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Nicotinamide riboside kinase 2 (NRK 2) (NmR-K 2) (EC 2.7.1.22) (Integrin beta-1-binding protein 3) (Muscle integrin-binding protein) (MIBP) (Nicotinic acid riboside kinase 2) (EC 2.7.1.173) (Ribosylnicotinamide kinase 2) (RNK 2) (Ribosylnicotinic acid kinase 2)

 NRK2_HUMAN              Reviewed;         230 AA.
Q9NPI5; B7ZKR3; Q52M81; Q9NZK3;
19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
01-OCT-2000, sequence version 1.
27-SEP-2017, entry version 122.
RecName: Full=Nicotinamide riboside kinase 2;
Short=NRK 2;
Short=NmR-K 2;
EC=2.7.1.22 {ECO:0000269|PubMed:17914902};
AltName: Full=Integrin beta-1-binding protein 3;
AltName: Full=Muscle integrin-binding protein;
Short=MIBP;
AltName: Full=Nicotinic acid riboside kinase 2;
EC=2.7.1.173 {ECO:0000269|PubMed:17914902};
AltName: Full=Ribosylnicotinamide kinase 2;
Short=RNK 2;
AltName: Full=Ribosylnicotinic acid kinase 2;
Name=NMRK2; Synonyms=ITGB1BP3, NRK2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY,
AND INTERACTION WITH ITGB1.
TISSUE=Heart;
PubMed=10613898; DOI=10.1083/jcb.147.7.1391;
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.
PubMed=15137942; DOI=10.1016/S0092-8674(04)00416-7;
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;
PubMed=14702039; DOI=10.1038/ng1285;
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 GENOMIC DNA].
PubMed=15057824; DOI=10.1038/nature02399;
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.;
"The DNA sequence and biology of human chromosome 19.";
Nature 428:529-535(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Liver;
PubMed=15489334; DOI=10.1101/gr.2596504;
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).
[7]
INTERACTION WITH INTEGRIN ALPHA-7/BETA-1.
PubMed=12941630; DOI=10.1016/S0012-1606(03)00304-X;
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).
[8]
SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, CATALYTIC
ACTIVITY, AND MUTAGENESIS OF ASP-35 AND GLU-100.
PubMed=17914902; DOI=10.1371/journal.pbio.0050263;
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).
-!- 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.
{ECO:0000269|PubMed:10613898, ECO:0000269|PubMed:15137942}.
-!- CATALYTIC ACTIVITY: ATP + 1-(beta-D-ribofuranosyl)-nicotinamide =
ADP + beta-nicotinamide D-ribonucleotide.
{ECO:0000269|PubMed:17914902}.
-!- CATALYTIC ACTIVITY: ATP + beta-D-ribosylnicotinate = ADP +
nicotinate beta-D-ribonucleotide. {ECO:0000269|PubMed:17914902}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=0.19 mM for nicotinamide riboside (with ATP as cosubstrate)
{ECO:0000269|PubMed:17914902};
KM=30 mM for nicotinamide riboside (with GTP as cosubstrate)
{ECO:0000269|PubMed:17914902};
KM=0.11 mM for tiazofurin (with ATP as cosubstrate)
{ECO:0000269|PubMed:17914902};
KM=0.063 mM for nicotinic acid riboside (with ATP as
cosubstrate) {ECO:0000269|PubMed:17914902};
KM=1.3 mM for uridine (with ATP as cosubstrate)
{ECO:0000269|PubMed:17914902};
-!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis.
{ECO:0000305|PubMed:17914902}.
-!- SUBUNIT: Monomer (By similarity). Interacts with ITGB1 alone or
when associated with alpha-7, but not with alpha-5. {ECO:0000250,
ECO:0000269|PubMed:10613898, ECO:0000269|PubMed:12941630}.
-!- INTERACTION:
Q9Y561:LRP12; NbExp=2; IntAct=EBI-514059, EBI-296693;
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9NPI5-1; Sequence=Displayed;
Name=2;
IsoId=Q9NPI5-3; Sequence=VSP_054332;
Note=No experimental confirmation available.;
-!- 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.
{ECO:0000269|PubMed:10613898}.
-!- INDUCTION: Down-regulated during myoblast differentiation.
{ECO:0000250}.
-!- SIMILARITY: Belongs to the uridine kinase family. NRK subfamily.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAF26711.1; Type=Miscellaneous discrepancy; Note=Aberrant splicing.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AF190819; AAF26711.1; ALT_SEQ; mRNA.
EMBL; AY611481; AAT11929.1; -; mRNA.
EMBL; AL365377; CAB96949.1; -; mRNA.
EMBL; AK001663; BAA91820.1; -; mRNA.
EMBL; AK022514; BAB14071.1; -; mRNA.
EMBL; AC011488; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC093637; AAH93637.1; -; mRNA.
EMBL; BC101575; AAI01576.1; -; mRNA.
EMBL; BC143329; AAI43330.1; -; mRNA.
CCDS; CCDS12115.1; -. [Q9NPI5-1]
CCDS; CCDS74259.1; -. [Q9NPI5-3]
RefSeq; NP_001276046.1; NM_001289117.1. [Q9NPI5-3]
RefSeq; NP_733778.1; NM_170678.2. [Q9NPI5-1]
UniGene; Hs.135458; -.
ProteinModelPortal; Q9NPI5; -.
SMR; Q9NPI5; -.
BioGrid; 118080; 3.
CORUM; Q9NPI5; -.
IntAct; Q9NPI5; 4.
MINT; MINT-1401053; -.
STRING; 9606.ENSP00000168977; -.
iPTMnet; Q9NPI5; -.
PhosphoSitePlus; Q9NPI5; -.
BioMuta; NMRK2; -.
DMDM; 50401178; -.
PaxDb; Q9NPI5; -.
PeptideAtlas; Q9NPI5; -.
PRIDE; Q9NPI5; -.
DNASU; 27231; -.
Ensembl; ENST00000168977; ENSP00000168977; ENSG00000077009. [Q9NPI5-1]
Ensembl; ENST00000593949; ENSP00000472581; ENSG00000077009. [Q9NPI5-3]
Ensembl; ENST00000616156; ENSP00000480091; ENSG00000077009. [Q9NPI5-3]
GeneID; 27231; -.
KEGG; hsa:27231; -.
UCSC; uc002lyz.4; human. [Q9NPI5-1]
CTD; 27231; -.
EuPathDB; HostDB:ENSG00000077009.13; -.
GeneCards; NMRK2; -.
HGNC; HGNC:17871; NMRK2.
HPA; HPA049909; -.
HPA; HPA054792; -.
HPA; HPA072450; -.
MIM; 608705; gene.
neXtProt; NX_Q9NPI5; -.
OpenTargets; ENSG00000077009; -.
PharmGKB; PA134938442; -.
eggNOG; KOG3308; Eukaryota.
eggNOG; COG0572; LUCA.
GeneTree; ENSGT00510000046782; -.
HOGENOM; HOG000043899; -.
HOVERGEN; HBG052669; -.
InParanoid; Q9NPI5; -.
KO; K10524; -.
OMA; PQKFARA; -.
OrthoDB; EOG091G0JV5; -.
PhylomeDB; Q9NPI5; -.
TreeFam; TF105395; -.
BRENDA; 2.7.1.173; 2681.
Reactome; R-HSA-196807; Nicotinate metabolism.
UniPathway; UPA00253; -.
GeneWiki; ITGB1BP3; -.
GenomeRNAi; 27231; -.
PRO; PR:Q9NPI5; -.
Proteomes; UP000005640; Chromosome 19.
Bgee; ENSG00000077009; -.
CleanEx; HS_ITGB1BP3; -.
ExpressionAtlas; Q9NPI5; baseline and differential.
Genevisible; Q9NPI5; HS.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005886; C:plasma membrane; IDA:HPA.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0050262; F:ribosylnicotinamide kinase activity; EXP:Reactome.
GO; GO:0061769; F:ribosylnicotinate kinase activity; EXP:Reactome.
GO; GO:0009435; P:NAD biosynthetic process; IEA:UniProtKB-UniPathway.
GO; GO:0019674; P:NAD metabolic process; TAS:Reactome.
GO; GO:0045662; P:negative regulation of myoblast differentiation; IEA:Ensembl.
InterPro; IPR027417; P-loop_NTPase.
SUPFAM; SSF52540; SSF52540; 1.
1: Evidence at protein level;
Alternative splicing; ATP-binding; Complete proteome; Kinase;
Magnesium; Metal-binding; Nucleotide-binding; Polymorphism;
Pyridine nucleotide biosynthesis; Reference proteome; Transferase.
CHAIN 1 230 Nicotinamide riboside kinase 2.
/FTId=PRO_0000215894.
NP_BIND 9 17 ATP. {ECO:0000250|UniProtKB:Q9NWW6}.
NP_BIND 134 136 ATP. {ECO:0000250|UniProtKB:Q9NWW6}.
NP_BIND 174 176 ATP. {ECO:0000250|UniProtKB:Q9NWW6}.
REGION 35 38 Substrate binding.
{ECO:0000250|UniProtKB:Q9NWW6}.
REGION 54 55 Substrate binding.
{ECO:0000250|UniProtKB:Q9NWW6}.
REGION 136 137 Substrate binding.
{ECO:0000250|UniProtKB:Q9NWW6}.
ACT_SITE 35 35 Proton acceptor.
{ECO:0000250|UniProtKB:Q9NWW6}.
METAL 16 16 Magnesium.
{ECO:0000250|UniProtKB:Q9NWW6}.
METAL 35 35 Magnesium.
{ECO:0000250|UniProtKB:Q9NWW6}.
BINDING 130 130 ATP. {ECO:0000250|UniProtKB:Q9NWW6}.
BINDING 131 131 Substrate.
{ECO:0000250|UniProtKB:Q9NWW6}.
VAR_SEQ 39 39 K -> KAPLFQ (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_054332.
VARIANT 178 178 E -> K (in dbSNP:rs16992131).
/FTId=VAR_024549.
MUTAGEN 35 35 D->A: Loss of activity.
{ECO:0000269|PubMed:17914902}.
MUTAGEN 100 100 E->A: Loss of activity.
{ECO:0000269|PubMed:17914902}.
SEQUENCE 230 AA; 26046 MW; 27F8275A596758E7 CRC64;
MKLIVGIGGM TNGGKTTLTN SLLRALPNCC VIHQDDFFKP QDQIAVGEDG FKQWDVLESL
DMEAMLDTVQ AWLSSPQKFA RAHGVSVQPE ASDTHILLLE GFLLYSYKPL VDLYSRRYFL
TVPYEECKWR RSTRNYTVPD PPGLFDGHVW PMYQKYRQEM EANGVEVVYL DGMKSREELF
REVLEDIQNS LLNRSQESAP SPARPARTQG PGRGCGHRTA RPAASQQDSM


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