Full text data of NAGK
NAGK
[Confidence: low (only semi-automatic identification from reviews)]
N-acetyl-D-glucosamine kinase; N-acetylglucosamine kinase; 2.7.1.59 (GlcNAc kinase)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
N-acetyl-D-glucosamine kinase; N-acetylglucosamine kinase; 2.7.1.59 (GlcNAc kinase)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q9UJ70
ID NAGK_HUMAN Reviewed; 344 AA.
AC Q9UJ70; B4DLZ5; Q53HD5; Q6IA84; Q9BS29; Q9BVP0; Q9NV37;
DT 01-NOV-2002, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 4.
DT 22-JAN-2014, entry version 117.
DE RecName: Full=N-acetyl-D-glucosamine kinase;
DE Short=N-acetylglucosamine kinase;
DE EC=2.7.1.59;
DE AltName: Full=GlcNAc kinase;
GN Name=NAGK;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RX PubMed=10824116; DOI=10.1046/j.1432-1327.2000.01360.x;
RA Hinderlich S., Berger M., Schwarzkopf M., Effertz K., Reutter W.;
RT "Molecular cloning and characterization of murine and human N-
RT acetylglucosamine kinase.";
RL Eur. J. Biochem. 267:3301-3308(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain, and Placenta;
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Cerebellum;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
RA Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
RA Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
RA Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
RA Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
RA Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
RA Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
RA Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
RA Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
RA Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
RA Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
RA Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
RA Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
RA Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
RA Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
RA Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
RA Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
RA Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
RA McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
RA Waterston R.H., Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2
RT and 4.";
RL Nature 434:724-731(2005).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS
RP ARG-38 AND VAL-60.
RC TISSUE=Kidney, and Skin;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP PROTEIN SEQUENCE OF 2-14.
RC TISSUE=Platelet;
RX PubMed=12665801; DOI=10.1038/nbt810;
RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,
RA Thomas G.R., Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass
RT spectrometric identification of sorted N-terminal peptides.";
RL Nat. Biotechnol. 21:566-569(2003).
RN [9]
RP PROTEIN SEQUENCE OF 245-261 AND 281-291, AND MASS SPECTROMETRY.
RC TISSUE=Brain, and Cajal-Retzius cell;
RA Lubec G., Afjehi-Sadat L.;
RL Submitted (MAR-2007) to UniProtKB.
RN [10]
RP PHOSPHORYLATION AT TYR-205.
RX PubMed=12112843;
RX DOI=10.1002/1615-9861(200206)2:6<642::AID-PROT642>3.0.CO;2-I;
RA Maguire P.B., Wynne K.J., Harney D.F., O'Donoghue N.M., Stephens G.,
RA Fitzgerald D.J.;
RT "Identification of the phosphotyrosine proteome from thrombin
RT activated platelets.";
RL Proteomics 2:642-648(2002).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-76, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-76, AND MASS
RP SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-76, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [14]
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.,
RA Buerckstuemmer T., 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 [15]
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=22692205; DOI=10.1074/jbc.M112.363549;
RA Bergfeld A.K., Pearce O.M., Diaz S.L., Pham T., Varki A.;
RT "Metabolism of vertebrate amino sugars with N-glycolyl groups:
RT elucidating the intracellular fate of the non-human sialic acid N-
RT glycolylneuraminic acid.";
RL J. Biol. Chem. 287:28865-28881(2012).
RN [16]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 1-345 IN COMPLEX WITH
RP SUBSTRATE AND ATP ANALOG, AND SUBUNIT.
RX PubMed=17010375; DOI=10.1016/j.jmb.2006.08.085;
RA Weihofen W.A., Berger M., Chen H., Saenger W., Hinderlich S.;
RT "Structures of human N-acetylglucosamine kinase in two complexes with
RT N-acetylglucosamine and with ADP/glucose: insights into substrate
RT specificity and regulation.";
RL J. Mol. Biol. 364:388-399(2006).
CC -!- FUNCTION: Converts endogenous N-acetylglucosamine (GlcNAc), a
CC major component of complex carbohydrates, from lysosomal
CC degradation or nutritional sources into GlcNAc 6-phosphate.
