Q9UJ70 (NAGK_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	344 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.16
Tissue specificity	Ubiquitous. Ref.1
Sequence similarities	Belongs to the eukaryotic-type N-acetylglucosamine kinase family.

Ontologies

Keywords
Coding sequence diversity	Alternative splicing Polymorphism
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Transferase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	N-acetylglucosamine metabolic process Traceable author statement Ref.1. Source: ProtInc N-acetylmannosamine metabolic process Traceable author statement Ref.1. Source: ProtInc N-acetylneuraminate catabolic process Traceable author statement Ref.15. Source: UniProtKB
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW N-acetylglucosamine kinase activity Inferred from direct assay Ref.15. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
LNX1	Q8TBB1	2	EBI-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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.8

Chain

2 – 344

343

N-acetyl-D-glucosamine kinase

PRO_0000096696

Regions

Nucleotide binding

6 – 13

8

ATP

Region

129 – 130

2

Substrate binding

Region

145 – 147

3

Substrate binding

Sites

Binding site

36

1

Substrate

Binding site

107

1

Substrate

Binding site

152

1

Substrate

Binding site

271

1

ATP

Binding site

275

1

ATP

Amino acid modifications

Modified residue

76

1

Phosphoserine Ref.11 Ref.12 Ref.13

Modified residue

205

1

Phosphotyrosine Ref.10

Natural variations

Alternative sequence

1

1

M → MRTRTGSQLAAREVTGSGAV PRQLEGRRCQAGRDANGGTS SDGSSSM in isoform 2.

VSP_044586

Natural variant

38

1

W → R. Ref.7
Corresponds to variant rs17856147 [ dbSNP | Ensembl ].

VAR_029763

Natural variant

60

1

A → V. Ref.7
Corresponds to variant rs17849984 [ dbSNP | Ensembl ].

VAR_029764

Experimental info

Sequence conflict

70

1

S → I in CAB61848. Ref.1

Sequence conflict

121

1

V → I in CAB61848. Ref.1

Sequence conflict

211

1

C → Y in BAD96365. Ref.4

Sequence conflict

286

1

A → V in BAA91923. Ref.2

Sequence conflict

324

1

G → R in BAA91923. Ref.2

Secondary structure

1

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344

Helix Strand Turn

Details...

Beta strand

4 – 10

7

Beta strand

15 – 21

7

Beta strand

26 – 32

7

Helix

37 – 40

4

Helix

42 – 60

19

Beta strand

64 – 66

3

Beta strand

68 – 75

8

Turn

76 – 79

4

Helix

81 – 94

14

Beta strand

98 – 100

3

Beta strand

102 – 106

5

Helix

107 – 115

9

Beta strand

120 – 134

15

Beta strand

136 – 138

3

Beta strand

140 – 144

5

Turn

148 – 150

3

Helix

156 – 171

16

Helix

182 – 192

11

Helix

197 – 201

5

Turn

202 – 207

6

Helix

210 – 214

5

Helix

217 – 225

9

Helix

229 – 249

21

Helix

250 – 252

3

Helix

255 – 258

4

Beta strand

259 – 262

4

Beta strand

264 – 270

7

Helix

271 – 275

5

Helix

276 – 290

15

Beta strand

300 – 309

10

Helix

312 – 321

10

Turn

322 – 324

3

Helix

331 – 334

4

Beta strand

335 – 342

8

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified January 23, 2007. Version 4. Checksum: FCBB6B328EF4D515	FASTA	344	37,376
	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
	Isoform 2 [UniParc]. Checksum: 2B2DD636C8C35ADF	FASTA	390	42,038
	10 20 30 40 50 60 MRTRTGSQLA AREVTGSGAV PRQLEGRRCQ AGRDANGGTS SDGSSSMAAI YGGVEGGGTR 70 80 90 100 110 120 SEVLLVSEDG KILAEADGLS TNHWLIGTDK CVERINEMVN RAKRKAGVDP LVPLRSLGLS 130 140 150 160 170 180 LSGGDQEDAG RILIEELRDR FPYLSESYLI TTDAAGSIAT ATPDGGVVLI SGTGSNCRLI 190 200 210 220 230 240 NPDGSESGCG GWGHMMGDEG SAYWIAHQAV KIVFDSIDNL EAAPHDIGYV KQAMFHYFQV 250 260 270 280 290 300 PDRLGILTHL YRDFDKCRFA GFCRKIAEGA QQGDPLSRYI FRKAGEMLGR HIVAVLPEID 310 320 330 340 350 360 PVLFQGKIGL PILCVGSVWK SWELLKEGFL LALTQGREIQ AQNFFSSFTL MKLRHSSALG 370 380 390 GASLGARHIG HLLPMDYSAN AIAFYSYTFS

References

	« Hide 'large scale' referencesShow '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. , 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. , 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. , 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, 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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]	"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.

IPI

IPI00296526.
IPI00939575.

RefSeq

NP_060037.3. NM_017567.4.

UniGene

Hs.7036.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2CH5	X-ray	1.90	A/B/C/D	1-344	[»]
2CH6	X-ray	2.72	A/B/C/D	1-344	[»]

ProteinModelPortal

Q9UJ70.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q9UJ70. 9 interactions.

MINT

MINT-1182067.

STRING

9606.ENSP00000244204.

PTM databases

PhosphoSite

Q9UJ70.

Polymorphism databases

DMDM

24638065.

2D gel databases

OGP

Q9UJ70.

Proteomic databases

PaxDb

Q9UJ70.

PeptideAtlas

Q9UJ70.

PRIDE

Q9UJ70.

Protocols and materials databases

DNASU

55577.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000244204; ENSP00000244204; ENSG00000124357.
ENST00000455662; ENSP00000389087; ENSG00000124357.

GeneID

55577.

KEGG

hsa:55577.

UCSC

uc002shq.4. human.

Organism-specific databases

CTD

55577.

GeneCards

GC02P071295.

H-InvDB

HIX0002147.

HGNC

HGNC:17174. NAGK.

HPA

HPA035207.

MIM

606828. gene.

neXtProt

NX_Q9UJ70.

PharmGKB

PA31436.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG2971.

HOGENOM

HOG000007248.

HOVERGEN

HBG052570.

InParanoid

Q9UJ70.

KO

K00884.

OMA

AFYSYTF.

PhylomeDB

Q9UJ70.

Enzyme and pathway databases

BRENDA

2.7.1.59. 2681.

UniPathway

UPA00629.

Gene expression databases

ArrayExpress

Q9UJ70.

Bgee

Q9UJ70.

CleanEx

HS_NAGK.

Genevestigator

Q9UJ70.

GermOnline

ENSG00000124357. Homo sapiens.

Family and domain databases

InterPro

IPR002731. ATPase_BadF.
[Graphical view]

Pfam

PF01869. BcrAD_BadFG. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

NAGK. human.

DrugBank

DB00141. N-Acetyl-D-glucosamine.

EvolutionaryTrace

Q9UJ70.

GenomeRNAi

55577.

NextBio

60080.

SOURCE

Search...

Entry information

Entry name

NAGK_HUMAN

Accession

Primary (citable) accession number: Q9UJ70
Secondary accession number(s): B4DLZ5 , Q53HD5, Q6IA84, Q9BS29, Q9BVP0, Q9NV37

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 2002
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 110 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.