GLCNE_HUMAN
ID GLCNE_HUMAN Reviewed; 722 AA.
AC Q9Y223; A6PZH2; A6PZH3; A7UNU7; B2R6E1; B7Z372; B7Z428; D3DRP7; F5H499;
AC H0YFA7; Q0VA94;
DT 15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 182.
DE RecName: Full=Bifunctional UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase;
DE AltName: Full=UDP-GlcNAc-2-epimerase/ManAc kinase;
DE Includes:
DE RecName: Full=UDP-N-acetylglucosamine 2-epimerase (hydrolyzing);
DE EC=3.2.1.183;
DE AltName: Full=UDP-GlcNAc-2-epimerase;
DE AltName: Full=Uridine diphosphate-N-acetylglucosamine-2-epimerase;
DE Includes:
DE RecName: Full=N-acetylmannosamine kinase;
DE EC=2.7.1.60;
DE AltName: Full=ManAc kinase;
GN Name=GNE; Synonyms=GLCNE;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RC TISSUE=Liver;
RX PubMed=10431835; DOI=10.1016/s0014-5793(99)00837-6;
RA Lucka L., Krause M., Danker K., Reutter W., Horstkorte R.;
RT "Primary structure and expression analysis of human UDP-N-acetyl-
RT glucosamine-2-epimerase/N-acetylmannosamine kinase, the bifunctional enzyme
RT in neuraminic acid biosynthesis.";
RL FEBS Lett. 454:341-344(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND VARIANTS
RP SIALURIA LEU-263; GLN-266 AND TRP-266.
RX PubMed=10330343; DOI=10.1086/302411;
RA Seppala R., Lehto V.-P., Gahl W.A.;
RT "Mutations in the human UDP-N-acetylglucosamine 2-epimerase gene define the
RT disease sialuria and the allosteric site of the enzyme.";
RL Am. J. Hum. Genet. 64:1563-1569(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Small intestine;
RA Wang S.S., Ryll T.;
RL Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
RA Huizing M., Anikster Y., Gahl W.A.;
RT "Organization of the human UDP-N-acetylglucosamine 2-epimerase gene and
RT characterization of a related pseudogene; relevance for mutation detection
RT in patients with sialuria.";
RL Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
RA Pramono Z.A.D., Lai P.S., Seah I.A.L., Ong B., Yee W.C.;
RT "mRNA analysis revealed splice mutation and expression alteration of GNE
RT gene in distal myopathy with rimmed vacuoles (DMRV) patients.";
RL Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 5), AND NUCLEOTIDE
RP SEQUENCE [MRNA] OF 24-694 (ISOFORM 3).
RC TISSUE=Hippocampus, and Tongue;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), NUCLEOTIDE SEQUENCE [MRNA] OF
RP 37-694 (ISOFORM 3), AND TISSUE SPECIFICITY.
RX PubMed=17597614; DOI=10.1016/j.febslet.2007.06.026;
RA Reinke S.O., Hinderlich S.;
RT "Prediction of three different isoforms of the human UDP-N-
RT acetylglucosamine 2-epimerase/N-acetylmannosamine kinase.";
RL FEBS Lett. 581:3327-3331(2007).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [11]
RP ACTIVITY REGULATION, AND INVOLVEMENT IN SIALURIA.
RX PubMed=2808337; DOI=10.1016/s0021-9258(19)84615-x;
RA Weiss P., Tietze F., Gahl W.A., Seppala R., Ashwell G.;
RT "Identification of the metabolic defect in sialuria.";
RL J. Biol. Chem. 264:17635-17636(1989).
RN [12]
RP FUNCTION.
RX PubMed=10334995; DOI=10.1126/science.284.5418.1372;
RA Keppler O.T., Hinderlich S., Langner J., Schwartz-Albiez R., Reutter W.,
RA Pawlita M.;
RT "UDP-GlcNAc 2-epimerase: a regulator of cell surface sialylation.";
RL Science 284:1372-1376(1999).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (2.84 ANGSTROMS) OF 406-720, AND SUBUNIT.
RX PubMed=19841673; DOI=10.1371/journal.pone.0007165;
RA Tong Y., Tempel W., Nedyalkova L., Mackenzie F., Park H.W.;
RT "Crystal structure of the N-acetylmannosamine kinase domain of GNE.";
RL PLoS ONE 4:E7165-E7165(2009).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (1.64 ANGSTROMS) OF 406-720 IN COMPLEX WITH ADP AND
RP N-ACETYLMANNOSAMINE, ZINC-BINDING SITES, ACTIVE SITE, AND SUBUNIT.
RX PubMed=22343627; DOI=10.1074/jbc.m111.318170;
RA Martinez J., Nguyen L.D., Hinderlich S., Zimmer R., Tauberger E.,
RA Reutter W., Saenger W., Fan H., Moniot S.;
RT "Crystal structures of N-acetylmannosamine kinase provide insights into
RT enzyme activity and inhibition.";
RL J. Biol. Chem. 287:13656-13665(2012).
RN [17]
RP VARIANT SIALURIA GLN-266.
RX PubMed=10356312; DOI=10.1006/mgme.1999.2852;
RA Ferreira H., Seppala R., Pinto R., Huizing M., Martins E., Braga A.C.,
RA Gomes L., Krasnewich D.M., Sa Miranda M.C., Gahl W.A.;
RT "Sialuria in a Portuguese girl: clinical, biochemical, and molecular
RT characteristics.";
RL Mol. Genet. Metab. 67:131-137(1999).
RN [18]
RP CHARACTERIZATION OF VARIANT SIALURIA GLN-266.
RX PubMed=11326336; DOI=10.1086/320598;
RA Leroy J.G., Seppala R., Huizing M., Dacremont G., De Simpel H.,
RA Van Coster R.N., Orvisky E., Krasnewich D.M., Gahl W.A.;
RT "Dominant inheritance of sialuria, an inborn error of feedback
RT inhibition.";
RL Am. J. Hum. Genet. 68:1419-1427(2001).
RN [19]
RP VARIANTS NM ASN-225; GLN-246; GLU-576; THR-631; MET-696 AND THR-712.
RX PubMed=11528398; DOI=10.1038/ng718;
RA Eisenberg I., Avidan N., Potikha T., Hochner H., Chen M., Olender T.,
RA Barash M., Shemesh M., Sadeh M., Grabov-Nardini G., Shmilevich I.,
RA Friedmann A., Karpati G., Bradley W.G., Baumbach L., Lancet D., Asher E.B.,
RA Beckmann J.S., Argov Z., Mitrani-Rosenbaum S.;
RT "The UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase gene is
RT mutated in recessive hereditary inclusion body myopathy.";
RL Nat. Genet. 29:83-87(2001).
RN [20]
RP VARIANT NM LEU-572.
RX PubMed=12325084; DOI=10.1002/ana.10341;
RA Arai A., Tanaka K., Ikeuchi T., Igarashi S., Kobayashi H., Asaka T.,
RA Date H., Saito M., Tanaka H., Kawasaki S., Uyama E., Mizusawa H.,
RA Fukuhara N., Tsuji S.;
RT "A novel mutation in the GNE gene and a linkage disequilibrium in Japanese
RT pedigrees.";
RL Ann. Neurol. 52:516-519(2002).
RN [21]
RP VARIANTS NM VAL-460 AND LEU-572.
RX PubMed=11916006; DOI=10.1007/s100380200004;
RA Kayashima T., Matsuo H., Satoh A., Ohta T., Yoshiura K., Matsumoto N.,
RA Nakane Y., Niikawa N., Kishino T.;
RT "Nonaka myopathy is caused by mutations in the UDP-N-acetylglucosamine-2-
RT epimerase/N-acetylmannosamine kinase gene (GNE).";
RL J. Hum. Genet. 47:77-79(2002).
RN [22]
RP VARIANTS NM ASN-225; GLN-246; TRP-246; VAL-460; VAL-524; LEU-572; GLU-576;
RP THR-631; HIS-675; MET-696 AND THR-712.
RX PubMed=12409274; DOI=10.1016/s1096-7192(02)00141-5;
RA Darvish D., Vahedifar P., Huo Y.;
RT "Four novel mutations associated with autosomal recessive inclusion body
RT myopathy (MIM: 600737).";
RL Mol. Genet. Metab. 77:252-256(2002).
RN [23]
RP VARIANTS NM LEU-572 AND VAL-631.
RX PubMed=12177386; DOI=10.1212/wnl.59.3.451;
RA Tomimitsu H., Ishikawa K., Shimizu J., Ohkoshi N., Kanazawa I.,
RA Mizusawa H.;
RT "Distal myopathy with rimmed vacuoles: novel mutations in the GNE gene.";
RL Neurology 59:451-454(2002).
RN [24]
RP VARIANTS NM GLN-132; VAL-176; CYS-177; GLN-306; ALA-331; TYR-378; THR-472;
RP LEU-572; THR-630 AND VAL-631.
RX PubMed=12473753; DOI=10.1212/01.wnl.0000041631.28557.c6;
RA Nishino I., Noguchi S., Murayama K., Driss A., Sugie K., Oya Y., Nagata T.,
RA Chida K., Takahashi T., Takusa Y., Ohi T., Nishimiya J., Sunohara N.,
RA Ciafaloni E., Kawai M., Aoki M., Nonaka I.;
RT "Distal myopathy with rimmed vacuoles is allelic to hereditary inclusion
RT body myopathy.";
RL Neurology 59:1689-1693(2002).
RN [25]
RP VARIANTS NM ALA-216 AND VAL-631.
RX PubMed=12473769; DOI=10.1212/01.wnl.0000039780.13681.ad;
RA Vasconcelos O.M., Raju R., Dalakas M.C.;
RT "GNE mutations in an American family with quadriceps-sparing IBM and lack
RT of mutations in s-IBM.";
RL Neurology 59:1776-1779(2002).
RN [26]
RP VARIANTS NM VAL-171 AND THR-712.
RX PubMed=12473780; DOI=10.1212/01.wnl.0000031808.04545.e0;
RA Broccolini A., Pescatori M., D'Amico A., Sabino A., Silvestri G., Ricci E.,
RA Servidei S., Tonali P.A., Mirabella M.;
RT "An Italian family with autosomal recessive inclusion-body myopathy and
RT mutations in the GNE gene.";
RL Neurology 59:1808-1809(2002).
RN [27]
RP VARIANTS NM LEU-36; PHE-200; ASN-225; GLN-246; VAL-303; TYR-378; VAL-460;
RP CYS-528; THR-557; LEU-572; GLU-576; THR-587; THR-631; VAL-631; MET-696 AND
RP THR-712.
RX PubMed=12497639; DOI=10.1002/humu.9100;
RA Eisenberg I., Grabov-Nardini G., Hochner H., Korner M., Sadeh M.,
RA Bertorini T., Bushby K., Castellan C., Felice K., Mendell J., Merlini L.,
RA Shilling C., Wirguin I., Argov Z., Mitrani-Rosenbaum S.;
RT "Mutations spectrum of GNE in hereditary inclusion body myopathy sparing
RT the quadriceps.";
RL Hum. Mutat. 21:99-99(2003).
RN [28]
RP VARIANT NM CYS-162.
RX PubMed=12811782; DOI=10.1002/mus.10391;
RA Del Bo R., Baron P., Prelle A., Serafini M., Moggio M., Di Fonzo A.,
RA Castagni M., Bresolin N., Comi G.P.;
RT "Novel missense mutation and large deletion of GNE gene in autosomal-
RT recessive inclusion-body myopathy.";
RL Muscle Nerve 28:113-117(2003).
RN [29]
RP VARIANTS NM THR-472 AND LEU-572.
RX PubMed=12913203; DOI=10.1212/01.wnl.0000061520.63546.8f;
RA Yabe I., Higashi T., Kikuchi S., Sasaki H., Fukazawa T., Yoshida K.,
RA Tashiro K.;
RT "GNE mutations causing distal myopathy with rimmed vacuoles with
RT inflammation.";
RL Neurology 61:384-386(2003).
RN [30]
RP VARIANTS NM SER-27; SER-206; GLN-246; SER-519 AND THR-600.
RX PubMed=15146476; DOI=10.1002/humu.9252;
RA Broccolini A., Ricci E., Cassandrini D., Gliubizzi C., Bruno C., Tonoli E.,
RA Silvestri G., Pescatori M., Rodolico C., Sinicropi S., Servidei S.,
RA Zara F., Minetti C., Tonali P.A., Mirabella M.;
RT "Novel GNE mutations in Italian families with autosomal recessive
RT hereditary inclusion-body myopathy.";
RL Hum. Mutat. 23:632-632(2004).
CC -!- FUNCTION: Regulates and initiates biosynthesis of N-acetylneuraminic
CC acid (NeuAc), a precursor of sialic acids. Plays an essential role in
CC early development (By similarity). Required for normal sialylation in
CC hematopoietic cells. Sialylation is implicated in cell adhesion, signal
CC transduction, tumorigenicity and metastatic behavior of malignant
CC cells. {ECO:0000250, ECO:0000269|PubMed:10334995}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + UDP-N-acetyl-alpha-D-glucosamine = H(+) + N-acetyl-D-
CC mannosamine + UDP; Xref=Rhea:RHEA:30683, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17122, ChEBI:CHEBI:57705,
CC ChEBI:CHEBI:58223; EC=3.2.1.183;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an N-acyl-D-mannosamine + ATP = ADP + an N-acyl-D-mannosamine
CC 6-phosphate + H(+); Xref=Rhea:RHEA:23832, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16062, ChEBI:CHEBI:30616, ChEBI:CHEBI:57666,
CC ChEBI:CHEBI:456216; EC=2.7.1.60;
CC -!- ACTIVITY REGULATION: Allosterically regulated (Probable); feedback
CC inhibited by cytidine monophosphate-N-acetylneuraminic acid (CMP-
CC Neu5Ac), the end product of neuraminic acid biosynthesis. Activity is
CC dependent on oligomerization. The monomer is inactive, whereas the
CC dimer catalyzes only the phosphorylation of N-acetylmannosamine; the
CC hexamer is fully active for both enzyme activities (By similarity). Up-
CC regulated after PKC-dependent phosphorylation. {ECO:0000250,
CC ECO:0000269|PubMed:2808337}.
CC -!- PATHWAY: Amino-sugar metabolism; N-acetylneuraminate biosynthesis.
CC -!- SUBUNIT: Homodimer and homohexamer. {ECO:0000269|PubMed:19841673,
CC ECO:0000269|PubMed:22343627}.
CC -!- INTERACTION:
CC Q9Y223; P12814: ACTN1; NbExp=3; IntAct=EBI-4291090, EBI-351710;
CC Q9Y223; Q6UY14-3: ADAMTSL4; NbExp=3; IntAct=EBI-4291090, EBI-10173507;
CC Q9Y223; Q969Y2: GTPBP3; NbExp=3; IntAct=EBI-4291090, EBI-740290;
CC Q9Y223; Q15323: KRT31; NbExp=3; IntAct=EBI-4291090, EBI-948001;
CC Q9Y223; P60370: KRTAP10-5; NbExp=3; IntAct=EBI-4291090, EBI-10172150;
CC Q9Y223; P60409: KRTAP10-7; NbExp=3; IntAct=EBI-4291090, EBI-10172290;
CC Q9Y223; P60410: KRTAP10-8; NbExp=3; IntAct=EBI-4291090, EBI-10171774;
CC Q9Y223; P60411: KRTAP10-9; NbExp=3; IntAct=EBI-4291090, EBI-10172052;
CC Q9Y223; Q9BQ66: KRTAP4-12; NbExp=3; IntAct=EBI-4291090, EBI-739863;
CC Q9Y223; P26371: KRTAP5-9; NbExp=3; IntAct=EBI-4291090, EBI-3958099;
CC Q9Y223; Q9BYQ4: KRTAP9-2; NbExp=3; IntAct=EBI-4291090, EBI-1044640;
CC Q9Y223; Q7Z3S9: NOTCH2NLA; NbExp=4; IntAct=EBI-4291090, EBI-945833;
CC Q9Y223; O43597: SPRY2; NbExp=3; IntAct=EBI-4291090, EBI-742487;
CC Q9Y223-2; Q6UY14-3: ADAMTSL4; NbExp=3; IntAct=EBI-11975289, EBI-10173507;
CC Q9Y223-2; Q6P5X5: C22orf39; NbExp=3; IntAct=EBI-11975289, EBI-7317823;
CC Q9Y223-2; P27918: CFP; NbExp=3; IntAct=EBI-11975289, EBI-9038570;
CC Q9Y223-2; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-11975289, EBI-3867333;
CC Q9Y223-2; Q16610: ECM1; NbExp=3; IntAct=EBI-11975289, EBI-947964;
CC Q9Y223-2; Q9UHF1: EGFL7; NbExp=3; IntAct=EBI-11975289, EBI-949532;
CC Q9Y223-2; P28799: GRN; NbExp=6; IntAct=EBI-11975289, EBI-747754;
CC Q9Y223-2; P49639: HOXA1; NbExp=5; IntAct=EBI-11975289, EBI-740785;
CC Q9Y223-2; Q5T749: KPRP; NbExp=3; IntAct=EBI-11975289, EBI-10981970;
CC Q9Y223-2; Q15323: KRT31; NbExp=3; IntAct=EBI-11975289, EBI-948001;
CC Q9Y223-2; O76011: KRT34; NbExp=3; IntAct=EBI-11975289, EBI-1047093;
CC Q9Y223-2; Q6A162: KRT40; NbExp=3; IntAct=EBI-11975289, EBI-10171697;
CC Q9Y223-2; P78385: KRT83; NbExp=3; IntAct=EBI-11975289, EBI-10221390;
CC Q9Y223-2; P78386: KRT85; NbExp=3; IntAct=EBI-11975289, EBI-1049371;
CC Q9Y223-2; O43790: KRT86; NbExp=3; IntAct=EBI-11975289, EBI-9996498;
CC Q9Y223-2; Q07627: KRTAP1-1; NbExp=3; IntAct=EBI-11975289, EBI-11959885;
CC Q9Y223-2; Q8IUG1: KRTAP1-3; NbExp=3; IntAct=EBI-11975289, EBI-11749135;
CC Q9Y223-2; P60409: KRTAP10-7; NbExp=3; IntAct=EBI-11975289, EBI-10172290;
