NmR-K 2
NRK 2
EC 2.7.1.22
Ribosylnicotinamide kinase 2
RNK 2
Nicotinic acid riboside kinase 2
EC 2.7.1.n4
Ribosylnicotinic acid kinase 2
Integrin beta-1-binding protein 3
Muscle integrin-binding protein
MIBP

Gene name

	Name:	ITGB1BP3
	Synonyms:	NRK2

From

Homo sapiens (Human)

[TaxID: 9606]

Taxonomy

Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.

Protein existence

1: Evidence at protein level;

References

[1]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, TISSUE SPECIFICITY, AND INTERACTION WITH ITGB1. TISSUE=Heart; DOI=10.1083/jcb.147.7.1391; PubMed=10613898 [NCBI, ExPASy, EBI, Israel, Japan] Li J., Mayne R., Wu C.; "A novel muscle-specific beta 1 integrin binding protein (MIBP) that modulates myogenic differentiation."; J. Cell Biol. 147:1391-1398(1999).
[2]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND FUNCTION. DOI=10.1016/S0092-8674(04)00416-7; PubMed=15137942 [NCBI, ExPASy, EBI, Israel, Japan] Bieganowski P., Brenner C.; "Discoveries of nicotinamide riboside as a nutrient and conserved NRK genes establish a Preiss-Handler independent route to NAD+ in fungi and humans."; Cell 117:495-502(2004).
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). The European IMAGE consortium; Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
[4]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). TISSUE=Teratocarcinoma; DOI=10.1038/ng1285; PubMed=14702039 [NCBI, ExPASy, EBI, Israel, Japan] Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.; "Complete sequencing and characterization of 21,243 full-length human cDNAs."; Nat. Genet. 36:40-45(2004).
[5]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). TISSUE=Liver; DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] The MGC Project Team; "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."; Genome Res. 14:2121-2127(2004).
[6]	INTERACTION WITH INTEGRIN ALPHA-7/BETA-1. DOI=10.1016/S0012-1606(03)00304-X; PubMed=12941630 [NCBI, ExPASy, EBI, Israel, Japan] Li J., Rao H., Burkin D., Kaufman S.J., Wu C.; "The muscle integrin binding protein (MIBP) interacts with alpha7beta1 integrin and regulates cell adhesion and laminin matrix deposition."; Dev. Biol. 261:209-219(2003).
[7]	SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF ASP-35 AND GLU-100. DOI=10.1371/journal.pbio.0050263; PubMed=17914902 [NCBI, ExPASy, EBI, Israel, Japan] Tempel W., Rabeh W.M., Bogan K.L., Belenky P., Wojcik M., Seidle H.F., Nedyalkova L., Yang T., Sauve A.A., Park H.-W., Brenner C.; "Nicotinamide riboside kinase structures reveal new pathways to NAD+."; PLoS Biol. 5:2220-2230(2007).

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.
CATALYTIC ACTIVITY: ATP + N-ribosylnicotinamide = ADP + nicotinamide ribonucleotide.
CATALYTIC ACTIVITY: ATP + D-ribosylnicotinate = ADP + nicotinate D-ribonucleotide.

BIOPHYSICOCHEMICAL PROPERTIES:

Kinetic parameters:	K_M=0.19 mM for nicotinamide riboside (with ATP as cosubstrate);
	K_M=30 mM for nicotinamide riboside (with GTP as cosubstrate);
	K_M=0.11 mM for tiazofurin (with ATP as cosubstrate);
	K_M=0.063 mM for nicotinic acid riboside (with ATP as cosubstrate);
	K_M=1.3 mM for uridine (with ATP as cosubstrate);

PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis .
SUBUNIT: Monomer (By similarity). Interacts with ITGB1 alone or when associated with alpha-7, but not with alpha-5.
INTERACTION:
Q9Y561:LRP12; NbExp=1; IntAct=EBI-514059, EBI-296693;
ALTERNATIVE PRODUCTS: 2 named isoforms [FASTA] produced by alternative splicing.

Name 1

Isoform ID Q9NPI5-1

This is the isoform sequence displayed in this entry.

Name 2

Isoform ID Q9NPI5-2

Features which should be applied to build the isoform sequence: VSP_012677.
TISSUE SPECIFICITY: Predominantly expressed in skeletal muscle and, at a much lower level, in the heart (at protein level). No expression in brain, kidney, liver, lung, pancreas nor placenta.
INDUCTION: Down-regulated during myoblast differentiation (By similarity).
SIMILARITY: Belongs to the uridine kinase family. NRK subfamily.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

AF190819; AAF26711.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AY611481; AAT11929.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AL365377; CAB96949.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AK001663; BAA91820.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AK022514; BAB14071.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC093637; AAH93637.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC101575; AAI01576.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_733778.1; -.

UniGene

Hs.135458

3D structure databases

ModBase

Q9NPI5.

Protein-protein interaction databases

IntAct

Q9NPI5; -.

Organism-specific databases

H-InvDB

HIX0014649; -.

HGNC

HGNC:17871; ITGB1BP3.

GenAtlas

ITGB1BP3.

MIM

608705; gene. [NCBI / EBI]

PharmGKB

PA134938442; -.

GeneCards

Q9NPI5.

Gene expression databases

ArrayExpress

Q9NPI5; -.

CleanEx

HS_ITGB1BP3; -.

GermOnline

ENSG00000077009; Homo sapiens.

Ontologies

GO:0005515;	Molecular function: protein binding (inferred from physical interaction from IntAct).
QuickGo view.

Family and domain databases

Genome annotation databases

Ensembl

ENSG00000077009; Homo sapiens. [Contig view]

GeneID

27231; -.

KEGG

hsa:27231; -.

NMPDR

fig|9606.3.peg.15403; -.

Phylogenomic databases

HOGENOM

Q9NPI5; -.

HOVERGEN

Q9NPI5; -.

Other

NextBio

50087; -.

SOURCE

ITGB1BP3; Homo sapiens.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Alternative splicing; ATP-binding; Kinase; Magnesium; Metal-binding; Nucleotide-binding; Polymorphism; Pyridine nucleotide biosynthesis; Transferase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 230`	`230`	`Nicotinamide riboside kinase 2.`	`PRO_0000215894`
`NP_BIND`	`9 17`	`9`	`ATP (By similarity).`
`ACT_SITE`	`35 35`		`Proton acceptor (By similarity).`
`METAL`	`16 16`		`Magnesium (By similarity).`
`METAL`	`35 35`		`Magnesium (By similarity).`
`BINDING`	`55 55`		`Substrate (By similarity).`
`BINDING`	`130 130`		`ATP (By similarity).`
`BINDING`	`131 131`		`Substrate (By similarity).`
`BINDING`	`134 134`		`ATP (By similarity).`
`VAR_SEQ`	`110 153`		`Missing (in isoform 2).`	`VSP_012677`
`VARIANT`	`178 178`	`1`	`E -> K (in dbSNP:rs16992131 [NCBI]).`	`VAR_024549`
`MUTAGEN`	`35 35`		`D->A: Loss of activity.`
`MUTAGEN`	`100 100`		`E->A: Loss of activity.`

Sequence information

Length: 230 AA [This is the length of the unprocessed precursor]

Molecular weight: 26046 Da [This is the MW of the unprocessed precursor]

CRC64: 27F8275A596758E7 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MKLIVGIGGM TNGGKTTLTN SLLRALPNCC VIHQDDFFKP QDQIAVGEDG FKQWDVLESL 

        70         80         90        100        110        120 
DMEAMLDTVQ AWLSSPQKFA RAHGVSVQPE ASDTHILLLE GFLLYSYKPL VDLYSRRYFL 

       130        140        150        160        170        180 
TVPYEECKWR RSTRNYTVPD PPGLFDGHVW PMYQKYRQEM EANGVEVVYL DGMKSREELF 

       190        200        210        220        230 
REVLEDIQNS LLNRSQESAP SPARPARTQG PGRGCGHRTA RPAASQQDSM

Q9NPI5 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools