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Q9UJ70 (NAGK_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 123. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
N-acetyl-D-glucosamine kinase

Short name=N-acetylglucosamine kinase
EC=2.7.1.59
Alternative name(s):
GlcNAc kinase
Gene names
Name:NAGK
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length344 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Converts endogenous N-acetylglucosamine (GlcNAc), a major component of complex carbohydrates, from lysosomal degradation or nutritional sources into GlcNAc 6-phosphate. Involved in the N-glycolylneuraminic acid (Neu5Gc) degradation pathway: although human is not able to catalyze formation of Neu5Gc due to the inactive CMAHP enzyme, Neu5Gc is present in food and must be degraded. Also has ManNAc kinase activity. Ref.15

Catalytic activity

ATP + N-acetyl-D-glucosamine = ADP + N-acetyl-D-glucosamine 6-phosphate. Ref.15

Pathway

Amino-sugar metabolism; N-acetylneuraminate degradation. Ref.15

Subunit structure

Homodimer. Ref.18

Tissue specificity

Ubiquitous. Ref.1

Sequence similarities

Belongs to the eukaryotic-type N-acetylglucosamine kinase family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

DACH1Q9UI363EBI-372578,EBI-347111
LNX1Q8TBB12EBI-372578,EBI-739832

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9UJ70-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q9UJ70-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MRTRTGSQLAAREVTGSGAVPRQLEGRRCQAGRDANGGTSSDGSSSM

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.8 Ref.16
Chain2 – 344343N-acetyl-D-glucosamine kinase
PRO_0000096696

Regions

Nucleotide binding6 – 138ATP
Region129 – 1302Substrate binding
Region145 – 1473Substrate binding

Sites

Binding site361Substrate
Binding site1071Substrate
Binding site1521Substrate
Binding site2711ATP
Binding site2751ATP

Amino acid modifications

Modified residue21N-acetylalanine Ref.16 Ref.17
Modified residue761Phosphoserine Ref.11 Ref.12 Ref.13
Modified residue2051Phosphotyrosine Ref.10

Natural variations

Alternative sequence11M → MRTRTGSQLAAREVTGSGAV PRQLEGRRCQAGRDANGGTS SDGSSSM in isoform 2.
VSP_044586
Natural variant381W → R. Ref.7
Corresponds to variant rs17856147 [ dbSNP | Ensembl ].
VAR_029763
Natural variant601A → V. Ref.7
Corresponds to variant rs17849984 [ dbSNP | Ensembl ].
VAR_029764

Experimental info

Sequence conflict701S → I in CAB61848. Ref.1
Sequence conflict1211V → I in CAB61848. Ref.1
Sequence conflict2111C → Y in BAD96365. Ref.4
Sequence conflict2861A → V in BAA91923. Ref.2
Sequence conflict3241G → R in BAA91923. Ref.2

Secondary structure

............................................................ 344
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: FCBB6B328EF4D515

FASTA34437,376
        10         20         30         40         50         60 
MAAIYGGVEG GGTRSEVLLV SEDGKILAEA DGLSTNHWLI GTDKCVERIN EMVNRAKRKA 

        70         80         90        100        110        120 
GVDPLVPLRS LGLSLSGGDQ EDAGRILIEE LRDRFPYLSE SYLITTDAAG SIATATPDGG 

       130        140        150        160        170        180 
VVLISGTGSN CRLINPDGSE SGCGGWGHMM GDEGSAYWIA HQAVKIVFDS IDNLEAAPHD 

       190        200        210        220        230        240 
IGYVKQAMFH YFQVPDRLGI LTHLYRDFDK CRFAGFCRKI AEGAQQGDPL SRYIFRKAGE 

       250        260        270        280        290        300 
MLGRHIVAVL PEIDPVLFQG KIGLPILCVG SVWKSWELLK EGFLLALTQG REIQAQNFFS 

       310        320        330        340 
SFTLMKLRHS SALGGASLGA RHIGHLLPMD YSANAIAFYS YTFS 

« Hide

Isoform 2 [UniParc].

