GNE
entrez
10020
canonical
uniprot
Q9Y223
canonical
ensembl
ENSG00000159921
resolver
ensp
ENSP00000379839
resolver
ensp
ENSP00000414760
resolver
ensp
ENSP00000437765
resolver
ensp
ENSP00000445117
resolver
ensp
ENSP00000494141
resolver
ensp
ENSP00000759172
resolver
enst
ENST00000543356
resolver
genesymbol
GNE
resolver
genesymbol_syn
GLCNE
resolver
genesymbol_syn
IBM2
resolver
hgnc
HGNC:23657
resolver
uniprot
A0A7I2SU25
resolver
uniprot
A6PZH2
resolver
uniprot
A6PZH3
resolver
uniprot
A7UNU7
resolver
uniprot
B2R6E1
resolver
uniprot
B7Z372
resolver
uniprot
B7Z428
resolver
uniprot
D3DRP7
resolver
uniprot
F5H499
resolver
uniprot
H0YFA7
resolver
uniprot
Q0VA94
resolver
uniprot_entry
A0A7I2SU25_HUMAN
resolver
uniprot_entry
GLCNE_HUMAN
resolver
uniprot_sec
A6PZH2
resolver
uniprot_sec
A6PZH3
resolver
uniprot_sec
A7UNU7
resolver
uniprot_sec
B2R6E1
resolver
uniprot_sec
B7Z372
resolver
uniprot_sec
B7Z428
resolver
uniprot_sec
D3DRP7
resolver
uniprot_sec
F5H499
resolver
uniprot_sec
H0YFA7
resolver
uniprot_sec
Q0VA94
resolver
activity_regulation
ACTIVITY REGULATION: The UDP-N-acetylglucosamine 2-epimerase activity, in contrast to the N-acetylmannosamine kinase activity, exhibits allosteric regulation by cytidine monophosphate-N-acetylneuraminic acid (CMP-Neu5Ac), the end product of neuraminic acid biosynthesis (PubMed:26980148, PubMed:2808337). Moreover, the activity is contingent upon the oligomeric state of the enzyme. The monomeric form is inactive, while the dimeric form selectively catalyzes the phosphorylation of N-acetylmannosamine. The hexameric form, on the other hand, demonstrates full proficiency in both enzyme activities (By similarity). Furthermore, the UDP-N-acetylglucosamine 2-epimerase activity is increased by PKC-mediated phosphorylation (By similarity). {ECO:0000250|UniProtKB:O35826, ECO:0000250|UniProtKB:Q91WG8, ECO:0000269|PubMed:26980148, ECO:0000269|PubMed:2808337}.
uniprot
proteins
amino_acid_sequence
MEKNGNNRKLRVCVATCNRADYSKLAPIMFGIKTEPEFFELDVVVLGSHLIDDYGNTYRMIEQDDFDINTRLHTIVRGEDEAAMVESVGLALVKLPDVLNRLKPDIMIVHGDRFDALALATSAALMNIRILHIEGGEVSGTIDDSIRHAITKLAHYHVCCTRSAEQHLISMCEDHDRILLAGCPSYDKLLSAKNKDYMSIIRMWLGDDVKSKDYIVALQHPVTTDIKHSIKMFELTLDALISFNKRTLVLFPNIDAGSKEMVRVMRKKGIEHHPNFRAVKHVPFDQFIQLVAHAGCMIGNSSCGVREVGAFGTPVINLGTRQIGRETGENVLHVRDADTQDKILQALHLQFGKQYPCSKIYGDGNAVPRILKFLKSIDLQEPLQKKFCFPPVKENISQDIDHILETLSALAVDLGGTNLRVAIVSMKGEIVKKYTQFNPKTYEERINLILQMCVEAAAEAVKLNCRILGVGISTGGRVNPREGIVLHSTKLIQEWNSVDLRTPLSDTLHLPVWVDNDGNCAALAERKFGQGKGLENFVTLITGTGIGGGIIHQHELIHGSSFCAAELGHLVVSLDGPDCSCGSHGCIEAYASGMALQREAKKLHDEDLLLVEGMSVPKDEAVGALHLIQAAKLGNAKAQSILRTAGTALGLGVVNILHTMNPSLVILSGVLASHYIHIVKDVIRQQALSSVQDVDVVVSDLVDPALLGAASMVLDYTTRRIY
uniprot
proteins
disease_involvement
DISEASE: Sialuria (SIALURIA) [MIM:269921]: In sialuria, free sialic acid accumulates in the cytoplasm and gram quantities of neuraminic acid are secreted in the urine. The metabolic defect involves lack of feedback inhibition of UDP-GlcNAc 2-epimerase by CMP-Neu5Ac, resulting in constitutive overproduction of free Neu5Ac. Clinical features include variable degrees of developmental delay, coarse facial features and hepatomegaly. Sialuria inheritance is autosomal dominant. {ECO:0000269|PubMed:10330343, ECO:0000269|PubMed:10356312, ECO:0000269|PubMed:11326336, ECO:0000269|PubMed:2808337}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Nonaka myopathy (NM) [MIM:605820]: An autosomal recessive myopathy characterized by early adult onset and progressive distal muscle weakness that preferentially affects the anterior tibial muscles, usually sparing the quadriceps femoris. Some individuals may have involvement of the upper limbs or proximal muscles. Muscle biopsy reveals presence of rimmed vacuoles. {ECO:0000269|PubMed:11528398, ECO:0000269|PubMed:11916006, ECO:0000269|PubMed:12177386, ECO:0000269|PubMed:12325084, ECO:0000269|PubMed:12409274, ECO:0000269|PubMed:12473753, ECO:0000269|PubMed:12473769, ECO:0000269|PubMed:12473780, ECO:0000269|PubMed:12497639, ECO:0000269|PubMed:12811782, ECO:0000269|PubMed:12913203, ECO:0000269|PubMed:14707127, ECO:0000269|PubMed:15146476, ECO:0000269|PubMed:16503651}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Thrombocytopenia 12 with or without myopathy (THC12) [MIM:620757]: A form of thrombocytopenia, a hematologic disorder defined by a decrease in the number of platelets in circulating blood, resulting in the potential for increased bleeding and decreased ability for clotting. THC12 is an autosomal recessive form manifesting from infancy or early childhood with bleeding episodes. Clinical features include petechiae, easy bruising, epistaxis, hematomas, menorrhagia, and increased bleeding after trauma or surgery. Rare patients may have thrombocytopenia without bleeding. Some affected individuals have myopathic features, usually apparent in the second or third decades of life. {ECO:0000269|PubMed:25257349, ECO:0000269|PubMed:30171045, ECO:0000269|PubMed:33198675, ECO:0000269|PubMed:34788986, ECO:0000269|PubMed:34858435, ECO:0000269|PubMed:35052006, ECO:0000269|PubMed:38237079}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
ec_number
2.7.1.60
uniprot
proteins
ec_number
3.2.1.183
uniprot
proteins
function
FUNCTION: Bifunctional enzyme that possesses both UDP-N-acetylglucosamine 2-epimerase and N-acetylmannosamine kinase activities, and serves as the initiator of the biosynthetic pathway leading to the production of N-acetylneuraminic acid (NeuAc), a critical precursor in the synthesis of sialic acids. By catalyzing this pivotal and rate-limiting step in sialic acid biosynthesis, this enzyme assumes a pivotal role in governing the regulation of cell surface sialylation, playing a role in embryonic angiogenesis (PubMed:10334995, PubMed:11326336, PubMed:14707127, PubMed:16503651, PubMed:2808337, PubMed:38237079). Sialic acids represent a category of negatively charged sugars that reside on the surface of cells as terminal components of glycoconjugates and mediate important functions in various cellular processes, including cell adhesion, signal transduction, and cellular recognition (PubMed:10334995, PubMed:14707127). {ECO:0000269|PubMed:10334995, ECO:0000269|PubMed:11326336, ECO:0000269|PubMed:14707127, ECO:0000269|PubMed:16503651, ECO:0000269|PubMed:2808337, ECO:0000269|PubMed:38237079}.
uniprot
proteins
mass_dalton
79275
uniprot
proteins
mutagenesis
MUTAGEN 517; /note="D->A,N: Loss of N-acylmannosamine kinase activity. Decreased affinity for N-acyl-D-mannosamine. No effect on structure."; /evidence="ECO:0000269|PubMed:22343627
uniprot
proteins
pathway_participation
PATHWAY: Amino-sugar metabolism; N-acetylneuraminate biosynthesis. {ECO:0000269|PubMed:14707127, ECO:0000269|PubMed:16503651}.
uniprot
proteins
post_translational_modification
PTM: Phosphorylated. Phosphorylation by PKC activates the UDP-N-acetylglucosamine 2-epimerase activity. {ECO:0000250|UniProtKB:Q91WG8}.
uniprot
proteins
protein_family
UDP-N-acetylglucosamine 2-epimerase family; ROK (NagC/XylR) family
uniprot
proteins
pubmed
10330343
uniprot
proteins
pubmed
10334995
uniprot
proteins
pubmed
10356312
uniprot
proteins
pubmed
10431835
uniprot
proteins
pubmed
11326336
uniprot
proteins
pubmed
11528398
uniprot
proteins
pubmed
11916006
uniprot
proteins
pubmed
12177386
uniprot
proteins
pubmed
12325084
uniprot
proteins
pubmed
12409274
uniprot
proteins
pubmed
12473753
uniprot
proteins
pubmed
12473769
uniprot
proteins
pubmed
12473780
uniprot
proteins
pubmed
12497639
uniprot
proteins
pubmed
12811782
uniprot
proteins
pubmed
12913203
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
14707127
uniprot
proteins
pubmed
15146476
uniprot
proteins
pubmed
15164053
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16503651
uniprot
proteins
pubmed
17597614
uniprot
proteins
pubmed
19841673
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
22343627
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
25257349
uniprot
proteins
pubmed
26980148
uniprot
proteins
pubmed
2808337
uniprot
proteins
pubmed
30171045
uniprot
proteins
pubmed
33198675
uniprot
proteins
pubmed
34788986
uniprot
proteins
pubmed
34858435
uniprot
proteins
pubmed
35052006
uniprot
proteins
pubmed
38237079
uniprot
proteins
sequence_length
722
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:O35826}.
uniprot
proteins