CC Involved in the N-glycolylneuraminic acid (Neu5Gc) degradation
CC pathway: although human is not able to catalyze formation of
CC Neu5Gc due to the inactive CMAHP enzyme, Neu5Gc is present in food
CC and must be degraded. Also has ManNAc kinase activity.
CC -!- CATALYTIC ACTIVITY: ATP + N-acetyl-D-glucosamine = ADP + N-acetyl-
CC D-glucosamine 6-phosphate.
CC -!- PATHWAY: Amino-sugar metabolism; N-acetylneuraminate degradation.
CC -!- SUBUNIT: Homodimer.
CC -!- INTERACTION:
CC Q9UI36:DACH1; NbExp=3; IntAct=EBI-372578, EBI-347111;
CC Q8TBB1:LNX1; NbExp=2; IntAct=EBI-372578, EBI-739832;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9UJ70-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9UJ70-2; Sequence=VSP_044586;
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- SIMILARITY: Belongs to the eukaryotic-type N-acetylglucosamine
CC kinase family.
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DR EMBL; AJ242910; CAB61848.1; -; mRNA.
DR EMBL; AK001812; BAA91923.1; -; mRNA.
DR EMBL; AK297224; BAG59707.1; -; mRNA.
DR EMBL; CR457271; CAG33552.1; -; mRNA.
DR EMBL; AK222645; BAD96365.1; -; mRNA.
DR EMBL; AC007881; AAY14748.1; -; Genomic_DNA.
DR EMBL; CH471053; EAW99780.1; -; Genomic_DNA.
DR EMBL; BC001029; AAH01029.1; -; mRNA.
DR EMBL; BC005371; AAH05371.1; -; mRNA.
DR RefSeq; NP_060037.3; NM_017567.4.
DR UniGene; Hs.7036; -.
DR PDB; 2CH5; X-ray; 1.90 A; A/B/C/D=1-344.
DR PDB; 2CH6; X-ray; 2.72 A; A/B/C/D=1-344.
DR PDBsum; 2CH5; -.
DR PDBsum; 2CH6; -.
DR ProteinModelPortal; Q9UJ70; -.
DR SMR; Q9UJ70; 2-344.
DR IntAct; Q9UJ70; 22.
DR MINT; MINT-1182067; -.
DR STRING; 9606.ENSP00000244204; -.
DR DrugBank; DB00141; N-Acetyl-D-glucosamine.
DR PhosphoSite; Q9UJ70; -.
DR DMDM; 24638065; -.
DR OGP; Q9UJ70; -.
DR PaxDb; Q9UJ70; -.
DR PeptideAtlas; Q9UJ70; -.
DR PRIDE; Q9UJ70; -.
DR DNASU; 55577; -.
DR Ensembl; ENST00000244204; ENSP00000244204; ENSG00000124357.
DR Ensembl; ENST00000455662; ENSP00000389087; ENSG00000124357.
DR GeneID; 55577; -.
DR KEGG; hsa:55577; -.
DR UCSC; uc002shp.4; human.
DR CTD; 55577; -.
DR GeneCards; GC02P071295; -.
DR H-InvDB; HIX0002147; -.
DR HGNC; HGNC:17174; NAGK.
DR HPA; HPA035207; -.
DR MIM; 606828; gene.
DR neXtProt; NX_Q9UJ70; -.
DR PharmGKB; PA31436; -.
DR eggNOG; COG2971; -.
DR HOGENOM; HOG000007248; -.
DR HOVERGEN; HBG052570; -.
DR InParanoid; Q9UJ70; -.
DR KO; K00884; -.
DR OMA; AFYSYTF; -.
DR OrthoDB; EOG7V1FR7; -.
DR PhylomeDB; Q9UJ70; -.
DR BRENDA; 2.7.1.59; 2681.
DR UniPathway; UPA00629; -.
DR ChiTaRS; NAGK; human.
DR EvolutionaryTrace; Q9UJ70; -.
DR GeneWiki; NAGK; -.
DR GenomeRNAi; 55577; -.
DR NextBio; 60080; -.
DR PRO; PR:Q9UJ70; -.
