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Reviewed, UniProtKB/Swiss-Prot Q9NPI5 (NRK2_HUMAN)

Last modified November 3, 2009. Version 60. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Nicotinamide riboside kinase 2
      Short name=NmR-K 2
      Short name=NRK 2
    EC=2.7.1.22
Alternative name(s):
    Ribosylnicotinamide kinase 2
      Short name=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
      Short name=MIBP
Gene names
Name: ITGB1BP3
Synonyms: NRK2
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length230 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence 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. Ref.1 Ref.2

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

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. Ref.1

Induction

Down-regulated during myoblast differentiation By similarity.

Sequence similarities

Belongs to the uridine kinase family. NRK subfamily.

Biophysicochemical properties

Kinetic parameters:

KM=0.19 mM for nicotinamide riboside (with ATP as cosubstrate)

KM=30 mM for nicotinamide riboside (with GTP as cosubstrate)

KM=0.11 mM for tiazofurin (with ATP as cosubstrate)

KM=0.063 mM for nicotinic acid riboside (with ATP as cosubstrate)

KM=1.3 mM for uridine (with ATP as cosubstrate)

Binary interactions

With

Entry

#Exp.

IntAct

Notes

LRP12Q9Y5611EBI-514059,EBI-296693

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9NPI5-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q9NPI5-2)

The sequence of this isoform differs from the canonical sequence as follows:
     110-153: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 230230Nicotinamide riboside kinase 2
PRO_0000215894

Regions

Nucleotide binding9 – 179ATP By similarity

Sites

Active site351Proton acceptor By similarity
Metal binding161Magnesium By similarity
Metal binding351Magnesium By similarity
Binding site551Substrate By similarity
Binding site1301ATP By similarity
Binding site1311Substrate By similarity
Binding site1341ATP By similarity

Natural variations

Alternative sequence110 – 15344Missing in isoform 2.
VSP_012677
Natural variant1781E → K: dbSNP rs16992131.
VAR_024549

Experimental info

Mutagenesis351D → A: Loss of activity. Ref.7
Mutagenesis1001E → A: Loss of activity. Ref.7

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 27F8275A596758E7

FASTA23026,046
        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 

« Hide

Isoform 2.

Checksum: 8DE757FC52983F0F
Show »

FASTA18620,638

References

« Hide 'large scale' references
[1]"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: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, TISSUE SPECIFICITY, INTERACTION WITH ITGB1.
Tissue: Heart.
[2]"Discoveries of nicotinamide riboside as a nutrient and conserved NRK genes establish a Preiss-Handler independent route to NAD+ in fungi and humans."
Bieganowski P., Brenner C.
Cell 117:495-502(2004) [PubMed: 15137942] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION.
[3]The European IMAGE consortium
Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[4]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
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. expand/collapse author list , 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.
Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Teratocarcinoma.
[5]"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] (ISOFORM 1).
Tissue: Liver.
[6]"The muscle integrin binding protein (MIBP) interacts with alpha7beta1 integrin and regulates cell adhesion and laminin matrix deposition."
Li J., Rao H., Burkin D., Kaufman S.J., Wu C.
Dev. Biol. 261:209-219(2003) [PubMed: 12941630] [Abstract]
Cited for: INTERACTION WITH INTEGRIN ALPHA-7/BETA-1.
[7]"Nicotinamide riboside kinase structures reveal new pathways to NAD+."
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.
PLoS Biol. 5:2220-2230(2007) [PubMed: 17914902] [Abstract]
Cited for: SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF ASP-35 AND GLU-100.

Cross-references

Sequence databases

AF190819 mRNA. Translation: AAF26711.1.
AY611481 mRNA. Translation: AAT11929.1.
AL365377 mRNA. Translation: CAB96949.1.
AK001663 mRNA. Translation: BAA91820.1.
AK022514 mRNA. Translation: BAB14071.1.
BC093637 mRNA. Translation: AAH93637.1.
BC101575 mRNA. Translation: AAI01576.1.
IPIIPI00004401.
IPI00009240.
RefSeqNP_733778.1.
UniGeneHs.135458

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

IntActQ9NPI5. 3 interactions.
STRINGQ9NPI5.

Proteomic databases

PRIDEQ9NPI5.

Genome annotation databases

EnsemblENST00000168977; ENSP00000168977; ENSG00000077009; Homo sapiens. [Genome view]
ENST00000395034; ENSP00000378475; ENSG00000077009; Homo sapiens. [Genome view]
GeneID27231.
KEGGhsa:27231.
NMPDRfig|9606.3.peg.15403.
UCSCuc002lyz.2. human.

Organism-specific databases

CTD27231.
GeneCardsGC19P003884.
H-InvDBHIX0014649.
HGNCHGNC:17871. ITGB1BP3.
MIM608705. gene.
PharmGKBPA134938442.
GenAtlasSearch...

Phylogenomic databases

HOGENOMQ9NPI5.
HOVERGENQ9NPI5.
OMAECKWRRS.

Gene expression databases

ArrayExpressQ9NPI5.
BgeeQ9NPI5.
CleanExHS_ITGB1BP3.
GenevestigatorQ9NPI5.
GermOnlineENSG00000077009. Homo sapiens.

Family and domain databases

ProtoNetSearch...

Other Resources

NextBio50087.
SOURCESearch...

Entry information

Entry nameNRK2_HUMAN
AccessionPrimary (citable) accession number: Q9NPI5
Secondary accession number(s): Q52M81, Q9NZK3
Entry history
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: October 1, 2000
Last modified: November 3, 2009
This is version 60 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

Human chromosome 19

Human chromosome 19: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents