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O95544

- NADK_HUMAN

UniProt

O95544 - NADK_HUMAN

Protein

NAD kinase

Gene

NADK

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 123 (01 Oct 2014)
      Sequence version 1 (01 May 1999)
      Previous versions | rss
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    Functioni

    Catalytic activityi

    ATP + NAD+ = ADP + NADP+.1 Publication

    Cofactori

    Divalent metal cations.1 Publication

    Kineticsi

    1. KM=3.3 mM for ATP1 Publication
    2. KM=0.54 mM for NAD1 Publication

    Vmax=6.7 µmol/min/mg enzyme1 Publication

    pH dependencei

    Optimum pH is 7.5.1 Publication

    Temperature dependencei

    Optimum temperature is 55 degrees Celsius.1 Publication

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. metal ion binding Source: UniProtKB-KW
    3. NAD+ kinase activity Source: UniProtKB

    GO - Biological processi

    1. ATP metabolic process Source: UniProtKB
    2. NAD metabolic process Source: Reactome
    3. NADP biosynthetic process Source: InterPro
    4. phosphorylation Source: UniProtKB
    5. small molecule metabolic process Source: Reactome
    6. vitamin metabolic process Source: Reactome
    7. water-soluble vitamin metabolic process Source: Reactome

    Keywords - Molecular functioni

    Kinase, Transferase

    Keywords - Ligandi

    ATP-binding, Metal-binding, NAD, NADP, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciMetaCyc:HS00233-MONOMER.
    BRENDAi2.7.1.23. 2681.
    ReactomeiREACT_11088. Nicotinate metabolism.
    SABIO-RKO95544.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    NAD kinase (EC:2.7.1.23)
    Alternative name(s):
    Poly(P)/ATP NAD kinase
    Gene namesi
    Name:NADK
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:29831. NADK.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: UniProtKB

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA142671298.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 446446NAD kinasePRO_0000120713Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei46 – 461Phosphoserine2 Publications
    Modified residuei48 – 481Phosphoserine2 Publications
    Modified residuei50 – 501Phosphoserine1 Publication
    Modified residuei64 – 641Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiO95544.
    PaxDbiO95544.
    PRIDEiO95544.

    PTM databases

    PhosphoSiteiO95544.

    Expressioni

    Tissue specificityi

    Widely expressed but not detected in skeletal muscle.1 Publication

    Gene expression databases

    ArrayExpressiO95544.
    BgeeiO95544.
    CleanExiHS_NADK.
    GenevestigatoriO95544.

    Organism-specific databases

    HPAiHPA048909.
    HPA053368.

    Interactioni

    Protein-protein interaction databases

    BioGridi122408. 12 interactions.
    IntActiO95544. 8 interactions.
    MINTiMINT-3296423.
    STRINGi9606.ENSP00000341679.

    Structurei

    Secondary structure

    1
    446
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni75 – 773
    Beta strandi78 – 803
    Turni84 – 863
    Beta strandi87 – 915
    Turni93 – 953
    Beta strandi97 – 1026
    Beta strandi106 – 1116
    Helixi116 – 1183
    Helixi119 – 13113
    Beta strandi135 – 1395
    Helixi140 – 1445
    Helixi146 – 1505
    Helixi155 – 1606
    Beta strandi162 – 1643
    Turni166 – 1683
    Turni172 – 1743
    Beta strandi176 – 1838
    Helixi186 – 1938
    Beta strandi195 – 1973
    Beta strandi201 – 2088
    Turni210 – 2123
    Beta strandi215 – 2173
    Helixi220 – 22910
    Beta strandi233 – 2375
    Beta strandi240 – 2456
    Beta strandi277 – 28913
    Beta strandi299 – 3035
    Beta strandi306 – 3116
    Beta strandi313 – 3197
    Helixi321 – 3255
    Helixi327 – 3304
    Beta strandi343 – 3497
    Beta strandi358 – 3603
    Beta strandi366 – 3705
    Beta strandi378 – 3825
    Beta strandi385 – 3906
    Beta strandi395 – 4006
    Beta strandi405 – 4084
    Helixi413 – 42412

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3PFNX-ray2.70A/B/C/D68-426[»]
    ProteinModelPortaliO95544.
    SMRiO95544. Positions 72-426.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO95544.