CC Q9Y223-2; P60410: KRTAP10-8; NbExp=5; IntAct=EBI-11975289, EBI-10171774;
CC Q9Y223-2; Q8IUC1: KRTAP11-1; NbExp=3; IntAct=EBI-11975289, EBI-1052037;
CC Q9Y223-2; P60328: KRTAP12-3; NbExp=3; IntAct=EBI-11975289, EBI-11953334;
CC Q9Y223-2; Q52LG2: KRTAP13-2; NbExp=3; IntAct=EBI-11975289, EBI-11953846;
CC Q9Y223-2; Q3SY46: KRTAP13-3; NbExp=3; IntAct=EBI-11975289, EBI-10241252;
CC Q9Y223-2; Q9BYP8: KRTAP17-1; NbExp=3; IntAct=EBI-11975289, EBI-11988175;
CC Q9Y223-2; Q3LHN2: KRTAP19-2; NbExp=5; IntAct=EBI-11975289, EBI-12196745;
CC Q9Y223-2; Q3SYF9: KRTAP19-7; NbExp=3; IntAct=EBI-11975289, EBI-10241353;
CC Q9Y223-2; Q9BYR8: KRTAP3-1; NbExp=3; IntAct=EBI-11975289, EBI-9996449;
CC Q9Y223-2; Q9BYR6: KRTAP3-3; NbExp=3; IntAct=EBI-11975289, EBI-3957694;
CC Q9Y223-2; A0A087WY89: KRTAP4-1; NbExp=3; IntAct=EBI-11975289, EBI-11957260;
CC Q9Y223-2; Q9BYQ6: KRTAP4-11; NbExp=3; IntAct=EBI-11975289, EBI-10302392;
CC Q9Y223-2; Q9BYR3: KRTAP4-4; NbExp=3; IntAct=EBI-11975289, EBI-11958132;
CC Q9Y223-2; P26371: KRTAP5-9; NbExp=3; IntAct=EBI-11975289, EBI-3958099;
CC Q9Y223-2; Q3LI64: KRTAP6-1; NbExp=3; IntAct=EBI-11975289, EBI-12111050;
CC Q9Y223-2; Q3LI66: KRTAP6-2; NbExp=3; IntAct=EBI-11975289, EBI-11962084;
CC Q9Y223-2; Q9BYQ4: KRTAP9-2; NbExp=3; IntAct=EBI-11975289, EBI-1044640;
CC Q9Y223-2; Q9BYQ3: KRTAP9-3; NbExp=3; IntAct=EBI-11975289, EBI-1043191;
CC Q9Y223-2; Q9BYQ0: KRTAP9-8; NbExp=3; IntAct=EBI-11975289, EBI-11958364;
CC Q9Y223-2; Q99750: MDFI; NbExp=3; IntAct=EBI-11975289, EBI-724076;
CC Q9Y223-2; Q8IV28: NID2; NbExp=3; IntAct=EBI-11975289, EBI-10261509;
CC Q9Y223-2; P0DPK4: NOTCH2NLC; NbExp=3; IntAct=EBI-11975289, EBI-22310682;
CC Q9Y223-2; O15496: PLA2G10; NbExp=3; IntAct=EBI-11975289, EBI-726466;
CC Q9Y223-2; O43609: SPRY1; NbExp=3; IntAct=EBI-11975289, EBI-3866665;
CC Q9Y223-2; O43610: SPRY3; NbExp=3; IntAct=EBI-11975289, EBI-12290641;
CC Q9Y223-2; P14373: TRIM27; NbExp=3; IntAct=EBI-11975289, EBI-719493;
CC Q9Y223-2; Q8IWZ5: TRIM42; NbExp=3; IntAct=EBI-11975289, EBI-5235829;
CC Q9Y223-2; Q15654: TRIP6; NbExp=3; IntAct=EBI-11975289, EBI-742327;
CC Q9Y223-2; O14817: TSPAN4; NbExp=3; IntAct=EBI-11975289, EBI-8652667;
CC Q9Y223-2; Q2TAL6: VWC2; NbExp=3; IntAct=EBI-11975289, EBI-11957238;
CC Q9Y223-2; Q9BRX9: WDR83; NbExp=3; IntAct=EBI-11975289, EBI-7705033;
CC Q9Y223-2; O76024: WFS1; NbExp=3; IntAct=EBI-11975289, EBI-720609;
CC Q9Y223-2; Q9NZC7-5: WWOX; NbExp=3; IntAct=EBI-11975289, EBI-12040603;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1; Synonyms=GNE1;
CC IsoId=Q9Y223-1; Sequence=Displayed;
CC Name=2; Synonyms=GNE2;
CC IsoId=Q9Y223-2; Sequence=VSP_041027;
CC Name=3; Synonyms=GNE3;
CC IsoId=Q9Y223-3; Sequence=VSP_041028;
CC Name=4;
CC IsoId=Q9Y223-4; Sequence=VSP_043474;
CC Name=5;
CC IsoId=Q9Y223-5; Sequence=VSP_043975, VSP_043976;
CC -!- TISSUE SPECIFICITY: Highest expression in liver and placenta. Also
CC found in heart, brain, lung, kidney, skeletal muscle and pancreas.
CC Isoform 1 is expressed in heart, brain, kidney, liver, placenta, lung,
CC spleen, pancreas, skeletal muscle and colon. Isoform 2 is expressed
CC mainly in placenta, but also in brain, kidney, liver, lung, pancreas
CC and colon. Isoform 3 is expressed at low level in kidney, liver,
CC placenta and colon. {ECO:0000269|PubMed:10330343,
CC ECO:0000269|PubMed:10431835, ECO:0000269|PubMed:17597614}.
CC -!- PTM: Phosphorylated by PKC. {ECO:0000250}.
CC -!- DISEASE: Sialuria (SIALURIA) [MIM:269921]: In sialuria, free sialic
CC acid accumulates in the cytoplasm and gram quantities of neuraminic
CC acid are secreted in the urine. The metabolic defect involves lack of
CC feedback inhibition of UDP-GlcNAc 2-epimerase by CMP-Neu5Ac, resulting
CC in constitutive overproduction of free Neu5Ac. Clinical features
CC include variable degrees of developmental delay, coarse facial features
CC and hepatomegaly. Sialuria inheritance is autosomal dominant.
