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Protein

Bifunctional UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase

Gene

Gne

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Regulates and initiates biosynthesis of N-acetylneuraminic acid (NeuAc), a precursor of sialic acids. Required for normal sialylation in hematopoietic cells. Sialylation is implicated in cell adhesion, signal transduction, tumorigenicity and metastatic behavior of malignant cells. Plays an essential role in early development (By similarity).By similarity

Catalytic activityi

UDP-N-acetyl-alpha-D-glucosamine + H2O = N-acetyl-D-mannosamine + UDP.1 Publication
ATP + N-acyl-D-mannosamine = ADP + N-acyl-D-mannosamine 6-phosphate.1 Publication

Enzyme regulationi

Allosterically regulated (By similarity); feedback inhibited by cytidine monophosphate-N-acetylneuraminic acid (CMP-Neu5Ac), the end product of neuraminic acid biosynthesis. Activity is dependent on oligomerization. The monomer is inactive, whereas the dimer catalyzes only the phosphorylation of N-acetylmannosamine, and the hexamer is fully active for both enzyme activities. Up-regulated after PKC-dependent phosphorylation.By similarity1 Publication

Pathwayi: N-acetylneuraminate biosynthesis

This protein is involved in the pathway N-acetylneuraminate biosynthesis, which is part of Amino-sugar metabolism.
View all proteins of this organism that are known to be involved in the pathway N-acetylneuraminate biosynthesis and in Amino-sugar metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei477SubstrateBy similarity1
Binding sitei489SubstrateBy similarity1
Active sitei517By similarity1
Binding sitei517SubstrateBy similarity1
Binding sitei566SubstrateBy similarity1
Metal bindingi569ZincBy similarity1
Binding sitei569SubstrateBy similarity1
Metal bindingi579ZincBy similarity1
Metal bindingi581ZincBy similarity1
Metal bindingi586ZincBy similarity1
Binding sitei588SubstrateBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi411 – 420ATPBy similarity10
Nucleotide bindingi543 – 552ATPBy similarity10

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionAllosteric enzyme, Hydrolase, Kinase, Multifunctional enzyme, Transferase
LigandATP-binding, Metal-binding, Nucleotide-binding, Zinc

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-14506
BRENDAi5.1.3.14 5301
ReactomeiR-RNO-4085001 Sialic acid metabolism
SABIO-RKiO35826
UniPathwayiUPA00630

Names & Taxonomyi

Protein namesi
Recommended name:
Bifunctional UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase
Alternative name(s):
UDP-GlcNAc-2-epimerase/ManAc kinase
Including the following 2 domains:
UDP-N-acetylglucosamine 2-epimerase (hydrolyzing) (EC:3.2.1.183)
Alternative name(s):
UDP-GlcNAc-2-epimerase
Uridine diphosphate-N-acetylglucosamine-2-epimerase
N-acetylmannosamine kinase (EC:2.7.1.60)
Alternative name(s):
ManAc kinase
Gene namesi
Name:Gne
Synonyms:Glcne
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 5

Organism-specific databases

RGDi69239 Gne

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi49H → A: Does not affect kinase activity; almost complete loss of epimerase activity; does not interfere with enzyme oligomerization. 1 Publication1
Mutagenesisi110H → A: Does not affect kinase activity; almost complete loss of epimerase activity; partial reduction of the dimerization process. 1 Publication1
Mutagenesisi132H → A: Does not affect kinase activity; almost complete loss of epimerase activity; partial reduction of the dimerization process. 1 Publication1
Mutagenesisi155H → A: Does not affect kinase activity; almost complete loss of epimerase activity; strong reduction of the dimerization process. 1 Publication1
Mutagenesisi157H → A: Does not affect kinase activity; almost complete loss of epimerase activity; strong reduction of the dimerization process. 1 Publication1
Mutagenesisi413D → K or N: Does not affect epimerase activity; does not affect feedback inhibition by CMP-Neu5Ac; almost complete loss of kinase activity; does not interfere with oligomerization. 1 Publication1
Mutagenesisi420R → M: Does not affect epimerase activity; does not affect feedback inhibition by CMP-Neu5Ac; almost complete loss of kinase activity; does not interfere with oligomerization. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000957181 – 722Bifunctional UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinaseAdd BLAST722

Post-translational modificationi

Phosphorylated by PKC.By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiO35826
PRIDEiO35826

PTM databases

iPTMnetiO35826
PhosphoSitePlusiO35826

Expressioni

Tissue specificityi

Widely expressed. Highest expression is observed in liver.2 Publications

Gene expression databases

BgeeiENSRNOG00000014365
ExpressionAtlasiO35826 baseline and differential
GenevisibleiO35826 RN

Interactioni

Subunit structurei

Homodimer and homohexamer.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
ZBTB16Q055162EBI-7109445,EBI-711925From Homo sapiens.