DR ArrayExpress; Q9UJ70; -.
DR Bgee; Q9UJ70; -.
DR CleanEx; HS_NAGK; -.
DR Genevestigator; Q9UJ70; -.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0045127; F:N-acetylglucosamine kinase activity; IDA:UniProtKB.
DR GO; GO:0009384; F:N-acylmannosamine kinase activity; IEA:Ensembl.
DR GO; GO:0006044; P:N-acetylglucosamine metabolic process; TAS:ProtInc.
DR GO; GO:0006051; P:N-acetylmannosamine metabolic process; TAS:ProtInc.
DR GO; GO:0019262; P:N-acetylneuraminate catabolic process; TAS:UniProtKB.
DR InterPro; IPR002731; ATPase_BadF.
DR Pfam; PF01869; BcrAD_BadFG; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; ATP-binding;
KW Complete proteome; Direct protein sequencing; Kinase;
KW Nucleotide-binding; Phosphoprotein; Polymorphism; Reference proteome;
KW Transferase.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 344 N-acetyl-D-glucosamine kinase.
FT /FTId=PRO_0000096696.
FT NP_BIND 6 13 ATP.
FT REGION 129 130 Substrate binding.
FT REGION 145 147 Substrate binding.
FT BINDING 36 36 Substrate.
FT BINDING 107 107 Substrate.
FT BINDING 152 152 Substrate.
FT BINDING 271 271 ATP.
FT BINDING 275 275 ATP.
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 76 76 Phosphoserine.
FT MOD_RES 205 205 Phosphotyrosine.
FT VAR_SEQ 1 1 M -> MRTRTGSQLAAREVTGSGAVPRQLEGRRCQAGRDAN
FT GGTSSDGSSSM (in isoform 2).
FT /FTId=VSP_044586.
FT VARIANT 38 38 W -> R (in dbSNP:rs17856147).
FT /FTId=VAR_029763.
FT VARIANT 60 60 A -> V (in dbSNP:rs17849984).
FT /FTId=VAR_029764.
FT CONFLICT 70 70 S -> I (in Ref. 1; CAB61848).
FT CONFLICT 121 121 V -> I (in Ref. 1; CAB61848).
FT CONFLICT 211 211 C -> Y (in Ref. 4; BAD96365).
FT CONFLICT 286 286 A -> V (in Ref. 2; BAA91923).
FT CONFLICT 324 324 G -> R (in Ref. 2; BAA91923).
FT STRAND 4 10
FT STRAND 15 21
FT STRAND 26 32
FT HELIX 37 40
FT HELIX 42 60
FT STRAND 64 66
FT STRAND 68 75
FT TURN 76 79
FT HELIX 81 94
FT STRAND 98 100
FT STRAND 102 106
FT HELIX 107 115
FT STRAND 120 134
FT STRAND 136 138
FT STRAND 140 144
FT TURN 148 150
FT HELIX 156 171
FT HELIX 182 192
FT HELIX 197 201
FT TURN 202 207
FT HELIX 210 214
FT HELIX 217 225
FT HELIX 229 249
FT HELIX 250 252
FT HELIX 255 258
FT STRAND 259 262
FT STRAND 264 270
FT HELIX 271 275
FT HELIX 276 290
FT STRAND 300 309
FT HELIX 312 321
FT TURN 322 324
FT HELIX 331 334
FT STRAND 335 342
SQ SEQUENCE 344 AA; 37376 MW; FCBB6B328EF4D515 CRC64;
MAAIYGGVEG GGTRSEVLLV SEDGKILAEA DGLSTNHWLI GTDKCVERIN EMVNRAKRKA
GVDPLVPLRS LGLSLSGGDQ EDAGRILIEE LRDRFPYLSE SYLITTDAAG SIATATPDGG
VVLISGTGSN CRLINPDGSE SGCGGWGHMM GDEGSAYWIA HQAVKIVFDS IDNLEAAPHD
IGYVKQAMFH YFQVPDRLGI LTHLYRDFDK CRFAGFCRKI AEGAQQGDPL SRYIFRKAGE
MLGRHIVAVL PEIDPVLFQG KIGLPILCVG SVWKSWELLK EGFLLALTQG REIQAQNFFS
SFTLMKLRHS SALGGASLGA RHIGHLLPMD YSANAIAFYS YTFS
//
ID NAGK_HUMAN Reviewed; 344 AA.
