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Protein

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

Gene

Gne

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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 (By similarity). Sialylation is implicated in cell adhesion, signal transduction, tumorigenicity and metastatic behavior of malignant cells. Plays an essential role in early development.By similarity1 Publication

Catalytic activityi

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

Enzyme regulationi

Allosterically regulated; 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; the hexamer is fully active for both enzyme activities (By similarity). Up-regulated after PKC-dependent phosphorylation.By similarity

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei477 – 4771SubstrateBy similarity
Binding sitei489 – 4891SubstrateBy similarity
Active sitei517 – 5171By similarity
Binding sitei517 – 5171SubstrateBy similarity
Binding sitei566 – 5661SubstrateBy similarity
Metal bindingi569 – 5691ZincBy similarity
Binding sitei569 – 5691SubstrateBy similarity
Metal bindingi579 – 5791ZincBy similarity
Metal bindingi581 – 5811ZincBy similarity
Metal bindingi586 – 5861ZincBy similarity
Binding sitei588 – 5881SubstrateBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi411 – 42010ATPBy similarity
Nucleotide bindingi543 – 55210ATPBy similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. catalytic activity Source: MGI
  3. hydrolase activity, hydrolyzing O-glycosyl compounds Source: InterPro
  4. metal ion binding Source: UniProtKB-KW
  5. N-acylmannosamine kinase activity Source: UniProtKB-EC

GO - Biological processi

  1. N-acetylglucosamine biosynthetic process Source: UniProtKB-UniPathway
  2. N-acetylneuraminate metabolic process Source: MGI
  3. UDP-N-acetylglucosamine metabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Kinase, Transferase

Keywords - Ligandi

ATP-binding, Metal-binding, Nucleotide-binding, Zinc

Enzyme and pathway databases

BRENDAi2.7.1.60. 3474.
3.2.1.183. 3474.
ReactomeiREACT_310546. Sialic acid metabolism.
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, Uae1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 4

Organism-specific databases

MGIiMGI:1354951. Gne.

Subcellular locationi

  1. Cytoplasm By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 722722Bifunctional UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinasePRO_0000095717Add
BLAST

Post-translational modificationi

Phosphorylated by PKC.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ91WG8.
PaxDbiQ91WG8.
PRIDEiQ91WG8.

PTM databases

PhosphoSiteiQ91WG8.

Expressioni

Tissue specificityi

Widely expressed. Highest expression in liver. Also found at high levels in lung, brain and kidney.1 Publication

Developmental stagei

In the embryo, expressed at day E7, E11 and E15.1 Publication

Gene expression databases

BgeeiQ91WG8.
CleanExiMM_GNE.
ExpressionAtlasiQ91WG8. baseline and differential.
GenevestigatoriQ91WG8.

Interactioni

Subunit structurei

Homodimer and homohexamer.By similarity

Protein-protein interaction databases

IntActiQ91WG8. 1 interaction.
MINTiMINT-1869927.

Structurei

3D structure databases

SMRiQ91WG8. Positions 9-376, 406-717.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – ?UDP-N-acetylglucosamine 2-epimerase
Regioni406 – 722317N-acetylmannosamine kinaseBy similarityAdd
BLAST

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

eggNOGiCOG0381.
GeneTreeiENSGT00390000017246.
HOGENOMiHOG000008254.
HOVERGENiHBG051733.
InParanoidiQ91WG8.
KOiK12409.

Family and domain databases

InterProiIPR001312. Hexokinase.
IPR000600. ROK.
IPR020004. UDP-GlcNAc_Epase.
IPR003331. UDP_GlcNAc_Epimerase_2.
[Graphical view]
PfamiPF02350. Epimerase_2. 1 hit.
PF00480. ROK. 1 hit.
[Graphical view]
PRINTSiPR00475. HEXOKINASE.
TIGRFAMsiTIGR03568. NeuC_NnaA. 1 hit.

Sequencei

Sequence statusi: Complete.

Q91WG8-1 [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 LASHYIHIVK DVIRQQALSS VQDVDVVVSD
710 720
LVDPALLGAA SMVLDYTTRR IH
Length:722
Mass (Da):79,199
Last modified:December 1, 2001 - v1
Checksum:i0DFDD681BFD17984
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti566 – 5672EL → DV in CAB36908 (PubMed:10103025).Curated
Sequence conflicti623 – 6231G → V in CAB36908 (PubMed:10103025).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ132236 mRNA. Translation: CAB36908.1.
BC015277 mRNA. Translation: AAH15277.1.
BC051254 mRNA. Translation: AAH51254.1.
AK033507 mRNA. Translation: BAC28328.1.
AK033691 mRNA. Translation: BAC28432.1.
CCDSiCCDS51170.1.
RefSeqiNP_001177343.1. NM_001190414.1.
NP_056643.3. NM_015828.3.
UniGeneiMm.256718.

Genome annotation databases

EnsembliENSMUST00000102936; ENSMUSP00000100000; ENSMUSG00000028479.
GeneIDi50798.
KEGGimmu:50798.
UCSCiuc008srm.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ132236 mRNA. Translation: CAB36908.1.
BC015277 mRNA. Translation: AAH15277.1.
BC051254 mRNA. Translation: AAH51254.1.
AK033507 mRNA. Translation: BAC28328.1.
AK033691 mRNA. Translation: BAC28432.1.
CCDSiCCDS51170.1.
RefSeqiNP_001177343.1. NM_001190414.1.
NP_056643.3. NM_015828.3.
UniGeneiMm.256718.

3D structure databases

SMRiQ91WG8. Positions 9-376, 406-717.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ91WG8. 1 interaction.
MINTiMINT-1869927.

PTM databases

PhosphoSiteiQ91WG8.

Proteomic databases

MaxQBiQ91WG8.
PaxDbiQ91WG8.
PRIDEiQ91WG8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000102936; ENSMUSP00000100000; ENSMUSG00000028479.
GeneIDi50798.
KEGGimmu:50798.
UCSCiuc008srm.2. mouse.

Organism-specific databases

CTDi10020.
MGIiMGI:1354951. Gne.

Phylogenomic databases

eggNOGiCOG0381.
GeneTreeiENSGT00390000017246.
HOGENOMiHOG000008254.
HOVERGENiHBG051733.
InParanoidiQ91WG8.
KOiK12409.

Enzyme and pathway databases

UniPathwayiUPA00630.
BRENDAi2.7.1.60. 3474.
3.2.1.183. 3474.
ReactomeiREACT_310546. Sialic acid metabolism.

Miscellaneous databases

ChiTaRSiGne. mouse.
NextBioi307809.
PROiQ91WG8.
SOURCEiSearch...

Gene expression databases

BgeeiQ91WG8.
CleanExiMM_GNE.
ExpressionAtlasiQ91WG8. baseline and differential.
GenevestigatoriQ91WG8.

Family and domain databases

InterProiIPR001312. Hexokinase.
IPR000600. ROK.
IPR020004. UDP-GlcNAc_Epase.
IPR003331. UDP_GlcNAc_Epimerase_2.
[Graphical view]
PfamiPF02350. Epimerase_2. 1 hit.
PF00480. ROK. 1 hit.
[Graphical view]
PRINTSiPR00475. HEXOKINASE.
TIGRFAMsiTIGR03568. NeuC_NnaA. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Tissue expression and amino acid sequence of murine UDP-N-acetylglucosamine-2-epimerase/N-acetylmannosamine kinase."
    Horstkorte R., Noehring S., Wiechens N., Schwarzkopf M., Danker K., Reutter W., Lucka L.
    Eur. J. Biochem. 260:923-927(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
    Strain: BALB/c.
    Tissue: Liver.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: FVB/N.
    Tissue: Colon.
  3. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 572-722.
    Strain: C57BL/6J.
    Tissue: Colon.
  4. "Protein kinase C phosphorylates and regulates UDP-N-acetylglucosamine-2-epimerase/N-acetylmannosamine kinase."
    Horstkorte R., Noehring S., Danker K., Effertz K., Reutter W., Lucka L.
    FEBS Lett. 470:315-318(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION.
  5. Cited for: FUNCTION.

Entry informationi

Entry nameiGLCNE_MOUSE
AccessioniPrimary (citable) accession number: Q91WG8
Secondary accession number(s): Q8CC83, Q8CCB0, Q9Z0P6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 15, 2004
Last sequence update: December 1, 2001
Last modified: April 1, 2015
This is version 112 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Allosteric enzyme, Complete proteome, Multifunctional enzyme, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.