Q01768 (NDKB_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Nucleoside diphosphate kinase B
Short name=NDK B
Short name=NDP kinase B
EC=2.7.4.6

Alternative name(s):
Histidine protein kinase NDKB
EC=2.7.13.3
P18
nm23-M2

Gene names

Name:

Nme2

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	152 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
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. Exhibits histidine protein kinase activity By similarity. Ref.8
Catalytic activity	ATP + nucleoside diphosphate = ADP + nucleoside triphosphate. ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
Cofactor	Magnesium By similarity.
Subunit structure	Hexamer of two different chains: A and B (A6, A5B, A4B2, A3B3, A2B4, AB5, B6). Interacts with AKAP13 By similarity. Interacts with CAPN8. Ref.6
Subcellular location	Cytoplasm. Cell membrane.
Tissue specificity	Expressed in the base region of the oxyntic and pyloric mucosae. Ref.6
Disruption phenotype	Impaired activation of the K+ channel KCNN4, resulting in defective T cell activation. Ref.8
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	Complete proteome Direct protein sequencing Reference proteome
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
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW nucleoside diphosphate kinase activity Inferred from electronic annotation. Source: EC protein binding Inferred from physical interaction. Source: IntAct protein histidine kinase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Itgb1	P09055	3	EBI-642573,EBI-644224

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 152	151	Nucleoside diphosphate kinase B		PRO_0000137118
Regions
	Region	2 – 66	65	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	2	1	N-acetylalanine By similarity
	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 Ref.7
	Modified residue	100	1	N6-acetyllysine By similarity
	Modified residue	128	1	N6-acetyllysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q01768 [UniParc]. Last modified April 1, 1993. Version 1. Checksum: 1A5C3F84C1FFC83C	FASTA	152	17,363
	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 HLWFKPEELI DYKSCAHDWV YE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning and functional expression of the second mouse nm23/NDP kinase gene, nm23-M2." Urano T., Takamiya K., Furukawa K., Shiku H. FEBS Lett. 309:358-362(1992) [PubMed: 1325378] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: C57BL/6.
[2]	Takeshi U. Submitted (SEP-1992) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: C57BL/6.
[3]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J.
[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]. Strain: C57BL/6. Tissue: Brain and Heart.
[5]	Lubec G., Klug S., Kang S.U. Submitted (APR-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 7-26; 57-66 AND 89-143, MASS SPECTROMETRY. Strain: C57BL/6. Tissue: Brain and Hippocampus.
[6]	"Stomach-specific calpain, nCL-2, localizes in mucus cells and proteolyzes the beta-subunit of coatomer complex, beta-COP." Hata S., Koyama S., Kawahara H., Doi N., Maeda T., Toyama-Sorimachi N., Abe K., Suzuki K., Sorimachi H. J. Biol. Chem. 281:11214-11224(2006) [PubMed: 16476741] [Abstract] Cited for: INTERACTION WITH CAPN8, TISSUE SPECIFICITY.
[7]	"Solid tumor proteome and phosphoproteome analysis by high resolution mass spectrometry." Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J., Faessler R., Mann M. J. Proteome Res. 7:5314-5326(2008) [PubMed: 19367708] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-94, MASS SPECTROMETRY. Tissue: Melanoma.
[8]	"Nucleoside diphosphate kinase B knock-out mice have impaired activation of the K+ channel KCa3.1, resulting in defective T cell activation." Di L., Srivastava S., Zhdanova O., Sun Y., Li Z., Skolnik E.Y. J. Biol. Chem. 285:38765-38771(2010) [PubMed: 20884616] [Abstract] Cited for: FUNCTION, DISRUPTION PHENOTYPE.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X68193 mRNA. Translation: CAA48275.1. AK012447 mRNA. Translation: BAB28246.1. BC066995 mRNA. Translation: AAH66995.1. BC086892 mRNA. Translation: AAH86892.1. BC086893 mRNA. Translation: AAH86893.1.
IPI	IPI00127417.
PIR	S29241.
RefSeq	NP_001070997.1. NM_001077529.1. NP_032731.1. NM_008705.4.
UniGene	Mm.1260.
3D structure databases
ProteinModelPortal	Q01768.
SMR	Q01768. Positions 2-152.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q01768. 6 interactions.
STRING	Q01768.
PTM databases
PhosphoSite	Q01768.
2D gel databases
SWISS-2DPAGE	Q01768.
PMMA-2DPAGE	Q01768.
REPRODUCTION-2DPAGE	Q01768.
Proteomic databases
PRIDE	Q01768.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000021217; ENSMUSP00000021217; ENSMUSG00000020857. ENSMUST00000072566; ENSMUSP00000103476; ENSMUSG00000020857.
GeneID	18103.
KEGG	mmu:18103.
Organism-specific databases
CTD	4831.
MGI	MGI:97356. Nme2.
Phylogenomic databases
eggNOG	roNOG13226.
HOGENOM	HBG445152.
HOVERGEN	HBG000423.
InParanoid	Q01768.
OMA	AANCERT.
OrthoDB	EOG4S1T8G.
PhylomeDB	Q01768.
Gene expression databases
ArrayExpress	Q01768.
Bgee	Q01768.
Genevestigator	Q01768.
GermOnline	ENSMUSG00000020857. Mus musculus.
Family and domain databases
InterPro	IPR001564. Nucleoside_diP_kinase. IPR023005. Nucleoside_diP_kinase_AS. [Graphical view]
Gene3D	G3DSA:3.30.70.141. NDK. 1 hit.
KO	K00940.
PANTHER	PTHR11349. Nuc_diP_kinase_core. 1 hit.
Pfam	PF00334. NDK. 1 hit. [Graphical view]
PRINTS	PR01243. NUCDPKINASE.
SMART	SM00562. NDK. 1 hit. [Graphical view]
SUPFAM	SSF54919. NDK. 1 hit.
PROSITE	PS00469. NDP_KINASES. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	293275.
SOURCE	Search...

Entry information

Entry name

NDKB_MOUSE

Accession

Primary (citable) accession number: Q01768

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1993
Last sequence update:	April 1, 1993
Last modified:	November 16, 2011
This is version 104 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program