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Q9UJ70

- NAGK_HUMAN

UniProt

Q9UJ70 - NAGK_HUMAN

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Protein

N-acetyl-D-glucosamine kinase

Gene
NAGK
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.1 Publication

Catalytic activityi

ATP + N-acetyl-D-glucosamine = ADP + N-acetyl-D-glucosamine 6-phosphate.1 Publication

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei36 – 361Substrate
Binding sitei107 – 1071Substrate
Binding sitei152 – 1521Substrate
Binding sitei271 – 2711ATP
Binding sitei275 – 2751ATP

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi6 – 138ATP

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. N-acetylglucosamine kinase activity Source: UniProtKB
  3. N-acylmannosamine kinase activity Source: Ensembl
  4. protein binding Source: IntAct

GO - Biological processi

  1. carbohydrate phosphorylation Source: GOC
  2. N-acetylglucosamine metabolic process Source: ProtInc
  3. N-acetylmannosamine metabolic process Source: ProtInc
  4. N-acetylneuraminate catabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.1.59. 2681.
UniPathwayiUPA00629.

Names & Taxonomyi

Protein namesi
Recommended name:
N-acetyl-D-glucosamine kinase (EC:2.7.1.59)
Short name:
N-acetylglucosamine kinase
Alternative name(s):
GlcNAc kinase
Gene namesi
Name:NAGK
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 2

Organism-specific databases

HGNCiHGNC:17174. NAGK.

Subcellular locationi

GO - Cellular componenti

  1. extracellular vesicular exosome Source: UniProt
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA31436.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed2 Publications
Chaini2 – 344343N-acetyl-D-glucosamine kinasePRO_0000096696Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine2 Publications
Modified residuei76 – 761Phosphoserine3 Publications
Modified residuei205 – 2051Phosphotyrosine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ9UJ70.
PaxDbiQ9UJ70.
PeptideAtlasiQ9UJ70.
PRIDEiQ9UJ70.

2D gel databases

OGPiQ9UJ70.

PTM databases

PhosphoSiteiQ9UJ70.

Expressioni

Tissue specificityi

Ubiquitous.1 Publication

Gene expression databases

ArrayExpressiQ9UJ70.
BgeeiQ9UJ70.
CleanExiHS_NAGK.
GenevestigatoriQ9UJ70.

Organism-specific databases

HPAiHPA035207.

Interactioni

Subunit structurei

Homodimer.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
DACH1Q9UI363EBI-372578,EBI-347111
LNX1Q8TBB12EBI-372578,EBI-739832

Protein-protein interaction databases

BioGridi120728. 39 interactions.
IntActiQ9UJ70. 22 interactions.
MINTiMINT-1182067.
STRINGi9606.ENSP00000244204.

Structurei

Secondary structure

1
344
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 107
Beta strandi15 – 217
Beta strandi26 – 327
Helixi37 – 404
Helixi42 – 6019
Beta strandi64 – 663
Beta strandi68 – 758
Turni76 – 794
Helixi81 – 9414
Beta strandi98 – 1003
Beta strandi102 – 1065
Helixi107 – 1159
Beta strandi120 – 13415
Beta strandi136 – 1383
Beta strandi140 – 1445
Turni148 – 1503
Helixi156 – 17116
Helixi182 – 19211
Helixi197 – 2015
Turni202 – 2076
Helixi210 – 2145
Helixi217 – 2259
Helixi229 – 24921
Helixi250 – 2523
Helixi255 – 2584
Beta strandi259 – 2624
Beta strandi264 – 2707
Helixi271 – 2755
Helixi276 – 29015
Beta strandi300 – 30910
Helixi312 – 32110
Turni322 – 3243
Helixi331 – 3344
Beta strandi335 – 3428

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2CH5X-ray1.90A/B/C/D1-344[»]
2CH6X-ray2.72A/B/C/D1-344[»]
ProteinModelPortaliQ9UJ70.
SMRiQ9UJ70. Positions 2-344.

Miscellaneous databases

EvolutionaryTraceiQ9UJ70.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni129 – 1302Substrate binding
Regioni145 – 1473Substrate binding

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG2971.
HOGENOMiHOG000007248.
HOVERGENiHBG052570.
InParanoidiQ9UJ70.
KOiK00884.
OMAiAFYSYTF.
OrthoDBiEOG7V1FR7.
PhylomeDBiQ9UJ70.
TreeFamiTF314158.

Family and domain databases

InterProiIPR002731. ATPase_BadF.
[Graphical view]
PfamiPF01869. BcrAD_BadFG. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9UJ70-1) [UniParc]FASTAAdd to Basket

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.

« Hide

MAAIYGGVEG GGTRSEVLLV SEDGKILAEA DGLSTNHWLI GTDKCVERIN    50
EMVNRAKRKA GVDPLVPLRS LGLSLSGGDQ EDAGRILIEE LRDRFPYLSE 100
SYLITTDAAG SIATATPDGG VVLISGTGSN CRLINPDGSE SGCGGWGHMM 150
GDEGSAYWIA HQAVKIVFDS IDNLEAAPHD IGYVKQAMFH YFQVPDRLGI 200
LTHLYRDFDK CRFAGFCRKI AEGAQQGDPL SRYIFRKAGE MLGRHIVAVL 250
PEIDPVLFQG KIGLPILCVG SVWKSWELLK EGFLLALTQG REIQAQNFFS 300
SFTLMKLRHS SALGGASLGA RHIGHLLPMD YSANAIAFYS YTFS 344
Length:344
Mass (Da):37,376
Last modified:January 23, 2007 - v4
Checksum:iFCBB6B328EF4D515
GO
Isoform 2 (identifier: Q9UJ70-2) [UniParc]FASTAAdd to Basket

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

Show »
Length:390
Mass (Da):42,038
Checksum:i2B2DD636C8C35ADF
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti38 – 381W → R.1 Publication
Corresponds to variant rs17856147 [ dbSNP | Ensembl ].
VAR_029763
Natural varianti60 – 601A → V.1 Publication
Corresponds to variant rs17849984 [ dbSNP | Ensembl ].
VAR_029764

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 11M → MRTRTGSQLAAREVTGSGAV PRQLEGRRCQAGRDANGGTS SDGSSSM in isoform 2. VSP_044586

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti70 – 701S → I in CAB61848. 1 Publication
Sequence conflicti121 – 1211V → I in CAB61848. 1 Publication
Sequence conflicti211 – 2111C → Y in BAD96365. 1 Publication
Sequence conflicti286 – 2861A → V in BAA91923. 1 Publication
Sequence conflicti324 – 3241G → R in BAA91923. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS33220.2. [Q9UJ70-2]
RefSeqiNP_060037.3. NM_017567.4. [Q9UJ70-2]
UniGeneiHs.7036.

Genome annotation databases

EnsembliENST00000244204; ENSP00000244204; ENSG00000124357. [Q9UJ70-1]
ENST00000455662; ENSP00000389087; ENSG00000124357. [Q9UJ70-2]
GeneIDi55577.
KEGGihsa:55577.
UCSCiuc002shp.4. human.
uc002shq.4. human. [Q9UJ70-1]

Polymorphism databases

DMDMi24638065.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS33220.2. [Q9UJ70-2 ]
RefSeqi NP_060037.3. NM_017567.4. [Q9UJ70-2 ]
UniGenei Hs.7036.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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 [» ]
ProteinModelPortali Q9UJ70.
SMRi Q9UJ70. Positions 2-344.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 120728. 39 interactions.
IntActi Q9UJ70. 22 interactions.
MINTi MINT-1182067.
STRINGi 9606.ENSP00000244204.

Chemistry

DrugBanki DB00141. N-Acetyl-D-glucosamine.

PTM databases

PhosphoSitei Q9UJ70.

Polymorphism databases

DMDMi 24638065.

2D gel databases

OGPi Q9UJ70.

Proteomic databases

MaxQBi Q9UJ70.
PaxDbi Q9UJ70.
PeptideAtlasi Q9UJ70.
PRIDEi Q9UJ70.

Protocols and materials databases

DNASUi 55577.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000244204 ; ENSP00000244204 ; ENSG00000124357 . [Q9UJ70-1 ]
ENST00000455662 ; ENSP00000389087 ; ENSG00000124357 . [Q9UJ70-2 ]
GeneIDi 55577.
KEGGi hsa:55577.
UCSCi uc002shp.4. human.
uc002shq.4. human. [Q9UJ70-1 ]

Organism-specific databases

CTDi 55577.
GeneCardsi GC02P071295.
H-InvDB HIX0002147.
HGNCi HGNC:17174. NAGK.
HPAi HPA035207.
MIMi 606828. gene.
neXtProti NX_Q9UJ70.
PharmGKBi PA31436.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG2971.
HOGENOMi HOG000007248.
HOVERGENi HBG052570.
InParanoidi Q9UJ70.
KOi K00884.
OMAi AFYSYTF.
OrthoDBi EOG7V1FR7.
PhylomeDBi Q9UJ70.
TreeFami TF314158.

Enzyme and pathway databases

UniPathwayi UPA00629 .
BRENDAi 2.7.1.59. 2681.

Miscellaneous databases

ChiTaRSi NAGK. human.
EvolutionaryTracei Q9UJ70.
GeneWikii NAGK.
GenomeRNAii 55577.
NextBioi 60080.
PROi Q9UJ70.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9UJ70.
Bgeei Q9UJ70.
CleanExi HS_NAGK.
Genevestigatori Q9UJ70.

Family and domain databases

InterProi IPR002731. ATPase_BadF.
[Graphical view ]
Pfami PF01869. BcrAD_BadFG. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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. 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. 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. 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.

Entry informationi

Entry nameiNAGK_HUMAN
AccessioniPrimary (citable) accession number: Q9UJ70
Secondary accession number(s): B4DLZ5
, Q53HD5, Q6IA84, Q9BS29, Q9BVP0, Q9NV37
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 2002
Last sequence update: January 23, 2007
Last modified: September 3, 2014
This is version 124 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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