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Protein

Nicotinamide riboside kinase 2

Gene

NMRK2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.2 Publications

Catalytic activityi

ATP + 1-(beta-D-ribofuranosyl)-nicotinamide = ADP + beta-nicotinamide D-ribonucleotide.
ATP + beta-D-ribosylnicotinate = ADP + nicotinate beta-D-ribonucleotide.

Kineticsi

  1. KM=0.19 mM for nicotinamide riboside (with ATP as cosubstrate)1 Publication
  2. KM=30 mM for nicotinamide riboside (with GTP as cosubstrate)1 Publication
  3. KM=0.11 mM for tiazofurin (with ATP as cosubstrate)1 Publication
  4. KM=0.063 mM for nicotinic acid riboside (with ATP as cosubstrate)1 Publication
  5. KM=1.3 mM for uridine (with ATP as cosubstrate)1 Publication

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi16 – 161MagnesiumBy similarity
Active sitei35 – 351Proton acceptorBy similarity
Metal bindingi35 – 351MagnesiumBy similarity
Binding sitei55 – 551SubstrateBy similarity
Binding sitei130 – 1301ATPBy similarity
Binding sitei131 – 1311SubstrateBy similarity
Binding sitei134 – 1341ATPBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi9 – 179ATPBy similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. metal ion binding Source: UniProtKB-KW
  3. ribosylnicotinamide kinase activity Source: UniProtKB-EC

GO - Biological processi

  1. NAD biosynthetic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Biological processi

Pyridine nucleotide biosynthesis

Keywords - Ligandi

ATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

UniPathwayiUPA00253.

Names & Taxonomyi

Protein namesi
Recommended name:
Nicotinamide riboside kinase 2 (EC:2.7.1.22)
Short name:
NRK 2
Short name:
NmR-K 2
Alternative name(s):
Integrin beta-1-binding protein 3
Muscle integrin-binding protein
Short name:
MIBP
Nicotinic acid riboside kinase 2 (EC:2.7.1.173)
Ribosylnicotinamide kinase 2
Short name:
RNK 2
Ribosylnicotinic acid kinase 2
Gene namesi
Name:NMRK2
Synonyms:ITGB1BP3, NRK2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 19

Organism-specific databases

HGNCiHGNC:17871. NMRK2.

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi35 – 351D → A: Loss of activity. 1 Publication
Mutagenesisi100 – 1001E → A: Loss of activity. 1 Publication

Organism-specific databases

PharmGKBiPA134938442.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 230230Nicotinamide riboside kinase 2PRO_0000215894Add
BLAST

Proteomic databases

PaxDbiQ9NPI5.
PRIDEiQ9NPI5.

PTM databases

PhosphoSiteiQ9NPI5.

Expressioni

Tissue specificityi

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.1 Publication

Inductioni

Down-regulated during myoblast differentiation.By similarity

Gene expression databases

BgeeiQ9NPI5.
CleanExiHS_ITGB1BP3.
ExpressionAtlasiQ9NPI5. baseline and differential.
GenevestigatoriQ9NPI5.

Organism-specific databases

HPAiHPA049909.

Interactioni

Subunit structurei

Monomer (By similarity). Interacts with ITGB1 alone or when associated with alpha-7, but not with alpha-5.By similarity2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
LRP12Q9Y5612EBI-514059,EBI-296693

Protein-protein interaction databases

BioGridi118080. 4 interactions.
IntActiQ9NPI5. 4 interactions.
MINTiMINT-1401053.
STRINGi9606.ENSP00000168977.

Structurei

3D structure databases

ProteinModelPortaliQ9NPI5.
SMRiQ9NPI5. Positions 3-191.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the uridine kinase family. NRK subfamily.Curated

Phylogenomic databases

eggNOGiCOG0572.
GeneTreeiENSGT00510000046782.
HOVERGENiHBG052669.
InParanoidiQ9NPI5.
KOiK10524.
OMAiLYNQVFE.
OrthoDBiEOG7JQBPF.
PhylomeDBiQ9NPI5.
TreeFamiTF105395.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR027417. P-loop_NTPase.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9NPI5-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MKLIVGIGGM TNGGKTTLTN SLLRALPNCC VIHQDDFFKP QDQIAVGEDG
60 70 80 90 100
FKQWDVLESL DMEAMLDTVQ AWLSSPQKFA RAHGVSVQPE ASDTHILLLE
110 120 130 140 150
GFLLYSYKPL VDLYSRRYFL TVPYEECKWR RSTRNYTVPD PPGLFDGHVW
160 170 180 190 200
PMYQKYRQEM EANGVEVVYL DGMKSREELF REVLEDIQNS LLNRSQESAP
210 220 230
SPARPARTQG PGRGCGHRTA RPAASQQDSM
Length:230
Mass (Da):26,046
Last modified:October 1, 2000 - v1
Checksum:i27F8275A596758E7
GO
Isoform 2 (identifier: Q9NPI5-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     39-39: K → KAPLFQ

Note: No experimental confirmation available.

Show »
Length:235
Mass (Da):26,602
Checksum:i20A4D09E207DB3A8
GO

Sequence cautioni

The sequence AAF26711.1 differs from that shown.Aberrant splicing.Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti178 – 1781E → K.
Corresponds to variant rs16992131 [ dbSNP | Ensembl ].
VAR_024549

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei39 – 391K → KAPLFQ in isoform 2. 1 PublicationVSP_054332

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF190819 mRNA. Translation: AAF26711.1. Sequence problems.
AY611481 mRNA. Translation: AAT11929.1.
AL365377 mRNA. Translation: CAB96949.1.
AK001663 mRNA. Translation: BAA91820.1.
AK022514 mRNA. Translation: BAB14071.1.
AC011488 Genomic DNA. No translation available.
BC093637 mRNA. Translation: AAH93637.1.
BC101575 mRNA. Translation: AAI01576.1.
BC143329 mRNA. Translation: AAI43330.1.
CCDSiCCDS12115.1. [Q9NPI5-1]
CCDS74259.1. [Q9NPI5-3]
RefSeqiNP_001276046.1. NM_001289117.1. [Q9NPI5-3]
NP_733778.1. NM_170678.2. [Q9NPI5-1]
UniGeneiHs.135458.

Genome annotation databases

EnsembliENST00000168977; ENSP00000168977; ENSG00000077009. [Q9NPI5-1]
ENST00000593949; ENSP00000472581; ENSG00000077009. [Q9NPI5-3]
ENST00000616156; ENSP00000480091; ENSG00000077009. [Q9NPI5-3]
GeneIDi27231.
KEGGihsa:27231.
UCSCiuc002lyz.4. human. [Q9NPI5-1]
uc010xia.2. human.

Polymorphism databases

DMDMi50401178.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF190819 mRNA. Translation: AAF26711.1. Sequence problems.
AY611481 mRNA. Translation: AAT11929.1.
AL365377 mRNA. Translation: CAB96949.1.
AK001663 mRNA. Translation: BAA91820.1.
AK022514 mRNA. Translation: BAB14071.1.
AC011488 Genomic DNA. No translation available.
BC093637 mRNA. Translation: AAH93637.1.
BC101575 mRNA. Translation: AAI01576.1.
BC143329 mRNA. Translation: AAI43330.1.
CCDSiCCDS12115.1. [Q9NPI5-1]
CCDS74259.1. [Q9NPI5-3]
RefSeqiNP_001276046.1. NM_001289117.1. [Q9NPI5-3]
NP_733778.1. NM_170678.2. [Q9NPI5-1]
UniGeneiHs.135458.

3D structure databases

ProteinModelPortaliQ9NPI5.
SMRiQ9NPI5. Positions 3-191.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi118080. 4 interactions.
IntActiQ9NPI5. 4 interactions.
MINTiMINT-1401053.
STRINGi9606.ENSP00000168977.

PTM databases

PhosphoSiteiQ9NPI5.

Polymorphism databases

DMDMi50401178.

Proteomic databases

PaxDbiQ9NPI5.
PRIDEiQ9NPI5.

Protocols and materials databases

DNASUi27231.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000168977; ENSP00000168977; ENSG00000077009. [Q9NPI5-1]
ENST00000593949; ENSP00000472581; ENSG00000077009. [Q9NPI5-3]
ENST00000616156; ENSP00000480091; ENSG00000077009. [Q9NPI5-3]
GeneIDi27231.
KEGGihsa:27231.
UCSCiuc002lyz.4. human. [Q9NPI5-1]
uc010xia.2. human.

Organism-specific databases

CTDi27231.
GeneCardsiGC19P003933.
HGNCiHGNC:17871. NMRK2.
HPAiHPA049909.
MIMi608705. gene.
neXtProtiNX_Q9NPI5.
PharmGKBiPA134938442.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0572.
GeneTreeiENSGT00510000046782.
HOVERGENiHBG052669.
InParanoidiQ9NPI5.
KOiK10524.
OMAiLYNQVFE.
OrthoDBiEOG7JQBPF.
PhylomeDBiQ9NPI5.
TreeFamiTF105395.

Enzyme and pathway databases

UniPathwayiUPA00253.

Miscellaneous databases

GeneWikiiITGB1BP3.
GenomeRNAii27231.
NextBioi35481178.
PROiQ9NPI5.
SOURCEiSearch...

Gene expression databases

BgeeiQ9NPI5.
CleanExiHS_ITGB1BP3.
ExpressionAtlasiQ9NPI5. baseline and differential.
GenevestigatoriQ9NPI5.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR027417. P-loop_NTPase.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), 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] [Europe PMC] [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.
    , 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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Teratocarcinoma.
  5. "The DNA sequence and biology of human chromosome 19."
    Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V.
    , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
    Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    Tissue: Liver.
  7. "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] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH INTEGRIN ALPHA-7/BETA-1.
  8. Cited for: SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF ASP-35 AND GLU-100.

Entry informationi

Entry nameiNRK2_HUMAN
AccessioniPrimary (citable) accession number: Q9NPI5
Secondary accession number(s): B7ZKR3, Q52M81, Q9NZK3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: October 1, 2000
Last modified: January 7, 2015
This is version 102 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 19
    Human chromosome 19: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.