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Bifunctional UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase (UDP-GlcNAc-2-epimerase/ManAc kinase) [Includes: UDP-N-acetylglucosamine 2-epimerase (hydrolyzing) (EC 3.2.1.183) (UDP-GlcNAc-2-epimerase) (Uridine diphosphate-N-acetylglucosamine-2-epimerase); N-acetylmannosamine kinase (EC 2.7.1.60) (ManAc kinase)]

 GLCNE_HUMAN             Reviewed;         722 AA.
Q9Y223; A6PZH2; A6PZH3; A7UNU7; B2R6E1; B7Z372; B7Z428; D3DRP7;
F5H499; H0YFA7; Q0VA94;
15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
01-NOV-1999, sequence version 1.
20-DEC-2017, entry version 154.
RecName: Full=Bifunctional UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase;
AltName: Full=UDP-GlcNAc-2-epimerase/ManAc kinase;
Includes:
RecName: Full=UDP-N-acetylglucosamine 2-epimerase (hydrolyzing);
EC=3.2.1.183;
AltName: Full=UDP-GlcNAc-2-epimerase;
AltName: Full=Uridine diphosphate-N-acetylglucosamine-2-epimerase;
Includes:
RecName: Full=N-acetylmannosamine kinase;
EC=2.7.1.60;
AltName: Full=ManAc kinase;
Name=GNE; Synonyms=GLCNE;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
TISSUE=Liver;
PubMed=10431835; DOI=10.1016/S0014-5793(99)00837-6;
Lucka L., Krause M., Danker K., Reutter W., Horstkorte R.;
"Primary structure and expression analysis of human UDP-N-acetyl-
glucosamine-2-epimerase/N-acetylmannosamine kinase, the bifunctional
enzyme in neuraminic acid biosynthesis.";
FEBS Lett. 454:341-344(1999).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND
VARIANTS SIALURIA LEU-263; GLN-266 AND TRP-266.
PubMed=10330343; DOI=10.1086/302411;
Seppala R., Lehto V.-P., Gahl W.A.;
"Mutations in the human UDP-N-acetylglucosamine 2-epimerase gene
define the disease sialuria and the allosteric site of the enzyme.";
Am. J. Hum. Genet. 64:1563-1569(1999).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Small intestine;
Wang S.S., Ryll T.;
Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
Huizing M., Anikster Y., Gahl W.A.;
"Organization of the human UDP-N-acetylglucosamine 2-epimerase gene
and characterization of a related pseudogene; relevance for mutation
detection in patients with sialuria.";
Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
Pramono Z.A.D., Lai P.S., Seah I.A.L., Ong B., Yee W.C.;
"mRNA analysis revealed splice mutation and expression alteration of
GNE gene in distal myopathy with rimmed vacuoles (DMRV) patients.";
Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 5), AND
NUCLEOTIDE SEQUENCE [MRNA] OF 24-694 (ISOFORM 3).
TISSUE=Hippocampus, and Tongue;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[7]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), NUCLEOTIDE SEQUENCE [MRNA] OF
37-694 (ISOFORM 3), AND TISSUE SPECIFICITY.
PubMed=17597614; DOI=10.1016/j.febslet.2007.06.026;
Reinke S.O., Hinderlich S.;
"Prediction of three different isoforms of the human UDP-N-
acetylglucosamine 2-epimerase/N-acetylmannosamine kinase.";
FEBS Lett. 581:3327-3331(2007).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164053; DOI=10.1038/nature02465;
Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E.,
Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
Kimberley A.M., King A., Knights A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S.,
Rogers J., Dunham I.;
"DNA sequence and analysis of human chromosome 9.";
Nature 429:369-374(2004).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[11]
ENZYME REGULATION, AND INVOLVEMENT IN SIALURIA.
PubMed=2808337;
Weiss P., Tietze F., Gahl W.A., Seppala R., Ashwell G.;
"Identification of the metabolic defect in sialuria.";
J. Biol. Chem. 264:17635-17636(1989).
[12]
FUNCTION.
PubMed=10334995; DOI=10.1126/science.284.5418.1372;
Keppler O.T., Hinderlich S., Langner J., Schwartz-Albiez R.,
Reutter W., Pawlita M.;
"UDP-GlcNAc 2-epimerase: a regulator of cell surface sialylation.";
Science 284:1372-1376(1999).
[13]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[14]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[15]
X-RAY CRYSTALLOGRAPHY (2.84 ANGSTROMS) OF 406-720, AND SUBUNIT.
PubMed=19841673; DOI=10.1371/journal.pone.0007165;
Tong Y., Tempel W., Nedyalkova L., Mackenzie F., Park H.W.;
"Crystal structure of the N-acetylmannosamine kinase domain of GNE.";
PLoS ONE 4:E7165-E7165(2009).
[16]
X-RAY CRYSTALLOGRAPHY (1.64 ANGSTROMS) OF 406-720 IN COMPLEX WITH ADP
AND N-ACETYLMANNOSAMINE, ZINC-BINDING SITES, ACTIVE SITE, AND SUBUNIT.
PubMed=22343627; DOI=10.1074/jbc.M111.318170;
Martinez J., Nguyen L.D., Hinderlich S., Zimmer R., Tauberger E.,
Reutter W., Saenger W., Fan H., Moniot S.;
"Crystal structures of N-acetylmannosamine kinase provide insights
into enzyme activity and inhibition.";
J. Biol. Chem. 287:13656-13665(2012).
[17]
VARIANT SIALURIA GLN-266.
