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Q91WG8

- GLCNE_MOUSE

UniProt

Q91WG8 - GLCNE_MOUSE

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Protein
Bifunctional UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase
Gene
Gne, Glcne, Uae1
Organism
Mus musculus (Mouse)
Status
Reviewed - 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.1 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.

Pathwayi

Sites

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

Regions

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

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. N-acylmannosamine kinase activity Source: UniProtKB-EC
  3. UDP-N-acetylglucosamine 2-epimerase activity Source: InterPro
  4. catalytic activity Source: MGI
  5. hydrolase activity Source: UniProtKB-KW
  6. metal ion binding Source: UniProtKB-KW
Complete GO annotation...

GO - Biological processi

  1. N-acetylglucosamine biosynthetic process Source: UniProtKB-UniPathway
  2. N-acetylneuraminate biosynthetic process Source: InterPro
  3. N-acetylneuraminate metabolic process Source: MGI
  4. UDP-N-acetylglucosamine metabolic process Source: InterPro
  5. lipopolysaccharide biosynthetic 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

ReactomeiREACT_202500. 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: Chromosome 4

Organism-specific databases

MGIiMGI:1354951. Gne.

Subcellular locationi

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 kinase
PRO_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

ArrayExpressiQ91WG8.
BgeeiQ91WG8.
CleanExiMM_GNE.
GenevestigatoriQ91WG8.

Interactioni

Subunit structurei

Homodimer and homohexamer By similarity.

Protein-protein interaction databases

IntActiQ91WG8. 1 interaction.
MINTiMINT-1869927.

Structurei

3D structure databases

ProteinModelPortaliQ91WG8.
SMRiQ91WG8. Positions 9-376, 406-717.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – ?UDP-N-acetylglucosamine 2-epimerase
Regioni406 – 722317N-acetylmannosamine kinase By similarity
Add
BLAST

Sequence similaritiesi

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

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

MEKNGNNRKL RVCVATCNRA DYSKLAPIMF GIKTEPAFFE LDVVVLGSHL    50
IDDYGNTYRM IEQDDFDINT RLHTIVRGED EAAMVESVGL ALVKLPDVLN 100
RLKPDIMIVH GDRFDALALA TSAALMNIRI LHIEGGEVSG TIDDSIRHAI 150
TKLAHYHVCC TRSAEQHLIS MCEDHDRILL AGCPSYDKLL SAKNKDYMSI 200
IRMWLGDDVK CKDYIVALQH PVTTDIKHSI KMFELTLDAL ISFNKRTLVL 250
FPNIDAGSKE MVRVMRKKGI EHHPNFRAVK HVPFDQFIQL VAHAGCMIGN 300
SSCGVREVGA FGTPVINLGT RQIGRETGEN VLHVRDADTQ DKILQALHLQ 350
FGKQYPCSKI YGDGNAVPRI LKFLKSIDLQ EPLQKKFCFP PVKENISQDI 400
DHILETLSAL AVDLGGTNLR VAIVSMKGEI VKKYTQFNPK TYEERISLIL 450
QMCVEAAAEA VKLNCRILGV GISTGGRVNP QEGVVLHSTK LIQEWNSVDL 500
RTPLSDTLHL PVWVDNDGNC AAMAERKFGQ GKGQENFVTL ITGTGIGGGI 550
IHQHELIHGS SFCAAELGHL VVSLDGPDCS CGSHGCIEAY ASGMALQREA 600
KKLHDEDLLL VEGMSVPKDE AVGALHLIQA AKLGNVKAQS ILRTAGTALG 650
LGVVNILHTM NPSLVILSGV LASHYIHIVK DVIRQQALSS VQDVDVVVSD 700
LVDPALLGAA SMVLDYTTRR IH 722
Length:722
Mass (Da):79,199
Last modified:December 1, 2001 - v1
Checksum:i0DFDD681BFD17984
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti566 – 5672EL → DV in CAB36908. 1 Publication
Sequence conflicti623 – 6231G → V in CAB36908. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS51170.1.
RefSeqi NP_001177343.1. NM_001190414.1.
NP_056643.3. NM_015828.3.
UniGenei Mm.256718.

3D structure databases

ProteinModelPortali Q91WG8.
SMRi Q91WG8. Positions 9-376, 406-717.
ModBasei Search...

Protein-protein interaction databases

IntActi Q91WG8. 1 interaction.
MINTi MINT-1869927.

PTM databases

PhosphoSitei Q91WG8.

Proteomic databases

MaxQBi Q91WG8.
PaxDbi Q91WG8.
PRIDEi Q91WG8.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000102936 ; ENSMUSP00000100000 ; ENSMUSG00000028479 .
GeneIDi 50798.
KEGGi mmu:50798.
UCSCi uc008srm.2. mouse.

Organism-specific databases

CTDi 10020.
MGIi MGI:1354951. Gne.

Phylogenomic databases

eggNOGi COG0381.
GeneTreei ENSGT00390000017246.
HOGENOMi HOG000008254.
HOVERGENi HBG051733.
InParanoidi Q91WG8.
KOi K12409.

Enzyme and pathway databases

UniPathwayi UPA00630 .
Reactomei REACT_202500. Sialic acid metabolism.

Miscellaneous databases

ChiTaRSi GNE. mouse.
NextBioi 307809.
PROi Q91WG8.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q91WG8.
Bgeei Q91WG8.
CleanExi MM_GNE.
Genevestigatori Q91WG8.

Family and domain databases

InterProi IPR001312. Hexokinase.
IPR000600. ROK.
IPR020004. UDP-GlcNAc_Epase.
IPR003331. UDP_GlcNAc_Epimerase_2.
[Graphical view ]
Pfami PF02350. Epimerase_2. 1 hit.
PF00480. ROK. 1 hit.
[Graphical view ]
PRINTSi PR00475. HEXOKINASE.
TIGRFAMsi TIGR03568. NeuC_NnaA. 1 hit.
ProtoNeti Search...

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: September 3, 2014
This is version 107 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

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