NRK1_HUMAN
ID NRK1_HUMAN Reviewed; 199 AA.
AC Q9NWW6; Q5W124; Q8N430;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Nicotinamide riboside kinase 1;
DE Short=NRK 1;
DE Short=NmR-K 1;
DE EC=2.7.1.22 {ECO:0000269|PubMed:17914902, ECO:0000269|PubMed:8809081};
DE AltName: Full=Nicotinic acid riboside kinase 1;
DE EC=2.7.1.173 {ECO:0000269|PubMed:17914902, ECO:0000269|PubMed:8809081};
DE AltName: Full=Ribosylnicotinamide kinase 1;
DE Short=RNK 1;
DE AltName: Full=Ribosylnicotinic acid kinase 1;
GN Name=NMRK1; Synonyms=C9orf95, NRK1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=15137942; DOI=10.1016/s0092-8674(04)00416-7;
RA Bieganowski P., Brenner C.;
RT "Discoveries of nicotinamide riboside as a nutrient and conserved NRK genes
RT establish a Preiss-Handler independent route to NAD+ in fungi and humans.";
RL Cell 117:495-502(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Colon, and Hippocampus;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RC TISSUE=Placenta;
RX PubMed=8809081; DOI=10.1006/abbi.1996.0409;
RA Sasiak K., Saunders P.P.;
RT "Purification and properties of a human nicotinamide ribonucleoside
RT kinase.";
RL Arch. Biochem. Biophys. 333:414-418(1996).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.32 ANGSTROMS) OF 2-189 IN COMPLEXES WITH ATP AND
RP SUBSTRATES, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP MUTAGENESIS OF ASP-36 AND GLU-98.
RX PubMed=17914902; DOI=10.1371/journal.pbio.0050263;
RA Tempel W., Rabeh W.M., Bogan K.L., Belenky P., Wojcik M., Seidle H.F.,
RA Nedyalkova L., Yang T., Sauve A.A., Park H.-W., Brenner C.;
RT "Nicotinamide riboside kinase structures reveal new pathways to NAD+.";
RL PLoS Biol. 5:2220-2230(2007).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) IN COMPLEXES WITH NUCLEOSIDE
RP MONOPHOSPHATE; ADP AND TIAZOFURIN, AND MUTAGENESIS OF LYS-16; ASP-36;
RP ASP-56 AND ASP-138.
RX PubMed=17698003; DOI=10.1016/j.str.2007.06.017;
RA Khan J.A., Xiang S., Tong L.;
RT "Crystal structure of human nicotinamide riboside kinase.";
RL Structure 15:1005-1013(2007).
CC -!- FUNCTION: Catalyzes the phosphorylation of nicotinamide riboside (NR)
CC and nicotinic acid riboside (NaR) to form nicotinamide mononucleotide
CC (NMN) and nicotinic acid mononucleotide (NaMN). The enzyme also
CC phosphorylates the antitumor drugs tiazofurin and 3-deazaguanosine.
CC {ECO:0000269|PubMed:15137942}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + beta-nicotinamide D-riboside = ADP + beta-nicotinamide
CC D-ribonucleotide + H(+); Xref=Rhea:RHEA:14017, ChEBI:CHEBI:14649,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15927, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:456216; EC=2.7.1.22;
CC Evidence={ECO:0000269|PubMed:17914902, ECO:0000269|PubMed:8809081};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + beta-D-ribosylnicotinate = ADP + H(+) + nicotinate beta-
CC D-ribonucleotide; Xref=Rhea:RHEA:25568, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:57502, ChEBI:CHEBI:58527,
CC ChEBI:CHEBI:456216; EC=2.7.1.173;
CC Evidence={ECO:0000269|PubMed:17914902, ECO:0000269|PubMed:8809081};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.088 mM for nicotinamide riboside (with ATP as cosubstrate)
CC {ECO:0000269|PubMed:17914902, ECO:0000269|PubMed:8809081};
CC KM=0.068 mM for nicotinamide riboside (with GTP as cosubstrate)
CC {ECO:0000269|PubMed:17914902, ECO:0000269|PubMed:8809081};
CC KM=0.27 mM for tiazofurin (with ATP as cosubstrate)
CC {ECO:0000269|PubMed:17914902, ECO:0000269|PubMed:8809081};
CC KM=0.051 mM for nicotinic acid riboside (with ATP as cosubstrate)
CC {ECO:0000269|PubMed:17914902, ECO:0000269|PubMed:8809081};
CC KM=17 mM for uridine (with ATP as cosubstrate)
CC {ECO:0000269|PubMed:17914902, ECO:0000269|PubMed:8809081};
CC pH dependence:
CC Optimum pH is 6.5-9. {ECO:0000269|PubMed:17914902,
CC ECO:0000269|PubMed:8809081};
CC -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis.
CC {ECO:0000305|PubMed:17914902}.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:8809081}.
CC -!- INTERACTION:
CC Q9NWW6; Q0VD86: INCA1; NbExp=3; IntAct=EBI-10315485, EBI-6509505;
CC Q9NWW6; Q4G0X4: KCTD21; NbExp=3; IntAct=EBI-10315485, EBI-11976683;
CC Q9NWW6; Q04864-2: REL; NbExp=3; IntAct=EBI-10315485, EBI-10829018;
CC Q9NWW6; Q86VP1: TAX1BP1; NbExp=6; IntAct=EBI-10315485, EBI-529518;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9NWW6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NWW6-2; Sequence=VSP_012676;
CC -!- SIMILARITY: Belongs to the uridine kinase family. NRK subfamily.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY611480; AAT11928.1; -; mRNA.
DR EMBL; AK000566; BAA91259.1; -; mRNA.
DR EMBL; AL133548; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471089; EAW62568.1; -; Genomic_DNA.
DR EMBL; BC001366; AAH01366.1; -; mRNA.
DR EMBL; BC036804; AAH36804.1; -; mRNA.
DR CCDS; CCDS47981.1; -. [Q9NWW6-2]
DR CCDS; CCDS6650.1; -. [Q9NWW6-1]
DR RefSeq; NP_001121075.1; NM_001127603.1. [Q9NWW6-2]
DR RefSeq; NP_001317607.1; NM_001330678.1.
DR RefSeq; NP_060351.1; NM_017881.2. [Q9NWW6-1]
DR RefSeq; XP_006717226.1; XM_006717163.2. [Q9NWW6-1]
DR RefSeq; XP_016870359.1; XM_017014870.1. [Q9NWW6-1]
DR RefSeq; XP_016870363.1; XM_017014874.1. [Q9NWW6-2]
DR PDB; 2P0E; X-ray; 1.80 A; A=2-189.
DR PDB; 2QG6; X-ray; 1.50 A; A=1-199.
DR 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.
DR PDB; 2QSY; X-ray; 1.95 A; A=2-189.
DR PDB; 2QSZ; X-ray; 1.90 A; A=2-189.
DR PDB; 2QT0; X-ray; 1.92 A; A=2-189.
DR PDB; 2QT1; X-ray; 1.32 A; A=2-189.
DR PDBsum; 2P0E; -.
DR PDBsum; 2QG6; -.
DR PDBsum; 2QL6; -.
DR PDBsum; 2QSY; -.
DR PDBsum; 2QSZ; -.
DR PDBsum; 2QT0; -.
DR PDBsum; 2QT1; -.
DR AlphaFoldDB; Q9NWW6; -.
DR SMR; Q9NWW6; -.
DR BioGRID; 120317; 6.
DR IntAct; Q9NWW6; 4.
DR STRING; 9606.ENSP00000354387; -.
DR iPTMnet; Q9NWW6; -.
DR PhosphoSitePlus; Q9NWW6; -.
DR BioMuta; NMRK1; -.
DR DMDM; 50401180; -.
DR EPD; Q9NWW6; -.
DR jPOST; Q9NWW6; -.
DR MassIVE; Q9NWW6; -.
