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Protein

N-acetyl-D-glucosamine kinase

Gene

NAGK

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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 – 361Substrate1 Publication
Binding sitei107 – 1071Substrate1 Publication
Binding sitei152 – 1521Substrate1 Publication
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

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: UniProtKB
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA31436.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed3 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 – 761Phosphoserine4 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

BgeeiQ9UJ70.
CleanExiHS_NAGK.
ExpressionAtlasiQ9UJ70. baseline and differential.
GenevestigatoriQ9UJ70.

Organism-specific databases

HPAiHPA035206.
HPA035207.

Interactioni

Subunit structurei

Homodimer.1 Publication

Binary interactionsi

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

Protein-protein interaction databases

BioGridi120728. 52 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 – 107Combined sources
Beta strandi15 – 217Combined sources
Beta strandi26 – 327Combined sources
Helixi37 – 404Combined sources
Helixi42 – 6019Combined sources
Beta strandi64 – 663Combined sources
Beta strandi68 – 758Combined sources
Turni76 – 794Combined sources
Helixi81 – 9414Combined sources
Beta strandi98 – 1003Combined sources
Beta strandi102 – 1065Combined sources
Helixi107 – 1159Combined sources
Beta strandi120 – 13415Combined sources
Beta strandi136 – 1383Combined sources
Beta strandi140 – 1445Combined sources
Turni148 – 1503Combined sources
Helixi156 – 17116Combined sources
Helixi182 – 19211Combined sources
Helixi197 – 2015Combined sources
Turni202 – 2076Combined sources
Helixi210 – 2145Combined sources
Helixi217 – 2259Combined sources
Helixi229 – 24921Combined sources
Helixi250 – 2523Combined sources
Helixi255 – 2584Combined sources
Beta strandi259 – 2624Combined sources
Beta strandi264 – 2707Combined sources
Helixi271 – 2755Combined sources
Helixi276 – 29015Combined sources
Beta strandi300 – 30910Combined sources
Helixi312 – 32110Combined sources
Turni322 – 3243Combined sources
Helixi331 – 3344Combined sources
Beta strandi335 – 3428Combined sources

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiQ9UJ70.

Family & Domainsi

Region

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

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG2971.
GeneTreeiENSGT00510000047418.
HOGENOMiHOG000007248.
HOVERGENiHBG052570.
InParanoidiQ9UJ70.
KOiK00884.
OMAiLLPMDYS.
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. AlignAdd to basket

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

        10         20         30         40         50
MAAIYGGVEG GGTRSEVLLV SEDGKILAEA DGLSTNHWLI GTDKCVERIN
60 70 80 90 100
EMVNRAKRKA GVDPLVPLRS LGLSLSGGDQ EDAGRILIEE LRDRFPYLSE
110 120 130 140 150
SYLITTDAAG SIATATPDGG VVLISGTGSN CRLINPDGSE SGCGGWGHMM
160 170 180 190 200
GDEGSAYWIA HQAVKIVFDS IDNLEAAPHD IGYVKQAMFH YFQVPDRLGI
210 220 230 240 250
LTHLYRDFDK CRFAGFCRKI AEGAQQGDPL SRYIFRKAGE MLGRHIVAVL
260 270 280 290 300
PEIDPVLFQG KIGLPILCVG SVWKSWELLK EGFLLALTQG REIQAQNFFS
310 320 330 340
SFTLMKLRHS SALGGASLGA RHIGHLLPMD YSANAIAFYS YTFS
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

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti70 – 701S → I in CAB61848 (PubMed:10824116).Curated
Sequence conflicti121 – 1211V → I in CAB61848 (PubMed:10824116).Curated
Sequence conflicti211 – 2111C → Y in BAD96365 (Ref. 4) Curated
Sequence conflicti286 – 2861A → V in BAA91923 (PubMed:14702039).Curated
Sequence conflicti324 – 3241G → R in BAA91923 (PubMed:14702039).Curated

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. 1 PublicationVSP_044586

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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]
ENST00000613852; ENSP00000477639; 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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

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

Protein-protein interaction databases

BioGridi120728. 52 interactions.
IntActiQ9UJ70. 22 interactions.
MINTiMINT-1182067.
STRINGi9606.ENSP00000244204.

Chemistry

DrugBankiDB00141. N-Acetyl-D-glucosamine.

PTM databases

PhosphoSiteiQ9UJ70.

Polymorphism databases

DMDMi24638065.

2D gel databases

OGPiQ9UJ70.

Proteomic databases

MaxQBiQ9UJ70.
PaxDbiQ9UJ70.
PeptideAtlasiQ9UJ70.
PRIDEiQ9UJ70.

Protocols and materials databases

DNASUi55577.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000244204; ENSP00000244204; ENSG00000124357. [Q9UJ70-1]
ENST00000455662; ENSP00000389087; ENSG00000124357. [Q9UJ70-2]
ENST00000613852; ENSP00000477639; ENSG00000124357. [Q9UJ70-2]
GeneIDi55577.
KEGGihsa:55577.
UCSCiuc002shp.4. human.
uc002shq.4. human. [Q9UJ70-1]

Organism-specific databases

CTDi55577.
GeneCardsiGC02P071295.
H-InvDBHIX0002147.
HGNCiHGNC:17174. NAGK.
HPAiHPA035206.
HPA035207.
MIMi606828. gene.
neXtProtiNX_Q9UJ70.
PharmGKBiPA31436.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG2971.
GeneTreeiENSGT00510000047418.
HOGENOMiHOG000007248.
HOVERGENiHBG052570.
InParanoidiQ9UJ70.
KOiK00884.
OMAiLLPMDYS.
OrthoDBiEOG7V1FR7.
PhylomeDBiQ9UJ70.
TreeFamiTF314158.

Enzyme and pathway databases

UniPathwayiUPA00629.
BRENDAi2.7.1.59. 2681.

Miscellaneous databases

ChiTaRSiNAGK. human.
EvolutionaryTraceiQ9UJ70.
GeneWikiiNAGK.
GenomeRNAii55577.
NextBioi60080.
PROiQ9UJ70.
SOURCEiSearch...

Gene expression databases

BgeeiQ9UJ70.
CleanExiHS_NAGK.
ExpressionAtlasiQ9UJ70. baseline and differential.
GenevestigatoriQ9UJ70.

Family and domain databases

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

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], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  18. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-76, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  19. "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: March 4, 2015
This is version 129 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.