Gne
entrez
114711
canonical
uniprot
O35826
canonical
ensembl
ENSRNOG00000014365
resolver
ensembl
ENSRNOG00055020776
resolver
ensembl
ENSRNOG00060004446
resolver
ensembl
ENSRNOG00065010137
resolver
ensp
ENSRNOP00000019532
resolver
ensp
ENSRNOP00000074334
resolver
ensp
ENSRNOP00000083164
resolver
ensp
ENSRNOP00055028775
resolver
ensp
ENSRNOP00060005686
resolver
ensp
ENSRNOP00065012414
resolver
enst
ENSRNOT00000019532
resolver
enst
ENSRNOT00000090490
resolver
enst
ENSRNOT00055035487
resolver
enst
ENSRNOT00060007528
resolver
enst
ENSRNOT00065016357
resolver
genesymbol
Gne
resolver
genesymbol_syn
Glcne
resolver
uniprot
A0A0G2K7T2
resolver
uniprot_entry
A0A0G2K7T2_RAT
resolver
uniprot_entry
GLCNE_RAT
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:9305887). 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 (PubMed:9305887). Furthermore, the UDP-N-acetylglucosamine 2-epimerase activity is increased by PKC-mediated phosphorylation (By similarity). {ECO:0000250|UniProtKB:Q91WG8, ECO:0000269|PubMed:9305887}.
uniprot
proteins
amino_acid_sequence
MEKNGNNRKLRVCVATCNRADYSKLAPIMFGIKTEPAFFELDVVVLGSHLIDDYGNTYRMIEQDDFDINTRLHTIVRGEDEAAMVESVGLALVKLPDVLNRLKPDIMIVHGDRFDALALATSAALMNIRILHIEGGEVSGTIDDSIRHAITKLAHYHVCCTRSAEQHLISMCEDHDRILLAGCPSYDKLLSAKNKDYMSIIRMWLGDDVKCKDYIVALQHPVTTDIKHSIKMFELTLDALISFNKRTLVLFPNIDAGSKEMVRVMRKKGIEHHPNFRAVKHVPFDQFIQLVAHAGCMIGNSSCGVREVGAFGTPVINLGTRQIGRETGENVLHVRDADTQDKILQALHLQFGKQYPCSKIYGDGNAVPRILKFLKSIDLQEPLQKKFCFPPVKENISQDIDHILETLSALAVDLGGTNLRVAIVSMKGEIVKKYTQFNPKTYEERISLILQMCVEAAAEAVKLNCRILGVGISTGGRVNPQEGVVLHSTKLIQEWNSVDLRTPLSDTLHLPVWVDNDGNCAAMAERKFGQGKGQENFVTLITGTGIGGGIIHQHELIHGSSFCAAELGHLVVSLDGPDCSCGSHGCIEAYASGMALQREAKKLHDEDLLLVEGMSVPKDEAVGALHLIQAAKLGNVKAQSILRTAGTALGLGVVNILHTMNPSLVILSGVLASHYIHIVRDVIRQQALSSVQDVDVVVSDLVDPALLGAASMVLDYTTRRIH
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 (PubMed:10497249, PubMed:9305887, PubMed:9305888). 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). {ECO:0000269|PubMed:10334995, ECO:0000269|PubMed:10497249, ECO:0000269|PubMed:9305887, ECO:0000269|PubMed:9305888}.
uniprot
proteins
mass_dalton
79227
uniprot
proteins
mutagenesis
MUTAGEN 49; /note="H->A: Loss UDP-N-acetylglucosamine 2-epimerase activity. No effect on N-acylmannosamine kinase activity. Does not interfere with enzyme oligomerization."; /evidence="ECO:0000269|PubMed:10497249"; MUTAGEN 110; /note="H->A: Loss UDP-N-acetylglucosamine 2-epimerase activity. No effect on N-acylmannosamine kinase activity. Partial reduction of the dimerization process."; /evidence="ECO:0000269|PubMed:10497249"; MUTAGEN 132; /note="H->A: Loss UDP-N-acetylglucosamine 2-epimerase activity. No effect on N-acylmannosamine kinase activity. Partial reduction of the dimerization process."; /evidence="ECO:0000269|PubMed:10497249"; MUTAGEN 155; /note="H->A: Loss UDP-N-acetylglucosamine 2-epimerase activity. No effect on N-acylmannosamine kinase activity. Strong reduction of the dimerization process."; /evidence="ECO:0000269|PubMed:10497249"; MUTAGEN 157; /note="H->A: Loss UDP-N-acetylglucosamine 2-epimerase activity. No effect on N-acylmannosamine kinase activity. Strong reduction of the dimerization process."; /evidence="ECO:0000269|PubMed:10497249"; MUTAGEN 413; /note="D->K,N: No effect on UDP-N-acetylglucosamine 2-epimerase activity. Does not affect feedback inhibition by CMP-Neu5Ac. Loss of N-acylmannosamine kinase activity. Does not interfere with oligomerization."; /evidence="ECO:0000269|PubMed:10497249"; MUTAGEN 420; /note="R->M: No effect on UDP-N-acetylglucosamine 2-epimerase activity. Does not affect feedback inhibition by CMP-Neu5Ac. Loss of N-acylmannosamine kinase activity. Does not interfere with oligomerization."; /evidence="ECO:0000269|PubMed:10497249
uniprot
proteins
pathway_participation
PATHWAY: Amino-sugar metabolism; N-acetylneuraminate biosynthesis. {ECO:0000269|PubMed:10497249, ECO:0000269|PubMed:9305887, ECO:0000269|PubMed:9305888}.
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
10103025
uniprot
proteins
pubmed
10334995
uniprot
proteins
pubmed
10497249
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
9305887
uniprot
proteins
pubmed
9305888
uniprot
proteins
sequence_length
722
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:9305887, ECO:0000269|PubMed:9305888}.
uniprot
proteins