DR MaxQB; Q9NWW6; -.
DR PaxDb; Q9NWW6; -.
DR PeptideAtlas; Q9NWW6; -.
DR PRIDE; Q9NWW6; -.
DR ProteomicsDB; 82992; -. [Q9NWW6-1]
DR ProteomicsDB; 82993; -. [Q9NWW6-2]
DR Antibodypedia; 27143; 185 antibodies from 23 providers.
DR DNASU; 54981; -.
DR Ensembl; ENST00000361092.9; ENSP00000354387.4; ENSG00000106733.21. [Q9NWW6-1]
DR Ensembl; ENST00000376808.8; ENSP00000366004.4; ENSG00000106733.21. [Q9NWW6-2]
DR GeneID; 54981; -.
DR KEGG; hsa:54981; -.
DR MANE-Select; ENST00000361092.9; ENSP00000354387.4; NM_017881.3; NP_060351.1.
DR UCSC; uc004ajr.5; human. [Q9NWW6-1]
DR CTD; 54981; -.
DR DisGeNET; 54981; -.
DR GeneCards; NMRK1; -.
DR HGNC; HGNC:26057; NMRK1.
DR HPA; ENSG00000106733; Low tissue specificity.
DR MIM; 608704; gene.
DR neXtProt; NX_Q9NWW6; -.
DR OpenTargets; ENSG00000106733; -.
DR PharmGKB; PA134946592; -.
DR VEuPathDB; HostDB:ENSG00000106733; -.
DR eggNOG; KOG3308; Eukaryota.
DR GeneTree; ENSGT00940000159384; -.
DR HOGENOM; CLU_058668_0_0_1; -.
DR InParanoid; Q9NWW6; -.
DR OMA; NCSRIEY; -.
DR PhylomeDB; Q9NWW6; -.
DR TreeFam; TF105395; -.
DR BRENDA; 2.7.1.173; 2681.
DR BRENDA; 2.7.1.22; 2681.
DR PathwayCommons; Q9NWW6; -.
DR Reactome; R-HSA-196807; Nicotinate metabolism.
DR SignaLink; Q9NWW6; -.
DR UniPathway; UPA00253; -.
DR BioGRID-ORCS; 54981; 10 hits in 1073 CRISPR screens.
DR ChiTaRS; NMRK1; human.
DR EvolutionaryTrace; Q9NWW6; -.
DR GenomeRNAi; 54981; -.
DR Pharos; Q9NWW6; Tbio.
DR PRO; PR:Q9NWW6; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q9NWW6; protein.
DR Bgee; ENSG00000106733; Expressed in cervix squamous epithelium and 199 other tissues.
DR ExpressionAtlas; Q9NWW6; baseline and differential.
DR Genevisible; Q9NWW6; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0050262; F:ribosylnicotinamide kinase activity; EXP:Reactome.
DR GO; GO:0061769; F:ribosylnicotinate kinase activity; EXP:Reactome.
DR GO; GO:0009435; P:NAD biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0019674; P:NAD metabolic process; TAS:Reactome.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; ATP-binding; Kinase; Magnesium;
KW Metal-binding; Nucleotide-binding; Pyridine nucleotide biosynthesis;
KW Reference proteome; Transferase.