    Family & Domainsi

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi326 – 3338Poly-Ala
    Compositional biasi437 – 4459Poly-Glu

    Sequence similaritiesi

    Belongs to the NAD kinase family.Curated

    Phylogenomic databases

    eggNOGiCOG0061.
    HOGENOMiHOG000176769.
    HOVERGENiHBG008249.
    KOiK00858.
    OMAiSAQRENC.
    OrthoDBiEOG7ZPNJT.
    PhylomeDBiO95544.
    TreeFamiTF324076.

    Family and domain databases

    Gene3Di2.60.200.30. 1 hit.
    3.40.50.10330. 1 hit.
    HAMAPiMF_00361. NAD_kinase.
    InterProiIPR017438. ATP-NAD_kinase_dom_1.
    IPR016064. ATP-NAD_kinase_PpnK-typ.
    IPR017437. ATP-NAD_kinase_PpnK-typ_all-b.
    IPR002504. PolyP/ATP_NADK.
    [Graphical view]
    PANTHERiPTHR20275. PTHR20275. 1 hit.
    PfamiPF01513. NAD_kinase. 1 hit.
    [Graphical view]
    SUPFAMiSSF111331. SSF111331. 2 hits.

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: O95544-1) [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

    MEMEQEKMTM NKELSPDAAA YCCSACHGDE TWSYNHPIRG RAKSRSLSAS    50
    PALGSTKEFR RTRSLHGPCP VTTFGPKACV LQNPQTIMHI QDPASQRLTW 100
    NKSPKSVLVI KKMRDASLLQ PFKELCTHLM EENMIVYVEK KVLEDPAIAS 150
    DESFGAVKKK FCTFREDYDD ISNQIDFIIC LGGDGTLLYA SSLFQGSVPP 200
    VMAFHLGSLG FLTPFSFENF QSQVTQVIEG NAAVVLRSRL KVRVVKELRG 250
    KKTAVHNGLG ENGSQAAGLD MDVGKQAMQY QVLNEVVIDR GPSSYLSNVD 300
    VYLDGHLITT VQGDGVIVST PTGSTAYAAA AGASMIHPNV PAIMITPICP 350
    HSLSFRPIVV PAGVELKIML SPEARNTAWV SFDGRKRQEI RHGDSISITT 400
    SCYPLPSICV RDPVSDWFES LAQCLHWNVR KKQAHFEEEE EEEEEG 446
    Length:446
    Mass (Da):49,228
    Last modified:May 1, 1999 - v1
    Checksum:i48CE7AF05EDD7E8B
    GO
    Isoform 2 (identifier: O95544-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         88-88: M → IATPLSLASQ...AGMGVGQATG
         131-131: E → EARGAGGKGAWGAHGVGGASIHITAPRVGSAGGMSRLALCFQ

    Show »
    Length:591
    Mass (Da):63,456
    Checksum:i9F81E711739713BA
    GO
    Isoform 3 (identifier: O95544-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         11-87: NKELSPDAAA...ACVLQNPQTI → GRPRVRQAWP...DPTPPSNACT

    Show »
    Length:423
    Mass (Da):46,446
    Checksum:iD83B07A90D5B6D0A
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti363 – 3631Missing in AAG44568. 1 PublicationCurated
    Sequence conflicti445 – 4451E → EE in BAB14412. 1 PublicationCurated
    Sequence conflicti446 – 4461G → EG in BAH12420. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti262 – 2621N → K.2 Publications
    Corresponds to variant rs4751 [ dbSNP | Ensembl ].
    VAR_034119

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei11 – 8777NKELS…NPQTI → GRPRVRQAWPGCCGHTGRLP AGRGYLASHMCDPAGAELIG DGMSDPTPPSNACT in isoform 3. 1 PublicationVSP_047312Add
    BLAST
    Alternative sequencei88 – 881M → IATPLSLASQLLPSPAVSHS GQGGVTGQVHVLPQPSDQGV LSGPRAARGQTAPQEEAVTQ EEVEALVCGHTQRWVPGPVY DAAAGGSGWAQLSLRAGMGV GQATG in isoform 2. 1 PublicationVSP_047313
    Alternative sequencei131 – 1311E → EARGAGGKGAWGAHGVGGAS IHITAPRVGSAGGMSRLALC FQ in isoform 2. 1 PublicationVSP_047314

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY090771 mRNA. Translation: AAM01195.1.
    AF250320 mRNA. Translation: AAG44568.1.
    AK023114 mRNA. Translation: BAB14412.1.
    AK290161 mRNA. Translation: BAF82850.1.
    AK296722 mRNA. Translation: BAH12420.1.
    AL031282 Genomic DNA. No translation available.
    CH471183 Genomic DNA. Translation: EAW56151.1.
    CH471183 Genomic DNA. Translation: EAW56152.1.
    BC001709 mRNA. Translation: AAH01709.1.
    CCDSiCCDS30565.1. [O95544-1]
    CCDS55562.1. [O95544-2]
    RefSeqiNP_001185922.1. NM_001198993.1. [O95544-1]
    NP_001185923.1. NM_001198994.1. [O95544-2]
    NP_001185924.1. NM_001198995.1.
    NP_075394.3. NM_023018.4. [O95544-1]
    XP_005244835.1. XM_005244778.1. [O95544-1]
    XP_006710900.1. XM_006710837.1. [O95544-1]
    UniGeneiHs.654792.
    Hs.731532.
    Hs.733075.

    Genome annotation databases

    EnsembliENST00000341426; ENSP00000341679; ENSG00000008130. [O95544-1]
    ENST00000341991; ENSP00000344340; ENSG00000008130. [O95544-1]
    ENST00000378625; ENSP00000367890; ENSG00000008130. [O95544-2]
    GeneIDi65220.
    KEGGihsa:65220.
    UCSCiuc001aic.3. human. [O95544-1]
    uc001aie.3. human.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY090771 mRNA. Translation: AAM01195.1 .
    AF250320 mRNA. Translation: AAG44568.1 .
    AK023114 mRNA. Translation: BAB14412.1 .
    AK290161 mRNA. Translation: BAF82850.1 .
    AK296722 mRNA. Translation: BAH12420.1 .
    AL031282 Genomic DNA. No translation available.
    CH471183 Genomic DNA. Translation: EAW56151.1 .
    CH471183 Genomic DNA. Translation: EAW56152.1 .
    BC001709 mRNA. Translation: AAH01709.1 .
    CCDSi CCDS30565.1. [O95544-1 ]
    CCDS55562.1. [O95544-2 ]
    RefSeqi NP_001185922.1. NM_001198993.1. [O95544-1 ]
    NP_001185923.1. NM_001198994.1. [O95544-2 ]
    NP_001185924.1. NM_001198995.1.
    NP_075394.3. NM_023018.4. [O95544-1 ]
    XP_005244835.1. XM_005244778.1. [O95544-1 ]
    XP_006710900.1. XM_006710837.1. [O95544-1 ]
    UniGenei Hs.654792.
    Hs.731532.
    Hs.733075.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3PFN X-ray 2.70 A/B/C/D 68-426 [» ]
    ProteinModelPortali O95544.
    SMRi O95544. Positions 72-426.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 122408. 12 interactions.
    IntActi O95544. 8 interactions.
    MINTi MINT-3296423.
    STRINGi 9606.ENSP00000341679.

    Chemistry

    BindingDBi O95544.
    ChEMBLi CHEMBL6177.

    PTM databases

    PhosphoSitei O95544.

    Proteomic databases

    MaxQBi O95544.
    PaxDbi O95544.
    PRIDEi O95544.

    Protocols and materials databases

    DNASUi 65220.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000341426 ; ENSP00000341679 ; ENSG00000008130 . [O95544-1 ]
    ENST00000341991 ; ENSP00000344340 ; ENSG00000008130 . [O95544-1 ]
    ENST00000378625 ; ENSP00000367890 ; ENSG00000008130 . [O95544-2 ]
    GeneIDi 65220.
    KEGGi hsa:65220.
    UCSCi uc001aic.3. human. [O95544-1 ]
    uc001aie.3. human.

    Organism-specific databases

    CTDi 65220.
    GeneCardsi GC01M001682.
    HGNCi HGNC:29831. NADK.
    HPAi HPA048909.
    HPA053368.
    MIMi 611616. gene.
    neXtProti NX_O95544.
    PharmGKBi PA142671298.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0061.
    HOGENOMi HOG000176769.
    HOVERGENi HBG008249.
    KOi K00858.
    OMAi SAQRENC.
    OrthoDBi EOG7ZPNJT.
    PhylomeDBi O95544.
    TreeFami TF324076.

    Enzyme and pathway databases

    BioCyci MetaCyc:HS00233-MONOMER.
    BRENDAi 2.7.1.23. 2681.
    Reactomei REACT_11088. Nicotinate metabolism.
    SABIO-RK O95544.

    Miscellaneous databases

    ChiTaRSi NADK. human.
    EvolutionaryTracei O95544.
    GeneWikii NAD%2B_kinase.
    GenomeRNAii 65220.
    NextBioi 67354.
    PROi O95544.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O95544.
    Bgeei O95544.
    CleanExi HS_NADK.
    Genevestigatori O95544.

    Family and domain databases

    Gene3Di 2.60.200.30. 1 hit.
    3.40.50.10330. 1 hit.
    HAMAPi MF_00361. NAD_kinase.
    InterProi IPR017438. ATP-NAD_kinase_dom_1.
    IPR016064. ATP-NAD_kinase_PpnK-typ.
    IPR017437. ATP-NAD_kinase_PpnK-typ_all-b.
    IPR002504. PolyP/ATP_NADK.
    [Graphical view ]
    PANTHERi PTHR20275. PTHR20275. 1 hit.
    Pfami PF01513. NAD_kinase. 1 hit.
    [Graphical view ]
    SUPFAMi SSF111331. SSF111331. 2 hits.
    ProtoNeti Search...

    Publicationsi

    1. "Structural and functional characterization of human NAD kinase."
      Lerner F., Niere M., Ludwig A., Ziegler M.
      Biochem. Biophys. Res. Commun. 288:69-74(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY, VARIANT LYS-262.
      Tissue: Fibroblast.
    2. Xu X., Yang Y., Gao G., Xiao H., Chen Z., Han Z.
      Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
      Tissue: Hypothalamus.
    3. "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 3).
      Tissue: Thalamus.
    4. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. 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] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT LYS-262.
      Tissue: Lymph.
    7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-46; SER-48; SER-50 AND SER-64, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    8. "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-46 AND SER-48, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    9. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    10. "Crystal structure of human NAD kinase."
      Structural genomics consortium (SGC)
      Submitted (NOV-2010) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 68-426.

    Entry informationi

    Entry nameiNADK_HUMAN
    AccessioniPrimary (citable) accession number: O95544
    Secondary accession number(s): A6NNN3
    , A8K296, B7Z434, F5GXR5, Q5QPS4, Q9H2P2, Q9H931
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2000
    Last sequence update: May 1, 1999
    Last modified: October 1, 2014
    This is version 123 of the entry and version 1 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, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3