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UniProtKB/Swiss-Prot entry Q9NWW6


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name NRK1_HUMAN
Primary accession number Q9NWW6
Secondary accession number Q8N430
Integrated into Swiss-Prot on July 19, 2004
Sequence was last modified on October 1, 2000 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 54)
Name and origin of the protein
Protein name Nicotinamide riboside kinase 1
Synonyms NmR-K 1
NRK 1
EC 2.7.1.22
Ribosylnicotinamide kinase 1
RNK 1
Nicotinic acid riboside kinase 1
EC 2.7.1.n4
Ribosylnicotinic acid kinase 1
Gene name
Name: NRK1
Synonyms: C9orf95
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND CATALYTIC ACTIVITY.
DOI=10.1016/S0092-8674(04)00416-7; PubMed=15137942 [NCBI, ExPASy, EBI, Israel, Japan]
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).
DOI=10.1038/ng1285; PubMed=14702039 [NCBI, ExPASy, EBI, Israel, Japan]
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].
DOI=10.1038/nature02465; PubMed=15164053 [NCBI, ExPASy, EBI, Israel, Japan]
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 MRNA] (ISOFORMS 1 AND 2).
TISSUE=Colon, and Hippocampus;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[5]
CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
TISSUE=Placenta;
DOI=10.1006/abbi.1996.0409; PubMed=8809081 [NCBI, ExPASy, EBI, Israel, Japan]
Sasiak K., Saunders P.P.;
"Purification and properties of a human nicotinamide ribonucleoside kinase.";
Arch. Biochem. Biophys. 333:414-418(1996).
[6]
X-RAY CRYSTALLOGRAPHY (1.32 ANGSTROMS) OF 2-189 IN COMPLEXES WITH SUBSTRATES, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF ASP-36 AND GLU-98.
DOI=10.1371/journal.pbio.0050263; PubMed=17914902 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[7]
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.
DOI=10.1016/j.str.2007.06.017; PubMed=17698003 [NCBI, ExPASy, EBI, Israel, Japan]
Khan J.A., Xiang S., Tong L.;
"Crystal structure of human nicotinamide riboside kinase.";
Structure 15:1005-1013(2007).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AY611480; AAT11928.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK000566; BAA91259.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL133548; CAH71571.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC001366; AAH01366.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC036804; AAH36804.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_001121075.1; -.
NP_060351.1; -.
UniGene Hs.494186
3D structure databases
PDB
2P0E; X-ray; 1.80 A; A=2-189.[ExPASy / RCSB / EBI]
2QG6; X-ray; 1.50 A; A=1-199.[ExPASy / RCSB / EBI]
2QL6; X-ray; 2.70 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P=1-199.[ExPASy / RCSB / EBI]
2QSY; X-ray; 1.95 A; A=2-189.[ExPASy / RCSB / EBI]
2QSZ; X-ray; 1.90 A; A=2-189.[ExPASy / RCSB / EBI]
2QT0; X-ray; 1.92 A; A=2-189.[ExPASy / RCSB / EBI]
2QT1; X-ray; 1.32 A; A=2-189.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 2P0E; -.
2QG6; -.
2QL6; -.
2QSY; -.
2QSZ; -.
2QT0; -.
2QT1; -.
ModBase Q9NWW6.
Organism-specific databases
H-InvDB HIX0008105; -.
HGNC HGNC:26057; C9orf95.
GenAtlas NRK1.
MIM 608704; gene. [NCBI / EBI]
PharmGKB PA134946592; -.
GeneCards Q9NWW6.
Gene expression databases
ArrayExpress Q9NWW6; -.
CleanEx HS_C9orf95; -.
GermOnline ENSG00000106733; Homo sapiens.
Ontologies
GO
GO:0005524; Molecular function: ATP binding (inferred from electronic annotation from InterPro).
GO:0000287; Molecular function: magnesium ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0050262; Molecular function: ribosylnicotinamide kinase activity (inferred from electronic annotation from EC).
GO:0019363; Biological process: pyridine nucleotide biosynthetic process (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR000764; Uridine_kin.
Graphical view of domain structure.
PRINTS PR00988; URIDINKINASE.
ProtoNet Q9NWW6.
Genome annotation databases
Ensembl ENSG00000106733; Homo sapiens. [Contig view]
GeneID 54981; -.
KEGG hsa:54981; -.
NMPDR fig|9606.3.peg.31434; -.
Phylogenomic databases
HOVERGEN Q9NWW6; -.
Other
NextBio 58250; -.
SOURCE NRK1; Homo sapiens.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Alternative splicing; ATP-binding; Kinase; Magnesium; Metal-binding; Nucleotide-binding; Pyridine nucleotide biosynthesis; Transferase.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   199  199     Nicotinamide riboside kinase 1. PRO_0000215891
NP_BIND   10    18  9     ATP. 
NP_BIND   172   174  3     ATP. 
ACT_SITE   36    36        Proton acceptor. 
METAL   17    17        Magnesium. 
METAL   36    36        Magnesium. 
BINDING   56    56        Substrate. 
BINDING   128   128        ATP. 
BINDING   129   129        Substrate. 
BINDING   132   132        ATP. 
VAR_SEQ   106   130        KPLDTIWNRSYFLTIPYEECKRRRS -> N (in isoform 2). VSP_012676
MUTAGEN   16    16        K->A: Loss of activity. 
MUTAGEN   36    36        D->A: Loss of activity. 
MUTAGEN   56    56        D->A: Loss of activity. 
MUTAGEN   98    98        E->A: Loss of activity. 
MUTAGEN   138   138        D->A: Almost no effect. 
STRAND   4    11  8      
HELIX   16    24  9      
STRAND   30    34  5      
HELIX   35    38  4      
HELIX   42    44  3      
HELIX   58    60  3      
HELIX   63    77  15      
STRAND   94    98  5      
HELIX   106   108  3      
TURN   109   111  3      
STRAND   113   119  7      
HELIX   122   131  10      
HELIX   142   145  4      
HELIX   147   157  11      
HELIX   158   160  3      
STRAND   166   169  4      
HELIX   174   185  12      
TURN   186   188  3      
Sequence information
Length: 199 AA [This is the length of the unprocessed precursor] Molecular weight: 23193 Da [This is the MW of the unprocessed precursor] CRC64: 0A0803461F40EA32 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MKTFIIGISG VTNSGKTTLA KNLQKHLPNC SVISQDDFFK PESEIETDKN GFLQYDVLEA 

        70         80         90        100        110        120 
LNMEKMMSAI SCWMESARHS VVSTDQESAE EIPILIIEGF LLFNYKPLDT IWNRSYFLTI 

       130        140        150        160        170        180 
PYEECKRRRS TRVYQPPDSP GYFDGHVWPM YLKYRQEMQD ITWEVVYLDG TKSEEDLFLQ 

       190 
VYEDLIQELA KQKCLQVTA 

Q9NWW6 in FASTA format

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