Reviewed, UniProtKB/Swiss-Prot P19804 (NDKB_RAT)

Names and origin

Protein names

Recommended name:
    Nucleoside diphosphate kinase B
      Short name=NDP kinase B
      Short name=NDK B
    EC=2.7.4.6
Alternative name(s):
    P18

Gene names

Name:

Nme2

Organism

Rattus norvegicus (Rat)

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	152 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	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 By similarity.
Catalytic activity	ATP + nucleoside diphosphate = ADP + nucleoside triphosphate.
Cofactor	Magnesium By similarity.
Subunit structure	Hexamer of two different chains: A and B (A6, A5B, A4B2, A3B3, A2B4, AB5, B6). Interacts with AKAP13 and CAPN8 By similarity.
Subcellular location	Cytoplasm. Cell membrane.
Post-translational modification	The N-terminus is blocked.
Sequence similarities	Belongs to the NDK family.

Ontologies

Keywords
Biological process	Nucleotide metabolism
Cellular component	Cell membrane Cytoplasm Membrane
Ligand	ATP-binding Magnesium Metal-binding Nucleotide-binding
Molecular function	Kinase Transferase
PTM	Acetylation Phosphoprotein
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	CTP biosynthetic process Inferred from electronic annotation. Source: InterPro GTP biosynthetic process Inferred from electronic annotation. Source: InterPro UTP biosynthetic process Inferred from electronic annotation. Source: InterPro negative regulation of apoptosis Inferred from sequence or structural similarity. Source: HGNC negative regulation of myeloid leukocyte differentiation Inferred from direct assay. Source: RGD nucleoside diphosphate phosphorylation Inferred from direct assay. Source: RGD positive regulation of cAMP biosynthetic process Inferred from mutant phenotype. Source: RGD positive regulation of epithelial cell proliferation Inferred from sequence or structural similarity. Source: HGNC positive regulation of keratinocyte differentiation Inferred from sequence or structural similarity. Source: HGNC
Cellular component	lamellipodium Inferred from sequence or structural similarity. Source: HGNC perinuclear region of cytoplasm Inferred from direct assay. Source: RGD plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell ruffle Inferred from sequence or structural similarity. Source: HGNC
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW nucleoside diphosphate kinase activity Inferred from direct assay. Source: RGD
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 152	152	Nucleoside diphosphate kinase B		PRO_0000137119
Regions
	Region	1 – 66	66	Interaction with AKAP13 By similarity
Sites
	Active site	118	1	Pros-phosphohistidine intermediate By similarity
	Binding site	12	1	ATP By similarity
	Binding site	60	1	ATP By similarity
	Binding site	88	1	ATP By similarity
	Binding site	94	1	ATP By similarity
	Binding site	105	1	ATP By similarity
	Binding site	115	1	ATP By similarity
Amino acid modifications
	Modified residue	12	1	N6-acetyllysine By similarity
	Modified residue	49	1	N6-acetyllysine By similarity
	Modified residue	52	1	Phosphotyrosine By similarity
	Modified residue	56	1	N6-acetyllysine By similarity
	Modified residue	85	1	N6-acetyllysine By similarity
	Modified residue	94	1	Phosphothreonine By similarity
	Modified residue	100	1	N6-acetyllysine By similarity
	Modified residue	128	1	N6-acetyllysine By similarity
Experimental info
	Sequence conflict	89	1	V → W in AAA42017. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	P19804-1 [UniParc]. Last modified February 1, 1991. Version 1. Checksum: 1A5C3F84C1F413EC	FASTA	152	17,283
	10 20 30 40 50 60 MANLERTFIA IKPDGVQRGL VGEIIKRFEQ KGFRLVAMKF LRASEEHLKQ HYIDLKDRPF 70 80 90 100 110 120 FPGLVKYMNS GPVVAMVWEG LNVVKTGRVM LGETNPADSK PGTIRGDFCI QVGRNIIHGS 130 140 150 DSVESAEKEI GLWFKPEELI DYKSCAHDWV YE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 2168422] [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: 1321145] [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: 1316151] [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: 15489334] [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, MASS SPECTROMETRY. Strain: Sprague-Dawley. Tissue: Brain and Spinal cord.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	M55331 mRNA. Translation: AAA41684.1. M91597 mRNA. Translation: AAA42017.1. BC086599 mRNA. Translation: AAH86599.1.
IPI	IPI00325189.
PIR	A38369. A41849.
RefSeq	NP_114021.2.
UniGene	Rn.927
3D structure databases
HSSP	HSSP built from PDB template 1NUE based on UniProtKB P22392.
SMR	P19804. Positions 2-152.
ModBase	Search...
Protein-protein interaction databases
STRING	P19804.
PTM databases
PhosphoSite	P19804.
Proteomic databases
PRIDE	P19804.
Genome annotation databases
Ensembl	ENSRNOT00000003611; ENSRNOP00000003611; ENSRNOG00000002671; Rattus norvegicus. [Genome view]
GeneID	83782.
KEGG	rno:83782.
NMPDR	fig|10116.3.peg.5894.
UCSC	NM_031833. rat.
Organism-specific databases
CTD	83782.
RGD	619877. Nme2.
Phylogenomic databases
HOVERGEN	P19804.
OMA	YERIDEP.
Enzyme and pathway databases
BRENDA	2.7.4.6. 248.
Gene expression databases
ArrayExpress	P19804.
Genevestigator	P19804.
GermOnline	ENSRNOG00000002671. Rattus norvegicus.
Family and domain databases
InterPro	IPR001564. Nuc_diP_kinase_core. [Graphical view]
Gene3D	G3DSA:3.30.70.141. NDK. 1 hit.
PANTHER	PTHR11349. Nuc_diP_kinase_core. 1 hit.
Pfam	PF00334. NDK. 1 hit. [Graphical view]
PRINTS	PR01243. NUCDPKINASE.
ProDom	PD001018. NDK. 1 hit. [Graphical view] [Entries sharing at least one domain]
SMART	SM00562. NDK. 1 hit. [Graphical view]
PROSITE	PS00469. NDP_KINASES. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	616343.

Entry information

Entry name

NDKB_RAT

Accession

Primary (citable) accession number: P19804

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1991
Last sequence update:	February 1, 1991
Last modified:	November 3, 2009
This is version 91 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)