Reviewed, UniProtKB/Swiss-Prot Q9WV85 (NDK3_MOUSE)

Names and origin

Protein names

Recommended name:
    Nucleoside diphosphate kinase 3
      Short name=NDP kinase 3
      Short name=NDK 3
    EC=2.7.4.6
Alternative name(s):
    Nucleoside diphosphate kinase C
      Short name=NDPKC
    nm23-M3
    DR-nm23

Gene names

Name:

Nme3

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

Protein attributes

Sequence length	169 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at transcript 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. Probably has a role in normal hematopoiesis by inhibition of granulocyte differentiation and induction of apoptosis By similarity.
Catalytic activity	ATP + nucleoside diphosphate = ADP + nucleoside triphosphate.
Cofactor	Magnesium By similarity.
Sequence similarities	Belongs to the NDK family.

Ontologies

Keywords
Biological process	Nucleotide metabolism
Ligand	ATP-binding Magnesium Metal-binding Nucleotide-binding
Molecular function	Kinase Transferase
PTM	Phosphoprotein
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	mitochondrion Inferred from direct assay. Source: MGI
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 electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 169	169	Nucleoside diphosphate kinase 3		PRO_0000137124
Sites
	Active site	135	1	Pros-phosphohistidine intermediate By similarity
	Binding site	29	1	ATP By similarity
	Binding site	77	1	ATP By similarity
	Binding site	105	1	ATP By similarity
	Binding site	111	1	ATP By similarity
	Binding site	122	1	ATP By similarity
	Binding site	132	1	ATP By similarity
Experimental info
	Sequence conflict	97	1	G → W in AAD38976. Ref.1
	Sequence conflict	127	1	M → V in AAG02199. Ref.2
	Sequence conflict	127	1	M → V in AAG02201. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q9WV85-1 [UniParc]. Last modified November 9, 2004. Version 3. Checksum: 53223C0601A6467C	FASTA	169	19,099
	10 20 30 40 50 60 MICLVLTIFA NLFPSAYSGV NERTFLAVKP DGVQRRLVGE IVRRFERKGF KLVALKLVQA 70 80 90 100 110 120 SEELLREHYV ELREKPFYSR LVKYMSSGPV VAMVWQGLDV VHASRALIGA TDPGDAMPGT 130 140 150 160 IRGDFCMEVG KNVIHGSDSV ESAHREIALW FREAELLCWE DSAGHWLYE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	Mehus J.G., Lambeth D.O. Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Characterization of the nm23-M2, nm23-M3 and nm23-M4 mouse genes: comparison with their human orthologs." Masse K., Dabernat S., Bourbon P.-M., Larou M., Amrein L., Barraud P., Perel Y., Camara M., Landry M., Lacombe M.L., Daniel J.-Y. Gene 296:87-97(2002) [PubMed: 12383506] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
[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. Tissue: Pancreas.
[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/6J. Tissue: Thymus.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF153449 mRNA. Translation: AAD38976.1. AF288689 mRNA. Translation: AAG02199.1. AF288691 Genomic DNA. Translation: AAG02201.1. AK007399 mRNA. Translation: BAB25013.1. BC028503 mRNA. Translation: AAH28503.1.
IPI	IPI00125450.
RefSeq	NP_062704.2.
UniGene	Mm.430765
3D structure databases
HSSP	HSSP built from PDB template 1JXV based on UniProtKB P15531.
SMR	Q9WV85. Positions 18-169.
ModBase	Search...
Protein-protein interaction databases
STRING	Q9WV85.
PTM databases
PhosphoSite	Q9WV85.
Proteomic databases
PRIDE	Q9WV85.
Genome annotation databases
Ensembl	ENSMUST00000024978; ENSMUSP00000024978; ENSMUSG00000073435; Mus musculus. [Genome view]
GeneID	79059.
KEGG	mmu:79059.
NMPDR	fig|10090.3.peg.2356.
UCSC	uc008ayz.1. mouse.
Organism-specific databases
CTD	79059.
MGI	MGI:1930182. Nme3.
Phylogenomic databases
HOGENOM	Q9WV85.
HOVERGEN	Q9WV85.
OMA	RLVKYMS.
Enzyme and pathway databases
BRENDA	2.7.4.6. 244.
Gene expression databases
ArrayExpress	Q9WV85.
Bgee	Q9WV85.
CleanEx	MM_NME3.
Genevestigator	Q9WV85.
GermOnline	ENSMUSG00000073435. Mus musculus.
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	349845.
SOURCE	Search...

Entry information

Entry name

NDK3_MOUSE

Accession

Primary (citable) accession number: Q9WV85
Secondary accession number(s): Q9D931, Q9EPA2

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 11, 2001
Last sequence update:	November 9, 2004
Last modified:	November 3, 2009
This is version 73 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)