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Q91WG8 (GLCNE_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 102. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Bifunctional UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase
Alternative name(s):
UDP-GlcNAc-2-epimerase/ManAc kinase

Including the following 2 domains:

  1. UDP-N-acetylglucosamine 2-epimerase (hydrolyzing)
    EC=3.2.1.183
    Alternative name(s):
    UDP-GlcNAc-2-epimerase
    Uridine diphosphate-N-acetylglucosamine-2-epimerase
  2. N-acetylmannosamine kinase
    EC=2.7.1.60
    Alternative name(s):
    ManAc kinase
Gene names
Name:Gne
Synonyms:Glcne, Uae1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length722 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.5

Catalytic activity

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 regulation

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.

Pathway

Amino-sugar metabolism; N-acetylneuraminate biosynthesis.

Subunit structure

Homodimer and homohexamer By similarity.

Subcellular location

Cytoplasm By similarity.

Tissue specificity

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

Developmental stage

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

Post-translational modification

Phosphorylated by PKC. Ref.4

Sequence similarities

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 722722Bifunctional UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase
PRO_0000095717

Regions

Nucleotide binding411 – 42010ATP By similarity
Nucleotide binding543 – 55210ATP By similarity
Region1 – ?UDP-N-acetylglucosamine 2-epimerase
Region406 – 722317N-acetylmannosamine kinase By similarity

Sites

Active site5171 By similarity
Metal binding5691Zinc By similarity
Metal binding5791Zinc By similarity
Metal binding5811Zinc By similarity
Metal binding5861Zinc By similarity
Binding site4771Substrate By similarity
Binding site4891Substrate By similarity
Binding site5171Substrate By similarity
Binding site5661Substrate By similarity
Binding site5691Substrate By similarity
Binding site5881Substrate By similarity

Experimental info

Sequence conflict566 – 5672EL → DV in CAB36908. Ref.1
Sequence conflict6231G → V in CAB36908. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q91WG8 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: 0DFDD681BFD17984

FASTA72279,199
        10         20         30         40         50         60 
MEKNGNNRKL RVCVATCNRA DYSKLAPIMF GIKTEPAFFE LDVVVLGSHL IDDYGNTYRM 

        70         80         90        100        110        120 
IEQDDFDINT RLHTIVRGED EAAMVESVGL ALVKLPDVLN RLKPDIMIVH GDRFDALALA 

       130        140        150        160        170        180 
TSAALMNIRI LHIEGGEVSG TIDDSIRHAI TKLAHYHVCC TRSAEQHLIS MCEDHDRILL 

       190        200        210        220        230        240 
AGCPSYDKLL SAKNKDYMSI IRMWLGDDVK CKDYIVALQH PVTTDIKHSI KMFELTLDAL 

       250        260        270        280        290        300 
ISFNKRTLVL FPNIDAGSKE MVRVMRKKGI EHHPNFRAVK HVPFDQFIQL VAHAGCMIGN 

       310        320        330        340        350        360 
SSCGVREVGA FGTPVINLGT RQIGRETGEN VLHVRDADTQ DKILQALHLQ FGKQYPCSKI 

       370        380        390        400        410        420 
YGDGNAVPRI LKFLKSIDLQ EPLQKKFCFP PVKENISQDI DHILETLSAL AVDLGGTNLR 

       430        440        450        460        470        480 
VAIVSMKGEI VKKYTQFNPK TYEERISLIL QMCVEAAAEA VKLNCRILGV GISTGGRVNP 

       490        500        510        520        530        540 
QEGVVLHSTK LIQEWNSVDL RTPLSDTLHL PVWVDNDGNC AAMAERKFGQ GKGQENFVTL 

       550        560        570        580        590        600 
ITGTGIGGGI IHQHELIHGS SFCAAELGHL VVSLDGPDCS CGSHGCIEAY ASGMALQREA 

       610        620        630        640        650        660 
KKLHDEDLLL VEGMSVPKDE AVGALHLIQA AKLGNVKAQS ILRTAGTALG LGVVNILHTM 

       670        680        690        700        710        720 
NPSLVILSGV LASHYIHIVK DVIRQQALSS VQDVDVVVSD LVDPALLGAA SMVLDYTTRR 


IH 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"Sialylation is essential for early development in mice."
Schwarzkopf M., Knobeloch K.-P., Rohde E., Hinderlich S., Wiechens N., Lucka L., Horak I., Reutter W., Horstkorte R.
Proc. Natl. Acad. Sci. U.S.A. 99:5267-5270(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_001177343.1. NM_001190414.1.
NP_056643.3. NM_015828.3.
UniGeneMm.256718.

3D structure databases

ProteinModelPortalQ91WG8.
SMRQ91WG8. Positions 9-717.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ91WG8. 1 interaction.
MINTMINT-1869927.

PTM databases

PhosphoSiteQ91WG8.

Proteomic databases

PaxDbQ91WG8.
PRIDEQ91WG8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000102936; ENSMUSP00000100000; ENSMUSG00000028479.
GeneID50798.
KEGGmmu:50798.
UCSCuc008srm.2. mouse.

Organism-specific databases

CTD10020.
MGIMGI:1354951. Gne.

Phylogenomic databases

eggNOGCOG0381.
GeneTreeENSGT00390000017246.
HOGENOMHOG000008254.
HOVERGENHBG051733.
InParanoidQ91WG8.
KOK12409.

Enzyme and pathway databases

UniPathwayUPA00630.

Gene expression databases

ArrayExpressQ91WG8.
BgeeQ91WG8.
CleanExMM_GNE.
GenevestigatorQ91WG8.

Family and domain databases

InterProIPR001312. Hexokinase.
IPR000600. ROK.
IPR020004. UDP-GlcNAc_Epase.
IPR003331. UDP_GlcNAc_Epimerase_2.
[Graphical view]
PfamPF02350. Epimerase_2. 1 hit.
PF00480. ROK. 1 hit.
[Graphical view]
PRINTSPR00475. HEXOKINASE.
TIGRFAMsTIGR03568. NeuC_NnaA. 1 hit.
ProtoNetSearch...

Other

ChiTaRSGNE. mouse.
NextBio307809.
PROQ91WG8.
SOURCESearch...

Entry information

Entry nameGLCNE_MOUSE
AccessionPrimary (citable) accession number: Q91WG8
Secondary accession number(s): Q8CC83, Q8CCB0, Q9Z0P6
Entry history
Integrated into UniProtKB/Swiss-Prot: March 15, 2004
Last sequence update: December 1, 2001
Last modified: March 19, 2014
This is version 102 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot