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Protein

Nicotinate phosphoribosyltransferase

Gene

NAPRT

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the conversion of nicotinic acid (NA) to NA mononucleotide (NaMN). Essential for NA to increase cellular NAD levels and prevent oxidative stress of the cells.1 Publication
Catalyzes the synthesis of beta-nicotinate D-ribonucleotide from nicotinate and 5-phospho-D-ribose 1-phosphate at the expense of ATP.By similarity

Catalytic activityi

Nicotinate + 5-phospho-alpha-D-ribose 1-diphosphate + ATP + H2O = beta-nicotinate D-ribonucleotide + diphosphate + ADP + phosphate.

Kineticsi

  1. KM=44.3 µM for nicotinic acid (in the presence of 3mM ATP)1 Publication
  2. KM=22.1 µM for 5-phosphoribosyl-1-pyrophosphate (in the presence of 3mM ATP)1 Publication
  3. KM=27.3 µM for nicotinic acid (in the presence of inorganic phosphate)1 Publication
  4. KM=38.2 µM for 5-phosphoribosyl-1-pyrophosphate (in the presence of inorganic phosphate)1 Publication

    Pathway: NAD(+) biosynthesis

    This protein is involved in step 1 of the subpathway that synthesizes nicotinate D-ribonucleotide from nicotinate.
    Proteins known to be involved in this subpathway in this organism are:
    1. Nicotinate phosphoribosyltransferase (NAPRT)
    This subpathway is part of the pathway NAD(+) biosynthesis, which is itself part of Cofactor biosynthesis.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes nicotinate D-ribonucleotide from nicotinate, the pathway NAD(+) biosynthesis and in Cofactor biosynthesis.

    GO - Molecular functioni

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Ligase, Transferase

    Keywords - Biological processi

    Pyridine nucleotide biosynthesis

    Enzyme and pathway databases

    BRENDAi6.3.4.21. 2681.
    ReactomeiREACT_11213. Nicotinamide salvaging.
    UniPathwayiUPA00253; UER00457.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Nicotinate phosphoribosyltransferase (EC:6.3.4.21)
    Short name:
    NAPRTase
    Alternative name(s):
    FHA-HIT-interacting protein
    Nicotinate phosphoribosyltransferase domain-containing protein 1
    Gene namesi
    Name:NAPRT
    Synonyms:FHIP, NAPRT1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640 Componentsi: Chromosome 8, Unplaced

    Organism-specific databases

    HGNCiHGNC:30450. NAPRT.

    Subcellular locationi

    GO - Cellular componenti

    • cytoplasm Source: HPA
    • cytosol Source: UniProtKB
    • extracellular exosome Source: UniProtKB
    • Golgi apparatus Source: HPA
    • nucleoplasm Source: HPA
    • nucleus Source: HPA
    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi19 – 191D → A: Complete loss of activity. 1 Publication
    Mutagenesisi21 – 211Y → A: Partial loss of activity in the presence of ATP, complete loss in the absence of ATP. 1 Publication
    Mutagenesisi169 – 1691G → A: Partial loss of activity. 1 Publication
    Mutagenesisi209 – 2091G → A: Partial loss of activity. 1 Publication
    Mutagenesisi213 – 2131H → A: Partial loss of activity. 1 Publication
    Mutagenesisi288 – 2881D → A: Partial loss of activity. 1 Publication
    Mutagenesisi318 – 3181R → A: Partial loss of activity in the presence of ATP, almost complete loss in the absence of ATP. 1 Publication
    Mutagenesisi357 – 3571N → A: Small loss of activity. 1 Publication
    Mutagenesisi379 – 3791G → A: Complete loss of activity. 1 Publication
    Mutagenesisi380 – 3801T → A: Partial loss of activity. 1 Publication
    Mutagenesisi381 – 3811S → A: Partial loss of activity. 1 Publication

    Organism-specific databases

    PharmGKBiPA142671293.

    Polymorphism and mutation databases

    DMDMi166221824.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 538538Nicotinate phosphoribosyltransferasePRO_0000315681Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei537 – 5371Phosphoserine6 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ6XQN6.
    PaxDbiQ6XQN6.
    PRIDEiQ6XQN6.