PubMed=10356312; DOI=10.1006/mgme.1999.2852;
Ferreira H., Seppala R., Pinto R., Huizing M., Martins E., Braga A.C.,
Gomes L., Krasnewich D.M., Sa Miranda M.C., Gahl W.A.;
"Sialuria in a Portuguese girl: clinical, biochemical, and molecular
characteristics.";
Mol. Genet. Metab. 67:131-137(1999).
[18]
CHARACTERIZATION OF VARIANT SIALURIA GLN-266.
PubMed=11326336; DOI=10.1086/320598;
Leroy J.G., Seppala R., Huizing M., Dacremont G., De Simpel H.,
Van Coster R.N., Orvisky E., Krasnewich D.M., Gahl W.A.;
"Dominant inheritance of sialuria, an inborn error of feedback
inhibition.";
Am. J. Hum. Genet. 68:1419-1427(2001).
[19]
VARIANTS NM ASN-225; GLN-246; GLU-576; THR-631; MET-696 AND THR-712.
PubMed=11528398; DOI=10.1038/ng718;
Eisenberg I., Avidan N., Potikha T., Hochner H., Chen M., Olender T.,
Barash M., Shemesh M., Sadeh M., Grabov-Nardini G., Shmilevich I.,
Friedmann A., Karpati G., Bradley W.G., Baumbach L., Lancet D.,
Asher E.B., Beckmann J.S., Argov Z., Mitrani-Rosenbaum S.;
"The UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase
gene is mutated in recessive hereditary inclusion body myopathy.";
Nat. Genet. 29:83-87(2001).
[20]
VARIANT NM LEU-572.
PubMed=12325084; DOI=10.1002/ana.10341;
Arai A., Tanaka K., Ikeuchi T., Igarashi S., Kobayashi H., Asaka T.,
Date H., Saito M., Tanaka H., Kawasaki S., Uyama E., Mizusawa H.,
Fukuhara N., Tsuji S.;
"A novel mutation in the GNE gene and a linkage disequilibrium in
Japanese pedigrees.";
Ann. Neurol. 52:516-519(2002).
[21]
VARIANTS NM VAL-460 AND LEU-572.
PubMed=11916006; DOI=10.1007/s100380200004;
Kayashima T., Matsuo H., Satoh A., Ohta T., Yoshiura K., Matsumoto N.,
Nakane Y., Niikawa N., Kishino T.;
"Nonaka myopathy is caused by mutations in the UDP-N-
acetylglucosamine-2-epimerase/N-acetylmannosamine kinase gene (GNE).";
J. Hum. Genet. 47:77-79(2002).
[22]
VARIANTS NM ASN-225; GLN-246; TRP-246; VAL-460; VAL-524; LEU-572;
GLU-576; THR-631; HIS-675; MET-696 AND THR-712.
PubMed=12409274; DOI=10.1016/S1096-7192(02)00141-5;
Darvish D., Vahedifar P., Huo Y.;
"Four novel mutations associated with autosomal recessive inclusion
body myopathy (MIM: 600737).";
Mol. Genet. Metab. 77:252-256(2002).
[23]
VARIANTS NM LEU-572 AND VAL-631.
PubMed=12177386; DOI=10.1212/WNL.59.3.451;
Tomimitsu H., Ishikawa K., Shimizu J., Ohkoshi N., Kanazawa I.,
Mizusawa H.;
"Distal myopathy with rimmed vacuoles: novel mutations in the GNE
gene.";
Neurology 59:451-454(2002).
[24]
VARIANTS NM GLN-132; VAL-176; CYS-177; GLN-306; ALA-331; TYR-378;
THR-472; LEU-572; THR-630 AND VAL-631.
PubMed=12473753; DOI=10.1212/01.WNL.0000041631.28557.C6;
Nishino I., Noguchi S., Murayama K., Driss A., Sugie K., Oya Y.,
Nagata T., Chida K., Takahashi T., Takusa Y., Ohi T., Nishimiya J.,
Sunohara N., Ciafaloni E., Kawai M., Aoki M., Nonaka I.;
"Distal myopathy with rimmed vacuoles is allelic to hereditary
inclusion body myopathy.";
Neurology 59:1689-1693(2002).
[25]
VARIANTS NM ALA-216 AND VAL-631.
PubMed=12473769; DOI=10.1212/01.WNL.0000039780.13681.AD;
Vasconcelos O.M., Raju R., Dalakas M.C.;
"GNE mutations in an American family with quadriceps-sparing IBM and
lack of mutations in s-IBM.";
Neurology 59:1776-1779(2002).
[26]
VARIANTS NM VAL-171 AND THR-712.
PubMed=12473780; DOI=10.1212/01.WNL.0000031808.04545.E0;
Broccolini A., Pescatori M., D'Amico A., Sabino A., Silvestri G.,
Ricci E., Servidei S., Tonali P.A., Mirabella M.;
"An Italian family with autosomal recessive inclusion-body myopathy
and mutations in the GNE gene.";
Neurology 59:1808-1809(2002).
[27]
VARIANTS NM LEU-36; PHE-200; ASN-225; GLN-246; VAL-303; TYR-378;
VAL-460; CYS-528; THR-557; LEU-572; GLU-576; THR-587; THR-631;
VAL-631; MET-696 AND THR-712.
PubMed=12497639; DOI=10.1002/humu.9100;
Eisenberg I., Grabov-Nardini G., Hochner H., Korner M., Sadeh M.,
Bertorini T., Bushby K., Castellan C., Felice K., Mendell J.,
Merlini L., Shilling C., Wirguin I., Argov Z., Mitrani-Rosenbaum S.;
"Mutations spectrum of GNE in hereditary inclusion body myopathy
sparing the quadriceps.";
Hum. Mutat. 21:99-99(2003).
[28]
VARIANT NM CYS-162.
PubMed=12811782; DOI=10.1002/mus.10391;
Del Bo R., Baron P., Prelle A., Serafini M., Moggio M., Di Fonzo A.,
Castagni M., Bresolin N., Comi G.P.;
"Novel missense mutation and large deletion of GNE gene in autosomal-
recessive inclusion-body myopathy.";
Muscle Nerve 28:113-117(2003).
[29]
VARIANTS NM THR-472 AND LEU-572.
PubMed=12913203; DOI=10.1212/01.WNL.0000061520.63546.8F;
Yabe I., Higashi T., Kikuchi S., Sasaki H., Fukazawa T., Yoshida K.,
Tashiro K.;
"GNE mutations causing distal myopathy with rimmed vacuoles with
inflammation.";
Neurology 61:384-386(2003).
[30]
VARIANTS NM SER-27; SER-206; GLN-246; SER-519 AND THR-600.
PubMed=15146476; DOI=10.1002/humu.9252;
Broccolini A., Ricci E., Cassandrini D., Gliubizzi C., Bruno C.,
Tonoli E., Silvestri G., Pescatori M., Rodolico C., Sinicropi S.,
Servidei S., Zara F., Minetti C., Tonali P.A., Mirabella M.;
"Novel GNE mutations in Italian families with autosomal recessive
hereditary inclusion-body myopathy.";
Hum. Mutat. 23:632-632(2004).
-!- FUNCTION: Regulates and initiates biosynthesis of N-
acetylneuraminic acid (NeuAc), a precursor of sialic acids. Plays
an essential role in early development (By similarity). Required
for normal sialylation in hematopoietic cells. Sialylation is
implicated in cell adhesion, signal transduction, tumorigenicity
and metastatic behavior of malignant cells. {ECO:0000250,
ECO:0000269|PubMed:10334995}.
-!- CATALYTIC ACTIVITY: UDP-N-acetyl-alpha-D-glucosamine + H(2)O = N-
acetyl-D-mannosamine + UDP.
-!- CATALYTIC ACTIVITY: ATP + N-acyl-D-mannosamine = ADP + N-acyl-D-
mannosamine 6-phosphate.
-!- ENZYME REGULATION: Allosterically regulated (Probable); 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. {ECO:0000250, ECO:0000269|PubMed:2808337}.
-!- PATHWAY: Amino-sugar metabolism; N-acetylneuraminate biosynthesis.
-!- SUBUNIT: Homodimer and homohexamer. {ECO:0000269|PubMed:19841673,
ECO:0000269|PubMed:22343627}.
-!- INTERACTION:
Q6UY14-3:ADAMTSL4; NbExp=3; IntAct=EBI-4291090, EBI-10173507;
Q9UHF1:EGFL7; NbExp=4; IntAct=EBI-11975289, EBI-949532;
Q969Y2:GTPBP3; NbExp=3; IntAct=EBI-4291090, EBI-740290;
Q15323:KRT31; NbExp=3; IntAct=EBI-4291090, EBI-948001;
P60370:KRTAP10-5; NbExp=3; IntAct=EBI-4291090, EBI-10172150;
P60409:KRTAP10-7; NbExp=3; IntAct=EBI-4291090, EBI-10172290;
P60410:KRTAP10-8; NbExp=3; IntAct=EBI-4291090, EBI-10171774;
P60411:KRTAP10-9; NbExp=3; IntAct=EBI-4291090, EBI-10172052;
Q9BQ66:KRTAP4-12; NbExp=3; IntAct=EBI-4291090, EBI-739863;
Q9BYR3:KRTAP4-4; NbExp=4; IntAct=EBI-11975289, EBI-11958132;
P26371:KRTAP5-9; NbExp=3; IntAct=EBI-4291090, EBI-3958099;
Q9BYQ4:KRTAP9-2; NbExp=3; IntAct=EBI-4291090, EBI-1044640;
Q7Z3S9:NOTCH2NL; NbExp=3; IntAct=EBI-4291090, EBI-945833;
O43597:SPRY2; NbExp=3; IntAct=EBI-4291090, EBI-742487;
Q15654:TRIP6; NbExp=4; IntAct=EBI-11975289, EBI-742327;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=5;
Name=1; Synonyms=GNE1;
IsoId=Q9Y223-1; Sequence=Displayed;
Name=2; Synonyms=GNE2;
IsoId=Q9Y223-2; Sequence=VSP_041027;
Name=3; Synonyms=GNE3;
IsoId=Q9Y223-3; Sequence=VSP_041028;
Name=4;
IsoId=Q9Y223-4; Sequence=VSP_043474;
Name=5;
IsoId=Q9Y223-5; Sequence=VSP_043975, VSP_043976;
-!- TISSUE SPECIFICITY: Highest expression in liver and placenta. Also
found in heart, brain, lung, kidney, skeletal muscle and pancreas.
Isoform 1 is expressed in heart, brain, kidney, liver, placenta,
lung, spleen, pancreas, skeletal muscle and colon. Isoform 2 is
expressed mainly in placenta, but also in brain, kidney, liver,
lung, pancreas and colon. Isoform 3 is expressed at low level in
kidney, liver, placenta and colon. {ECO:0000269|PubMed:10330343,
ECO:0000269|PubMed:10431835, ECO:0000269|PubMed:17597614}.
-!- PTM: Phosphorylated by PKC. {ECO:0000250}.
-!- DISEASE: Sialuria (SIALURIA) [MIM:269921]: In sialuria, free
sialic acid accumulates in the cytoplasm and gram quantities of
neuraminic acid are secreted in the urine. The metabolic defect
involves lack of feedback inhibition of UDP-GlcNAc 2-epimerase by
CMP-Neu5Ac, resulting in constitutive overproduction of free
Neu5Ac. Clinical features include variable degrees of
developmental delay, coarse facial features and hepatomegaly.
Sialuria inheritance is autosomal dominant.
{ECO:0000269|PubMed:10330343, ECO:0000269|PubMed:10356312,
ECO:0000269|PubMed:11326336, ECO:0000269|PubMed:2808337}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- DISEASE: Nonaka myopathy (NM) [MIM:605820]: Autosomal recessive
muscular disorder, allelic to inclusion body myopathy 2. It is
characterized by weakness of the anterior compartment of the lower
limbs with onset in early adulthood, and sparing of the quadriceps
muscles. As the inclusion body myopathy, NM is histologically
characterized by the presence of numerous rimmed vacuoles without
inflammatory changes in muscle specimens.
{ECO:0000269|PubMed:11528398, ECO:0000269|PubMed:11916006,
ECO:0000269|PubMed:12177386, ECO:0000269|PubMed:12325084,
ECO:0000269|PubMed:12409274, ECO:0000269|PubMed:12473753,
ECO:0000269|PubMed:12473769, ECO:0000269|PubMed:12473780,
ECO:0000269|PubMed:12497639, ECO:0000269|PubMed:12811782,
ECO:0000269|PubMed:12913203, ECO:0000269|PubMed:15146476}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- SIMILARITY: In the N-terminal section; belongs to the UDP-N-
acetylglucosamine 2-epimerase family. {ECO:0000305}.
-!- SIMILARITY: In the C-terminal section; belongs to the ROK
(NagC/XylR) family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAH12414.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AJ238764; CAB42607.1; -; mRNA.
EMBL; AF051852; AAD32251.1; -; mRNA.
EMBL; AF155663; AAD38197.1; -; mRNA.
EMBL; AF317635; AAG31661.1; -; Genomic_DNA.
EMBL; EU093084; ABU55403.1; -; mRNA.
EMBL; AK295562; BAH12108.1; -; mRNA.
EMBL; AK296687; BAH12414.1; ALT_INIT; mRNA.
EMBL; AK312539; BAG35438.1; -; mRNA.
EMBL; AM697708; CAM91424.1; -; mRNA.
EMBL; AM697709; CAM91425.1; -; mRNA.
EMBL; AL158830; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471071; EAW58307.1; -; Genomic_DNA.
EMBL; CH471071; EAW58309.1; -; Genomic_DNA.
EMBL; BC121179; AAI21180.1; -; mRNA.
CCDS; CCDS47965.1; -. [Q9Y223-2]
CCDS; CCDS55308.1; -. [Q9Y223-5]
CCDS; CCDS55309.1; -. [Q9Y223-4]
CCDS; CCDS55310.1; -. [Q9Y223-3]
CCDS; CCDS6602.1; -. [Q9Y223-1]
RefSeq; NP_001121699.1; NM_001128227.2. [Q9Y223-2]
RefSeq; NP_001177312.1; NM_001190383.1. [Q9Y223-4]
RefSeq; NP_001177313.1; NM_001190384.1. [Q9Y223-5]
RefSeq; NP_001177317.1; NM_001190388.1. [Q9Y223-3]
RefSeq; NP_005467.1; NM_005476.5. [Q9Y223-1]
RefSeq; XP_016869656.1; XM_017014167.1. [Q9Y223-1]
UniGene; Hs.5920; -.
PDB; 2YHW; X-ray; 1.64 A; A=406-720.
PDB; 2YHY; X-ray; 1.82 A; A=406-720.
PDB; 2YI1; X-ray; 2.15 A; A=406-720.
PDB; 3EO3; X-ray; 2.84 A; A/B/C=406-720.
PDB; 4ZHT; X-ray; 2.69 A; A/B/C/D=1-405.
PDBsum; 2YHW; -.
PDBsum; 2YHY; -.
PDBsum; 2YI1; -.
PDBsum; 3EO3; -.
PDBsum; 4ZHT; -.
ProteinModelPortal; Q9Y223; -.
SMR; Q9Y223; -.
BioGrid; 115337; 28.
IntAct; Q9Y223; 53.
STRING; 9606.ENSP00000379839; -.
iPTMnet; Q9Y223; -.
PhosphoSitePlus; Q9Y223; -.
BioMuta; GNE; -.
DMDM; 45476991; -.
EPD; Q9Y223; -.
PaxDb; Q9Y223; -.
PeptideAtlas; Q9Y223; -.
PRIDE; Q9Y223; -.
DNASU; 10020; -.
Ensembl; ENST00000377902; ENSP00000367134; ENSG00000159921. [Q9Y223-1]
Ensembl; ENST00000396594; ENSP00000379839; ENSG00000159921. [Q9Y223-2]
Ensembl; ENST00000447283; ENSP00000414760; ENSG00000159921. [Q9Y223-4]
Ensembl; ENST00000539208; ENSP00000445117; ENSG00000159921. [Q9Y223-5]
Ensembl; ENST00000539815; ENSP00000439155; ENSG00000159921. [Q9Y223-1]
Ensembl; ENST00000543356; ENSP00000437765; ENSG00000159921. [Q9Y223-3]
GeneID; 10020; -.
KEGG; hsa:10020; -.
UCSC; uc010mlg.5; human. [Q9Y223-1]
CTD; 10020; -.
DisGeNET; 10020; -.
EuPathDB; HostDB:ENSG00000159921.14; -.
GeneCards; GNE; -.
