Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P22392

- NDKB_HUMAN

UniProt

P22392 - NDKB_HUMAN

Protein

Nucleoside diphosphate kinase B

Gene

NME2

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

    Major role in the synthesis of nucleoside triphosphates other than ATP. Negatively regulates Rho activity by interacting with AKAP13/LBC. Acts as a transcriptional activator of the MYC gene; binds DNA non-specifically (PubMed:8392752). Exhibits histidine protein kinase activity.3 Publications

    Catalytic activityi

    ATP + nucleoside diphosphate = ADP + nucleoside triphosphate.
    ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.

    Cofactori

    Magnesium.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei12 – 121ATP
    Binding sitei60 – 601ATP
    Binding sitei88 – 881ATP
    Binding sitei94 – 941ATP
    Binding sitei105 – 1051ATP
    Binding sitei115 – 1151ATP
    Active sitei118 – 1181Pros-phosphohistidine intermediate1 Publication

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. DNA binding Source: UniProtKB-KW
    3. metal ion binding Source: UniProtKB-KW
    4. nucleoside diphosphate kinase activity Source: UniProtKB
    5. protein binding Source: UniProtKB
    6. protein histidine kinase activity Source: UniProtKB-EC
    7. sequence-specific DNA binding transcription factor activity Source: UniProtKB

    GO - Biological processi

    1. cell adhesion Source: HGNC
    2. CTP biosynthetic process Source: InterPro
    3. GTP biosynthetic process Source: InterPro
    4. integrin-mediated signaling pathway Source: UniProtKB
    5. negative regulation of apoptotic process Source: HGNC
    6. nucleobase-containing small molecule interconversion Source: Reactome
    7. nucleobase-containing small molecule metabolic process Source: Reactome
    8. nucleoside triphosphate biosynthetic process Source: UniProtKB
    9. positive regulation of epithelial cell proliferation Source: HGNC
    10. positive regulation of keratinocyte differentiation Source: HGNC
    11. positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
    12. regulation of epidermis development Source: HGNC
    13. regulation of transcription, DNA-templated Source: UniProtKB
    14. small molecule metabolic process Source: Reactome
    15. transcription, DNA-templated Source: UniProtKB-KW
    16. UTP biosynthetic process Source: InterPro

    Keywords - Molecular functioni

    Activator, Kinase, Transferase

    Keywords - Biological processi

    Nucleotide metabolism, Transcription, Transcription regulation

    Keywords - Ligandi

    ATP-binding, DNA-binding, Magnesium, Metal-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciMetaCyc:HS04463-MONOMER.
    ReactomeiREACT_21330. Synthesis and interconversion of nucleotide di- and triphosphates.
    SignaLinkiP22392.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Nucleoside diphosphate kinase B (EC:2.7.4.6)
    Short name:
    NDK B
    Short name:
    NDP kinase B
    Alternative name(s):
    C-myc purine-binding transcription factor PUF
    Histidine protein kinase NDKB (EC:2.7.13.3)
    nm23-H2
    Gene namesi
    Name:NME2
    Synonyms:NM23B
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 17

    Organism-specific databases

    HGNCiHGNC:7850. NME2.

    Subcellular locationi

    Cytoplasm. Nucleus. Cell projectionlamellipodium. Cell projectionruffle
    Note: Isoform 2 is mainly cytoplasmic and isoform 1 and isoform 2 are excluded from the nucleolus. Colocalizes with ITGB1 and ITGB1BP1 at the edge or peripheral ruffles and lamellipodia during the early stages of cell spreading on fibronectin or collagen but not on vitronectin or laminin substrates.

    GO - Cellular componenti

    1. cell periphery Source: UniProtKB
    2. cytoplasm Source: UniProtKB
    3. cytosol Source: Reactome
    4. extracellular vesicular exosome Source: UniProt
    5. lamellipodium Source: HGNC
    6. nucleus Source: UniProt
    7. ruffle Source: HGNC

    Keywords - Cellular componenti

    Cell projection, Cytoplasm, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA162398077.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 152151Nucleoside diphosphate kinase BPRO_0000137117Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine1 Publication
    Modified residuei128 – 1281N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiP22392.
    PRIDEiP22392.

    2D gel databases

    DOSAC-COBS-2DPAGEP22392.
    OGPiP22392.
    UCD-2DPAGEP22392.

    PTM databases

    PhosphoSiteiP22392.

    Expressioni

    Tissue specificityi

    Ubiquitously expressed.1 Publication

    Gene expression databases

    BgeeiP22392.
    GenevestigatoriP22392.

    Organism-specific databases

    HPAiCAB002169.
    CAB040571.
    HPA008467.
    HPA041113.

    Interactioni

    Subunit structurei

    Hexamer of two different chains: A and B (A6, A5B, A4B2, A3B3, A2B4, AB5, B6). Interacts with CAPN8 By similarity. Interacts with AKAP13. Interacts ITGB1BP1 (via C-terminal domain region).By similarity3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ITGB1BP1O14713-17EBI-713693,EBI-2127367
    NME1P155312EBI-713693,EBI-741141

    Protein-protein interaction databases

    BioGridi110895. 42 interactions.
    576341. 8 interactions.
    IntActiP22392. 18 interactions.
    MINTiMINT-1429922.
    STRINGi9606.ENSP00000376886.

    Structurei

    Secondary structure

    1
    152
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi6 – 116
    Helixi13 – 175
    Helixi21 – 3111
    Beta strandi34 – 418
    Helixi45 – 517
    Helixi53 – 553
    Helixi61 – 688
    Beta strandi73 – 808
    Helixi83 – 919
    Helixi96 – 983
    Helixi104 – 1085
    Helixi112 – 1143
    Beta strandi117 – 1193
    Helixi123 – 13311
    Helixi136 – 1383
    Helixi147 – 1504

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1NSKX-ray2.80L/N/O/R/T/U1-152[»]
    1NUEX-ray2.00A/B/C/D/E/F2-152[»]
    3BBBX-ray1.30A/B/C/D/E/F2-152[»]
    3BBCX-ray1.70A/B/C/D/E/F2-152[»]
    3BBFX-ray1.70A/B/C/D/E/F2-152[»]
    ProteinModelPortaliP22392.
    SMRiP22392. Positions 2-152.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP22392.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni2 – 6665Interaction with AKAP13Add
    BLAST

    Sequence similaritiesi

    Belongs to the NDK family.Curated

    Phylogenomic databases

    HOGENOMiHOG000224564.
    HOVERGENiHBG000423.
    InParanoidiP22392.
    KOiK00940.
    OrthoDBiEOG7GJ6FG.
    PhylomeDBiP22392.
    TreeFamiTF106373.

    Family and domain databases

    Gene3Di3.30.70.141. 1 hit.
    HAMAPiMF_00451. NDP_kinase.
    InterProiIPR001564. Nucleoside_diP_kinase.
    IPR023005. Nucleoside_diP_kinase_AS.
    [Graphical view]
    PfamiPF00334. NDK. 1 hit.
    [Graphical view]
    PRINTSiPR01243. NUCDPKINASE.
    SMARTiSM00562. NDK. 1 hit.
    [Graphical view]
    SUPFAMiSSF54919. SSF54919. 1 hit.
    PROSITEiPS00469. NDP_KINASES. 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: P22392-1) [UniParc]FASTAAdd to Basket

    Also known as: NM23-H2

    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

    MANLERTFIA IKPDGVQRGL VGEIIKRFEQ KGFRLVAMKF LRASEEHLKQ    50
    HYIDLKDRPF FPGLVKYMNS GPVVAMVWEG LNVVKTGRVM LGETNPADSK 100
    PGTIRGDFCI QVGRNIIHGS DSVKSAEKEI SLWFKPEELV DYKSCAHDWV 150
    YE 152
    Length:152
    Mass (Da):17,298
    Last modified:August 1, 1991 - v1
    Checksum:i1A5C3F84D7AD272C
    GO
    Isoform 3 (identifier: P22392-2) [UniParc]FASTAAdd to Basket

    Also known as: NM23-LV

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

    Note: Based on a naturally occurring readthrough transcript which produces an NME1-NME2 fusion protein. Initiator Met-1 is removed (By similarity). Contains a N-acetylalanine at position 2 (By similarity).By similarity

    Show »
    Length:267
    Mass (Da):30,137
    Checksum:i3AB02272AF24AAC3
    GO

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 11M → MANCERTFIAIKPDGVQRGL VGEIIKRFEQKGFRLVGLKF MQASEDLLKEHYVDLKDRPF FAGLVKYMHSGPVVAMVWEG LNVVKTGRVMLGETNPADSK PGTIRGDFCIQVGRTM in isoform 3. 2 PublicationsVSP_036708

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X58965 mRNA. Translation: CAB37870.1.
    M36981 mRNA. Translation: AAA36369.1.
    L16785 mRNA. Translation: AAA60228.1.
    DQ109675 mRNA. Translation: AAZ82097.1.
    AC005839 Genomic DNA. No translation available.
    BC002476 mRNA. Translation: AAH02476.1.
    BC133029 mRNA. Translation: AAI33030.1.
    BC133031 mRNA. Translation: AAI33032.1.
    U29200 Genomic DNA. Translation: AAA86745.1.
    CCDSiCCDS11580.1. [P22392-1]
    PIRiA49798.
    RefSeqiNP_001018146.1. NM_001018136.2. [P22392-2]
    NP_001018147.1. NM_001018137.2. [P22392-1]
    NP_001018148.1. NM_001018138.1. [P22392-1]
    NP_001018149.1. NM_001018139.2. [P22392-1]
    NP_002503.1. NM_002512.3. [P22392-1]
    UniGeneiHs.463456.

    Genome annotation databases

    EnsembliENST00000393193; ENSP00000376889; ENSG00000011052. [P22392-2]
    GeneIDi4831.
    654364.
    KEGGihsa:4831.
    hsa:654364.
    UCSCiuc002itj.3. human. [P22392-2]
    uc002itl.3. human. [P22392-1]

    Polymorphism databases

    DMDMi127983.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X58965 mRNA. Translation: CAB37870.1 .
    M36981 mRNA. Translation: AAA36369.1 .
    L16785 mRNA. Translation: AAA60228.1 .
    DQ109675 mRNA. Translation: AAZ82097.1 .
    AC005839 Genomic DNA. No translation available.
    BC002476 mRNA. Translation: AAH02476.1 .
    BC133029 mRNA. Translation: AAI33030.1 .
    BC133031 mRNA. Translation: AAI33032.1 .
    U29200 Genomic DNA. Translation: AAA86745.1 .
    CCDSi CCDS11580.1. [P22392-1 ]
    PIRi A49798.
    RefSeqi NP_001018146.1. NM_001018136.2. [P22392-2 ]
    NP_001018147.1. NM_001018137.2. [P22392-1 ]
    NP_001018148.1. NM_001018138.1. [P22392-1 ]
    NP_001018149.1. NM_001018139.2. [P22392-1 ]
    NP_002503.1. NM_002512.3. [P22392-1 ]
    UniGenei Hs.463456.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1NSK X-ray 2.80 L/N/O/R/T/U 1-152 [» ]
    1NUE X-ray 2.00 A/B/C/D/E/F 2-152 [» ]
    3BBB X-ray 1.30 A/B/C/D/E/F 2-152 [» ]
    3BBC X-ray 1.70 A/B/C/D/E/F 2-152 [» ]
    3BBF X-ray 1.70 A/B/C/D/E/F 2-152 [» ]
    ProteinModelPortali P22392.
    SMRi P22392. Positions 2-152.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 110895. 42 interactions.
    576341. 8 interactions.
    IntActi P22392. 18 interactions.
    MINTi MINT-1429922.
    STRINGi 9606.ENSP00000376886.

    Chemistry

    ChEMBLi CHEMBL2160.

    PTM databases

    PhosphoSitei P22392.

    Polymorphism databases

    DMDMi 127983.

    2D gel databases

    DOSAC-COBS-2DPAGE P22392.
    OGPi P22392.
    UCD-2DPAGE P22392.

    Proteomic databases

    MaxQBi P22392.
    PRIDEi P22392.

    Protocols and materials databases

    DNASUi 4831.
    654364.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000393193 ; ENSP00000376889 ; ENSG00000011052 . [P22392-2 ]
    GeneIDi 4831.
    654364.
    KEGGi hsa:4831.
    hsa:654364.
    UCSCi uc002itj.3. human. [P22392-2 ]
    uc002itl.3. human. [P22392-1 ]

    Organism-specific databases

    CTDi 4831.
    654364.
    GeneCardsi GC17P049242.
    HGNCi HGNC:7850. NME2.
    HPAi CAB002169.
    CAB040571.
    HPA008467.
    HPA041113.
    MIMi 156491. gene.
    neXtProti NX_P22392.
    PharmGKBi PA162398077.
    GenAtlasi Search...

    Phylogenomic databases

    HOGENOMi HOG000224564.
    HOVERGENi HBG000423.
    InParanoidi P22392.
    KOi K00940.
    OrthoDBi EOG7GJ6FG.
    PhylomeDBi P22392.
    TreeFami TF106373.

    Enzyme and pathway databases

    BioCyci MetaCyc:HS04463-MONOMER.
    Reactomei REACT_21330. Synthesis and interconversion of nucleotide di- and triphosphates.
    SignaLinki P22392.

    Miscellaneous databases

    ChiTaRSi NME2. human.
    EvolutionaryTracei P22392.
    GeneWikii NME1-NME2.
    NME2.
    NextBioi 18612.
    PROi P22392.
    SOURCEi Search...

    Gene expression databases

    Bgeei P22392.
    Genevestigatori P22392.

    Family and domain databases

    Gene3Di 3.30.70.141. 1 hit.
    HAMAPi MF_00451. NDP_kinase.
    InterProi IPR001564. Nucleoside_diP_kinase.
    IPR023005. Nucleoside_diP_kinase_AS.
    [Graphical view ]
    Pfami PF00334. NDK. 1 hit.
    [Graphical view ]
    PRINTSi PR01243. NUCDPKINASE.
    SMARTi SM00562. NDK. 1 hit.
    [Graphical view ]
    SUPFAMi SSF54919. SSF54919. 1 hit.
    PROSITEi PS00469. NDP_KINASES. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Identification of a second human nm23 gene, nm23-H2."
      Stahl J.A., Leone A., Rosengard A.M., Porter L., Liotta L.A., Steeg P.S., King C.R.
      Cancer Res. 51:445-449(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. "Nucleoside diphosphate kinase from human erythrocytes. Structural characterization of the two polypeptide chains responsible for heterogeneity of the hexameric enzyme."
      Gilles A.-M., Presecan E., Vonica A., Lascu I.
      J. Biol. Chem. 266:8784-8789(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE (ISOFORM 1), SUBUNIT, ACTIVE SITE.
    3. "Human c-myc transcription factor PuF identified as nm23-H2 nucleoside diphosphate kinase, a candidate suppressor of tumor metastasis."
      Postel E.H., Berberich S.J., Flint S.J., Ferrone C.A.
      Science 261:478-480(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    4. "Read-through transcript from NM23-H1 into the neighboring NM23-H2 gene encodes a novel protein, NM23-LV."
      Valentijn L.J., Koster J., Versteeg R.
      Genomics 87:483-489(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
      Tissue: Neuroblastoma.
    5. "DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
      Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L.
      , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
      Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [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] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
      Tissue: Eye.
    7. "Characterization of the human nm23-H2 promoter region and localization of the microsatellite D17S396."
      Seifert M., Seib T., Engel M., Dooley S., Welter C.
      Biochem. Biophys. Res. Commun. 215:910-914(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-18.
    8. "Integrin cytoplasmic domain-associated protein 1alpha (ICAP-1alpha) interacts directly with the metastasis suppressor nm23-H2, and both proteins are targeted to newly formed cell adhesion sites upon integrin engagement."
      Fournier H.N., Dupe-Manet S., Bouvard D., Lacombe M.L., Marie C., Block M.R., Albiges-Rizo C.
      J. Biol. Chem. 277:20895-20902(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ITGB1BP1, SUBCELLULAR LOCATION.
    9. "Lbc proto-oncogene product binds to and could be negatively regulated by metastasis suppressor nm23-H2."
      Iwashita S., Fujii M., Mukai H., Ono Y., Miyamoto M.
      Biochem. Biophys. Res. Commun. 320:1063-1068(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH AKAP13.
    10. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [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].
    11. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-128, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. "Reversible histidine phosphorylation in mammalian cells: a teeter-totter formed by nucleoside diphosphate kinase and protein histidine phosphatase 1."
      Wieland T., Hippe H.J., Ludwig K., Zhou X.B., Korth M., Klumpp S.
      Methods Enzymol. 471:379-402(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS HISTIDINE PROTEIN KINASE.
    13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. "The crystal structure of a human nucleoside diphosphate kinase, NM23-H2."
      Webb P.A., Perisic O., Mendola C.E., Backer J.M., Williams R.L.
      J. Mol. Biol. 251:574-587(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
    15. "X-ray structure of human nucleoside diphosphate kinase B complexed with GDP at 2-A resolution."
      Morera S., Lacombe M.-L., Xu Y., Lebras G., Janin J.
      Structure 3:1307-1314(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2 ANGSTROMS).

    Entry informationi

    Entry nameiNDKB_HUMAN
    AccessioniPrimary (citable) accession number: P22392
    Secondary accession number(s): A8MWA3, Q1WM23, Q6LCT6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1991
    Last sequence update: August 1, 1991
    Last modified: October 1, 2014
    This is version 177 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, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 17
      Human chromosome 17: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3