Protein-protein interaction databases

BioGridi250408, 5 interactors
IntActiO35826, 5 interactors
MINTiO35826
STRINGi10116.ENSRNOP00000019532

Structurei

3D structure databases

ProteinModelPortaliO35826
SMRiO35826
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – ?UDP-N-acetylglucosamine 2-epimerase
Regioni406 – 722N-acetylmannosamine kinaseBy similarityAdd BLAST317

Sequence similaritiesi

In the N-terminal section; belongs to the UDP-N-acetylglucosamine 2-epimerase family.Curated
In the C-terminal section; belongs to the ROK (NagC/XylR) family.Curated

Phylogenomic databases

eggNOGiENOG410IE3W Eukaryota
COG0381 LUCA
COG1940 LUCA
GeneTreeiENSGT00390000017246
HOGENOMiHOG000008254
HOVERGENiHBG051733
InParanoidiO35826
KOiK12409
PhylomeDBiO35826

Family and domain databases

CDDicd03786 GT1_UDP-GlcNAc_2-Epimerase, 1 hit
InterProiView protein in InterPro
IPR000600 ROK
IPR020004 UDP-GlcNAc_Epase
IPR003331 UDP_GlcNAc_Epimerase_2_dom
PANTHERiPTHR18964 PTHR18964, 1 hit
PfamiView protein in Pfam
PF02350 Epimerase_2, 1 hit
PF00480 ROK, 1 hit
TIGRFAMsiTIGR03568 NeuC_NnaA, 1 hit

Sequencei

Sequence statusi: Complete.

O35826-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEKNGNNRKL RVCVATCNRA DYSKLAPIMF GIKTEPAFFE LDVVVLGSHL
60 70 80 90 100
IDDYGNTYRM IEQDDFDINT RLHTIVRGED EAAMVESVGL ALVKLPDVLN
110 120 130 140 150
RLKPDIMIVH GDRFDALALA TSAALMNIRI LHIEGGEVSG TIDDSIRHAI
160 170 180 190 200
TKLAHYHVCC TRSAEQHLIS MCEDHDRILL AGCPSYDKLL SAKNKDYMSI
210 220 230 240 250
IRMWLGDDVK CKDYIVALQH PVTTDIKHSI KMFELTLDAL ISFNKRTLVL
260 270 280 290 300
FPNIDAGSKE MVRVMRKKGI EHHPNFRAVK HVPFDQFIQL VAHAGCMIGN
310 320 330 340 350
SSCGVREVGA FGTPVINLGT RQIGRETGEN VLHVRDADTQ DKILQALHLQ
360 370 380 390 400
FGKQYPCSKI YGDGNAVPRI LKFLKSIDLQ EPLQKKFCFP PVKENISQDI
410 420 430 440 450
DHILETLSAL AVDLGGTNLR VAIVSMKGEI VKKYTQFNPK TYEERISLIL
460 470 480 490 500
QMCVEAAAEA VKLNCRILGV GISTGGRVNP QEGVVLHSTK LIQEWNSVDL
510 520 530 540 550
RTPLSDTLHL PVWVDNDGNC AAMAERKFGQ GKGQENFVTL ITGTGIGGGI
560 570 580 590 600
IHQHELIHGS SFCAAELGHL VVSLDGPDCS CGSHGCIEAY ASGMALQREA
610 620 630 640 650
KKLHDEDLLL VEGMSVPKDE AVGALHLIQA AKLGNVKAQS ILRTAGTALG
660 670 680 690 700
LGVVNILHTM NPSLVILSGV LASHYIHIVR DVIRQQALSS VQDVDVVVSD
710 720
LVDPALLGAA SMVLDYTTRR IH
Length:722
Mass (Da):79,227
Last modified:January 1, 1998 - v1
Checksum:i0DFDC84E833C7984
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y07744 mRNA Translation: CAA69024.1
BC062011 mRNA Translation: AAH62011.1
RefSeqiNP_446217.1, NM_053765.2
XP_006238070.1, XM_006238008.1
XP_006238071.1, XM_006238009.3
UniGeneiRn.18753

Genome annotation databases

EnsembliENSRNOT00000019532; ENSRNOP00000019532; ENSRNOG00000014365
GeneIDi114711
KEGGirno:114711
UCSCiRGD:69239 rat

Similar proteinsi

Entry informationi

Entry nameiGLCNE_RAT
AccessioniPrimary (citable) accession number: O35826
Entry historyiIntegrated into UniProtKB/Swiss-Prot: March 15, 2004
Last sequence update: January 1, 1998
Last modified: March 28, 2018
This is version 128 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome
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Main funding by: National Institutes of Health