Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Nucleoside diphosphate kinase B

Gene

NME2

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

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

Mg2+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

  • ATP binding Source: UniProtKB-KW
  • DNA binding Source: UniProtKB-KW
  • metal ion binding Source: UniProtKB-KW
  • nucleoside diphosphate kinase activity Source: UniProtKB
  • protein histidine kinase activity Source: UniProtKB-EC
  • sequence-specific DNA binding transcription factor activity Source: UniProtKB

GO - Biological processi

  • activation of mitophagy in response to mitochondrial depolarization Source: ParkinsonsUK-UCL
  • cell adhesion Source: HGNC
  • CTP biosynthetic process Source: InterPro
  • GTP biosynthetic process Source: InterPro
  • integrin-mediated signaling pathway Source: UniProtKB
  • negative regulation of apoptotic process Source: HGNC
  • nucleobase-containing small molecule interconversion Source: Reactome
  • nucleobase-containing small molecule metabolic process Source: Reactome
  • nucleoside triphosphate biosynthetic process Source: UniProtKB
  • positive regulation of epithelial cell proliferation Source: HGNC
  • positive regulation of keratinocyte differentiation Source: HGNC
  • positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  • purine nucleotide metabolic process Source: GO_Central
  • pyrimidine nucleotide metabolic process Source: GO_Central
  • regulation of epidermis development Source: HGNC
  • regulation of transcription, DNA-templated Source: UniProtKB
  • small molecule metabolic process Source: Reactome
  • transcription, DNA-templated Source: UniProtKB-KW
  • UTP biosynthetic process Source: InterPro
Complete GO annotation...

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 Componenti: 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

  • cell periphery Source: UniProtKB
  • cytoplasm Source: UniProtKB
  • cytosol Source: GO_Central
  • extracellular exosome Source: UniProtKB
  • intracellular Source: GO_Central
  • lamellipodium Source: HGNC
  • nucleus Source: UniProtKB
  • ruffle Source: HGNC
Complete GO annotation...

Keywords - Cellular componenti

Cell projection, Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA162398077.

Chemistry

DrugBankiDB00718. Adefovir Dipivoxil.
DB00709. Lamivudine.
DB00300. Tenofovir.

Polymorphism and mutation databases

BioMutaiNME2.
DMDMi127983.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 152152Nucleoside diphosphate kinase BPRO_0000137117Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
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.
ExpressionAtlasiP22392. baseline.
GenevisibleiP22392. HS.

Organism-specific databases

HPAiCAB002169.
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. 53 interactions.
576341. 8 interactions.
DIPiDIP-50179N.
IntActiP22392. 18 interactions.
MINTiMINT-1429922.
STRINGi9606.ENSP00000376889.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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
Regioni1 – 6666Interaction with AKAP13Add
BLAST

Sequence similaritiesi

Belongs to the NDK family.Curated

Phylogenomic databases

GeneTreeiENSGT00760000119146.
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.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

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

        10         20         30         40         50
MANLERTFIA IKPDGVQRGL VGEIIKRFEQ KGFRLVAMKF LRASEEHLKQ
60 70 80 90 100
HYIDLKDRPF FPGLVKYMNS GPVVAMVWEG LNVVKTGRVM LGETNPADSK
110 120 130 140 150
PGTIRGDFCI QVGRNIIHGS DSVKSAEKEI SLWFKPEELV DYKSCAHDWV

YE
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 similarity1 Publication
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:
EMBLi
GenBanki
DDBJi
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]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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...

Protein-protein interaction databases

BioGridi110895. 53 interactions.
576341. 8 interactions.
DIPiDIP-50179N.
IntActiP22392. 18 interactions.
MINTiMINT-1429922.
STRINGi9606.ENSP00000376889.

Chemistry

ChEMBLiCHEMBL2160.
DrugBankiDB00718. Adefovir Dipivoxil.
DB00709. Lamivudine.
DB00300. Tenofovir.

PTM databases

PhosphoSiteiP22392.

Polymorphism and mutation databases

BioMutaiNME2.
DMDMi127983.

2D gel databases

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

Proteomic databases

MaxQBiP22392.
PRIDEiP22392.

Protocols and materials databases

DNASUi4831.
654364.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi4831.
654364.
GeneCardsiGC17P049230.
GC17P049242.
HGNCiHGNC:7850. NME2.
HPAiCAB002169.
HPA041113.
MIMi156491. gene.
neXtProtiNX_P22392.
PharmGKBiPA162398077.
GenAtlasiSearch...

Phylogenomic databases

GeneTreeiENSGT00760000119146.
HOGENOMiHOG000224564.
HOVERGENiHBG000423.
InParanoidiP22392.
KOiK00940.
OrthoDBiEOG7GJ6FG.
PhylomeDBiP22392.
TreeFamiTF106373.

Enzyme and pathway databases

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

Miscellaneous databases

ChiTaRSiNME2. human.
EvolutionaryTraceiP22392.
GeneWikiiNME1-NME2.
NME2.
NextBioi18612.
PROiP22392.
SOURCEiSearch...

Gene expression databases

BgeeiP22392.
ExpressionAtlasiP22392. baseline.
GenevisibleiP22392. HS.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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 (ISOFORM 3), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS] (ISOFORM 3).
  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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  16. "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).
  17. "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: June 24, 2015
This is version 185 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

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.