FT CHAIN 1..199
FT /note="Nicotinamide riboside kinase 1"
FT /id="PRO_0000215891"
FT ACT_SITE 36
FT /note="Proton acceptor"
FT /evidence="ECO:0000269|PubMed:17914902,
FT ECO:0007744|PDB:2QT0"
FT BINDING 10..18
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:17698003,
FT ECO:0000269|PubMed:17914902, ECO:0007744|PDB:2P0E,
FT ECO:0007744|PDB:2QG6, ECO:0007744|PDB:2QL6,
FT ECO:0007744|PDB:2QSY, ECO:0007744|PDB:2QSZ,
FT ECO:0007744|PDB:2QT0, ECO:0007744|PDB:2QT1"
FT BINDING 17
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:17914902,
FT ECO:0007744|PDB:2QSY"
FT BINDING 36..39
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:17698003,
FT ECO:0000269|PubMed:17914902, ECO:0007744|PDB:2P0E,
FT ECO:0007744|PDB:2QL6, ECO:0007744|PDB:2QT0,
FT ECO:0007744|PDB:2QT1"
FT BINDING 36
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:17914902,
FT ECO:0007744|PDB:2QT0"
FT BINDING 55..56
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:17698003,
FT ECO:0000269|PubMed:17914902, ECO:0007744|PDB:2P0E,
FT ECO:0007744|PDB:2QL6, ECO:0007744|PDB:2QT0,
FT ECO:0007744|PDB:2QT1"
FT BINDING 128
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:17914902,
FT ECO:0007744|PDB:2P0E"
FT BINDING 129
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:17914902,
FT ECO:0007744|PDB:2P0E, ECO:0007744|PDB:2QL6,
FT ECO:0007744|PDB:2QT0, ECO:0007744|PDB:2QT1"
FT BINDING 132..134
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:17698003,
FT ECO:0000269|PubMed:17914902, ECO:0007744|PDB:2P0E,
FT ECO:0007744|PDB:2QG6, ECO:0007744|PDB:2QSY,
FT ECO:0007744|PDB:2QSZ, ECO:0007744|PDB:2QT0,
FT ECO:0007744|PDB:2QT1"
FT BINDING 134..135
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:17698003,
FT ECO:0000269|PubMed:17914902, ECO:0007744|PDB:2P0E,
FT ECO:0007744|PDB:2QL6, ECO:0007744|PDB:2QT0"
FT BINDING 172..174
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:17914902,
FT ECO:0007744|PDB:2QSY, ECO:0007744|PDB:2QT0"
FT VAR_SEQ 106..130
FT /note="KPLDTIWNRSYFLTIPYEECKRRRS -> N (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_012676"
FT MUTAGEN 16
FT /note="K->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:17698003"
FT MUTAGEN 36
FT /note="D->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:17698003,
FT ECO:0000269|PubMed:17914902"
FT MUTAGEN 56
FT /note="D->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:17698003"
FT MUTAGEN 98
FT /note="E->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:17914902"
FT MUTAGEN 138
FT /note="D->A: Almost no effect."
FT /evidence="ECO:0000269|PubMed:17698003"
FT STRAND 4..11
FT /evidence="ECO:0007829|PDB:2QT1"
FT HELIX 16..24
FT /evidence="ECO:0007829|PDB:2QT1"
FT STRAND 30..34
FT /evidence="ECO:0007829|PDB:2QT1"
FT HELIX 35..38
FT /evidence="ECO:0007829|PDB:2QT1"
FT HELIX 42..44
FT /evidence="ECO:0007829|PDB:2QT1"
FT HELIX 58..60
FT /evidence="ECO:0007829|PDB:2QT1"
FT HELIX 63..77
FT /evidence="ECO:0007829|PDB:2QT1"
FT STRAND 94..98
FT /evidence="ECO:0007829|PDB:2QT1"
FT HELIX 106..108
FT /evidence="ECO:0007829|PDB:2QT1"
FT TURN 109..111
FT /evidence="ECO:0007829|PDB:2QT1"
FT STRAND 113..119
FT /evidence="ECO:0007829|PDB:2QT1"
FT HELIX 122..131
FT /evidence="ECO:0007829|PDB:2QT1"
FT HELIX 142..145
FT /evidence="ECO:0007829|PDB:2QT1"
FT HELIX 147..157
FT /evidence="ECO:0007829|PDB:2QT1"
FT HELIX 158..160
FT /evidence="ECO:0007829|PDB:2QT1"
FT STRAND 166..169
FT /evidence="ECO:0007829|PDB:2QT1"
FT HELIX 174..185
FT /evidence="ECO:0007829|PDB:2QT1"
FT TURN 186..188
FT /evidence="ECO:0007829|PDB:2QT1"
SQ 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