Checksum: 2B2DD636C8C35ADF
Show »

FASTA39042,038

References

« Hide 'large scale' references
[1]"Molecular cloning and characterization of murine and human N-acetylglucosamine kinase."
Hinderlich S., Berger M., Schwarzkopf M., Effertz K., Reutter W.
Eur. J. Biochem. 267:3301-3308(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
[2]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
Tissue: Brain and Placenta.
[3]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[4]Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Cerebellum.
[5]"Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. expand/collapse author list , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANTS ARG-38 AND VAL-60.
Tissue: Kidney and Skin.
[8]"Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."
Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.
Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-14.
Tissue: Platelet.
[9]Lubec G., Afjehi-Sadat L.
Submitted (MAR-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 245-261 AND 281-291, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Brain and Cajal-Retzius cell.
[10]"Identification of the phosphotyrosine proteome from thrombin activated platelets."
Maguire P.B., Wynne K.J., Harney D.F., O'Donoghue N.M., Stephens G., Fitzgerald D.J.
Proteomics 2:642-648(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT TYR-205.
[11]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-76, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[12]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-76, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[13]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-76, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[14]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]"Metabolism of vertebrate amino sugars with N-glycolyl groups: elucidating the intracellular fate of the non-human sialic acid N-glycolylneuraminic acid."
Bergfeld A.K., Pearce O.M., Diaz S.L., Pham T., Varki A.
J. Biol. Chem. 287:28865-28881(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY, PATHWAY.
[16]"Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[17]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[18]"Structures of human N-acetylglucosamine kinase in two complexes with N-acetylglucosamine and with ADP/glucose: insights into substrate specificity and regulation."
Weihofen W.A., Berger M., Chen H., Saenger W., Hinderlich S.
J. Mol. Biol. 364:388-399(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 1-345 IN COMPLEX WITH SUBSTRATE AND ATP ANALOG, SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ242910 mRNA. Translation: CAB61848.1.
AK001812 mRNA. Translation: BAA91923.1.
AK297224 mRNA. Translation: BAG59707.1.
CR457271 mRNA. Translation: CAG33552.1.
AK222645 mRNA. Translation: BAD96365.1.
AC007881 Genomic DNA. Translation: AAY14748.1.
CH471053 Genomic DNA. Translation: EAW99780.1.
BC001029 mRNA. Translation: AAH01029.1.
BC005371 mRNA. Translation: AAH05371.1.
CCDSCCDS33220.2. [Q9UJ70-2]
RefSeqNP_060037.3. NM_017567.4. [Q9UJ70-2]
UniGeneHs.7036.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2CH5X-ray1.90A/B/C/D1-344[»]
2CH6X-ray2.72A/B/C/D1-344[»]
ProteinModelPortalQ9UJ70.
SMRQ9UJ70. Positions 2-344.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid120728. 39 interactions.
IntActQ9UJ70. 22 interactions.
MINTMINT-1182067.
STRING9606.ENSP00000244204.

Chemistry

DrugBankDB00141. N-Acetyl-D-glucosamine.

PTM databases

PhosphoSiteQ9UJ70.

Polymorphism databases

DMDM24638065.

2D gel databases

OGPQ9UJ70.

Proteomic databases

MaxQBQ9UJ70.
PaxDbQ9UJ70.
PeptideAtlasQ9UJ70.
PRIDEQ9UJ70.

Protocols and materials databases

DNASU55577.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000244204; ENSP00000244204; ENSG00000124357. [Q9UJ70-1]
ENST00000455662; ENSP00000389087; ENSG00000124357. [Q9UJ70-2]
GeneID55577.
KEGGhsa:55577.
UCSCuc002shq.4. human. [Q9UJ70-1]

Organism-specific databases

CTD55577.
GeneCardsGC02P071295.
H-InvDBHIX0002147.
HGNCHGNC:17174. NAGK.
HPAHPA035207.
MIM606828. gene.
neXtProtNX_Q9UJ70.
PharmGKBPA31436.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG2971.
HOGENOMHOG000007248.
HOVERGENHBG052570.
InParanoidQ9UJ70.
KOK00884.
OMAAFYSYTF.
OrthoDBEOG7V1FR7.
PhylomeDBQ9UJ70.
TreeFamTF314158.

Enzyme and pathway databases

BRENDA2.7.1.59. 2681.
UniPathwayUPA00629.

Gene expression databases

ArrayExpressQ9UJ70.
BgeeQ9UJ70.
CleanExHS_NAGK.
GenevestigatorQ9UJ70.

Family and domain databases

InterProIPR002731. ATPase_BadF.
[Graphical view]
PfamPF01869. BcrAD_BadFG. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSNAGK. human.
EvolutionaryTraceQ9UJ70.
GeneWikiNAGK.
GenomeRNAi55577.
NextBio60080.
PROQ9UJ70.
SOURCESearch...

Entry information

Entry nameNAGK_HUMAN
AccessionPrimary (citable) accession number: Q9UJ70
Secondary accession number(s): B4DLZ5 expand/collapse secondary AC list , Q53HD5, Q6IA84, Q9BS29, Q9BVP0, Q9NV37
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 2002
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 123 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM