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Q6XQN6 (PNCB_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 81. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Nicotinate phosphoribosyltransferase

Short name=NAPRTase
EC=6.3.4.21
Alternative name(s):
FHA-HIT-interacting protein
Nicotinate phosphoribosyltransferase domain-containing protein 1
Gene names
Name:NAPRT1
Synonyms:FHIP
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length538 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.1

Catalyzes the synthesis of beta-nicotinate D-ribonucleotide from nicotinate and 5-phospho-D-ribose 1-phosphate at the expense of ATP By similarity. Ref.1

Catalytic activity

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

Pathway

Cofactor biosynthesis; NAD(+) biosynthesis; nicotinate D-ribonucleotide from nicotinate: step 1/1.

Subcellular location

Cytoplasmcytosol Ref.1.

Sequence similarities

Belongs to the NAPRTase family.

Biophysicochemical properties

Kinetic parameters:

KM=44.3 µM for nicotinic acid (in the presence of 3mM ATP) Ref.10

KM=22.1 µM for 5-phosphoribosyl-1-pyrophosphate (in the presence of 3mM ATP)

KM=27.3 µM for nicotinic acid (in the presence of inorganic phosphate)

KM=38.2 µM for 5-phosphoribosyl-1-pyrophosphate (in the presence of inorganic phosphate)

Sequence caution

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

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

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q6XQN6-1)

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.
Isoform 2 (identifier: Q6XQN6-2)

The sequence of this isoform differs from the canonical sequence as follows:
     517-517: Y → YQVGGGGPPCHSALCAPALTLPTAPVLCSL
Note: No experimental confirmation available.
Isoform 3 (identifier: Q6XQN6-3)

The sequence of this isoform differs from the canonical sequence as follows:
     469-481: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 538538Nicotinate phosphoribosyltransferase
PRO_0000315681

Amino acid modifications

Modified residue5371Phosphoserine Ref.4 Ref.5 Ref.6 Ref.7 Ref.9

Natural variations

Alternative sequence469 – 48113Missing in isoform 3.
VSP_030610
Alternative sequence5171Y → YQVGGGGPPCHSALCAPALT LPTAPVLCSL in isoform 2.
VSP_030612
Natural variant571A → V.
Corresponds to variant rs896950 [ dbSNP | Ensembl ].
VAR_038275

Experimental info

Mutagenesis191D → A: Complete loss of activity. Ref.10
Mutagenesis211Y → A: Partial loss of activity in the presence of ATP, complete loss in the absence of ATP. Ref.10
Mutagenesis1691G → A: Partial loss of activity. Ref.10
Mutagenesis2091G → A: Partial loss of activity. Ref.10
Mutagenesis2131H → A: Partial loss of activity. Ref.10
Mutagenesis2881D → A: Partial loss of activity. Ref.10
Mutagenesis3181R → A: Partial loss of activity in the presence of ATP, almost complete loss in the absence of ATP. Ref.10
Mutagenesis3571N → A: Small loss of activity. Ref.10
Mutagenesis3791G → A: Complete loss of activity. Ref.10
Mutagenesis3801T → A: Partial loss of activity. Ref.10
Mutagenesis3811S → A: Partial loss of activity. Ref.10
Sequence conflict1551L → V in AAP69603. Ref.2
Sequence conflict1551L → V in AAP69604. Ref.2
Sequence conflict1551L → V in AAP69605. Ref.2
Sequence conflict2241V → A in BAF75377. Ref.1
Sequence conflict2461A → T in BAF75377. Ref.1
Sequence conflict3751V → A in BAF75377. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified January 15, 2008. Version 2.
Checksum: 26DF39885CBB1C9B

FASTA53857,578
        10         20         30         40         50         60 
MAAEQDPEAR AAARPLLTDL YQATMALGYW RAGRARDAAE FELFFRRCPF GGAFALAAGL 

        70         80         90        100        110        120 
RDCVRFLRAF RLRDADVQFL ASVLPPDTDP AFFEHLRALD CSEVTVRALP EGSLAFPGVP 

       130        140        150        160        170        180 
LLQVSGPLLV VQLLETPLLC LVSYASLVAT NAARLRLIAG PEKRLLEMGL RRAQGPDGGL 

