NAGK_MOUSE
ID NAGK_MOUSE Reviewed; 343 AA.
AC Q9QZ08;
DT 01-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=N-acetyl-D-glucosamine kinase;
DE Short=N-acetylglucosamine kinase;
DE EC=2.7.1.59 {ECO:0000269|PubMed:10824116};
DE AltName: Full=GlcNAc kinase;
GN Name=Nagk; Synonyms=Gnk;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, SUBUNIT, AND
RP CATALYTIC ACTIVITY.
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].
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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-76, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Kidney, Lung, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [4]
RP 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).
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 (PubMed:10824116). Also has
CC N-acetylmannosamine (ManNAc) kinase activity (PubMed:10824116).
CC Involved in the N-glycolylneuraminic acid (Neu5Gc) degradation pathway
CC (PubMed:22692205). {ECO:0000269|PubMed:10824116,
CC 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:10824116};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17418;
CC Evidence={ECO:0000305|PubMed:10824116};
CC -!- PATHWAY: Amino-sugar metabolism; N-acetylneuraminate degradation.
CC {ECO:0000269|PubMed:22692205}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:10824116}.
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; AJ242909; CAB61849.1; -; mRNA.
DR EMBL; BC004689; AAH04689.1; -; mRNA.
DR CCDS; CCDS20286.1; -.
DR RefSeq; NP_062415.1; NM_019542.2.
DR AlphaFoldDB; Q9QZ08; -.
DR SMR; Q9QZ08; -.
DR BioGRID; 207820; 7.
DR IntAct; Q9QZ08; 2.
DR STRING; 10090.ENSMUSP00000042026; -.
DR iPTMnet; Q9QZ08; -.
DR PhosphoSitePlus; Q9QZ08; -.
DR REPRODUCTION-2DPAGE; Q9QZ08; -.
DR EPD; Q9QZ08; -.
DR jPOST; Q9QZ08; -.
DR MaxQB; Q9QZ08; -.
DR PaxDb; Q9QZ08; -.
DR PRIDE; Q9QZ08; -.
DR ProteomicsDB; 287431; -.
DR Antibodypedia; 31185; 299 antibodies from 27 providers.
DR DNASU; 56174; -.
DR Ensembl; ENSMUST00000037376; ENSMUSP00000042026; ENSMUSG00000034744.
DR GeneID; 56174; -.
DR KEGG; mmu:56174; -.
DR UCSC; uc009coh.2; mouse.
DR CTD; 55577; -.
DR MGI; MGI:1860418; Nagk.
DR VEuPathDB; HostDB:ENSMUSG00000034744; -.
DR eggNOG; KOG1794; Eukaryota.
DR GeneTree; ENSGT00510000047418; -.
DR HOGENOM; CLU_016274_0_0_1; -.
DR InParanoid; Q9QZ08; -.
DR OMA; DTMGSMF; -.
DR PhylomeDB; Q9QZ08; -.
DR TreeFam; TF314158; -.
DR BRENDA; 2.7.1.59; 3474.
DR Reactome; R-MMU-446210; Synthesis of UDP-N-acetyl-glucosamine.
DR SABIO-RK; Q9QZ08; -.
DR UniPathway; UPA00629; -.
DR BioGRID-ORCS; 56174; 3 hits in 71 CRISPR screens.
DR ChiTaRS; Nagk; mouse.
DR PRO; PR:Q9QZ08; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q9QZ08; protein.
DR Bgee; ENSMUSG00000034744; Expressed in embryonic brain and 264 other tissues.
DR ExpressionAtlas; Q9QZ08; baseline and differential.
DR Genevisible; Q9QZ08; MM.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0045127; F:N-acetylglucosamine kinase activity; IDA:MGI.
DR GO; GO:0009384; F:N-acylmannosamine kinase activity; IDA:MGI.
DR GO; GO:0006044; P:N-acetylglucosamine metabolic process; IDA:MGI.
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 Acetylation; ATP-binding; Kinase; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9UJ70"
FT CHAIN 2..343
FT /note="N-acetyl-D-glucosamine kinase"
FT /id="PRO_0000096697"
FT BINDING 13
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9UJ70"
FT BINDING 36
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9UJ70"
FT BINDING 107
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9UJ70"
FT BINDING 127
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9UJ70"
FT BINDING 129..130
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9UJ70"
FT BINDING 145..147
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9UJ70"
FT BINDING 152
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9UJ70"
FT BINDING 214
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9UJ70"
FT BINDING 271
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9UJ70"
FT BINDING 275
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9UJ70"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q9UJ70"
FT MOD_RES 76
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 205
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9UJ70"
SQ SEQUENCE 343 AA; 37268 MW; A3832E98C9B3228E CRC64;
MAALYGGVEG GGTRSKVLLL SEDGQILAEA DGLSTNHWLI GTDQCVERIN EMVDRAKQKA
GVDPLVPLRS LGLSLSGGEQ EDAVRLLIEE LRHRFPNLSE NYLITTDAAG SIATATPDGG
IVLISGTGSN CRLINPDGSE SGCGGWGHMM GDEGSAYWIA HQAVKIVFDS IDNLEAAPHD
IGHVKQAMFD YFQVPDRLGI LTHLYRDFDK CKFAGFCQKI AEGAHQGDPL SRYIFRKAGE
MLGRHVVAVL PEIDPVLFQG ELGLPILCVG SVWKSWELLK EGFLLALTLG REQQAQNSFS
SFTLMKLRHS SALGGASLGA RHIGYHLPMD YSINAIAFYS YTF
