NAGK_HUMAN
ID NAGK_HUMAN Reviewed; 344 AA.
AC Q9UJ70; B4DLZ5; Q53HD5; Q6IA84; Q9BS29; Q9BVP0; Q9NV37;
DT 01-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 187.
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; 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.
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., 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 [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., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., 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., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., 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., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 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., 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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS ARG-38 AND
RP 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 project:
RT 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., Thomas G.R.,
RA Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass spectrometric
RT 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 IDENTIFICATION BY MASS
RP 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 activated
RT platelets.";
RL Proteomics 2:642-648(2002).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-76, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT 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., 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 [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: elucidating
RT the intracellular fate of the non-human sialic acid N-glycolylneuraminic
RT acid.";
RL J. Biol. Chem. 287:28865-28881(2012).
RN [16]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [17]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
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., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-76, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-76, AND IDENTIFICATION BY
RP 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 [20]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 1-345 IN COMPLEXES WITH SUBSTRATE;
RP GLUCOSE AND ADP, 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 N-
RT acetylglucosamine and with ADP/glucose: insights into substrate specificity
RT and regulation.";
RL J. Mol. Biol. 364:388-399(2006).
CC -!- FUNCTION: Converts endogenous N-acetylglucosamine (GlcNAc), a major
CC component of complex carbohydrates, from lysosomal degradation or
CC nutritional sources into GlcNAc 6-phosphate. Involved in the N-
CC glycolylneuraminic acid (Neu5Gc) degradation pathway: although human is
CC not able to catalyze formation of Neu5Gc due to the inactive CMAHP
CC enzyme, Neu5Gc is present in food and must be degraded. Also has ManNAc
CC kinase activity. {ECO:0000269|PubMed:22692205}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + N-acetyl-D-glucosamine = ADP + H(+) + N-acetyl-D-
CC glucosamine 6-phosphate; Xref=Rhea:RHEA:17417, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:57513, ChEBI:CHEBI:456216,
CC ChEBI:CHEBI:506227; EC=2.7.1.59;
CC Evidence={ECO:0000269|PubMed:22692205};
CC -!- PATHWAY: Amino-sugar metabolism; N-acetylneuraminate degradation.
CC {ECO:0000269|PubMed:22692205}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:17010375}.
CC -!- INTERACTION:
CC Q9UJ70; Q9NZ32: ACTR10; NbExp=3; IntAct=EBI-372578, EBI-2559426;
CC Q9UJ70; P42773: CDKN2C; NbExp=4; IntAct=EBI-372578, EBI-711290;
CC Q9UJ70; Q9UI36: DACH1; NbExp=3; IntAct=EBI-372578, EBI-347111;
CC Q9UJ70; Q9UI36-2: DACH1; NbExp=5; IntAct=EBI-372578, EBI-10186082;
CC Q9UJ70; Q8TBB1: LNX1; NbExp=3; IntAct=EBI-372578, EBI-739832;
CC Q9UJ70; P50221: MEOX1; NbExp=3; IntAct=EBI-372578, EBI-2864512;
CC Q9UJ70; Q04864: REL; NbExp=3; IntAct=EBI-372578, EBI-307352;
CC Q9UJ70; O00560: SDCBP; NbExp=5; IntAct=EBI-372578, EBI-727004;
CC Q9UJ70; Q99081: TCF12; NbExp=3; IntAct=EBI-372578, EBI-722877;
CC Q9UJ70; B2R7W0; NbExp=3; IntAct=EBI-372578, EBI-10175537;
CC Q9UJ70-2; Q15327: ANKRD1; NbExp=3; IntAct=EBI-11526455, EBI-5653378;
CC Q9UJ70-2; P55212: CASP6; NbExp=3; IntAct=EBI-11526455, EBI-718729;
CC Q9UJ70-2; P06307: CCK; NbExp=3; IntAct=EBI-11526455, EBI-6624398;
CC Q9UJ70-2; P42773: CDKN2C; NbExp=3; IntAct=EBI-11526455, EBI-711290;
CC Q9UJ70-2; Q9UI36-2: DACH1; NbExp=3; IntAct=EBI-11526455, EBI-10186082;
CC Q9UJ70-2; P13473-2: LAMP2; NbExp=3; IntAct=EBI-11526455, EBI-21591415;
CC Q9UJ70-2; P25800: LMO1; NbExp=5; IntAct=EBI-11526455, EBI-8639312;
CC Q9UJ70-2; Q8TBB1: LNX1; NbExp=3; IntAct=EBI-11526455, EBI-739832;
CC Q9UJ70-2; P13995: MTHFD2; NbExp=3; IntAct=EBI-11526455, EBI-1058895;
CC Q9UJ70-2; Q96HA8: NTAQ1; NbExp=5; IntAct=EBI-11526455, EBI-741158;
CC Q9UJ70-2; O00560: SDCBP; NbExp=3; IntAct=EBI-11526455, EBI-727004;
CC Q9UJ70-2; Q9Y371: SH3GLB1; NbExp=3; IntAct=EBI-11526455, EBI-2623095;
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. {ECO:0000269|PubMed:10824116}.
CC -!- SIMILARITY: Belongs to the eukaryotic-type N-acetylglucosamine kinase
CC family. {ECO:0000305}.
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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 CCDS; CCDS33220.2; -. [Q9UJ70-1]
DR RefSeq; NP_060037.3; NM_017567.4. [Q9UJ70-1]
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 AlphaFoldDB; Q9UJ70; -.
DR SMR; Q9UJ70; -.
DR BioGRID; 120728; 171.
DR IntAct; Q9UJ70; 75.
DR MINT; Q9UJ70; -.
DR STRING; 9606.ENSP00000477639; -.
DR ChEMBL; CHEMBL4295978; -.
DR DrugBank; DB00141; N-Acetylglucosamine.
DR iPTMnet; Q9UJ70; -.
DR PhosphoSitePlus; Q9UJ70; -.
DR SwissPalm; Q9UJ70; -.
DR BioMuta; NAGK; -.
DR DMDM; 24638065; -.
DR OGP; Q9UJ70; -.
DR CPTAC; CPTAC-242; -.
DR CPTAC; CPTAC-243; -.
DR EPD; Q9UJ70; -.
DR jPOST; Q9UJ70; -.
DR MassIVE; Q9UJ70; -.
DR MaxQB; Q9UJ70; -.
DR PaxDb; Q9UJ70; -.
DR PeptideAtlas; Q9UJ70; -.
DR PRIDE; Q9UJ70; -.
DR ProteomicsDB; 84593; -. [Q9UJ70-1]
DR Antibodypedia; 31185; 299 antibodies from 27 providers.
DR DNASU; 55577; -.
DR Ensembl; ENST00000244204.11; ENSP00000244204.5; ENSG00000124357.13. [Q9UJ70-1]
DR Ensembl; ENST00000455662.6; ENSP00000389087.2; ENSG00000124357.13. [Q9UJ70-2]
DR Ensembl; ENST00000613852.4; ENSP00000477639.1; ENSG00000124357.13. [Q9UJ70-2]
DR GeneID; 55577; -.
DR KEGG; hsa:55577; -.
DR MANE-Select; ENST00000244204.11; ENSP00000244204.5; NM_017567.6; NP_060037.4.
DR UCSC; uc002shp.4; human. [Q9UJ70-1]
DR CTD; 55577; -.
DR DisGeNET; 55577; -.
DR GeneCards; NAGK; -.
DR HGNC; HGNC:17174; NAGK.
DR HPA; ENSG00000124357; Low tissue specificity.
DR MIM; 606828; gene.
DR neXtProt; NX_Q9UJ70; -.
DR OpenTargets; ENSG00000124357; -.
DR PharmGKB; PA31436; -.
DR VEuPathDB; HostDB:ENSG00000124357; -.
DR eggNOG; KOG1794; Eukaryota.
DR GeneTree; ENSGT00510000047418; -.
DR InParanoid; Q9UJ70; -.
DR OrthoDB; 1572762at2759; -.
DR PhylomeDB; Q9UJ70; -.
DR TreeFam; TF314158; -.
DR BRENDA; 2.7.1.59; 2681.
DR PathwayCommons; Q9UJ70; -.
DR Reactome; R-HSA-446210; Synthesis of UDP-N-acetyl-glucosamine.
DR SABIO-RK; Q9UJ70; -.
DR SignaLink; Q9UJ70; -.
DR UniPathway; UPA00629; -.
DR BioGRID-ORCS; 55577; 17 hits in 1077 CRISPR screens.
DR ChiTaRS; NAGK; human.
DR EvolutionaryTrace; Q9UJ70; -.
DR GeneWiki; NAGK; -.
DR GenomeRNAi; 55577; -.
DR Pharos; Q9UJ70; Tbio.
DR PRO; PR:Q9UJ70; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q9UJ70; protein.
DR Bgee; ENSG00000124357; Expressed in monocyte and 195 other tissues.
DR ExpressionAtlas; Q9UJ70; baseline and differential.
DR Genevisible; Q9UJ70; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0045127; F:N-acetylglucosamine kinase activity; IDA:UniProtKB.
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 InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR039758; NAGK_prok_euk.
DR PANTHER; PTHR12862; PTHR12862; 1.
DR Pfam; PF01869; BcrAD_BadFG; 1.