GeneReviews; GNE; -.
HGNC; HGNC:23657; GNE.
HPA; HPA007045; -.
HPA; HPA027258; -.
MalaCards; GNE; -.
MIM; 269921; phenotype.
MIM; 600737; phenotype.
MIM; 603824; gene.
MIM; 605820; phenotype.
neXtProt; NX_Q9Y223; -.
OpenTargets; ENSG00000159921; -.
Orphanet; 602; Distal myopathy, Nonaka type.
Orphanet; 3166; Sialuria.
PharmGKB; PA134987566; -.
eggNOG; ENOG410IE3W; Eukaryota.
eggNOG; COG0381; LUCA.
eggNOG; COG1940; LUCA.
GeneTree; ENSGT00390000017246; -.
HOGENOM; HOG000008254; -.
HOVERGEN; HBG051733; -.
InParanoid; Q9Y223; -.
KO; K12409; -.
OMA; IAMCEDH; -.
OrthoDB; EOG091G025K; -.
PhylomeDB; Q9Y223; -.
TreeFam; TF332239; -.
BRENDA; 2.7.1.60; 2681.
BRENDA; 3.2.1.183; 2681.
BRENDA; 5.1.3.14; 2681.
Reactome; R-HSA-4085001; Sialic acid metabolism.
Reactome; R-HSA-4085011; Defective GNE causes sialuria, Nonaka myopathy and inclusion body myopathy 2.
UniPathway; UPA00630; -.
ChiTaRS; GNE; human.
EvolutionaryTrace; Q9Y223; -.
GeneWiki; GNE_(gene); -.
GenomeRNAi; 10020; -.
PRO; PR:Q9Y223; -.
Proteomes; UP000005640; Chromosome 9.
Bgee; ENSG00000159921; -.
CleanEx; HS_GNE; -.
Genevisible; Q9Y223; HS.
GO; GO:0005737; C:cytoplasm; TAS:ProtInc.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0009384; F:N-acylmannosamine kinase activity; TAS:Reactome.
GO; GO:0008761; F:UDP-N-acetylglucosamine 2-epimerase activity; TAS:Reactome.
GO; GO:0007155; P:cell adhesion; TAS:ProtInc.
GO; GO:0006045; P:N-acetylglucosamine biosynthetic process; IEA:UniProtKB-UniPathway.
GO; GO:0006054; P:N-acetylneuraminate metabolic process; TAS:ProtInc.
GO; GO:0006047; P:UDP-N-acetylglucosamine metabolic process; IEA:InterPro.
CDD; cd03786; GT1_UDP-GlcNAc_2-Epimerase; 1.
InterPro; IPR000600; ROK.
InterPro; IPR020004; UDP-GlcNAc_Epase.
InterPro; IPR003331; UDP_GlcNAc_Epimerase_2_dom.
PANTHER; PTHR18964; PTHR18964; 1.
Pfam; PF02350; Epimerase_2; 1.
Pfam; PF00480; ROK; 1.
TIGRFAMs; TIGR03568; NeuC_NnaA; 1.
1: Evidence at protein level;
3D-structure; Allosteric enzyme; Alternative splicing; ATP-binding;
Complete proteome; Cytoplasm; Disease mutation; Hydrolase; Kinase;
Metal-binding; Multifunctional enzyme; Nucleotide-binding;
Phosphoprotein; Reference proteome; Transferase; Zinc.
CHAIN 1 722 Bifunctional UDP-N-acetylglucosamine 2-
epimerase/N-acetylmannosamine kinase.
/FTId=PRO_0000095716.
NP_BIND 411 420 ATP.
NP_BIND 543 552 ATP.
REGION 1 ? UDP-N-acetylglucosamine 2-epimerase.
REGION 406 722 N-acetylmannosamine kinase.
ACT_SITE 517 517 {ECO:0000269|PubMed:22343627}.
METAL 569 569 Zinc.
METAL 579 579 Zinc.
METAL 581 581 Zinc.
METAL 586 586 Zinc.
BINDING 477 477 Substrate.
BINDING 489 489 Substrate.
BINDING 517 517 Substrate.
BINDING 566 566 Substrate.
BINDING 569 569 Substrate.
BINDING 588 588 Substrate.
VAR_SEQ 1 59 Missing (in isoform 5).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_043975.
VAR_SEQ 1 55 MEKNGNNRKLRVCVATCNRADYSKLAPIMFGIKTEPEFFEL
DVVVLGSHLIDDYG -> MPIGDCSVAAKPRKQLLCSLFQT
TLGYRARASGWKPMVICRGSHAFKDLI (in isoform
3). {ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:17597614}.
/FTId=VSP_041028.
VAR_SEQ 1 1 M -> METYGYLQRESCFQGPHELYFKNLSKRNKQIM (in
isoform 2).
{ECO:0000303|PubMed:17597614}.
/FTId=VSP_041027.
VAR_SEQ 206 256 Missing (in isoform 5).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_043976.
VAR_SEQ 471 544 Missing (in isoform 4).
{ECO:0000303|Ref.5}.
/FTId=VSP_043474.
VARIANT 27 27 P -> S (in NM).
{ECO:0000269|PubMed:15146476}.
/FTId=VAR_021771.
VARIANT 36 36 P -> L (in NM).
{ECO:0000269|PubMed:12497639}.
/FTId=VAR_017945.
VARIANT 132 132 H -> Q (in NM).
{ECO:0000269|PubMed:12473753}.
/FTId=VAR_021772.
VARIANT 162 162 R -> C (in NM; dbSNP:rs769215411).
{ECO:0000269|PubMed:12811782}.
/FTId=VAR_021773.
VARIANT 171 171 M -> V (in NM; dbSNP:rs121908634).
{ECO:0000269|PubMed:12473780}.
/FTId=VAR_021774.
VARIANT 176 176 D -> V (in NM; dbSNP:rs139425890).
{ECO:0000269|PubMed:12473753}.
/FTId=VAR_021775.
VARIANT 177 177 R -> C (in NM; dbSNP:rs539332585).
{ECO:0000269|PubMed:12473753}.
/FTId=VAR_021776.
VARIANT 200 200 I -> F (in NM; dbSNP:rs369328625).
{ECO:0000269|PubMed:12497639}.
/FTId=VAR_017946.
VARIANT 206 206 G -> S (in NM; moderate phenotype with
unusual involvement of quadriceps;
dbSNP:rs766266918).
{ECO:0000269|PubMed:15146476}.
/FTId=VAR_021777.
VARIANT 216 216 V -> A (in NM; dbSNP:rs779694939).
{ECO:0000269|PubMed:12473769}.
/FTId=VAR_021778.
VARIANT 225 225 D -> N (in NM; dbSNP:rs121908630).
{ECO:0000269|PubMed:11528398,
ECO:0000269|PubMed:12409274,
ECO:0000269|PubMed:12497639}.
/FTId=VAR_017947.
VARIANT 246 246 R -> Q (in NM; dbSNP:rs121908629).
{ECO:0000269|PubMed:11528398,
ECO:0000269|PubMed:12409274,
ECO:0000269|PubMed:12497639,
ECO:0000269|PubMed:15146476}.
/FTId=VAR_017948.
VARIANT 246 246 R -> W (in NM; dbSNP:rs773729410).
{ECO:0000269|PubMed:12409274}.
/FTId=VAR_017949.
VARIANT 263 263 R -> L (in SIALURIA; strong reduction of
feedback inhibition by CMP-Neu5Ac;
dbSNP:rs121908623).
{ECO:0000269|PubMed:10330343}.
/FTId=VAR_017950.
VARIANT 266 266 R -> Q (in SIALURIA; abolishes feedback
inhibition by CMP-Neu5Ac;
dbSNP:rs121908622).
{ECO:0000269|PubMed:10330343,
ECO:0000269|PubMed:10356312,
ECO:0000269|PubMed:11326336}.
/FTId=VAR_017951.
VARIANT 266 266 R -> W (in sialuria; dbSNP:rs121908621).
{ECO:0000269|PubMed:10330343}.
/FTId=VAR_017952.
VARIANT 303 303 C -> V (in NM; requires 2 nucleotide
substitutions; dbSNP:rs121908633).
{ECO:0000269|PubMed:12497639}.
/FTId=VAR_017953.
VARIANT 306 306 R -> Q (in NM).
{ECO:0000269|PubMed:12473753}.
/FTId=VAR_021779.
VARIANT 331 331 V -> A (in NM).
{ECO:0000269|PubMed:12473753}.
/FTId=VAR_021780.
VARIANT 378 378 D -> Y (in NM; dbSNP:rs199877522).
{ECO:0000269|PubMed:12473753,
ECO:0000269|PubMed:12497639}.
/FTId=VAR_017954.
VARIANT 460 460 A -> V (in NM; dbSNP:rs121908631).
{ECO:0000269|PubMed:11916006,
ECO:0000269|PubMed:12409274,
ECO:0000269|PubMed:12497639}.
/FTId=VAR_017955.
VARIANT 472 472 I -> T (in NM).
{ECO:0000269|PubMed:12473753,
ECO:0000269|PubMed:12913203}.
/FTId=VAR_021781.
VARIANT 519 519 N -> S (in NM).
{ECO:0000269|PubMed:15146476}.
/FTId=VAR_021782.
VARIANT 524 524 A -> V (in NM; dbSNP:rs764698870).
{ECO:0000269|PubMed:12409274}.
/FTId=VAR_017956.
VARIANT 528 528 F -> C (in NM; dbSNP:rs986773986).
{ECO:0000269|PubMed:12497639}.
/FTId=VAR_017957.
VARIANT 557 557 I -> T (in NM; dbSNP:rs886043979).
{ECO:0000269|PubMed:12497639}.
/FTId=VAR_017958.
VARIANT 572 572 V -> L (in NM; dbSNP:rs121908632).
{ECO:0000269|PubMed:11916006,
ECO:0000269|PubMed:12177386,
ECO:0000269|PubMed:12325084,
ECO:0000269|PubMed:12409274,
ECO:0000269|PubMed:12473753,
ECO:0000269|PubMed:12497639,
ECO:0000269|PubMed:12913203}.
/FTId=VAR_017959.
VARIANT 576 576 G -> E (in NM; dbSNP:rs121908625).
{ECO:0000269|PubMed:11528398,
ECO:0000269|PubMed:12409274,
ECO:0000269|PubMed:12497639}.
/FTId=VAR_017960.
VARIANT 587 587 I -> T (in NM; dbSNP:rs748949603).
{ECO:0000269|PubMed:12497639}.
/FTId=VAR_017961.
VARIANT 600 600 A -> T (in NM; dbSNP:rs387906347).
{ECO:0000269|PubMed:15146476}.
/FTId=VAR_021783.
VARIANT 630 630 A -> T (in NM).
{ECO:0000269|PubMed:12473753}.
/FTId=VAR_021784.
VARIANT 631 631 A -> T (in NM; dbSNP:rs121908626).
{ECO:0000269|PubMed:11528398,
ECO:0000269|PubMed:12409274,
ECO:0000269|PubMed:12497639}.
/FTId=VAR_017962.