AC Q9UJ70; B4DLZ5; Q53HD5; Q6IA84; Q9BS29; Q9BVP0; Q9NV37;
DT 01-NOV-2002, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 4.
DT 22-JAN-2014, entry version 117.
DE RecName: Full=N-acetyl-D-glucosamine kinase;
DE Short=N-acetylglucosamine kinase;
DE EC=2.7.1.59;
DE AltName: Full=GlcNAc kinase;
GN Name=NAGK;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RX PubMed=10824116; DOI=10.1046/j.1432-1327.2000.01360.x;
RA Hinderlich S., Berger M., Schwarzkopf M., Effertz K., Reutter W.;
RT "Molecular cloning and characterization of murine and human N-
RT acetylglucosamine kinase.";
RL Eur. J. Biochem. 267:3301-3308(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain, and Placenta;
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Cerebellum;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
RA Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
RA Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
RA Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
RA Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
RA Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
RA Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
RA Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
RA Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
RA Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
RA Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
RA Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
RA Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
RA Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
RA Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
RA Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
RA Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
RA Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
RA McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
RA Waterston R.H., Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2
RT and 4.";
RL Nature 434:724-731(2005).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS
RP ARG-38 AND VAL-60.
RC TISSUE=Kidney, and Skin;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP PROTEIN SEQUENCE OF 2-14.
RC TISSUE=Platelet;
RX PubMed=12665801; DOI=10.1038/nbt810;
RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,
RA Thomas G.R., Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass
RT spectrometric identification of sorted N-terminal peptides.";
RL Nat. Biotechnol. 21:566-569(2003).
RN [9]
RP PROTEIN SEQUENCE OF 245-261 AND 281-291, AND MASS SPECTROMETRY.
RC TISSUE=Brain, and Cajal-Retzius cell;
RA Lubec G., Afjehi-Sadat L.;
RL Submitted (MAR-2007) to UniProtKB.
RN [10]
RP PHOSPHORYLATION AT TYR-205.
RX PubMed=12112843;
RX DOI=10.1002/1615-9861(200206)2:6<642::AID-PROT642>3.0.CO;2-I;
RA Maguire P.B., Wynne K.J., Harney D.F., O'Donoghue N.M., Stephens G.,
RA Fitzgerald D.J.;
RT "Identification of the phosphotyrosine proteome from thrombin
RT activated platelets.";
RL Proteomics 2:642-648(2002).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-76, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-76, AND MASS
RP SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-76, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [14]
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.,
RA Buerckstuemmer T., 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 [15]
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=22692205; DOI=10.1074/jbc.M112.363549;
RA Bergfeld A.K., Pearce O.M., Diaz S.L., Pham T., Varki A.;
RT "Metabolism of vertebrate amino sugars with N-glycolyl groups:
RT elucidating the intracellular fate of the non-human sialic acid N-
RT glycolylneuraminic acid.";
RL J. Biol. Chem. 287:28865-28881(2012).
RN [16]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 1-345 IN COMPLEX WITH
RP SUBSTRATE AND ATP ANALOG, AND SUBUNIT.
RX PubMed=17010375; DOI=10.1016/j.jmb.2006.08.085;
RA Weihofen W.A., Berger M., Chen H., Saenger W., Hinderlich S.;
RT "Structures of human N-acetylglucosamine kinase in two complexes with
RT N-acetylglucosamine and with ADP/glucose: insights into substrate
RT specificity and regulation.";
RL J. Mol. Biol. 364:388-399(2006).
CC -!- FUNCTION: Converts endogenous N-acetylglucosamine (GlcNAc), a
CC major component of complex carbohydrates, from lysosomal
CC degradation or nutritional sources into GlcNAc 6-phosphate.
CC Involved in the N-glycolylneuraminic acid (Neu5Gc) degradation
CC pathway: although human is not able to catalyze formation of
CC Neu5Gc due to the inactive CMAHP enzyme, Neu5Gc is present in food
CC and must be degraded. Also has ManNAc kinase activity.
CC -!- CATALYTIC ACTIVITY: ATP + N-acetyl-D-glucosamine = ADP + N-acetyl-
CC D-glucosamine 6-phosphate.
CC -!- PATHWAY: Amino-sugar metabolism; N-acetylneuraminate degradation.
CC -!- SUBUNIT: Homodimer.
CC -!- INTERACTION:
CC Q9UI36:DACH1; NbExp=3; IntAct=EBI-372578, EBI-347111;
CC Q8TBB1:LNX1; NbExp=2; IntAct=EBI-372578, EBI-739832;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9UJ70-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9UJ70-2; Sequence=VSP_044586;
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- SIMILARITY: Belongs to the eukaryotic-type N-acetylglucosamine
CC kinase family.
CC -----------------------------------------------------------------------
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DR EMBL; AJ242910; CAB61848.1; -; mRNA.
DR EMBL; AK001812; BAA91923.1; -; mRNA.
DR EMBL; AK297224; BAG59707.1; -; mRNA.
DR EMBL; CR457271; CAG33552.1; -; mRNA.
DR EMBL; AK222645; BAD96365.1; -; mRNA.
DR EMBL; AC007881; AAY14748.1; -; Genomic_DNA.
DR EMBL; CH471053; EAW99780.1; -; Genomic_DNA.
DR EMBL; BC001029; AAH01029.1; -; mRNA.
DR EMBL; BC005371; AAH05371.1; -; mRNA.
DR RefSeq; NP_060037.3; NM_017567.4.
DR UniGene; Hs.7036; -.
DR PDB; 2CH5; X-ray; 1.90 A; A/B/C/D=1-344.
DR PDB; 2CH6; X-ray; 2.72 A; A/B/C/D=1-344.
DR PDBsum; 2CH5; -.
DR PDBsum; 2CH6; -.
DR ProteinModelPortal; Q9UJ70; -.
DR SMR; Q9UJ70; 2-344.
DR IntAct; Q9UJ70; 22.
DR MINT; MINT-1182067; -.
DR STRING; 9606.ENSP00000244204; -.
DR DrugBank; DB00141; N-Acetyl-D-glucosamine.
DR PhosphoSite; Q9UJ70; -.
DR DMDM; 24638065; -.
DR OGP; Q9UJ70; -.
DR PaxDb; Q9UJ70; -.
DR PeptideAtlas; Q9UJ70; -.
DR PRIDE; Q9UJ70; -.
DR DNASU; 55577; -.
DR Ensembl; ENST00000244204; ENSP00000244204; ENSG00000124357.
DR Ensembl; ENST00000455662; ENSP00000389087; ENSG00000124357.
DR GeneID; 55577; -.
DR KEGG; hsa:55577; -.
DR UCSC; uc002shp.4; human.
DR CTD; 55577; -.
DR GeneCards; GC02P071295; -.
DR H-InvDB; HIX0002147; -.
DR HGNC; HGNC:17174; NAGK.
DR HPA; HPA035207; -.
DR MIM; 606828; gene.
DR neXtProt; NX_Q9UJ70; -.
DR PharmGKB; PA31436; -.
DR eggNOG; COG2971; -.
DR HOGENOM; HOG000007248; -.
DR HOVERGEN; HBG052570; -.
DR InParanoid; Q9UJ70; -.
DR KO; K00884; -.
DR OMA; AFYSYTF; -.
DR OrthoDB; EOG7V1FR7; -.
DR PhylomeDB; Q9UJ70; -.
DR BRENDA; 2.7.1.59; 2681.
DR UniPathway; UPA00629; -.
DR ChiTaRS; NAGK; human.
DR EvolutionaryTrace; Q9UJ70; -.
DR GeneWiki; NAGK; -.
DR GenomeRNAi; 55577; -.
DR NextBio; 60080; -.
DR PRO; PR:Q9UJ70; -.
DR ArrayExpress; Q9UJ70; -.
DR Bgee; Q9UJ70; -.
DR CleanEx; HS_NAGK; -.
DR Genevestigator; Q9UJ70; -.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0045127; F:N-acetylglucosamine kinase activity; IDA:UniProtKB.
DR GO; GO:0009384; F:N-acylmannosamine kinase activity; IEA:Ensembl.
DR GO; GO:0006044; P:N-acetylglucosamine metabolic process; TAS:ProtInc.
DR GO; GO:0006051; P:N-acetylmannosamine metabolic process; TAS:ProtInc.
DR GO; GO:0019262; P:N-acetylneuraminate catabolic process; TAS:UniProtKB.
DR InterPro; IPR002731; ATPase_BadF.
DR Pfam; PF01869; BcrAD_BadFG; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; ATP-binding;
KW Complete proteome; Direct protein sequencing; Kinase;
KW Nucleotide-binding; Phosphoprotein; Polymorphism; Reference proteome;
KW Transferase.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 344 N-acetyl-D-glucosamine kinase.
FT /FTId=PRO_0000096696.
FT NP_BIND 6 13 ATP.
FT REGION 129 130 Substrate binding.
FT REGION 145 147 Substrate binding.
FT BINDING 36 36 Substrate.
FT BINDING 107 107 Substrate.
FT BINDING 152 152 Substrate.
FT BINDING 271 271 ATP.
FT BINDING 275 275 ATP.
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 76 76 Phosphoserine.
FT MOD_RES 205 205 Phosphotyrosine.
FT VAR_SEQ 1 1 M -> MRTRTGSQLAAREVTGSGAVPRQLEGRRCQAGRDAN
FT GGTSSDGSSSM (in isoform 2).
FT /FTId=VSP_044586.
FT VARIANT 38 38 W -> R (in dbSNP:rs17856147).
FT /FTId=VAR_029763.
FT VARIANT 60 60 A -> V (in dbSNP:rs17849984).
FT /FTId=VAR_029764.
FT CONFLICT 70 70 S -> I (in Ref. 1; CAB61848).
FT CONFLICT 121 121 V -> I (in Ref. 1; CAB61848).
FT CONFLICT 211 211 C -> Y (in Ref. 4; BAD96365).
FT CONFLICT 286 286 A -> V (in Ref. 2; BAA91923).
FT CONFLICT 324 324 G -> R (in Ref. 2; BAA91923).
FT STRAND 4 10
FT STRAND 15 21
FT STRAND 26 32
FT HELIX 37 40
FT HELIX 42 60
FT STRAND 64 66
FT STRAND 68 75
FT TURN 76 79
FT HELIX 81 94
FT STRAND 98 100
FT STRAND 102 106
FT HELIX 107 115
FT STRAND 120 134
FT STRAND 136 138
FT STRAND 140 144
FT TURN 148 150
FT HELIX 156 171
FT HELIX 182 192
FT HELIX 197 201
FT TURN 202 207
FT HELIX 210 214
FT HELIX 217 225
FT HELIX 229 249
FT HELIX 250 252
FT HELIX 255 258
FT STRAND 259 262
FT STRAND 264 270
FT HELIX 271 275
FT HELIX 276 290
FT STRAND 300 309
FT HELIX 312 321
FT TURN 322 324
FT HELIX 331 334
FT STRAND 335 342
SQ SEQUENCE 344 AA; 37376 MW; FCBB6B328EF4D515 CRC64;
MAAIYGGVEG GGTRSEVLLV SEDGKILAEA DGLSTNHWLI GTDKCVERIN EMVNRAKRKA
GVDPLVPLRS LGLSLSGGDQ EDAGRILIEE LRDRFPYLSE SYLITTDAAG SIATATPDGG
VVLISGTGSN CRLINPDGSE SGCGGWGHMM GDEGSAYWIA HQAVKIVFDS IDNLEAAPHD
IGYVKQAMFH YFQVPDRLGI LTHLYRDFDK CRFAGFCRKI AEGAQQGDPL SRYIFRKAGE
MLGRHIVAVL PEIDPVLFQG KIGLPILCVG SVWKSWELLK EGFLLALTQG REIQAQNFFS
SFTLMKLRHS SALGGASLGA RHIGHLLPMD YSANAIAFYS YTFS
//
MIM
606828
*RECORD*
*FIELD* NO
606828
*FIELD* TI
*606828 N-ACETYLGLUCOSAMINE KINASE; NAGK
;;GlcNAc KINASE; GNK
*FIELD* TX
DESCRIPTION
read more
N-acetylglucosamine kinase (NAGK; EC 2.7.1.59) converts endogenous
N-acetylglucosamine (GlcNAc), a major component of complex
carbohydrates, from lysosomal degradation or nutritional sources into
GlcNAc 6-phosphate. NAGK belongs to the group of N-acetylhexosamine
kinases and is a prominent salvage enzyme of amino sugar metabolism in
mammals.
