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Q91WG8

- GLCNE_MOUSE

UniProt

Q91WG8 - GLCNE_MOUSE

Protein

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

Gene

Gne

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 108 (01 Oct 2014)
      Sequence version 1 (01 Dec 2001)
      Previous versions | rss
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    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 Source: UniProtKB-KW
    4. metal ion binding Source: UniProtKB-KW
    5. N-acylmannosamine kinase activity Source: UniProtKB-EC
    6. UDP-N-acetylglucosamine 2-epimerase activity Source: InterPro

    GO - Biological processi

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

    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

    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

    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.
    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

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    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

    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:
    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...
    MobiDBi 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

    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: October 1, 2014
    This is version 108 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