CC {ECO:0000269|PubMed:10330343, ECO:0000269|PubMed:10356312,
CC ECO:0000269|PubMed:11326336, ECO:0000269|PubMed:2808337}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- DISEASE: Nonaka myopathy (NM) [MIM:605820]: Autosomal recessive
CC muscular disorder, allelic to inclusion body myopathy 2. It is
CC characterized by weakness of the anterior compartment of the lower
CC limbs with onset in early adulthood, and sparing of the quadriceps
CC muscles. As the inclusion body myopathy, NM is histologically
CC characterized by the presence of numerous rimmed vacuoles without
CC inflammatory changes in muscle specimens. {ECO:0000269|PubMed:11528398,
CC ECO:0000269|PubMed:11916006, ECO:0000269|PubMed:12177386,
CC ECO:0000269|PubMed:12325084, ECO:0000269|PubMed:12409274,
CC ECO:0000269|PubMed:12473753, ECO:0000269|PubMed:12473769,
CC ECO:0000269|PubMed:12473780, ECO:0000269|PubMed:12497639,
CC ECO:0000269|PubMed:12811782, ECO:0000269|PubMed:12913203,
CC ECO:0000269|PubMed:15146476}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: In the N-terminal section; belongs to the UDP-N-
CC acetylglucosamine 2-epimerase family. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the ROK (NagC/XylR)
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAH12414.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AJ238764; CAB42607.1; -; mRNA.
DR EMBL; AF051852; AAD32251.1; -; mRNA.
DR EMBL; AF155663; AAD38197.1; -; mRNA.
DR EMBL; AF317635; AAG31661.1; -; Genomic_DNA.
DR EMBL; EU093084; ABU55403.1; -; mRNA.
DR EMBL; AK295562; BAH12108.1; -; mRNA.
DR EMBL; AK296687; BAH12414.1; ALT_INIT; mRNA.
DR EMBL; AK312539; BAG35438.1; -; mRNA.
DR EMBL; AM697708; CAM91424.1; -; mRNA.
DR EMBL; AM697709; CAM91425.1; -; mRNA.
DR EMBL; AL158830; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471071; EAW58307.1; -; Genomic_DNA.
DR EMBL; CH471071; EAW58309.1; -; Genomic_DNA.
DR EMBL; BC121179; AAI21180.1; -; mRNA.
DR CCDS; CCDS47965.1; -. [Q9Y223-2]
DR CCDS; CCDS55308.1; -. [Q9Y223-5]
DR CCDS; CCDS55309.1; -. [Q9Y223-4]
DR CCDS; CCDS6602.1; -. [Q9Y223-1]
DR RefSeq; NP_001121699.1; NM_001128227.2. [Q9Y223-2]
DR RefSeq; NP_001177312.1; NM_001190383.1. [Q9Y223-4]
DR RefSeq; NP_001177313.1; NM_001190384.1. [Q9Y223-5]
DR RefSeq; NP_001177317.1; NM_001190388.1.
DR RefSeq; NP_005467.1; NM_005476.5. [Q9Y223-1]
DR RefSeq; XP_016869656.1; XM_017014167.1. [Q9Y223-1]
DR PDB; 2YHW; X-ray; 1.64 A; A=406-720.
DR PDB; 2YHY; X-ray; 1.82 A; A=406-720.
DR PDB; 2YI1; X-ray; 2.15 A; A=406-720.
DR PDB; 3EO3; X-ray; 2.84 A; A/B/C=406-720.
DR PDB; 4ZHT; X-ray; 2.69 A; A/B/C/D=1-405.
DR PDBsum; 2YHW; -.
DR PDBsum; 2YHY; -.
DR PDBsum; 2YI1; -.
DR PDBsum; 3EO3; -.
DR PDBsum; 4ZHT; -.
DR AlphaFoldDB; Q9Y223; -.
DR SMR; Q9Y223; -.
DR BioGRID; 115337; 93.
DR IntAct; Q9Y223; 65.
DR STRING; 9606.ENSP00000379839; -.
DR BindingDB; Q9Y223; -.
DR ChEMBL; CHEMBL4523504; -.
DR iPTMnet; Q9Y223; -.
DR MetOSite; Q9Y223; -.
DR PhosphoSitePlus; Q9Y223; -.
DR BioMuta; GNE; -.
DR DMDM; 45476991; -.
DR EPD; Q9Y223; -.
DR jPOST; Q9Y223; -.
DR MassIVE; Q9Y223; -.
DR MaxQB; Q9Y223; -.
DR PaxDb; Q9Y223; -.
DR PeptideAtlas; Q9Y223; -.
DR PRIDE; Q9Y223; -.
DR ProteomicsDB; 38009; -.
DR ProteomicsDB; 85604; -. [Q9Y223-1]
DR ProteomicsDB; 85605; -. [Q9Y223-2]
DR ProteomicsDB; 85606; -. [Q9Y223-3]
DR ProteomicsDB; 85607; -. [Q9Y223-4]
DR ProteomicsDB; 85608; -. [Q9Y223-5]
DR Antibodypedia; 2058; 248 antibodies from 27 providers.
DR DNASU; 10020; -.
DR Ensembl; ENST00000396594.8; ENSP00000379839.3; ENSG00000159921.20. [Q9Y223-2]
DR Ensembl; ENST00000447283.6; ENSP00000414760.2; ENSG00000159921.20. [Q9Y223-4]
DR Ensembl; ENST00000539208.5; ENSP00000445117.1; ENSG00000159921.20. [Q9Y223-5]
DR Ensembl; ENST00000642385.2; ENSP00000494141.2; ENSG00000159921.20. [Q9Y223-1]
DR GeneID; 10020; -.
DR KEGG; hsa:10020; -.
DR MANE-Select; ENST00000642385.2; ENSP00000494141.2; NM_005476.7; NP_005467.1.
DR UCSC; uc010mlg.5; human. [Q9Y223-1]
DR CTD; 10020; -.
DR DisGeNET; 10020; -.
DR GeneCards; GNE; -.
DR GeneReviews; GNE; -.
DR HGNC; HGNC:23657; GNE.
DR HPA; ENSG00000159921; Group enriched (intestine, liver, salivary gland).
DR MalaCards; GNE; -.
DR MIM; 269921; phenotype.
DR MIM; 600737; phenotype.
DR MIM; 603824; gene.
DR MIM; 605820; phenotype.
DR neXtProt; NX_Q9Y223; -.
DR OpenTargets; ENSG00000159921; -.
DR Orphanet; 602; GNE myopathy.
DR Orphanet; 438207; Severe autosomal recessive macrothrombocytopenia.
DR Orphanet; 3166; Sialuria.
DR PharmGKB; PA134987566; -.
DR VEuPathDB; HostDB:ENSG00000159921; -.
DR eggNOG; ENOG502QUGI; Eukaryota.
DR GeneTree; ENSGT00390000017246; -.
DR HOGENOM; CLU_023411_0_0_1; -.
DR InParanoid; Q9Y223; -.
DR OrthoDB; 225119at2759; -.
DR PhylomeDB; Q9Y223; -.
DR TreeFam; TF332239; -.
DR BRENDA; 2.7.1.60; 2681.
DR BRENDA; 3.2.1.183; 2681.
DR BRENDA; 5.1.3.14; 2681.
DR PathwayCommons; Q9Y223; -.
DR Reactome; R-HSA-4085001; Sialic acid metabolism.
DR Reactome; R-HSA-4085011; Defective GNE causes sialuria, NK and IBM2.
DR SignaLink; Q9Y223; -.
DR SIGNOR; Q9Y223; -.
DR UniPathway; UPA00630; -.
DR BioGRID-ORCS; 10020; 37 hits in 1089 CRISPR screens.
DR ChiTaRS; GNE; human.
DR EvolutionaryTrace; Q9Y223; -.
DR GeneWiki; GNE_(gene); -.
DR GenomeRNAi; 10020; -.
DR Pharos; Q9Y223; Tbio.
DR PRO; PR:Q9Y223; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q9Y223; protein.
DR Bgee; ENSG00000159921; Expressed in mucosa of sigmoid colon and 205 other tissues.
DR Genevisible; Q9Y223; HS.
DR GO; GO:0005737; C:cytoplasm; TAS:ProtInc.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009384; F:N-acylmannosamine kinase activity; IBA:GO_Central.
DR GO; GO:0008761; F:UDP-N-acetylglucosamine 2-epimerase activity; IBA:GO_Central.
DR GO; GO:0007155; P:cell adhesion; TAS:ProtInc.
DR GO; GO:0006045; P:N-acetylglucosamine biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006054; P:N-acetylneuraminate metabolic process; TAS:ProtInc.
DR GO; GO:0006047; P:UDP-N-acetylglucosamine metabolic process; IEA:InterPro.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR000600; ROK.
DR InterPro; IPR020004; UDP-GlcNAc_Epase.
DR InterPro; IPR003331; UDP_GlcNAc_Epimerase_2_dom.
DR PANTHER; PTHR18964; PTHR18964; 1.
DR Pfam; PF02350; Epimerase_2; 1.
DR Pfam; PF00480; ROK; 1.
DR SUPFAM; SSF53067; SSF53067; 1.
DR TIGRFAMs; TIGR03568; NeuC_NnaA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Allosteric enzyme; Alternative splicing; ATP-binding;
KW Cytoplasm; Disease variant; Hydrolase; Kinase; Metal-binding;
KW Multifunctional enzyme; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Transferase; Zinc.
FT CHAIN 1..722
FT /note="Bifunctional UDP-N-acetylglucosamine 2-epimerase/N-
FT acetylmannosamine kinase"
FT /id="PRO_0000095716"
FT REGION 1..?
FT /note="UDP-N-acetylglucosamine 2-epimerase"
FT REGION 406..722
FT /note="N-acetylmannosamine kinase"
FT ACT_SITE 517
FT /evidence="ECO:0000269|PubMed:22343627"
FT BINDING 411..420
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 477
FT /ligand="substrate"
FT BINDING 489
FT /ligand="substrate"
FT BINDING 517
FT /ligand="substrate"
FT BINDING 543..552
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 566
FT /ligand="substrate"
FT BINDING 569
FT /ligand="substrate"
FT BINDING 569
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT BINDING 579
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT BINDING 581
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT BINDING 586
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT BINDING 588
FT /ligand="substrate"
FT VAR_SEQ 1..59
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_043975"
FT VAR_SEQ 1..55
FT /note="MEKNGNNRKLRVCVATCNRADYSKLAPIMFGIKTEPEFFELDVVVLGSHLID
FT DYG -> MPIGDCSVAAKPRKQLLCSLFQTTLGYRARASGWKPMVICRGSHAFKDLI
FT (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:17597614"
FT /id="VSP_041028"
FT VAR_SEQ 1
FT /note="M -> METYGYLQRESCFQGPHELYFKNLSKRNKQIM (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:17597614"
FT /id="VSP_041027"
FT VAR_SEQ 206..256
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_043976"
FT VAR_SEQ 471..544
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|Ref.5"
FT /id="VSP_043474"
FT VARIANT 27
FT /note="P -> S (in NM; dbSNP:rs1554664064)"
FT /evidence="ECO:0000269|PubMed:15146476"
FT /id="VAR_021771"
FT VARIANT 36
FT /note="P -> L (in NM)"
FT /evidence="ECO:0000269|PubMed:12497639"
FT /id="VAR_017945"
FT VARIANT 132
FT /note="H -> Q (in NM)"
FT /evidence="ECO:0000269|PubMed:12473753"
FT /id="VAR_021772"
FT VARIANT 162
FT /note="R -> C (in NM; dbSNP:rs769215411)"
FT /evidence="ECO:0000269|PubMed:12811782"
FT /id="VAR_021773"
FT VARIANT 171
FT /note="M -> V (in NM; dbSNP:rs121908634)"
FT /evidence="ECO:0000269|PubMed:12473780"
FT /id="VAR_021774"
FT VARIANT 176
FT /note="D -> V (in NM; dbSNP:rs139425890)"
FT /evidence="ECO:0000269|PubMed:12473753"
FT /id="VAR_021775"
FT VARIANT 177
FT /note="R -> C (in NM; dbSNP:rs539332585)"
