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Q9NPI5

- NRK2_HUMAN

UniProt

Q9NPI5 - NRK2_HUMAN

Protein

Nicotinamide riboside kinase 2

Gene

NMRK2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 100 (01 Oct 2014)
      Sequence version 1 (01 Oct 2000)
      Previous versions | rss
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    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. protein binding Source: IntAct
    4. ribosylnicotinamide kinase activity Source: UniProtKB-EC

    GO - Biological processi

    1. NAD biosynthetic process Source: UniProtKB-UniPathway
    2. negative regulation of myoblast differentiation Source: Ensembl

    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.

    Subcellular locationi

    GO - Cellular componenti

    1. intracellular Source: Ensembl

    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

    ArrayExpressiQ9NPI5.
    BgeeiQ9NPI5.
    CleanExiHS_ITGB1BP3.
    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.
    HOVERGENiHBG052669.
    InParanoidiQ9NPI5.
    KOiK10524.
    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

    MKLIVGIGGM TNGGKTTLTN SLLRALPNCC VIHQDDFFKP QDQIAVGEDG    50
    FKQWDVLESL DMEAMLDTVQ AWLSSPQKFA RAHGVSVQPE ASDTHILLLE 100
    GFLLYSYKPL VDLYSRRYFL TVPYEECKWR RSTRNYTVPD PPGLFDGHVW 150
    PMYQKYRQEM EANGVEVVYL DGMKSREELF REVLEDIQNS LLNRSQESAP 200
    SPARPARTQG PGRGCGHRTA RPAASQQDSM 230
    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. Reason: Aberrant splicing.

    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:
    EMBL
    GenBank
    DDBJ
    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]
    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]
    GeneIDi27231.
    KEGGihsa:27231.
    UCSCiuc002lyz.4. human. [Q9NPI5-1]

    Polymorphism databases

    DMDMi50401178.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS12115.1. [Q9NPI5-1 ]
    RefSeqi NP_001276046.1. NM_001289117.1. [Q9NPI5-3 ]
    NP_733778.1. NM_170678.2. [Q9NPI5-1 ]
    UniGenei Hs.135458.

    3D structure databases

    ProteinModelPortali Q9NPI5.
    SMRi Q9NPI5. Positions 3-191.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 118080. 4 interactions.
    IntActi Q9NPI5. 4 interactions.
    MINTi MINT-1401053.
    STRINGi 9606.ENSP00000168977.

    PTM databases

    PhosphoSitei Q9NPI5.

    Polymorphism databases

    DMDMi 50401178.

    Proteomic databases

    PaxDbi Q9NPI5.
    PRIDEi Q9NPI5.

    Protocols and materials databases

    DNASUi 27231.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000168977 ; ENSP00000168977 ; ENSG00000077009 . [Q9NPI5-1 ]
    ENST00000593949 ; ENSP00000472581 ; ENSG00000077009 . [Q9NPI5-3 ]
    GeneIDi 27231.
    KEGGi hsa:27231.
    UCSCi uc002lyz.4. human. [Q9NPI5-1 ]

    Organism-specific databases

    CTDi 27231.
    GeneCardsi GC19P003933.
    HGNCi HGNC:17871. NMRK2.
    HPAi HPA049909.
    MIMi 608705. gene.
    neXtProti NX_Q9NPI5.
    PharmGKBi PA134938442.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0572.
    HOVERGENi HBG052669.
    InParanoidi Q9NPI5.
    KOi K10524.
    OrthoDBi EOG7JQBPF.
    PhylomeDBi Q9NPI5.
    TreeFami TF105395.

    Enzyme and pathway databases

    UniPathwayi UPA00253 .

    Miscellaneous databases

    GeneWikii ITGB1BP3.
    GenomeRNAii 27231.
    NextBioi 35481178.
    PROi Q9NPI5.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9NPI5.
    Bgeei Q9NPI5.
    CleanExi HS_ITGB1BP3.
    Genevestigatori Q9NPI5.

    Family and domain databases

    Gene3Di 3.40.50.300. 1 hit.
    InterProi IPR027417. P-loop_NTPase.
    [Graphical view ]
    SUPFAMi SSF52540. SSF52540. 1 hit.
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 100 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