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Q9UJ70

- NAGK_HUMAN

UniProt

Q9UJ70 - NAGK_HUMAN

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
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    • History
      Entry version 125 (01 Oct 2014)
      Sequence version 4 (23 Jan 2007)
      Previous versions | rss
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    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
    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

    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

    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 – 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.
    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.
    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

    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. 1 PublicationCurated
    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:
    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

    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: October 1, 2014
    This is version 125 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