VARIANT 631 631 A -> V (in NM; dbSNP:rs62541771).
{ECO:0000269|PubMed:12177386,
ECO:0000269|PubMed:12473753,
ECO:0000269|PubMed:12473769,
ECO:0000269|PubMed:12497639}.
/FTId=VAR_017963.
VARIANT 675 675 Y -> H (in NM).
{ECO:0000269|PubMed:12409274}.
/FTId=VAR_017964.
VARIANT 696 696 V -> M (in NM; dbSNP:rs121908627).
{ECO:0000269|PubMed:11528398,
ECO:0000269|PubMed:12409274,
ECO:0000269|PubMed:12497639}.
/FTId=VAR_017965.
VARIANT 712 712 M -> T (in NM; dbSNP:rs28937594).
{ECO:0000269|PubMed:11528398,
ECO:0000269|PubMed:12409274,
ECO:0000269|PubMed:12473780,
ECO:0000269|PubMed:12497639}.
/FTId=VAR_017966.
CONFLICT 338 338 D -> G (in Ref. 6; BAH12108).
{ECO:0000305}.
CONFLICT 359 359 K -> R (in Ref. 6; BAH12414).
{ECO:0000305}.
CONFLICT 364 364 G -> V (in Ref. 6; BAH12108).
{ECO:0000305}.
CONFLICT 382 382 P -> L (in Ref. 6; BAH12108).
{ECO:0000305}.
CONFLICT 498 498 V -> A (in Ref. 6; BAH12108).
{ECO:0000305}.
CONFLICT 521 521 A -> V (in Ref. 6; BAH12414).
{ECO:0000305}.
STRAND 10 16 {ECO:0000244|PDB:4ZHT}.
HELIX 19 33 {ECO:0000244|PDB:4ZHT}.
TURN 36 38 {ECO:0000244|PDB:4ZHT}.
STRAND 39 46 {ECO:0000244|PDB:4ZHT}.
HELIX 47 50 {ECO:0000244|PDB:4ZHT}.
HELIX 52 54 {ECO:0000244|PDB:4ZHT}.
HELIX 58 63 {ECO:0000244|PDB:4ZHT}.
STRAND 68 72 {ECO:0000244|PDB:4ZHT}.
STRAND 77 80 {ECO:0000244|PDB:4ZHT}.
HELIX 81 102 {ECO:0000244|PDB:4ZHT}.
STRAND 105 113 {ECO:0000244|PDB:4ZHT}.
HELIX 114 125 {ECO:0000244|PDB:4ZHT}.
STRAND 129 134 {ECO:0000244|PDB:4ZHT}.
HELIX 142 153 {ECO:0000244|PDB:4ZHT}.
STRAND 155 161 {ECO:0000244|PDB:4ZHT}.
HELIX 162 170 {ECO:0000244|PDB:4ZHT}.
HELIX 175 177 {ECO:0000244|PDB:4ZHT}.
STRAND 178 180 {ECO:0000244|PDB:4ZHT}.
HELIX 185 189 {ECO:0000244|PDB:4ZHT}.
HELIX 197 205 {ECO:0000244|PDB:4ZHT}.
STRAND 215 218 {ECO:0000244|PDB:4ZHT}.
HELIX 223 225 {ECO:0000244|PDB:4ZHT}.
HELIX 226 243 {ECO:0000244|PDB:4ZHT}.
STRAND 247 250 {ECO:0000244|PDB:4ZHT}.
HELIX 258 267 {ECO:0000244|PDB:4ZHT}.
HELIX 270 272 {ECO:0000244|PDB:4ZHT}.
STRAND 276 280 {ECO:0000244|PDB:4ZHT}.
HELIX 284 292 {ECO:0000244|PDB:4ZHT}.
STRAND 295 299 {ECO:0000244|PDB:4ZHT}.
HELIX 302 306 {ECO:0000244|PDB:4ZHT}.
HELIX 308 311 {ECO:0000244|PDB:4ZHT}.
STRAND 315 320 {ECO:0000244|PDB:4ZHT}.
TURN 321 324 {ECO:0000244|PDB:4ZHT}.
STRAND 331 335 {ECO:0000244|PDB:4ZHT}.
HELIX 340 350 {ECO:0000244|PDB:4ZHT}.
HELIX 366 376 {ECO:0000244|PDB:4ZHT}.
STRAND 406 414 {ECO:0000244|PDB:2YHW}.
STRAND 416 425 {ECO:0000244|PDB:2YHW}.
STRAND 430 437 {ECO:0000244|PDB:2YHW}.
HELIX 442 462 {ECO:0000244|PDB:2YHW}.
STRAND 465 479 {ECO:0000244|PDB:2YHW}.
TURN 480 483 {ECO:0000244|PDB:2YHW}.
STRAND 484 487 {ECO:0000244|PDB:2YHW}.
STRAND 492 494 {ECO:0000244|PDB:2YHW}.
STRAND 496 499 {ECO:0000244|PDB:2YHW}.
HELIX 501 508 {ECO:0000244|PDB:2YHW}.
STRAND 512 516 {ECO:0000244|PDB:2YHW}.
HELIX 517 527 {ECO:0000244|PDB:2YHW}.
TURN 530 533 {ECO:0000244|PDB:2YHW}.
STRAND 537 552 {ECO:0000244|PDB:2YHW}.
HELIX 567 569 {ECO:0000244|PDB:2YHW}.
STRAND 571 574 {ECO:0000244|PDB:2YHW}.
STRAND 584 586 {ECO:0000244|PDB:2YHW}.
HELIX 587 591 {ECO:0000244|PDB:2YHW}.
