Reviewed, UniProtKB/Swiss-Prot Q9UJ70 (NAGK_HUMAN)

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) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › 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. Also has ManNAc kinase activity By similarity.
Catalytic activity	ATP + N-acetyl-D-glucosamine = ADP + N-acetyl-D-glucosamine 6-phosphate.
Subunit structure	Homodimer. Ref.13
Tissue specificity	Ubiquitous. Ref.1
Sequence similarities	Belongs to the eukaryotic-type N-acetylglucosamine kinase family.

Ontologies

Keywords
Coding sequence diversity	Polymorphism
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Transferase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	N-acetylglucosamine metabolic process Ref.1 Traceable author statement. Source: ProtInc N-acetylmannosamine metabolic process Ref.1 Traceable author statement. Source: ProtInc
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW N-acetylglucosamine kinase activity Inferred from electronic annotation. Source: EC protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
DCP2	Q8IU60	1	EBI-372578,EBI-521577
LNX1	Q8TBB1	1	EBI-372578,EBI-739832

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.7

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.10

Modified residue

205

1

Phosphotyrosine Ref.9

Natural variations

Natural variant

38

1

W → R: dbSNP rs17856147. Ref.6

VAR_029763

Natural variant

60

1

A → V: dbSNP rs17849984. Ref.6

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

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

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

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)
	Q9UJ70-1 [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

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: 10824116] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], 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: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: 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].
[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]. 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: 15815621] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANTS ARG-38 AND VAL-60. Tissue: Kidney and Skin.
[7]	"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: 12665801] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-14. Tissue: Platelet.
[8]	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.
[9]	"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: 12112843] [Abstract] Cited for: PHOSPHORYLATION AT TYR-205.
[10]	"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: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-76, MASS SPECTROMETRY.
[11]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[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: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-76, MASS SPECTROMETRY. Tissue: T-cell.
[13]	"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: 17010375] [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

EMBLGenBankDDBJ

AJ242910 mRNA. Translation: CAB61848.1.
AK001812 mRNA. Translation: BAA91923.1.
CR457271 mRNA. Translation: CAG33552.1.
AK222645 mRNA. Translation: BAD96365.1.
AC007881 Genomic DNA. Translation: AAY14748.1.
BC001029 mRNA. Translation: AAH01029.1.
BC005371 mRNA. Translation: AAH05371.1.

IPI

IPI00939575.

RefSeq

NP_060037.2.

UniGene

Hs.7036

3D structure databases

PDBPDBe

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	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

Q9UJ70. 5 interactions.

STRING

Q9UJ70.

PTM databases

PhosphoSite

Q9UJ70.

2-D gel databases

OGP

Q9UJ70.

Proteomic databases

PeptideAtlas

Q9UJ70.

PRIDE

Q9UJ70.

Genome annotation databases

Ensembl

ENST00000244204; ENSP00000244204; ENSG00000124357; Homo sapiens. [Genome view]
ENST00000455662; ENSP00000389087; ENSG00000124357; Homo sapiens. [Genome view]

GeneID

55577.

KEGG

hsa:55577.

NMPDR

fig|9606.3.peg.18016.

UCSC

uc002shp.2. human.

Organism-specific databases

CTD

55577.

GeneCards

GC02P071207.

H-InvDB

HIX0002147.

HGNC

HGNC:17174. NAGK.

MIM

606828. gene.

PharmGKB

PA31436.

GenAtlas

Search...

Phylogenomic databases

HOVERGEN

Q9UJ70.

InParanoid

Q9UJ70.

OrthoDB

EOG9X9B2T.

Enzyme and pathway databases

BRENDA

2.7.1.59. 247.

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 Resources

DrugBank

DB00141. N-Acetyl-D-glucosamine.

NextBio

60080.

SOURCE

Search...

Entry information

Entry name

NAGK_HUMAN

Accession

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

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 2002
Last sequence update:	January 23, 2007
Last modified:	December 15, 2009
This is version 79 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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.