 2-epimerase/ManNAc kinase or GNE. The N-terminal domain carries out UDP-GlcNAc epimerase function, whereas the C-terminal domain is responsible for ManNAc kinase activity
-
-
?
ATP + N-acyl-D-mannosamine
ADP + N-acyl-D-mannosamine 6-phosphate
-
-
-
-
?
ATP + N-acyl-D-mannosamine
ADP + N-acyl-D-mannosamine 6-phosphate
-
-
-
?
ATP + N-acyl-D-mannosamine
ADP + N-acyl-D-mannosamine 6-phosphate
-
-
-
?
ATP + N-acyl-D-mannosamine
ADP + N-acyl-D-mannosamine 6-phosphate
-
key and rate limiting enzyme in the synthesis of N-acetylneuraminic acid and therefore of nearly all other sialic acids, enzyme mutations can cause hereditary inclusion body myopathy
-
-
?
ATP + N-acyl-D-mannosamine
ADP + N-acyl-D-mannosamine 6-phosphate
-
key enzyme in the synthesis of N-acetylneuraminic acid and therefore of nearly all other sialic acids, essential for early embryonic development, enzyme involved in several genetic disorders such as sialuria, hereditary inclusion body myopathy, and Nonaka myopathy
-
-
?
ATP + N-acyl-D-mannosamine
ADP + N-acyl-D-mannosamine 6-phosphate
key enzyme in the synthesis of N-acetylneuraminic acid and therefore of nearly all other sialic acids, mutations in the enzyme causes hereditary inclusion body myopathy
-
-
?
ATP + N-acyl-D-mannosamine
ADP + N-acyl-D-mannosamine 6-phosphate
-
key enzyme in the synthesis of N-acetylneuraminic acid and therefore of nearly all other sialic acids, reduced activity causes distal myopathy with rimmed vacuoles
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
Mg2+
required, Mg2+ is octahedrically coordinated with the beta-phosphate-O3 atom and Asp-413-Odelta2 in the axial positions, whereas four water molecules occupy the equatorial sites
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(2Z)-1-(4-chlorophenyl)-3-(2-hydroxy-5-nitrophenyl)-2-(1H-1,2,4-triazol-1-yl)prop-2-en-1-one
-
FMP-209613
(2Z)-3-(4-fluorophenyl)-1-(4-methylphenyl)-2-(1H-1,2,4-triazol-1-yl)prop-2-en-1-one
-
FMP-209617
1,3-dimethyl-4-(trifluoromethyl)-1,7-dihydro-6H-pyrazolo[3,4-b]pyridin-6-one
-
-
4-(trifluoromethyl)pyridine-2-carboxylic acid
-
also named 4-(trifluoromethyl)picolinic acid
5-(anthracen-9-ylmethylidene)-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
-
FMP-402534
7-nitro-10-(3-nitrophenyl)pyrimido[4,5-b]quinoline-2,4(3H,10H)-dione
-
FMP-200208
N-[4-[(E)-(3,5-dioxo-1-phenylpyrazolidin-4-ylidene)methyl]phenyl]acetamide
-
FMP-100705
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.011
(2Z)-1-(4-chlorophenyl)-3-(2-hydroxy-5-nitrophenyl)-2-(1H-1,2,4-triazol-1-yl)prop-2-en-1-one
Homo sapiens
-
at pH 8.0 and 37°C
2.5
1,3-dimethyl-4-(trifluoromethyl)-1,7-dihydro-6H-pyrazolo[3,4-b]pyridin-6-one
Homo sapiens
-
IC50 above 2.5 mM, at pH 8.0 and 37°C
0.4
1,6-dimethyl-2-oxo-4-(trifluoromethyl)-1,2-dihydropyridine-3-carbonitrile
Homo sapiens
-
at pH 8.0 and 37°C
0.0072
2,3-bis[(2-hydroxyethyl)sulfanyl]naphthalene-1,4-dione
Homo sapiens
-
at pH 8.0 and 37°C
2.5
2-ethyl-4-(trifluoromethyl)-2,7-dihydro-6H-pyrazolo[3,4-b]pyridin-6-one
Homo sapiens
-
IC50 above 2.5 mM, at pH 8.0 and 37°C
2.5
2-hydroxy-6-propyl-4-(trifluoromethyl)pyridine-3-carbonitrile
Homo sapiens
-
IC50 above 2.5 mM, at pH 8.0 and 37°C
0.9
2-methoxy-4-(trifluoromethyl)pyridine-3-carboxylic acid
Homo sapiens
-
at pH 8.0 and 37°C
0.0006
5-(anthracen-9-ylmethylidene)-2-thioxodihydropyrimidine-4,6(1H,5H)-dione
Homo sapiens
-
at pH 8.0 and 37°C
2.5
5-(cyanomethyl)pyridine-2-carboxylic acid
Homo sapiens
-
IC50 above 2.5 mM, at pH 8.0 and 37°C
2.5
6-cyclopropyl-4-(trifluoromethyl)-1H-pyrazolo[3,4-b]pyridin-3-amine
Homo sapiens
-
IC50 above 2.5 mM, at pH 8.0 and 37°C
0.0004
N-[4-[(E)-(3,5-dioxo-1-phenylpyrazolidin-4-ylidene)methyl]phenyl]acetamide
Homo sapiens
-
at pH 8.0 and 37°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
hereditary inclusion body myopathy patients carrying M712T mutation and healthy donors
UniProt
human cell lines promyeolytic leukaemia HL-60, HeLa S3, chronic myelogenous leukaemia K-562, lymphoblastic leukaemia MOLT-4, Burkitt's lymphoma Raji, colorectal adenocarcinoma SW480, lung carcinoma A549 and melanoma G361
UniProt
isoform 2; bifunctional UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase, isoform GNE2
UniProt
isoform 3; bifunctional UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase, isoform GNE3
UniProt
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
physiological function
GNE exerts transcriptional control on genes related to endoplasmic reticulum stress. Association of low GNE activity and anoikis susceptibility
additional information
epimerase enzymatic activity of isozymes GNE3 and GNE8 is likely absent, since the deleted fragment contains important substrate binding residues in homologous bacterial epimerases. Isozymes hGNE5-hGNE8 have a 53-residue deletion, which is assigned a role in substrate(UDP-GlcNAc) binding
malfunction
all cases of hereditary inclusion body myopathy and distal myopathy with rimmed vacuoles are caused by mutations
malfunction
mutations cause sialurea or inclusion body myopathy/Nonaka myopathy
malfunction
enzyme mutations can cause sialuria and hereditary inclusion body myopathy. Sialuria patients have a heterozygous missense mutation affecting the allosteric site of GNE, leading to loss of feedback inhibition of GNE-epimerase activity by CMP-Neu5Ac, resulting in excessive sialic acid production. HIBM and its allelic Japanese disorder, distal myopathy with rimmed vacuoles, or DMRV, is an autosomal recessive neuromuscular disorder of adult onset, characterized byslowly progressive muscle weakness and atrophy
malfunction
heterozygous UDP-GlcNAc 2-epimerase and N-acetylmannosamine kinase domain mutations in the GNE gene result in a less severe GNE myopathy phenotype compared to homozygous N-acetylmannosamine kinase domain mutations, screening study of mutant individuals, genotypes of the GNE myopathy patient population and phenotypes, overview
malfunction
silencing of GNE sensitizes pancreatic cancer cells to anoikis, an apoptosis program activated on loss of matrix anchorage. A loss of GNE enzyme activity in cells renders them anoikis-susceptible after transfection with the tumor suppressor p16. ManNAc incubation reduces anoikis susceptibility, phenotype, overview. Enzyme up-regulation occurs predominantly in pancreatic cancer but also in other malignancies
malfunction
-
stable knock-down of UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase in HEK-293 cells dramatically increases incorporation of N-acetylmannosamine analogues into glycoproteins of HEK-293 cells
malfunction
enzyme mutation affects beta1-integrin-mediated cell adhesion process
metabolism
UDP-GlcNAc 2-epimerase/ManNAc kinase (GNE) catalyzes the first two committed steps in sialic acid synthesis
metabolism
-
UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase is the key enzyme in the sialic acid biosynthetic pathway
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). GLCNE_HUMAN
722
0
79275
Swiss-Prot
other Location (Reliability: 5)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
79000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hexamer
homodimer
additional information
homodimer
kinase domain: in solution, with small populations of monomer and higher-order oligomer in equilibrium with the dimer, gel filtration
additional information
bifunctional UDP-N-acetylglucosamine-2-epimerase/N-acetylmannosamine kinase interacts with alpha-actinin 1, the non-muscle form of alpha-actinin, which is expressed in skeletal muscle
additional information
the GNE enzyme consists of two enzymatic domains, sequence comparisons, secondary structures, and modeling of isozymes hGNE1-hGNE8, hGNE2 and hGNE7 display a 31-residue N-terminal extension compared to hGNE1. hGNE3 and hGNE8 contain a 55 residue N-terminal deletion, and a 50-residue N-terminal extension compared to hGNE1
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ManNAc kinase in complex with its substrate ManNAc, its product ManNAc 6-phosphate, with or without ADP, vapor diffusion at 18°C, mixing 0.002 ml of 15 mg/ml protein in 10 mM Tris-HCl, pH 8.0, 150 mM NaCl, and 2 mM ManNAc, with 0.002 ml of reservoir solution containing 0.2 M calcium acetate, 0.1 M sodiumcacodylate, pH 6.5, and 40% PEG 300, 5 days, X-ray diffraction structure determination and analysis at 1.64-2.10 A resolution. No crystals by co-crystallization of hMNK with ManNAc and ADP, ATP, AMPPCP, or AMPPNP, but ternary complexes are obtained by soaking crystals of the binary hMNK-ManNAc complex replacing stepwise their mother liquor with solutions containing 0.1 M sodium cacodylate, pH 6.5, 50% PEG 300, and 20 mM ADPor ATP or nonhydrolyzable ATP derivatives
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
A630T
A631V
C13S
D176V
G576R
the mutation is associated with distal myopathy with rimmed vacuoles
M712T
M743T
the mutation, which is associated with GNE myopathy, has a 10fold lower binding affinity to alpha-actinin 2 than the intact enzyme
V572L
additional information
A630T
homozygous mutant of the N-acetylmannose kinase domain, involved in GNE myopathy
C13S
the mutation is associated with distal myopathy with rimmed vacuoles
D176V
the mutation leads to impaired N-acetylmannosamine kinase activity (40.58% of wild type activity)
M712T
homozygous mutant of the N-acetylmannose kinase domain, involved in GNE myopathy
V572L
homozygous mutant of the N-acetylmannose kinase domain, involved in GNE myopathy
V572L
the mutation leads to impaired N-acetylmannosamine kinase activity (15.9% of wild type activity)
additional information
-
different mutations found in patients with distal myopathy with rimmed vacuoles, D378Y, V331A, D177C, D176V, H132Q and C13S in the epimerase domain are mostly without effect on the kinase activity, V572L, A524V, I472T, A630T, A631V, and G708S in the kinase domain some of which causes a dramatic decrease of kinase activity, some of the mutations affects both activities
additional information
-
naturally occurring mutations in patients with hereditary inclusion body myopathy, mutations G135V, V216A, R246W, A631V, and M217T identified, mutations severely affect both activities of the bifunctional enzyme
additional information
homozygote and heterozygte mutants of the epimerase and the kinase domains of the enzyme, respectively, overview
additional information
-
stable knock-down of UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase in HEK-293 cells by RNAi dramatically increases incorporation of N-acetylmannosamine analogues into glycoproteins of HEK-293 cells. HEK293 cells transfected with sh68- and sh70-shRNA almost completely loose GNE mRNA expression, while other shRNAs are less effective. Peanut agglutinin, recognizing asialo structures, reveals a 3-4fold higher binding affinity to GNE knock-down cells compared to controls
additional information
the enzyme is silenced or overexpressed in human pancreatic carcinoma cells, gene expression profiling, enzymatic activity, transcriptions levels, and cell cycle analysis, overview
additional information
-
the enzyme is silenced or overexpressed in human pancreatic carcinoma cells, gene expression profiling, enzymatic activity, transcriptions levels, and cell cycle analysis, overview
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cDNA cloned and sequenced, expressed in Escherichia coli HB101 or INValphaF'
cloning of isozymes hGNE1-hGNE8, DNA and amino acid sequence determination and analysis, quantitative real-time PCR expression analysis and sequence comparisons
expression of GFP-tagged enzyme in HEK-293 cells, the expression is efficiently blocked by sh70-shRNA, sh68 has no effect on GNE protein expression because its target sequence at the 3'-UTR is not present in the GFP-hGNE vector construct
-
His-tag, kinase domain expressed in Escherichia coli BL21(D3) CodonPlus-RIL
wild type an mutated proteins expressed as Myc-tag fusion proteins in COS-7 cells
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
GNE up-regulation occurs predominantly in pancreatic cancer but also in other malignancies
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
molecular biology
-
GNE-deficient cells, with dramatically increased incorporation of N-acetylmannosamine analogues into glycoproteins, can efficiently be decorated with reactive functional groups, which can be employed in bioorthogonal functionalization strategies for fluorescence labelling or biotinylation
medicine
clinical relevance of the enzyme in the basic defect in sialuria
medicine
no siginificant difference in the binding kinetics of alpha-activin 1 with either wild-type or mutant UDP-N-acetylglucosamine-2-epimerase/N-acetylmannosamine kinase involved in hereditary inclusion body myopathy
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Hinderlich, S.; Berger, M.; Schwarzkopf, M.; Effertz, K.; Reutter, W.
Molecular cloning and characterization of murine and human N-acetylglucosamine kinase
Eur. J. Biochem.
267
3301-3308
2000
Homo sapiens, Mus musculus
Zeitler, R.; Giannis, A.; Danneschewski, S.; Henk, E.; Henk, T.; Bauer, C.; Reutter, W.; Sandhoff, K.
Inhibition of N-acetylglucosamine kinase and N-acetylmannosamine kinase by 3-O-methyl-N-acetyl-D-glucosamine in vitro
Eur. J. Biochem.
204
1165-1168
1992
Homo sapiens, Rattus norvegicus, Rattus norvegicus Wistar
Lucka, L.; Krause, M.; Danker, K.; Reutter, W.; Horstkorte, R.
Primary structure and expression analysis of human UDP-N-acetyl-glucosamine-2-epimerase/N-acetylmannosamine kinase, the bifunctional enzyme in neuraminic acid biosynthesis
FEBS Lett.
454
341-344
1999
Homo sapiens (Q9Y223)
Krause, S.; Hinderlich, S.; Amsili, S.; Horstkorte, R.; Wiendl, H.; Argov, Z.; Mitrani-Rosenbaum, S.; Lochmueller, H.
Localization of UDP-GlcNAc 2-epimerase/ManAc kinase (GNE) in the Golgi complex and the nucleus of mammalian cells
Exp. Cell Res.
304
365-379
2005
Homo sapiens, Mus musculus
Hinderlich, S.; Salama, I.; Eisenberg, I.; Potikha, T.; Mantey, L.R.; Yarema, K.J.; Horstkorte, R.; Argov, Z.; Sadeh, M.; Reutter, W.; Mitrani-Rosenbaum, S.
The homozygous M712T mutation of UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase results in reduced enzyme activities but not in altered overall cellular sialylation in hereditary inclusion body myopathy
FEBS Lett.
566
105-109
2004
Homo sapiens (Q9Y223), Homo sapiens
Sparks, S.E.; Ciccone, C.; Lalor, M.; Orvisky, E.; Klootwijk, R.; Savelkoul, P.J.; Dalakas, M.C.; Krasnewich, D.M.; Gahl, W.A.; Huizing, M.
Use of a cell-free system to determine UDP-N-acetylglucosamine 2-epimerase and N-acetylmannosamine kinase activities in human hereditary inclusion body myopathy
Glycobiology
15
1102-1110
2005
Homo sapiens
Noguchi, S.; Keira, Y.; Murayama, K.; Ogawa, M.; Fujita, M.; Kawahara, G.; Oya, Y.; Imazawa, M.; Goto, Y.I.; Hayashi, Y.K.; Nonaka, I.; Nishino, I.
Reduction of UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase activity and sialylation in distal myopathy with rimmed vacuoles
J. Biol. Chem.
279
11402-11407
2004
Homo sapiens
Penner, J.; Mantey, L.R.; Elgavish, S.; Ghaderi, D.; Cirak, S.; Berger, M.; Krause, S.; Lucka, L.; Voit, T.; Mitrani-Rosenbaum, S.; Hinderlich, S.
Influence of UDP-GlcNAc 2-epimerase/ManNAc kinase mutant proteins on hereditary inclusion body myopathy
Biochemistry
45
2968-2977
2006
Homo sapiens
Reinke, S.O.; Hinderlich, S.
Prediction of three different isoforms of the human UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase
FEBS Lett.
581
3327-3331
2007
Homo sapiens (Q9Y223)
Wang, Z.; Sun, Z.; Li, A.V.; Yarema, K.J.
Roles for UDP-GlcNAc 2-epimerase/ManNAc 6-kinase outside of sialic acid biosynthesis: modulation of sialyltransferase and BiP expression, GM3 and GD3 biosynthesis, proliferation, and apoptosis, and ERK1/2 phosphorylation
J. Biol. Chem.
281
27016-27028
2006
Homo sapiens
Amsili, S.; Zer, H.; Hinderlich, S.; Krause, S.; Becker-Cohen, M.; MacArthur, D.G.; North, K.N.; Mitrani-Rosenbaum, S.
UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase (GNE) binds to alpha-actinin 1: novel pathways in skeletal muscle?
