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Nicotinamide riboside kinase 1 (NRK 1) (NmR-K 1) (EC 2.7.1.22) (Nicotinic acid riboside kinase 1) (EC 2.7.1.173) (Ribosylnicotinamide kinase 1) (RNK 1) (Ribosylnicotinic acid kinase 1)

 NRK1_HUMAN              Reviewed;         199 AA.
Q9NWW6; Q5W124; Q8N430;
19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
01-OCT-2000, sequence version 1.
27-SEP-2017, entry version 127.
RecName: Full=Nicotinamide riboside kinase 1;
Short=NRK 1;
Short=NmR-K 1;
EC=2.7.1.22 {ECO:0000269|PubMed:17914902, ECO:0000269|PubMed:8809081};
AltName: Full=Nicotinic acid riboside kinase 1;
EC=2.7.1.173 {ECO:0000269|PubMed:17914902, ECO:0000269|PubMed:8809081};
AltName: Full=Ribosylnicotinamide kinase 1;
Short=RNK 1;
AltName: Full=Ribosylnicotinic acid kinase 1;
Name=NMRK1; Synonyms=C9orf95, NRK1;
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, AND CATALYTIC
ACTIVITY.
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).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164053; DOI=10.1038/nature02465;
Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E.,
Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
Kimberley A.M., King A., Knights A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S.,
Rogers J., Dunham I.;
"DNA sequence and analysis of human chromosome 9.";
Nature 429:369-374(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Colon, and Hippocampus;
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).
[6]
CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
TISSUE=Placenta;
PubMed=8809081; DOI=10.1006/abbi.1996.0409;
Sasiak K., Saunders P.P.;
"Purification and properties of a human nicotinamide ribonucleoside
kinase.";
Arch. Biochem. Biophys. 333:414-418(1996).
[7]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[8]
X-RAY CRYSTALLOGRAPHY (1.32 ANGSTROMS) OF 2-189 IN COMPLEXES WITH ATP
AND SUBSTRATES, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES,
AND MUTAGENESIS OF ASP-36 AND GLU-98.
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).
[9]
X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) IN COMPLEXES WITH NUCLEOSIDE
MONOPHOSPHATE; ADP AND TIAZOFURIN, AND MUTAGENESIS OF LYS-16; ASP-36;
ASP-56 AND ASP-138.
PubMed=17698003; DOI=10.1016/j.str.2007.06.017;
Khan J.A., Xiang S., Tong L.;
"Crystal structure of human nicotinamide riboside kinase.";
Structure 15:1005-1013(2007).
-!- FUNCTION: Catalyzes the phosphorylation of nicotinamide riboside
(NR) and nicotinic acid riboside (NaR) to form nicotinamide
mononucleotide (NMN) and nicotinic acid mononucleotide (NaMN). The
enzyme also phosphorylates the antitumor drugs tiazofurin and 3-
deazaguanosine. {ECO:0000269|PubMed:15137942}.
-!- CATALYTIC ACTIVITY: ATP + 1-(beta-D-ribofuranosyl)-nicotinamide =
ADP + beta-nicotinamide D-ribonucleotide.
{ECO:0000269|PubMed:17914902, ECO:0000269|PubMed:8809081}.
-!- CATALYTIC ACTIVITY: ATP + beta-D-ribosylnicotinate = ADP +
nicotinate beta-D-ribonucleotide. {ECO:0000269|PubMed:17914902,
ECO:0000269|PubMed:8809081}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=0.088 mM for nicotinamide riboside (with ATP as cosubstrate)
{ECO:0000269|PubMed:17914902, ECO:0000269|PubMed:8809081};
KM=0.068 mM for nicotinamide riboside (with GTP as cosubstrate)
{ECO:0000269|PubMed:17914902, ECO:0000269|PubMed:8809081};
KM=0.27 mM for tiazofurin (with ATP as cosubstrate)
{ECO:0000269|PubMed:17914902, ECO:0000269|PubMed:8809081};
KM=0.051 mM for nicotinic acid riboside (with ATP as
cosubstrate) {ECO:0000269|PubMed:17914902,
ECO:0000269|PubMed:8809081};
KM=17 mM for uridine (with ATP as cosubstrate)
{ECO:0000269|PubMed:17914902, ECO:0000269|PubMed:8809081};
pH dependence:
Optimum pH is 6.5-9. {ECO:0000269|PubMed:17914902,
ECO:0000269|PubMed:8809081};
-!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis.
{ECO:0000305|PubMed:17914902}.
-!- SUBUNIT: Monomer. {ECO:0000269|PubMed:8809081}.
-!- INTERACTION:
Q04864-2:REL; NbExp=4; IntAct=EBI-10315485, EBI-10829018;
Q86VP1:TAX1BP1; NbExp=5; IntAct=EBI-10315485, EBI-529518;
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9NWW6-1; Sequence=Displayed;
Name=2;
IsoId=Q9NWW6-2; Sequence=VSP_012676;
Note=No experimental confirmation available.;
-!- SIMILARITY: Belongs to the uridine kinase family. NRK subfamily.
{ECO:0000305}.
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EMBL; AY611480; AAT11928.1; -; mRNA.
EMBL; AK000566; BAA91259.1; -; mRNA.
EMBL; AL133548; CAH71570.1; -; Genomic_DNA.
EMBL; AL133548; CAH71571.1; -; Genomic_DNA.
EMBL; CH471089; EAW62568.1; -; Genomic_DNA.
EMBL; BC001366; AAH01366.1; -; mRNA.
EMBL; BC036804; AAH36804.1; -; mRNA.
CCDS; CCDS47981.1; -. [Q9NWW6-2]
CCDS; CCDS6650.1; -. [Q9NWW6-1]
RefSeq; NP_001121075.1; NM_001127603.1. [Q9NWW6-2]
RefSeq; NP_001317607.1; NM_001330678.1.
RefSeq; NP_060351.1; NM_017881.2. [Q9NWW6-1]
RefSeq; XP_006717226.1; XM_006717163.2. [Q9NWW6-1]
RefSeq; XP_016870359.1; XM_017014870.1. [Q9NWW6-1]
RefSeq; XP_016870363.1; XM_017014874.1. [Q9NWW6-2]
UniGene; Hs.494186; -.
PDB; 2P0E; X-ray; 1.80 A; A=2-189.
PDB; 2QG6; X-ray; 1.50 A; A=1-199.
PDB; 2QL6; X-ray; 2.70 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P=1-199.
PDB; 2QSY; X-ray; 1.95 A; A=2-189.
PDB; 2QSZ; X-ray; 1.90 A; A=2-189.
PDB; 2QT0; X-ray; 1.92 A; A=2-189.
PDB; 2QT1; X-ray; 1.32 A; A=2-189.
PDBsum; 2P0E; -.
PDBsum; 2QG6; -.
PDBsum; 2QL6; -.
PDBsum; 2QSY; -.
PDBsum; 2QSZ; -.
PDBsum; 2QT0; -.
PDBsum; 2QT1; -.
ProteinModelPortal; Q9NWW6; -.
SMR; Q9NWW6; -.
BioGrid; 120317; 2.
IntAct; Q9NWW6; 3.
STRING; 9606.ENSP00000354387; -.
iPTMnet; Q9NWW6; -.
PhosphoSitePlus; Q9NWW6; -.
BioMuta; NMRK1; -.
DMDM; 50401180; -.
EPD; Q9NWW6; -.
MaxQB; Q9NWW6; -.
PaxDb; Q9NWW6; -.
PeptideAtlas; Q9NWW6; -.
PRIDE; Q9NWW6; -.
DNASU; 54981; -.
Ensembl; ENST00000361092; ENSP00000354387; ENSG00000106733. [Q9NWW6-1]
Ensembl; ENST00000376808; ENSP00000366004; ENSG00000106733. [Q9NWW6-2]
GeneID; 54981; -.
KEGG; hsa:54981; -.
UCSC; uc004ajr.5; human. [Q9NWW6-1]
CTD; 54981; -.
EuPathDB; HostDB:ENSG00000106733.20; -.
GeneCards; NMRK1; -.
HGNC; HGNC:26057; NMRK1.
HPA; HPA049795; -.
MIM; 608704; gene.
neXtProt; NX_Q9NWW6; -.
OpenTargets; ENSG00000106733; -.
PharmGKB; PA134946592; -.
eggNOG; KOG3308; Eukaryota.
eggNOG; COG0572; LUCA.
GeneTree; ENSGT00510000046782; -.
HOGENOM; HOG000043899; -.
HOVERGEN; HBG052669; -.
InParanoid; Q9NWW6; -.
KO; K10524; -.
PhylomeDB; Q9NWW6; -.
TreeFam; TF105395; -.
BRENDA; 2.7.1.173; 2681.
Reactome; R-HSA-196807; Nicotinate metabolism.
UniPathway; UPA00253; -.
ChiTaRS; NMRK1; human.
EvolutionaryTrace; Q9NWW6; -.
GenomeRNAi; 54981; -.
PRO; PR:Q9NWW6; -.
Proteomes; UP000005640; Chromosome 9.
Bgee; ENSG00000106733; -.
CleanEx; HS_C9orf95; -.
ExpressionAtlas; Q9NWW6; baseline and differential.