       190        200        210        220        230        240 
TASTYSYLGG FDSSSNVLAG QLRGVPVAGT LAHSFVTSFS GSEVPPDPML APAAGEGPGV 

       250        260        270        280        290        300 
DLAAKAQVWL EQVCAHLGLG VQEPHPGERA AFVAYALAFP RAFQGLLDTY SVWRSGLPNF 

       310        320        330        340        350        360 
LAVALALGEL GYRAVGVRLD SGDLLQQAQE IRKVFRAAAA QFQVPWLESV LIVVSNNIDE 

       370        380        390        400        410        420 
EALARLAQEG SEVNVIGIGT SVVTCPQQPS LGGVYKLVAV GGQPRMKLTE DPEKQTLPGS 

       430        440        450        460        470        480 
KAAFRLLGSD GSPLMDMLQL AEEPVPQAGQ ELRVWPPGAQ EPCTVRPAQV EPLLRLCLQQ 

       490        500        510        520        530 
GQLCEPLPSL AESRALAQLS LSRLSPEHRR LRSPAQYQVV LSERLQALVN SLCAGQSP 

« Hide

Isoform 2 [UniParc].

Checksum: 3FFE59FEFD270DF9
Show »

FASTA56760,291
Isoform 3 [UniParc].

Checksum: E18F7E02CB00ABF4
Show »

FASTA52556,099

References

« Hide 'large scale' references
[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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_001273758.1. NM_001286829.1.
NP_660202.3. NM_145201.5.
UniGeneHs.493164.

3D structure databases

ProteinModelPortalQ6XQN6.
SMRQ6XQN6. Positions 16-522.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid125001. 9 interactions.
STRING9606.ENSP00000401508.

PTM databases

PhosphoSiteQ6XQN6.

Polymorphism databases

DMDM166221824.

Proteomic databases

PaxDbQ6XQN6.
PRIDEQ6XQN6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000426292; ENSP00000390949; ENSG00000147813. [Q6XQN6-3]
ENST00000449291; ENSP00000401508; ENSG00000147813. [Q6XQN6-1]
GeneID93100.
KEGGhsa:93100.
UCSCuc003yym.4. human. [Q6XQN6-1]
uc003yyn.4. human. [Q6XQN6-3]

Organism-specific databases

CTD93100.
GeneCardsGC08M144656.
HGNCHGNC:30450. NAPRT1.
HPAHPA023739.
HPA024017.
MIM611552. gene.
neXtProtNX_Q6XQN6.
PharmGKBPA142671293.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1488.
HOVERGENHBG062439.
InParanoidQ6XQN6.
KOK00763.
PhylomeDBQ6XQN6.
TreeFamTF314732.

Enzyme and pathway databases

BRENDA2.4.2.11. 2681.
ReactomeREACT_111217. Metabolism.
REACT_116125. Disease.
UniPathwayUPA00253; UER00457.

Gene expression databases

ArrayExpressQ6XQN6.
BgeeQ6XQN6.
CleanExHS_NAPRT1.
GenevestigatorQ6XQN6.

Family and domain databases

InterProIPR007229. Nic_PRibTrfase-Fam.
IPR006405. Nic_PRibTrfase_pncB.
IPR002638. Quinolinate_PRibosylTrfase_C.
[Graphical view]
PfamPF04095. NAPRTase. 2 hits.
[Graphical view]
PIRSFPIRSF000484. NAPRT. 1 hit.
SUPFAMSSF51690. SSF51690. 2 hits.
TIGRFAMsTIGR01513. NAPRTase_put. 1 hit.
ProtoNetSearch...

Other

ChiTaRSNAPRT1. human.
GenomeRNAi93100.
NextBio77980.
PROQ6XQN6.
SOURCESearch...

Entry information

Entry namePNCB_HUMAN
AccessionPrimary (citable) accession number: Q6XQN6
Secondary accession number(s): A7BFI3 expand/collapse secondary AC list , Q6PJL1, Q6XQN4, Q6XQN5, Q8N5E8, Q9BRG0
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: January 15, 2008
Last modified: April 16, 2014
This is version 81 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 8

Human chromosome 8: entries, gene names and cross-references to MIM