DR SUPFAM; SSF53067; SSF53067; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; ATP-binding;
KW Direct protein sequencing; Kinase; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:12665801,
FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378"
FT CHAIN 2..344
FT /note="N-acetyl-D-glucosamine kinase"
FT /id="PRO_0000096696"
FT BINDING 13
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305|PubMed:17010375,
FT ECO:0007744|PDB:2CH6"
FT BINDING 36
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:17010375,
FT ECO:0007744|PDB:2CH5"
FT BINDING 107
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:17010375,
FT ECO:0007744|PDB:2CH5"
FT BINDING 127
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305|PubMed:17010375,
FT ECO:0007744|PDB:2CH6"
FT BINDING 129..130
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:17010375,
FT ECO:0007744|PDB:2CH5"
FT BINDING 145..147
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:17010375,
FT ECO:0007744|PDB:2CH5"
FT BINDING 152
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:17010375,
FT ECO:0007744|PDB:2CH5"
FT BINDING 214
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305|PubMed:17010375,
FT ECO:0007744|PDB:2CH6"
FT BINDING 271
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305|PubMed:17010375,
FT ECO:0007744|PDB:2CH6"
FT BINDING 275
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305|PubMed:17010375,
FT ECO:0007744|PDB:2CH6"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22223895,
FT ECO:0007744|PubMed:22814378"
FT MOD_RES 76
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 205
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:12112843"
FT VAR_SEQ 1
FT /note="M -> MRTRTGSQLAAREVTGSGAVPRQLEGRRCQAGRDANGGTSSDGSSSM
FT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_044586"
FT VARIANT 38
FT /note="W -> R (in dbSNP:rs17856147)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_029763"
FT VARIANT 60
FT /note="A -> V (in dbSNP:rs17849984)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_029764"
FT CONFLICT 70
FT /note="S -> I (in Ref. 1; CAB61848)"
FT /evidence="ECO:0000305"
FT CONFLICT 121
FT /note="V -> I (in Ref. 1; CAB61848)"
FT /evidence="ECO:0000305"
FT CONFLICT 211
FT /note="C -> Y (in Ref. 4; BAD96365)"
FT /evidence="ECO:0000305"
FT CONFLICT 286
FT /note="A -> V (in Ref. 2; BAA91923)"
FT /evidence="ECO:0000305"
FT CONFLICT 324
FT /note="G -> R (in Ref. 2; BAA91923)"
FT /evidence="ECO:0000305"
FT STRAND 4..10
FT /evidence="ECO:0007829|PDB:2CH5"
FT STRAND 15..21
FT /evidence="ECO:0007829|PDB:2CH5"
FT STRAND 26..32
FT /evidence="ECO:0007829|PDB:2CH5"
FT HELIX 37..40
FT /evidence="ECO:0007829|PDB:2CH5"
FT HELIX 42..60
FT /evidence="ECO:0007829|PDB:2CH5"
FT STRAND 64..66
FT /evidence="ECO:0007829|PDB:2CH6"
FT STRAND 68..75
FT /evidence="ECO:0007829|PDB:2CH5"
FT TURN 76..79
FT /evidence="ECO:0007829|PDB:2CH5"
FT HELIX 81..94
FT /evidence="ECO:0007829|PDB:2CH5"
FT STRAND 98..100
FT /evidence="ECO:0007829|PDB:2CH5"
FT STRAND 102..106
FT /evidence="ECO:0007829|PDB:2CH5"
FT HELIX 107..115
FT /evidence="ECO:0007829|PDB:2CH5"
FT STRAND 120..134
FT /evidence="ECO:0007829|PDB:2CH5"
FT STRAND 136..138
FT /evidence="ECO:0007829|PDB:2CH6"
FT STRAND 140..144
FT /evidence="ECO:0007829|PDB:2CH5"
FT TURN 148..150
FT /evidence="ECO:0007829|PDB:2CH5"
FT HELIX 156..171
FT /evidence="ECO:0007829|PDB:2CH5"
FT HELIX 182..192
FT /evidence="ECO:0007829|PDB:2CH5"
FT HELIX 197..201
FT /evidence="ECO:0007829|PDB:2CH5"
FT TURN 202..207
FT /evidence="ECO:0007829|PDB:2CH5"
FT HELIX 210..214
FT /evidence="ECO:0007829|PDB:2CH5"
FT HELIX 217..225
FT /evidence="ECO:0007829|PDB:2CH5"
FT HELIX 229..249
FT /evidence="ECO:0007829|PDB:2CH5"
FT HELIX 250..252
FT /evidence="ECO:0007829|PDB:2CH5"
FT HELIX 255..258
FT /evidence="ECO:0007829|PDB:2CH5"
FT STRAND 259..262
FT /evidence="ECO:0007829|PDB:2CH6"
FT STRAND 264..270
FT /evidence="ECO:0007829|PDB:2CH5"
FT HELIX 271..275
FT /evidence="ECO:0007829|PDB:2CH5"
FT HELIX 276..290
FT /evidence="ECO:0007829|PDB:2CH5"
FT STRAND 300..309
FT /evidence="ECO:0007829|PDB:2CH5"
FT HELIX 312..321
FT /evidence="ECO:0007829|PDB:2CH5"
FT TURN 322..324
FT /evidence="ECO:0007829|PDB:2CH5"
FT HELIX 331..334
FT /evidence="ECO:0007829|PDB:2CH5"
FT STRAND 335..342
FT /evidence="ECO:0007829|PDB:2CH5"
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