    PTM databases

    PhosphoSiteiQ6XQN6.

    Expressioni

    Gene expression databases

    BgeeiQ6XQN6.
    CleanExiHS_NAPRT1.
    ExpressionAtlasiQ6XQN6. baseline and differential.
    GenevisibleiQ6XQN6. HS.

    Organism-specific databases

    HPAiCAB068206.
    CAB068207.
    HPA023739.
    HPA024017.

    Interactioni

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CCDC57Q2TAC23EBI-10254820,EBI-2808286
    EHMT2A2ABF93EBI-10254820,EBI-10174566
    GRAMD3Q96HH93EBI-10254872,EBI-2832937
    KRT40Q6A1623EBI-10254820,EBI-10171697
    RBPMSQ930623EBI-10254872,EBI-740322

    Protein-protein interaction databases

    BioGridi125001. 14 interactions.
    IntActiQ6XQN6. 5 interactions.
    STRINGi9606.ENSP00000401508.

    Structurei

    3D structure databases

    ProteinModelPortaliQ6XQN6.
    SMRiQ6XQN6. Positions 16-522.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the NAPRTase family.Curated

    Phylogenomic databases

    eggNOGiCOG1488.
    GeneTreeiENSGT00390000002664.
    HOVERGENiHBG062439.
    InParanoidiQ6XQN6.
    KOiK00763.
    PhylomeDBiQ6XQN6.
    TreeFamiTF314732.

    Family and domain databases

    InterProiIPR007229. Nic_PRibTrfase-Fam.
    IPR006405. Nic_PRibTrfase_pncB.
    IPR002638. Quinolinate_PRibosylTrfase_C.
    [Graphical view]
    PANTHERiPTHR11098. PTHR11098. 1 hit.
    PfamiPF04095. NAPRTase. 2 hits.
    [Graphical view]
    PIRSFiPIRSF000484. NAPRT. 1 hit.
    SUPFAMiSSF51690. SSF51690. 2 hits.
    TIGRFAMsiTIGR01513. NAPRTase_put. 1 hit.

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

    Isoform 1 (identifier: Q6XQN6-1) [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

            10         20         30         40         50
    MAAEQDPEAR AAARPLLTDL YQATMALGYW RAGRARDAAE FELFFRRCPF
    60 70 80 90 100
    GGAFALAAGL RDCVRFLRAF RLRDADVQFL ASVLPPDTDP AFFEHLRALD
    110 120 130 140 150
    CSEVTVRALP EGSLAFPGVP LLQVSGPLLV VQLLETPLLC LVSYASLVAT
    160 170 180 190 200
    NAARLRLIAG PEKRLLEMGL RRAQGPDGGL TASTYSYLGG FDSSSNVLAG
    210 220 230 240 250
    QLRGVPVAGT LAHSFVTSFS GSEVPPDPML APAAGEGPGV DLAAKAQVWL
    260 270 280 290 300
    EQVCAHLGLG VQEPHPGERA AFVAYALAFP RAFQGLLDTY SVWRSGLPNF
    310 320 330 340 350
    LAVALALGEL GYRAVGVRLD SGDLLQQAQE IRKVFRAAAA QFQVPWLESV
    360 370 380 390 400
    LIVVSNNIDE EALARLAQEG SEVNVIGIGT SVVTCPQQPS LGGVYKLVAV
    410 420 430 440 450
    GGQPRMKLTE DPEKQTLPGS KAAFRLLGSD GSPLMDMLQL AEEPVPQAGQ
    460 470 480 490 500
    ELRVWPPGAQ EPCTVRPAQV EPLLRLCLQQ GQLCEPLPSL AESRALAQLS
    510 520 530
    LSRLSPEHRR LRSPAQYQVV LSERLQALVN SLCAGQSP
    Length:538
    Mass (Da):57,578
    Last modified:January 15, 2008 - v2
    Checksum:i26DF39885CBB1C9B
    GO
    Isoform 2 (identifier: Q6XQN6-2) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         517-517: Y → YQVGGGGPPCHSALCAPALTLPTAPVLCSL

    Note: No experimental confirmation available.
    Show »
    Length:567
    Mass (Da):60,291
    Checksum:i3FFE59FEFD270DF9
    GO
    Isoform 3 (identifier: Q6XQN6-3) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         469-481: Missing.

    Note: No experimental confirmation available.
    Show »
    Length:525
    Mass (Da):56,099
    Checksum:iE18F7E02CB00ABF4
    GO

    Sequence cautioni

    The sequence AAH06284.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
    The sequence AAH32466.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti155 – 1551L → V in AAP69603 (Ref. 2) Curated
    Sequence conflicti155 – 1551L → V in AAP69604 (Ref. 2) Curated
    Sequence conflicti155 – 1551L → V in AAP69605 (Ref. 2) Curated
    Sequence conflicti224 – 2241V → A in BAF75377 (PubMed:17604275).Curated
    Sequence conflicti246 – 2461A → T in BAF75377 (PubMed:17604275).Curated
    Sequence conflicti375 – 3751V → A in BAF75377 (PubMed:17604275).Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti57 – 571A → V.
    Corresponds to variant rs896950 [ dbSNP | Ensembl ].
    VAR_038275

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei469 – 48113Missing in isoform 3. 1 PublicationVSP_030610Add
    BLAST
    Alternative sequencei517 – 5171Y → YQVGGGGPPCHSALCAPALT LPTAPVLCSL in isoform 2. 1 PublicationVSP_030612

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AB242230 mRNA. Translation: BAF75377.1.
    AY214325 mRNA. Translation: AAP69603.1.
    AY214326 mRNA. Translation: AAP69604.1.
    AY214327 mRNA. Translation: AAP69605.1.
    BC006284 mRNA. Translation: AAH06284.2. Different initiation.
    BC032466 mRNA. Translation: AAH32466.1. Different initiation.
    CCDSiCCDS6403.2. [Q6XQN6-1]
    CCDS69555.1. [Q6XQN6-3]
    RefSeqiNP_001273758.1. NM_001286829.1. [Q6XQN6-3]
    NP_660202.3. NM_145201.5. [Q6XQN6-1]
    UniGeneiHs.493164.

    Genome annotation databases

    EnsembliENST00000426292; ENSP00000390949; ENSG00000147813. [Q6XQN6-3]
    ENST00000449291; ENSP00000401508; ENSG00000147813. [Q6XQN6-1]
    ENST00000621955; ENSP00000480017; ENSG00000278488. [Q6XQN6-1]
    GeneIDi93100.
    KEGGihsa:93100.
    UCSCiuc003yym.4. human. [Q6XQN6-1]
    uc003yyn.4. human. [Q6XQN6-3]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AB242230 mRNA. Translation: BAF75377.1.
    AY214325 mRNA. Translation: AAP69603.1.
    AY214326 mRNA. Translation: AAP69604.1.
    AY214327 mRNA. Translation: AAP69605.1.
    BC006284 mRNA. Translation: AAH06284.2. Different initiation.
    BC032466 mRNA. Translation: AAH32466.1. Different initiation.
    CCDSiCCDS6403.2. [Q6XQN6-1]
    CCDS69555.1. [Q6XQN6-3]
    RefSeqiNP_001273758.1. NM_001286829.1. [Q6XQN6-3]
    NP_660202.3. NM_145201.5. [Q6XQN6-1]
    UniGeneiHs.493164.

    3D structure databases

    ProteinModelPortaliQ6XQN6.
    SMRiQ6XQN6. Positions 16-522.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi125001. 14 interactions.
    IntActiQ6XQN6. 5 interactions.
    STRINGi9606.ENSP00000401508.

    PTM databases

    PhosphoSiteiQ6XQN6.

    Polymorphism and mutation databases

    DMDMi166221824.

    Proteomic databases

    MaxQBiQ6XQN6.
    PaxDbiQ6XQN6.
    PRIDEiQ6XQN6.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000426292; ENSP00000390949; ENSG00000147813. [Q6XQN6-3]
    ENST00000449291; ENSP00000401508; ENSG00000147813. [Q6XQN6-1]
    ENST00000621955; ENSP00000480017; ENSG00000278488. [Q6XQN6-1]
    GeneIDi93100.
    KEGGihsa:93100.
    UCSCiuc003yym.4. human. [Q6XQN6-1]
    uc003yyn.4. human. [Q6XQN6-3]

    Organism-specific databases

    CTDi93100.
    GeneCardsiGC08M144656.
    HGNCiHGNC:30450. NAPRT.
    HPAiCAB068206.
    CAB068207.
    HPA023739.
    HPA024017.
    MIMi611552. gene.
    neXtProtiNX_Q6XQN6.
    PharmGKBiPA142671293.
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiCOG1488.
    GeneTreeiENSGT00390000002664.
    HOVERGENiHBG062439.
    InParanoidiQ6XQN6.
    KOiK00763.
    PhylomeDBiQ6XQN6.
    TreeFamiTF314732.

    Enzyme and pathway databases

    UniPathwayiUPA00253; UER00457.
    BRENDAi6.3.4.21. 2681.
    ReactomeiREACT_11213. Nicotinamide salvaging.

    Miscellaneous databases

    ChiTaRSiFAM160A2. human.
    GenomeRNAii93100.
    NextBioi77980.
    PROiQ6XQN6.
    SOURCEiSearch...

    Gene expression databases

    BgeeiQ6XQN6.
    CleanExiHS_NAPRT1.
    ExpressionAtlasiQ6XQN6. baseline and differential.
    GenevisibleiQ6XQN6. HS.

    Family and domain databases

    InterProiIPR007229. Nic_PRibTrfase-Fam.
    IPR006405. Nic_PRibTrfase_pncB.
    IPR002638. Quinolinate_PRibosylTrfase_C.
    [Graphical view]
    PANTHERiPTHR11098. PTHR11098. 1 hit.
    PfamiPF04095. NAPRTase. 2 hits.
    [Graphical view]
    PIRSFiPIRSF000484. NAPRT. 1 hit.
    SUPFAMiSSF51690. SSF51690. 2 hits.
    TIGRFAMsiTIGR01513. NAPRTase_put. 1 hit.
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Elevation of cellular NAD levels by nicotinic acid and involvement of nicotinic acid phosphoribosyltransferase in human cells."
      Hara N., Yamada K., Shibata T., Osago H., Hashimoto T., Tsuchiya M.
      J. Biol. Chem. 282:24574-24582(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION.
    2. "Identification of nicotinate phosphoribosyltransferase as a novel FHA-HIT interaction protein (FHIP)."
      Huang C.-H., Chen H., Chen Y.
      Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3).
    3. "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] (ISOFORM 1).
      Tissue: Placenta.
    4. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-537, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    5. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
      Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
      Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-537, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-537, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    7. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-537, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    9. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-537, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    10. "Characterization of human nicotinate phosphoribosyltransferase: Kinetic studies, structure prediction and functional analysis by site-directed mutagenesis."
      Galassi L., Di Stefano M., Brunetti L., Orsomando G., Amici A., Ruggieri S., Magni G.
      Biochimie 94:300-309(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: BIOPHYSICOCHEMICAL PROPERTIES, CHARACTERIZATION, 3D-STRUCTURE MODELING, MUTAGENESIS OF ASP-19; TYR-21; GLY-169; GLY-209; HIS-213; ASP-288; ARG-318; ASN-357; GLY-379; THR-380 AND SER-381.
    11. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
      Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
      J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-537, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.

    Entry informationi

    Entry nameiPNCB_HUMAN
    AccessioniPrimary (citable) accession number: Q6XQN6
    Secondary accession number(s): A7BFI3
    , Q6PJL1, Q6XQN4, Q6XQN5, Q8N5E8, Q9BRG0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 15, 2008
    Last sequence update: January 15, 2008
    Last modified: June 24, 2015
    This is version 95 of the entry and version 2 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 8
      Human chromosome 8: 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

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.