CLONING
Using the mouse Nagk sequence to search the human EST database,
Hinderlich et al. (2000) obtained a complete cDNA encoding NAGK. The
predicted 344-amino acid NAGK protein contains the 5 sequence motifs
necessary for the binding of ATP by sugar kinases. NAGK shares 91.6%
amino acid similarity with mouse Nagk.
Using Northern blot analysis, Hinderlich et al. (2000) detected a
1.35-kb NAGK transcript in all tissues and cancer cell lines tested.
They detected enzyme activity in all mouse tissues examined, with
highest enzymatic activity in testis.
GENE FUNCTION
Hinderlich et al. (2000) functionally expressed murine Nagk in E. coli
and detected GlcNAc kinase activity as well as ManNAc kinase activity.
They hypothesized that NAGK has a general role in the catabolic pathways
of GlcNAc as well as of ManNAc.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the NAGK
gene to chromosome 2 (TMAP A006G04).
*FIELD* RF
1. Hinderlich, S.; Berger, M.; Schwarzkopf, M.; Effertz, K.; Reutter,
W.: Molecular cloning and characterization of murine and human N-acetylglucosamine
kinase. Europ. J. Biochem. 267: 3301-3308, 2000.
*FIELD* CD
Dawn Watkins-Chow: 4/4/2002
*FIELD* ED
mgross: 04/04/2002
*RECORD*
*FIELD* NO
606828
*FIELD* TI
*606828 N-ACETYLGLUCOSAMINE KINASE; NAGK
;;GlcNAc KINASE; GNK
*FIELD* TX
DESCRIPTION
read more
N-acetylglucosamine kinase (NAGK; EC 2.7.1.59) converts endogenous
N-acetylglucosamine (GlcNAc), a major component of complex
carbohydrates, from lysosomal degradation or nutritional sources into
GlcNAc 6-phosphate. NAGK belongs to the group of N-acetylhexosamine
kinases and is a prominent salvage enzyme of amino sugar metabolism in
mammals.
CLONING
Using the mouse Nagk sequence to search the human EST database,
Hinderlich et al. (2000) obtained a complete cDNA encoding NAGK. The
predicted 344-amino acid NAGK protein contains the 5 sequence motifs
necessary for the binding of ATP by sugar kinases. NAGK shares 91.6%
amino acid similarity with mouse Nagk.
Using Northern blot analysis, Hinderlich et al. (2000) detected a
1.35-kb NAGK transcript in all tissues and cancer cell lines tested.
They detected enzyme activity in all mouse tissues examined, with
highest enzymatic activity in testis.
GENE FUNCTION
Hinderlich et al. (2000) functionally expressed murine Nagk in E. coli
and detected GlcNAc kinase activity as well as ManNAc kinase activity.
They hypothesized that NAGK has a general role in the catabolic pathways
of GlcNAc as well as of ManNAc.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the NAGK
gene to chromosome 2 (TMAP A006G04).
*FIELD* RF
1. Hinderlich, S.; Berger, M.; Schwarzkopf, M.; Effertz, K.; Reutter,
W.: Molecular cloning and characterization of murine and human N-acetylglucosamine
kinase. Europ. J. Biochem. 267: 3301-3308, 2000.
*FIELD* CD
Dawn Watkins-Chow: 4/4/2002
*FIELD* ED
mgross: 04/04/2002