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
Rattus norvegicus (Rat)
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. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate. Negatively regulates Rho activity by interacting with AKAP13/LBC. Exhibits histidine protein kinase activity (By similarity).By similarity

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 – 121ATPBy similarity
Binding sitei60 – 601ATPBy similarity
Binding sitei88 – 881ATPBy similarity
Binding sitei94 – 941ATPBy similarity
Binding sitei105 – 1051ATPBy similarity
Binding sitei115 – 1151ATPBy similarity
Active sitei118 – 1181Pros-phosphohistidine intermediateBy similarity

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • drug binding Source: RGD
  • enzyme binding Source: RGD
  • fatty acid binding Source: RGD
  • intermediate filament binding Source: RGD
  • metal ion binding Source: UniProtKB-KW
  • nucleoside diphosphate kinase activity Source: RGD
  • protein histidine kinase activity Source: UniProtKB-EC
  • protein serine/threonine kinase activity Source: RGD

GO - Biological processi

  • cellular response to fatty acid Source: RGD
  • cellular response to glucose stimulus Source: RGD
  • cellular response to oxidative stress Source: RGD
  • CTP biosynthetic process Source: RGD
  • GTP biosynthetic process Source: RGD
  • integrin-mediated signaling pathway Source: UniProtKB
  • negative regulation of apoptotic process Source: HGNC
  • negative regulation of myeloid leukocyte differentiation Source: RGD
  • nucleoside diphosphate phosphorylation Source: RGD
  • positive regulation of cAMP biosynthetic process Source: RGD
  • positive regulation of epithelial cell proliferation Source: HGNC
  • positive regulation of keratinocyte differentiation Source: HGNC
  • positive regulation of neuron projection development Source: RGD
  • positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  • protein autophosphorylation Source: RGD
  • protein oligomerization Source: RGD
  • regulation of epidermis development Source: HGNC
  • response to growth hormone Source: RGD
  • UTP biosynthetic process Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Biological processi

Nucleotide metabolism

Keywords - Ligandi

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

Enzyme and pathway databases

SABIO-RKP19804.

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):
Histidine protein kinase NDKB (EC:2.7.13.3)
P18
Gene namesi
Name:Nme2
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 10

Organism-specific databases

RGDi619877. Nme2.

Subcellular locationi

  • Cytoplasm By similarity
  • Nucleus By similarity
  • Cell projectionlamellipodium By similarity
  • Cell projectionruffle By similarity

  • Note: 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.By similarity

GO - Cellular componenti

  • cell periphery Source: UniProtKB
  • cytoplasm Source: UniProtKB
  • lamellipodium Source: HGNC
  • mitochondrial membrane Source: RGD
  • nucleus Source: UniProtKB-SubCell
  • perinuclear region of cytoplasm Source: RGD
  • ruffle Source: HGNC
Complete GO annotation...

Keywords - Cellular componenti

Cell projection, Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 152152Nucleoside diphosphate kinase BPRO_0000137119Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei128 – 1281N6-acetyllysineBy similarity

Post-translational modificationi

The N-terminus is blocked.

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiP19804.
PRIDEiP19804.

2D gel databases

World-2DPAGE0004:P19804.

PTM databases

iPTMnetiP19804.
PhosphoSiteiP19804.
SwissPalmiP19804.

Expressioni

Gene expression databases

GenevisibleiP19804. RN.

Interactioni

Subunit structurei

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

GO - Molecular functioni

  • enzyme binding Source: RGD
  • intermediate filament binding Source: RGD

Protein-protein interaction databases

BioGridi249827. 4 interactions.
IntActiP19804. 1 interaction.
MINTiMINT-233154.
STRINGi10116.ENSRNOP00000003611.

Structurei

3D structure databases

ProteinModelPortaliP19804.
SMRiP19804. Positions 2-152.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 6666Interaction with AKAP13By similarityAdd
BLAST

Sequence similaritiesi

Belongs to the NDK family.Curated

Phylogenomic databases

eggNOGiKOG0888. Eukaryota.
COG0105. LUCA.
GeneTreeiENSGT00760000119146.
HOGENOMiHOG000224564.
HOVERGENiHBG000423.
InParanoidiP19804.
KOiK00940.
OMAiENELVDW.
OrthoDBiEOG7GJ6FG.
PhylomeDBiP19804.
TreeFamiTF106373.