HELIX 593 605 {ECO:0000244|PDB:2YHW}.
HELIX 624 632 {ECO:0000244|PDB:2YHW}.
HELIX 636 659 {ECO:0000244|PDB:2YHW}.
STRAND 663 669 {ECO:0000244|PDB:2YHW}.
HELIX 672 686 {ECO:0000244|PDB:2YHW}.
HELIX 689 691 {ECO:0000244|PDB:2YHW}.
STRAND 695 698 {ECO:0000244|PDB:2YHW}.
HELIX 704 716 {ECO:0000244|PDB:2YHW}.
SEQUENCE 722 AA; 79275 MW; 4D7D049B06B00077 CRC64;
MEKNGNNRKL RVCVATCNRA DYSKLAPIMF GIKTEPEFFE LDVVVLGSHL IDDYGNTYRM
IEQDDFDINT RLHTIVRGED EAAMVESVGL ALVKLPDVLN RLKPDIMIVH GDRFDALALA
TSAALMNIRI LHIEGGEVSG TIDDSIRHAI TKLAHYHVCC TRSAEQHLIS MCEDHDRILL
AGCPSYDKLL SAKNKDYMSI IRMWLGDDVK SKDYIVALQH PVTTDIKHSI KMFELTLDAL
ISFNKRTLVL FPNIDAGSKE MVRVMRKKGI EHHPNFRAVK HVPFDQFIQL VAHAGCMIGN
SSCGVREVGA FGTPVINLGT RQIGRETGEN VLHVRDADTQ DKILQALHLQ FGKQYPCSKI
YGDGNAVPRI LKFLKSIDLQ EPLQKKFCFP PVKENISQDI DHILETLSAL AVDLGGTNLR
VAIVSMKGEI VKKYTQFNPK TYEERINLIL QMCVEAAAEA VKLNCRILGV GISTGGRVNP
REGIVLHSTK LIQEWNSVDL RTPLSDTLHL PVWVDNDGNC AALAERKFGQ GKGLENFVTL
ITGTGIGGGI IHQHELIHGS SFCAAELGHL VVSLDGPDCS CGSHGCIEAY ASGMALQREA
KKLHDEDLLL VEGMSVPKDE AVGALHLIQA AKLGNAKAQS ILRTAGTALG LGVVNILHTM
NPSLVILSGV LASHYIHIVK DVIRQQALSS VQDVDVVVSD LVDPALLGAA SMVLDYTTRR
IY


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EIAAB34261 AGE,GlcNAc 2-epimerase,Homo sapiens,Human,N-acetyl-D-glucosamine 2-epimerase,N-acylglucosamine 2-epimerase,RENBP,Renin-binding protein,RnBP
EIAAB34258 AGE,Canis familiaris,Canis lupus familiaris,Dog,GlcNAc 2-epimerase,N-acetyl-D-glucosamine 2-epimerase,N-acylglucosamine 2-epimerase,RENBP,Renin-binding protein,RnBP
EIAAB11961 Bos taurus,Bovine,Chondroitin-glucuronate 5-epimerase,Dermatan-sulfate epimerase,DS epimerase,DSE
EIAAB11962 Chondroitin-glucuronate 5-epimerase,Dermatan-sulfate epimerase,DS epimerase,Dse,Mouse,Mus musculus,Sart2,SART-2,Squamous cell carcinoma antigen recognized by T-cells 2
EIAAB11963 Chondroitin-glucuronate 5-epimerase,Dermatan-sulfate epimerase,DS epimerase,DSE,Homo sapiens,Human,SART2,SART-2,Squamous cell carcinoma antigen recognized by T-cells 2
CSB-EL009609RA Rat Bifunctional UDP-N-acetylglucosamine 2-epimerase_N-acetylmannosamine kinase(GNE) ELISA kit 96T
CSB-EL009609MO Mouse Bifunctional UDP-N-acetylglucosamine 2-epimerase_N-acetylmannosamine kinase(GNE) ELISA kit 96T
CSB-EL009609RA Rat Bifunctional UDP-N-acetylglucosamine 2-epimerase_N-acetylmannosamine kinase(GNE) ELISA kit SpeciesRat 96T
CSB-EL009609HU Human Bifunctional UDP-N-acetylglucosamine 2-epimerase_N-acetylmannosamine kinase(GNE) ELISA kit 96T
CSB-EL009609HU Human Bifunctional UDP-N-acetylglucosamine 2-epimerase_N-acetylmannosamine kinase(GNE) ELISA kit SpeciesHuman 96T
CSB-EL009609MO Mouse Bifunctional UDP-N-acetylglucosamine 2-epimerase_N-acetylmannosamine kinase(GNE) ELISA kit SpeciesMouse 96T
EIAAB26289 GlcNAc kinase,Homo sapiens,Human,N-acetyl-D-glucosamine kinase,N-acetylglucosamine kinase,NAGK
EIAAB26286 GlcNAc kinase,N-acetyl-D-glucosamine kinase,N-acetylglucosamine kinase,Nagk,Rat,Rattus norvegicus
EIAAB26287 Bos taurus,Bovine,GlcNAc kinase,N-acetyl-D-glucosamine kinase,N-acetylglucosamine kinase,NAGK
EIAAB26288 GlcNAc kinase,Gnk,Mouse,Mus musculus,N-acetyl-D-glucosamine kinase,N-acetylglucosamine kinase,Nagk
29-593 HSD17B6 has both oxidoreductase and epimerase activities and is involved in androgen catabolism. The oxidoreductase activity can convert 3 alpha-adiol to dihydrotestosterone, while the epimerase activ 0.1 mg


 

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