Q9D7C9 (NRK2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Nicotinamide riboside kinase 2
Short name=NRK 2
Short name=NmR-K 2
EC=2.7.1.22

Alternative name(s):
Integrin beta-1-binding protein 3
Muscle integrin-binding protein
Short name=MIBP
Nicotinic acid riboside kinase 2
EC=2.7.1.n4
Ribosylnicotinamide kinase 2
Short name=RNK 2
Ribosylnicotinic acid kinase 2

Gene names

Name:	Itgb1bp3
Synonyms:	Nrk2

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	195 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the phosphorylation of nicotinamide riboside (NR) and nicotinic acid riboside (NaR) to form nicotinamide mononucleotide (NMN) and nicotinic acid mononucleotide (NaMN). Reduces laminin matrix deposition and cell adhesion to laminin, but not to fibronectin. Involved in the regulation of PXN at the protein level and of PXN tyrosine phosphorylation. May play a role in the regulation of terminal myogenesis By similarity. Ref.3
Catalytic activity	ATP + N-ribosylnicotinamide = ADP + nicotinamide ribonucleotide. ATP + D-ribosylnicotinate = ADP + nicotinate D-ribonucleotide.
Pathway	Cofactor biosynthesis; NAD(+) biosynthesis.
Subunit structure	Monomer By similarity. Interacts with ITGB1 alone or when associated with alpha-7, but not with alpha-5.
Tissue specificity	Expressed in skeletal muscle (at protein level). Ref.3
Induction	Down-regulated during myoblast differentiation. Ref.3
Sequence similarities	Belongs to the uridine kinase family. NRK subfamily.

Ontologies

Keywords
Biological process	Pyridine nucleotide biosynthesis
Ligand	ATP-binding Magnesium Metal-binding Nucleotide-binding
Molecular function	Kinase Transferase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	negative regulation of myoblast differentiation Inferred from direct assay Ref.3. Source: MGI pyridine nucleotide biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	intracellular Inferred from physical interaction Ref.3. Source: MGI
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW protein binding Inferred from physical interaction Ref.3. Source: MGI ribosylnicotinamide 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 – 195	195	Nicotinamide riboside kinase 2		PRO_0000215895
Regions
	Nucleotide binding	9 – 17	9	ATP By similarity
Sites
	Active site	35	1	Proton acceptor By similarity
	Metal binding	16	1	Magnesium By similarity
	Metal binding	35	1	Magnesium By similarity
	Binding site	55	1	Substrate By similarity
	Binding site	130	1	ATP By similarity
	Binding site	131	1	Substrate By similarity
	Binding site	134	1	ATP By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9D7C9 [UniParc]. Last modified June 1, 2001. Version 1. Checksum: 83B0FB3F52738455	FASTA	195	22,375
	10 20 30 40 50 60 MKLIIGIGGV TNGGKTTLTN SLLKALPNCC VIHQDDFFKP QDQIAVGEDG FKQWDVLESL 70 80 90 100 110 120 DMETMLSTVQ AWVKDPHKFA RAHGVSLQSG ASDTHVLLLE GFLLYSYRPL VDLYSQRYFL 130 140 150 160 170 180 TVPYEECKRR RRSRTYMVPD PPGLFDGHVW PMYQKYRREM EQDGVEVVYL DGMKSPEGLF 190 HQVLEDIQNR LLNTS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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: Bone and Tongue.
[2]	"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.
[3]	"A novel muscle-specific beta 1 integrin binding protein (MIBP) that modulates myogenic differentiation." Li J., Mayne R., Wu C. J. Cell Biol. 147:1391-1398(1999) [PubMed: 10613898] [Abstract] Cited for: FUNCTION, TISSUE SPECIFICITY, INDUCTION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AK009352 mRNA. Translation: BAB26235.1. AK137483 mRNA. Translation: BAE23375.1. BC119244 mRNA. Translation: AAI19245.1. BC119246 mRNA. Translation: AAI19247.1.
IPI	IPI00110162.
RefSeq	NP_081396.1. NM_027120.2.
UniGene	Mm.437211.
3D structure databases
ProteinModelPortal	Q9D7C9.
SMR	Q9D7C9. Positions 2-191.
ModBase	Search...
Protein-protein interaction databases
STRING	Q9D7C9.
Proteomic databases
PRIDE	Q9D7C9.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000005069; ENSMUSP00000005069; ENSMUSG00000004939.
GeneID	69564.
KEGG	mmu:69564.
NMPDR	fig|10090.3.peg.14097.
UCSC	uc007ggn.1. mouse.
Organism-specific databases
CTD	27231.
MGI	MGI:1916814. Itgb1bp3.
Phylogenomic databases
GeneTree	ENSGT00510000046782.
HOGENOM	HBG444823.
HOVERGEN	HBG052669.
InParanoid	Q9D7C9.
OMA	RALPNCC.
OrthoDB	EOG4868DH.
PhylomeDB	Q9D7C9.
Gene expression databases
ArrayExpress	Q9D7C9.
Bgee	Q9D7C9.
CleanEx	MM_ITGB1BP3.
Genevestigator	Q9D7C9.
GermOnline	ENSMUSG00000004939. Mus musculus.
Family and domain databases
KO	K10524.
ProtoNet	Search...
Other
NextBio	329790.
SOURCE	Search...

Entry information

Entry name

NRK2_MOUSE

Accession

Primary (citable) accession number: Q9D7C9
Secondary accession number(s): Q0VEG2, Q3UV96

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 19, 2004
Last sequence update:	June 1, 2001
Last modified:	November 16, 2011
This is version 64 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program