PLoS ONE
3
e2477
2008
Homo sapiens (Q9Y223)
Ishihara, S.; Tomimitsu, H.; Fujigasaki, H.; Saito, F.; Mizusawa, H.
UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase in nuclei and rimmed vacuoles of muscle fibers in DMRV (distal myopathy with rimmed vacuoles)
J. Med. Dent. Sci.
55
181-187
2008
Homo sapiens (Q9Y223)
Tong, Y.; Tempel, W.; Nedyalkova, L.; Mackenzie, F.; Park, H.W.
Crystal structure of the N-acetylmannosamine kinase domain of GNE
PLoS ONE
4
e7165
2009
Homo sapiens (Q9Y223), Homo sapiens
Moeller, H.; Boehrsch, V.; Lucka, L.; Hackenberger, C.P.; Hinderlich, S.
Efficient metabolic oligosaccharide engineering of glycoproteins by UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase (GNE) knock-down
Mol. Biosyst.
7
2245-2251
2011
Homo sapiens
Yardeni, T.; Choekyi, T.; Jacobs, K.; Ciccone, C.; Patzel, K.; Anikster, Y.; Gahl, W.A.; Kurochkina, N.; Huizing, M.
Identification, tissue distribution, and molecular modeling of novel human isoforms of the key enzyme in sialic acid synthesis, UDP-GlcNAc 2-epimerase/ManNAc kinase
Biochemistry
50
8914-8925
2011
Homo sapiens (Q9Y223)
Kemmner, W.; Kessel, P.; Sanchez-Ruderisch, H.; Moeller, H.; Hinderlich, S.; Schlag, P.M.; Detjen, K.
Loss of UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase (GNE) induces apoptotic processes in pancreatic carcinoma cells
FASEB J.
26
938-946
2012
Homo sapiens (Q9Y223), Homo sapiens
Martinez, J.; Nguyen, L.; Hinderlich, S.; Zimmer, R.; Tauberger, E.; Reutter, W.; Saenger, W.; Fan, H.; Moniot, S.
Crystal structures of N-acetylmannosamine kinase provide insights into enzyme activity and inhibition
J. Biol. Chem.
287
13656-13665
2012
Homo sapiens (Q9Y223), Homo sapiens
Mori-Yoshimura, M.; Monma, K.; Suzuki, N.; Aoki, M.; Kumamoto, T.; Tanaka, K.; Tomimitsu, H.; Nakano, S.; Sonoo, M.; Shimizu, J.; Sugie, K.; Nakamura, H.; Oya, Y.; Hayashi, Y.K.; Malicdan, M.C.; Noguchi, S.; Murata, M.; Nishino, I.
Heterozygous UDP-GlcNAc 2-epimerase and N-acetylmannosamine kinase domain mutations in the GNE gene result in a less severe GNE myopathy phenotype compared to homozygous N-acetylmannosamine kinase domain mutations
J. Neurol. Sci.
318
100-105
2012
Homo sapiens (Q9Y223)
Grover, S.; Arya, R.
Role of UDP-N-acetylglucosamine2-epimerase/N-acetylmannosamine kinase (GNE) in beta1-integrin-mediated cell adhesion
Mol. Neurobiol.
50
257-273
2014
Homo sapiens (Q9Y223)
Harazi, A.; Becker-Cohen, M.; Zer, H.; Moshel, O.; Hinderlich, S.; Mitrani-Rosenbaum, S.
The interaction of UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase (GNE) and alpha-actinin 2 is altered in GNE myopathy M743T mutant
Mol. Neurobiol.
54
2928-2938
2017
Homo sapiens (Q9Y223)
Liu, N.; Wang, Z.K.; Wang, H.X.; Li, Y.; Niu, Z.H.; Yu, X.F.
Muscle biopsy and UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase gene mutation analysis in two Chinese patients with distal myopathy with rimmed vacuoles
NeuroReport
26
598-601
2015
Homo sapiens (Q9Y223)
Hinderlich, S.; Weidemann, W.; Yardeni, T.; Horstkorte, R.; Huizing, M.
UDP-GlcNAc 2-epimerase/ManNAc kinase (GNE): A master regulator of sialic acid synthesis
Top. Curr. Chem.
366
97-138
2015
Homo sapiens (Q9Y223)
-
Aretz, J.; Wratil, P.; Wamhoff, E.; Nguyen, H.; Reutter, W.; Rademacher, C.
Fragment screening of N-acetylmannosamine kinase reveals noncarbohydrate inhibitors
Can. J. Chem.
94
920-926
2016
Homo sapiens
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