FT /evidence="ECO:0000269|PubMed:12473753"
FT /id="VAR_021776"
FT VARIANT 200
FT /note="I -> F (in NM; dbSNP:rs369328625)"
FT /evidence="ECO:0000269|PubMed:12497639"
FT /id="VAR_017946"
FT VARIANT 206
FT /note="G -> S (in NM; moderate phenotype with unusual
FT involvement of quadriceps; dbSNP:rs766266918)"
FT /evidence="ECO:0000269|PubMed:15146476"
FT /id="VAR_021777"
FT VARIANT 216
FT /note="V -> A (in NM; dbSNP:rs779694939)"
FT /evidence="ECO:0000269|PubMed:12473769"
FT /id="VAR_021778"
FT VARIANT 225
FT /note="D -> N (in NM; dbSNP:rs121908630)"
FT /evidence="ECO:0000269|PubMed:11528398,
FT ECO:0000269|PubMed:12409274, ECO:0000269|PubMed:12497639"
FT /id="VAR_017947"
FT VARIANT 246
FT /note="R -> Q (in NM; dbSNP:rs121908629)"
FT /evidence="ECO:0000269|PubMed:11528398,
FT ECO:0000269|PubMed:12409274, ECO:0000269|PubMed:12497639,
FT ECO:0000269|PubMed:15146476"
FT /id="VAR_017948"
FT VARIANT 246
FT /note="R -> W (in NM; dbSNP:rs773729410)"
FT /evidence="ECO:0000269|PubMed:12409274"
FT /id="VAR_017949"
FT VARIANT 263
FT /note="R -> L (in SIALURIA; strong reduction of feedback
FT inhibition by CMP-Neu5Ac; dbSNP:rs121908623)"
FT /evidence="ECO:0000269|PubMed:10330343"
FT /id="VAR_017950"
FT VARIANT 266
FT /note="R -> Q (in SIALURIA; abolishes feedback inhibition
FT by CMP-Neu5Ac; dbSNP:rs121908622)"
FT /evidence="ECO:0000269|PubMed:10330343,
FT ECO:0000269|PubMed:10356312, ECO:0000269|PubMed:11326336"
FT /id="VAR_017951"
FT VARIANT 266
FT /note="R -> W (in sialuria; dbSNP:rs121908621)"
FT /evidence="ECO:0000269|PubMed:10330343"
FT /id="VAR_017952"
FT VARIANT 303
FT /note="C -> V (in NM; requires 2 nucleotide substitutions;
FT dbSNP:rs121908633)"
FT /evidence="ECO:0000269|PubMed:12497639"
FT /id="VAR_017953"
FT VARIANT 306
FT /note="R -> Q (in NM; dbSNP:rs1455785164)"
FT /evidence="ECO:0000269|PubMed:12473753"
FT /id="VAR_021779"
FT VARIANT 331
FT /note="V -> A (in NM)"
FT /evidence="ECO:0000269|PubMed:12473753"
FT /id="VAR_021780"
FT VARIANT 378
FT /note="D -> Y (in NM; dbSNP:rs199877522)"
FT /evidence="ECO:0000269|PubMed:12473753,
FT ECO:0000269|PubMed:12497639"
FT /id="VAR_017954"
FT VARIANT 460
FT /note="A -> V (in NM; dbSNP:rs121908631)"
FT /evidence="ECO:0000269|PubMed:11916006,
FT ECO:0000269|PubMed:12409274, ECO:0000269|PubMed:12497639"
FT /id="VAR_017955"
FT VARIANT 472
FT /note="I -> T (in NM)"
FT /evidence="ECO:0000269|PubMed:12473753,
FT ECO:0000269|PubMed:12913203"
FT /id="VAR_021781"
FT VARIANT 519
FT /note="N -> S (in NM; dbSNP:rs1554658910)"
FT /evidence="ECO:0000269|PubMed:15146476"
FT /id="VAR_021782"
FT VARIANT 524
FT /note="A -> V (in NM; dbSNP:rs764698870)"
FT /evidence="ECO:0000269|PubMed:12409274"
FT /id="VAR_017956"
FT VARIANT 528
FT /note="F -> C (in NM; dbSNP:rs986773986)"
FT /evidence="ECO:0000269|PubMed:12497639"
FT /id="VAR_017957"
FT VARIANT 557
FT /note="I -> T (in NM; dbSNP:rs886043979)"
FT /evidence="ECO:0000269|PubMed:12497639"
FT /id="VAR_017958"
FT VARIANT 572
FT /note="V -> L (in NM; dbSNP:rs121908632)"
FT /evidence="ECO:0000269|PubMed:11916006,
FT ECO:0000269|PubMed:12177386, ECO:0000269|PubMed:12325084,
FT ECO:0000269|PubMed:12409274, ECO:0000269|PubMed:12473753,
FT ECO:0000269|PubMed:12497639, ECO:0000269|PubMed:12913203"
FT /id="VAR_017959"
FT VARIANT 576
FT /note="G -> E (in NM; dbSNP:rs121908625)"
FT /evidence="ECO:0000269|PubMed:11528398,
FT ECO:0000269|PubMed:12409274, ECO:0000269|PubMed:12497639"
FT /id="VAR_017960"
FT VARIANT 587
FT /note="I -> T (in NM; dbSNP:rs748949603)"
FT /evidence="ECO:0000269|PubMed:12497639"
FT /id="VAR_017961"
FT VARIANT 600
FT /note="A -> T (in NM; dbSNP:rs387906347)"
FT /evidence="ECO:0000269|PubMed:15146476"
FT /id="VAR_021783"
FT VARIANT 630
FT /note="A -> T (in NM; dbSNP:rs1382191649)"
FT /evidence="ECO:0000269|PubMed:12473753"
FT /id="VAR_021784"
FT VARIANT 631
FT /note="A -> T (in NM; dbSNP:rs121908626)"
FT /evidence="ECO:0000269|PubMed:11528398,
FT ECO:0000269|PubMed:12409274, ECO:0000269|PubMed:12497639"
FT /id="VAR_017962"
FT VARIANT 631
FT /note="A -> V (in NM; dbSNP:rs62541771)"
FT /evidence="ECO:0000269|PubMed:12177386,
FT ECO:0000269|PubMed:12473753, ECO:0000269|PubMed:12473769,
FT ECO:0000269|PubMed:12497639"
FT /id="VAR_017963"
FT VARIANT 675
FT /note="Y -> H (in NM; dbSNP:rs1191857860)"
FT /evidence="ECO:0000269|PubMed:12409274"
FT /id="VAR_017964"