Genevisible; Q9NWW6; HS.
GO; GO:0005829; C:cytosol; TAS:Reactome.
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.
InterPro; IPR027417; P-loop_NTPase.
SUPFAM; SSF52540; SSF52540; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; ATP-binding; Complete proteome;
Kinase; Magnesium; Metal-binding; Nucleotide-binding;
Pyridine nucleotide biosynthesis; Reference proteome; Transferase.
CHAIN 1 199 Nicotinamide riboside kinase 1.
/FTId=PRO_0000215891.
NP_BIND 10 18 ATP. {ECO:0000244|PDB:2P0E,
ECO:0000244|PDB:2QG6,
ECO:0000244|PDB:2QL6,
ECO:0000244|PDB:2QSY,
ECO:0000244|PDB:2QSZ,
ECO:0000244|PDB:2QT0,
ECO:0000244|PDB:2QT1,
ECO:0000269|PubMed:17698003,
ECO:0000269|PubMed:17914902}.
NP_BIND 132 134 ATP. {ECO:0000244|PDB:2P0E,
ECO:0000244|PDB:2QG6,
ECO:0000244|PDB:2QSY,
ECO:0000244|PDB:2QSZ,
ECO:0000244|PDB:2QT0,
ECO:0000244|PDB:2QT1,
ECO:0000269|PubMed:17698003,
ECO:0000269|PubMed:17914902}.
NP_BIND 172 174 ATP. {ECO:0000244|PDB:2QSY,
ECO:0000244|PDB:2QT0,
ECO:0000269|PubMed:17914902}.
REGION 36 39 Substrate binding. {ECO:0000244|PDB:2P0E,
ECO:0000244|PDB:2QL6,
ECO:0000244|PDB:2QT0,
ECO:0000244|PDB:2QT1,
ECO:0000269|PubMed:17698003,
ECO:0000269|PubMed:17914902}.
REGION 55 56 Substrate binding. {ECO:0000244|PDB:2P0E,
ECO:0000244|PDB:2QL6,
ECO:0000244|PDB:2QT0,
ECO:0000244|PDB:2QT1,
ECO:0000269|PubMed:17698003,
ECO:0000269|PubMed:17914902}.
REGION 134 135 Substrate binding. {ECO:0000244|PDB:2P0E,
ECO:0000244|PDB:2QL6,
ECO:0000244|PDB:2QT0,
ECO:0000269|PubMed:17698003,
ECO:0000269|PubMed:17914902}.
ACT_SITE 36 36 Proton acceptor. {ECO:0000244|PDB:2QT0,
ECO:0000269|PubMed:17914902}.
METAL 17 17 Magnesium. {ECO:0000244|PDB:2QSY,
ECO:0000269|PubMed:17914902}.
METAL 36 36 Magnesium. {ECO:0000244|PDB:2QT0,
ECO:0000269|PubMed:17914902}.
BINDING 128 128 ATP. {ECO:0000244|PDB:2P0E,
ECO:0000269|PubMed:17914902}.
BINDING 129 129 Substrate. {ECO:0000244|PDB:2P0E,
ECO:0000244|PDB:2QL6,
ECO:0000244|PDB:2QT0,
ECO:0000244|PDB:2QT1,
ECO:0000269|PubMed:17914902}.
VAR_SEQ 106 130 KPLDTIWNRSYFLTIPYEECKRRRS -> N (in
isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_012676.
MUTAGEN 16 16 K->A: Loss of activity.
{ECO:0000269|PubMed:17698003}.
MUTAGEN 36 36 D->A: Loss of activity.
{ECO:0000269|PubMed:17698003,
ECO:0000269|PubMed:17914902}.
MUTAGEN 56 56 D->A: Loss of activity.
{ECO:0000269|PubMed:17698003}.
MUTAGEN 98 98 E->A: Loss of activity.
{ECO:0000269|PubMed:17914902}.
MUTAGEN 138 138 D->A: Almost no effect.
{ECO:0000269|PubMed:17698003}.
STRAND 4 11 {ECO:0000244|PDB:2QT1}.
HELIX 16 24 {ECO:0000244|PDB:2QT1}.
STRAND 30 34 {ECO:0000244|PDB:2QT1}.
HELIX 35 38 {ECO:0000244|PDB:2QT1}.
HELIX 42 44 {ECO:0000244|PDB:2QT1}.
HELIX 58 60 {ECO:0000244|PDB:2QT1}.
HELIX 63 77 {ECO:0000244|PDB:2QT1}.
STRAND 94 98 {ECO:0000244|PDB:2QT1}.
HELIX 106 108 {ECO:0000244|PDB:2QT1}.
TURN 109 111 {ECO:0000244|PDB:2QT1}.