Family and domain databases

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]
PROSITEiPS00469. NDP_KINASES. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P19804-1 [UniParc]FASTAAdd to basket

« 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 DSVESAEKEI GLWFKPEELI DYKSCAHDWV

YE
Length:152
Mass (Da):17,283
Last modified:February 1, 1991 - v1
Checksum:i1A5C3F84C1F413EC
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti89 – 891V → W in AAA42017 (PubMed:1316151).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M55331 mRNA. Translation: AAA41684.1.
M91597 mRNA. Translation: AAA42017.1.
BC086599 mRNA. Translation: AAH86599.1.
PIRiA41849. A38369.
RefSeqiNP_114021.2. NM_031833.2.
UniGeneiRn.927.

Genome annotation databases

EnsembliENSRNOT00000003611; ENSRNOP00000003611; ENSRNOG00000002671.
GeneIDi83782.
KEGGirno:83782.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M55331 mRNA. Translation: AAA41684.1.
M91597 mRNA. Translation: AAA42017.1.
BC086599 mRNA. Translation: AAH86599.1.
PIRiA41849. A38369.
RefSeqiNP_114021.2. NM_031833.2.
UniGeneiRn.927.

3D structure databases

ProteinModelPortaliP19804.
SMRiP19804. Positions 2-152.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi249827. 4 interactions.
IntActiP19804. 1 interaction.
MINTiMINT-233154.
STRINGi10116.ENSRNOP00000003611.

PTM databases

iPTMnetiP19804.
PhosphoSiteiP19804.
SwissPalmiP19804.

2D gel databases

World-2DPAGE0004:P19804.

Proteomic databases

PaxDbiP19804.
PRIDEiP19804.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000003611; ENSRNOP00000003611; ENSRNOG00000002671.
GeneIDi83782.
KEGGirno:83782.

Organism-specific databases

CTDi4831.
RGDi619877. Nme2.

Phylogenomic databases

eggNOGiKOG0888. Eukaryota.
COG0105. LUCA.
GeneTreeiENSGT00760000119146.
HOGENOMiHOG000224564.
HOVERGENiHBG000423.
InParanoidiP19804.
KOiK00940.
OMAiENELVDW.
OrthoDBiEOG7GJ6FG.
PhylomeDBiP19804.
TreeFamiTF106373.

Enzyme and pathway databases

SABIO-RKP19804.

Miscellaneous databases

NextBioi616343.
PROiP19804.

Gene expression databases

GenevisibleiP19804. RN.

Family and domain databases

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]
PROSITEiPS00469. NDP_KINASES. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Isolation and characterization of a cDNA clone encoding rat nucleoside diphosphate kinase."
    Kimura N., Shimada N., Nomura K., Watanabe K.
    J. Biol. Chem. 265:15744-15749(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
    Strain: Wistar.
  2. "Isolation and characterization of a gene encoding rat nucleoside diphosphate kinase."
    Ishikawa N., Shimada N., Munakata Y., Watanabe K., Kimura N.
    J. Biol. Chem. 267:14366-14372(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "A cromoglycate binding protein from rat mast cells of a leukemia line is a nucleoside diphosphate kinase."
    Hemmerich S., Yarden Y., Pecht I.
    Biochemistry 31:4574-4579(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Sprague-Dawley.
    Tissue: Mast cell.
  4. "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].
    Tissue: Brain.
  5. Lubec G., Afjehi-Sadat L., Kang S.U.
    Submitted (JUL-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 7-26; 57-66; 89-114 AND 129-143, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: Sprague-Dawley.
    Tissue: Brain and Spinal cord.

Entry informationi

Entry nameiNDKB_RAT
AccessioniPrimary (citable) accession number: P19804
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: February 1, 1991
Last modified: May 11, 2016
This is version 149 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

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 one 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.