FT VARIANT 696
FT /note="V -> M (in NM; dbSNP:rs121908627)"
FT /evidence="ECO:0000269|PubMed:11528398,
FT ECO:0000269|PubMed:12409274, ECO:0000269|PubMed:12497639"
FT /id="VAR_017965"
FT VARIANT 712
FT /note="M -> T (in NM; dbSNP:rs28937594)"
FT /evidence="ECO:0000269|PubMed:11528398,
FT ECO:0000269|PubMed:12409274, ECO:0000269|PubMed:12473780,
FT ECO:0000269|PubMed:12497639"
FT /id="VAR_017966"
FT CONFLICT 338
FT /note="D -> G (in Ref. 6; BAH12108)"
FT /evidence="ECO:0000305"
FT CONFLICT 359
FT /note="K -> R (in Ref. 6; BAH12414)"
FT /evidence="ECO:0000305"
FT CONFLICT 364
FT /note="G -> V (in Ref. 6; BAH12108)"
FT /evidence="ECO:0000305"
FT CONFLICT 382
FT /note="P -> L (in Ref. 6; BAH12108)"
FT /evidence="ECO:0000305"
FT CONFLICT 498
FT /note="V -> A (in Ref. 6; BAH12108)"
FT /evidence="ECO:0000305"
FT CONFLICT 521
FT /note="A -> V (in Ref. 6; BAH12414)"
FT /evidence="ECO:0000305"
FT STRAND 10..16
FT /evidence="ECO:0007829|PDB:4ZHT"
FT HELIX 19..33
FT /evidence="ECO:0007829|PDB:4ZHT"
FT TURN 36..38
FT /evidence="ECO:0007829|PDB:4ZHT"
FT STRAND 39..46
FT /evidence="ECO:0007829|PDB:4ZHT"
FT HELIX 47..50
FT /evidence="ECO:0007829|PDB:4ZHT"
FT HELIX 52..54
FT /evidence="ECO:0007829|PDB:4ZHT"
FT HELIX 58..63
FT /evidence="ECO:0007829|PDB:4ZHT"
FT STRAND 68..72
FT /evidence="ECO:0007829|PDB:4ZHT"
FT STRAND 77..80
FT /evidence="ECO:0007829|PDB:4ZHT"
FT HELIX 81..102
FT /evidence="ECO:0007829|PDB:4ZHT"
FT STRAND 105..113
FT /evidence="ECO:0007829|PDB:4ZHT"
FT HELIX 114..125
FT /evidence="ECO:0007829|PDB:4ZHT"
FT STRAND 129..134
FT /evidence="ECO:0007829|PDB:4ZHT"
FT HELIX 142..153
FT /evidence="ECO:0007829|PDB:4ZHT"
FT STRAND 155..161
FT /evidence="ECO:0007829|PDB:4ZHT"
FT HELIX 162..170
FT /evidence="ECO:0007829|PDB:4ZHT"
FT HELIX 175..177
FT /evidence="ECO:0007829|PDB:4ZHT"
FT STRAND 178..180
FT /evidence="ECO:0007829|PDB:4ZHT"
FT HELIX 185..189
FT /evidence="ECO:0007829|PDB:4ZHT"
FT HELIX 197..205
FT /evidence="ECO:0007829|PDB:4ZHT"
FT STRAND 215..218
FT /evidence="ECO:0007829|PDB:4ZHT"
FT HELIX 223..225
FT /evidence="ECO:0007829|PDB:4ZHT"
FT HELIX 226..243
FT /evidence="ECO:0007829|PDB:4ZHT"
FT STRAND 247..250
FT /evidence="ECO:0007829|PDB:4ZHT"
FT HELIX 258..267
FT /evidence="ECO:0007829|PDB:4ZHT"
FT HELIX 270..272
FT /evidence="ECO:0007829|PDB:4ZHT"
FT STRAND 276..280
FT /evidence="ECO:0007829|PDB:4ZHT"
FT HELIX 284..292
FT /evidence="ECO:0007829|PDB:4ZHT"
FT STRAND 295..299
FT /evidence="ECO:0007829|PDB:4ZHT"
FT HELIX 302..306
FT /evidence="ECO:0007829|PDB:4ZHT"
FT HELIX 308..311
FT /evidence="ECO:0007829|PDB:4ZHT"
FT STRAND 315..320
FT /evidence="ECO:0007829|PDB:4ZHT"
FT TURN 321..324
FT /evidence="ECO:0007829|PDB:4ZHT"
FT STRAND 331..335
FT /evidence="ECO:0007829|PDB:4ZHT"
FT HELIX 340..350
FT /evidence="ECO:0007829|PDB:4ZHT"
FT HELIX 366..376
FT /evidence="ECO:0007829|PDB:4ZHT"
FT STRAND 406..414
FT /evidence="ECO:0007829|PDB:2YHW"
FT STRAND 416..425
FT /evidence="ECO:0007829|PDB:2YHW"
FT STRAND 430..437
FT /evidence="ECO:0007829|PDB:2YHW"
FT HELIX 442..462
FT /evidence="ECO:0007829|PDB:2YHW"
FT STRAND 465..479
FT /evidence="ECO:0007829|PDB:2YHW"
FT TURN 480..483
FT /evidence="ECO:0007829|PDB:2YHW"
FT STRAND 484..487
FT /evidence="ECO:0007829|PDB:2YHW"
FT STRAND 492..494
FT /evidence="ECO:0007829|PDB:2YHW"
FT STRAND 496..499
FT /evidence="ECO:0007829|PDB:2YHW"
FT HELIX 501..508
FT /evidence="ECO:0007829|PDB:2YHW"
FT STRAND 512..516
FT /evidence="ECO:0007829|PDB:2YHW"
FT HELIX 517..527
FT /evidence="ECO:0007829|PDB:2YHW"
FT TURN 530..533
FT /evidence="ECO:0007829|PDB:2YHW"
FT STRAND 537..552
FT /evidence="ECO:0007829|PDB:2YHW"
FT HELIX 567..569
FT /evidence="ECO:0007829|PDB:2YHW"
FT STRAND 571..574
FT /evidence="ECO:0007829|PDB:2YHW"
FT STRAND 584..586
FT /evidence="ECO:0007829|PDB:2YHW"
FT HELIX 587..591
FT /evidence="ECO:0007829|PDB:2YHW"
FT HELIX 593..605
FT /evidence="ECO:0007829|PDB:2YHW"
FT HELIX 624..632
FT /evidence="ECO:0007829|PDB:2YHW"
FT HELIX 636..659
FT /evidence="ECO:0007829|PDB:2YHW"
FT STRAND 663..669
FT /evidence="ECO:0007829|PDB:2YHW"
FT HELIX 672..686
FT /evidence="ECO:0007829|PDB:2YHW"
FT HELIX 689..691
FT /evidence="ECO:0007829|PDB:2YHW"
FT STRAND 695..698
FT /evidence="ECO:0007829|PDB:2YHW"
FT HELIX 704..716
FT /evidence="ECO:0007829|PDB:2YHW"
SQ 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