STRAND 113 119 {ECO:0000244|PDB:2QT1}.
HELIX 122 131 {ECO:0000244|PDB:2QT1}.
HELIX 142 145 {ECO:0000244|PDB:2QT1}.
HELIX 147 157 {ECO:0000244|PDB:2QT1}.
HELIX 158 160 {ECO:0000244|PDB:2QT1}.
STRAND 166 169 {ECO:0000244|PDB:2QT1}.
HELIX 174 185 {ECO:0000244|PDB:2QT1}.
TURN 186 188 {ECO:0000244|PDB:2QT1}.
SEQUENCE 199 AA; 23193 MW; 0A0803461F40EA32 CRC64;
MKTFIIGISG VTNSGKTTLA KNLQKHLPNC SVISQDDFFK PESEIETDKN GFLQYDVLEA
LNMEKMMSAI SCWMESARHS VVSTDQESAE EIPILIIEGF LLFNYKPLDT IWNRSYFLTI
PYEECKRRRS TRVYQPPDSP GYFDGHVWPM YLKYRQEMQD ITWEVVYLDG TKSEEDLFLQ
VYEDLIQELA KQKCLQVTA


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EIAAB24784 GCK family kinase MiNK,Map4k6,MAPK_ERK kinase kinase kinase 6,MEK kinase kinase 6,MEKKK 6,Mink,Mink1,Misshapen_NIK-related kinase,Misshapen-like kinase 1,Mitogen-activated protein kinase kinase kinase
EIAAB25239 C-JUN N-terminal kinase kinase 1,Dual specificity mitogen-activated protein kinase kinase 4,JNK kinase 1,JNK-activating kinase 1,JNKK 1,Jnkk1,MAP kinase kinase 4,Map2k4,MAPK_ERK kinase 4,MAPKK 4,MEK 4
EIAAB25244 c-Jun N-terminal kinase kinase 2,Dual specificity mitogen-activated protein kinase kinase 7,JNK kinase 2,JNK-activating kinase 2,JNKK 2,MAP kinase kinase 7,Map2k7,MAPK_ERK kinase 7,MAPKK 7,MEK 7,Mkk7,
EIAAB25245 c-Jun N-terminal kinase kinase 2,Dual specificity mitogen-activated protein kinase kinase 7,JNK kinase 2,JNK-activating kinase 2,JNKK 2,MAP kinase kinase 7,Map2k7,MAPK_ERK kinase 7,MAPKK 7,MEK 7,Rat,R
EIAAB25246 c-Jun N-terminal kinase kinase 2,Dual specificity mitogen-activated protein kinase kinase 7,Homo sapiens,Human,JNK kinase 2,JNK-activating kinase 2,JNKK 2,JNKK2,MAP kinase kinase 7,MAP2K7,MAPK_ERK kin
EIAAB25240 c-Jun N-terminal kinase kinase 1,Dual specificity mitogen-activated protein kinase kinase 4,Homo sapiens,Human,JNK-activating kinase 1,JNKK,JNKK1,MAP kinase kinase 4,MAP2K4,MAPK_ERK kinase 4,MAPKK 4,M
E4119h Human Nicotinamide Riboside Kinase 1 ELISA Kit 96T
DFB18_RAT Human ELISA Kit FOR Nicotinamide riboside kinase 1 96T
TM11B_MOUSE Human ELISA Kit FOR Nicotinamide riboside kinase 1 96T
E0108h Human ELISA Kit FOR Nicotinamide riboside kinase 1 96T
CSB-EL011883HU Human Nicotinamide riboside kinase 2(ITGB1BP3) ELISA kit 96T
CSB-EL011883MO Mouse Nicotinamide riboside kinase 2(ITGB1BP3) ELISA kit 96T
CSB-EL004360HU Human Nicotinamide riboside kinase 1(C9orf95) ELISA kit 96T
CSB-EL011883MO Mouse Nicotinamide riboside kinase 2(ITGB1BP3) ELISA kit SpeciesMouse 96T
CSB-EL004360HU Human Nicotinamide riboside kinase 1(C9orf95) ELISA kit SpeciesHuman 96T
CSB-EL011883HU Human Nicotinamide riboside kinase 2(ITGB1BP3) ELISA kit SpeciesHuman 96T
NRK1_RAT ELISA Kit FOR Nicotinamide riboside kinase 1; organism: Rat; gene name: Nrk1 96T
NRK1_MOUSE ELISA Kit FOR Nicotinamide riboside kinase 1; organism: Mouse; gene name: Nrk1 96T
NRK2_MOUSE ELISA Kit FOR Nicotinamide riboside kinase 2; organism: Mouse; gene name: Itgb1bp3 96T


 

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