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Reviewed, UniProtKB/Swiss-Prot P00491 (PNPH_HUMAN)

Last modified June 16, 2009. Version 108. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Purine nucleoside phosphorylase
      Short name=PNP
    EC=2.4.2.1
Alternative name(s):
    Inosine phosphorylase
Gene names
Name: NP
Synonyms: PNP
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length289 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Catalytic activity

Purine nucleoside + phosphate = purine + alpha-D-ribose 1-phosphate.

Subunit structure

Homotrimer.

Involvement in disease

Defects in NP are the cause of nucleoside phosphorylase deficiency (NP deficiency) [MIM:164050]. It leads to a severe T-cell immunodeficiency with neurologic disorder in children.

Sequence similarities

Belongs to the PNP/MTAP phosphorylase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 289289Purine nucleoside phosphorylase
PRO_0000184536

Amino acid modifications

Modified residue11N-acetylmethionine Ref.7

Natural variations

Natural variant511G → S: dbSNP rs1049564. Ref.1 Ref.2 Ref.3 Ref.4 Ref.10
VAR_002243
Natural variant891E → K in NP deficiency.
VAR_002244
Natural variant1281D → G in NP deficiency.
VAR_002245
Natural variant1741A → P in NP deficiency.
VAR_002246
Natural variant1921Y → C in NP deficiency.
VAR_010653
Natural variant2341R → P in NP deficiency.
VAR_002247

Secondary structure

............................................. 289
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P00491-1 [UniParc].

Last modified May 30, 2006. Version 2.
Checksum: 91622FB1D26479D3

FASTA28932,118
        10         20         30         40         50         60 
MENGYTYEDY KNTAEWLLSH TKHRPQVAII CGSGLGGLTD KLTQAQIFDY GEIPNFPRST 

        70         80         90        100        110        120 
VPGHAGRLVF GFLNGRACVM MQGRFHMYEG YPLWKVTFPV RVFHLLGVDT LVVTNAAGGL 

       130        140        150        160        170        180 
NPKFEVGDIM LIRDHINLPG FSGQNPLRGP NDERFGDRFP AMSDAYDRTM RQRALSTWKQ 

       190        200        210        220        230        240 
MGEQRELQEG TYVMVAGPSF ETVAECRVLQ KLGADAVGMS TVPEVIVARH CGLRVFGFSL 

       250        260        270        280 
ITNKVIMDYE SLEKANHEEV LAAGKQAAQK LEQFVSILMA SIPLPDKAS 

« Hide

References

« Hide 'large scale' references
[1]"Human purine nucleoside phosphorylase cDNA sequence and genomic clone characterization."
Williams S.R., Goddard J.M., Martin D.W. Jr.
Nucleic Acids Res. 12:5779-5787(1984) [PubMed: 6087295] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT SER-51.
[2]"A human purine nucleoside phosphorylase deficiency caused by a single base change."
Williams S.R., Gekeler V., McIvor R.S., Martin D.W. Jr.
J. Biol. Chem. 262:2332-2338(1987) [PubMed: 3029074] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT NP DEFICIENCY LYS-89, VARIANT SER-51.
[3]"Genetic variation in genes associated with arsenic metabolism: glutathione S-transferase omega 1-1 and purine nucleoside phosphorylase polymorphisms in European and indigenous Americans."
Yu L., Kalla K., Guthrie E., Vidrine A., Klimecki W.T.
Environ. Health Perspect. 111:1421-1427(2003) [PubMed: 12928150] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT SER-51.
[4]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
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. expand/collapse author list , 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.
Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT SER-51.
Tissue: Tongue.
[5]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[6]"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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Ovary.
[7]Bienvenut W.V., Claeys D.
Submitted (FEB-2006) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 1-22; 42-58; 68-76; 96-148; 212-229; 235-265 AND 271-287, ACETYLATION AT MET-1, MASS SPECTROMETRY.
Tissue: Platelet.
[8]Colinge J., Superti-Furga G., Bennett K.L.
Submitted (OCT-2008) to UniProtKB
Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[9]"Three-dimensional structure of human erythrocytic purine nucleoside phosphorylase at 3.2-A resolution."
Ealick S.E., Rule S.A., Carter D.C., Greenhough T.J., Babu Y.S., Cook W.J., Habash J., Helliwell J.R., Stoeckler J.D., Parks R.E. Jr., Chen S.-F., Bugg C.E.
J. Biol. Chem. 265:1812-1820(1990) [PubMed: 2104852] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS).
[10]"Molecular analysis of mutations in a patient with purine nucleoside phosphorylase deficiency."
Aust M.R., Andrews L.G., Barrett M.J., Norby-Slycord C.J., Markert M.L.
Am. J. Hum. Genet. 51:763-772(1992) [PubMed: 1384322] [Abstract]
Cited for: VARIANT SER-51, VARIANTS NP DEFICIENCY GLY-128 AND PRO-234.
[11]"Two novel missense and frameshift mutations in exons 5 and 6 of the purine nucleoside phosphorylase (PNP) gene in a severe combined immunodeficiency (SCID) patient."
Pannicke U., Tuchschmid P., Friedrich W., Bartram C.R., Schwarz K.
Hum. Genet. 98:706-709(1996) [PubMed: 8931706] [Abstract]
Cited for: VARIANT NP DEFICIENCY CYS-192.
+Additional computationally mapped references.

Web resources

NPbase

NP mutation db

GeneReviews

Cross-references

Sequence databases

X00737 mRNA. Translation: CAA25320.1.
M13953 expand/collapse EMBL AC list , J02672, M13951, M13952 Genomic DNA. Translation: AAA36460.1.
AY817667 Genomic DNA. Translation: AAV68044.1.
AK313490 mRNA. Translation: BAG36272.1.
CR407607 mRNA. Translation: CAG28535.1.
BC104206 mRNA. Translation: AAI04207.1.
BC104207 mRNA. Translation: AAI04208.1.
BC106074 mRNA. Translation: AAI06075.1.
IPIIPI00871140.
PIRPHHUPN. A00578.
RefSeqNP_000261.2.
UniGeneHs.75514

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1M73X-ray2.30E2-289[»]
1PF7X-ray2.60E1-289[»]
1PWYX-ray2.80E2-289[»]
1RCTX-ray2.80E2-289[»]
1RFGX-ray2.90E2-289[»]
1RR6X-ray2.50A1-289[»]
1RSZX-ray2.20A1-289[»]
1RT9X-ray2.30A1-289[»]
1ULAX-ray2.75A1-289[»]
1ULBX-ray2.75A1-289[»]
1V2HX-ray2.70E2-289[»]
1V3QX-ray2.80E2-289[»]
1V41X-ray2.85E2-289[»]
1V45X-ray2.86E2-289[»]
1YRYX-ray2.80E1-289[»]
2A0WX-ray2.28A1-289[»]
2A0XX-ray2.28A1-289[»]
2A0YX-ray2.28A1-289[»]
2OC4X-ray2.59A1-289[»]
2OC9X-ray2.59A1-289[»]
2ON6X-ray2.50A1-289[»]
2Q7OX-ray2.90E1-289[»]
3BGSX-ray2.10A1-289[»]
3GB9X-ray2.30A/B/C1-289[»]
3GGSX-ray2.52A/B/C1-289[»]
ModBaseSearch...

Protein-protein interaction databases

IntActP00491. 10 interactions.

2-D gel databases

Aarhus/Ghent-2DPAGE2108. IEF.
OGPP00491.

Proteomic databases

PRIDEP00491.

Genome annotation databases

EnsemblENSG00000198805. Homo sapiens. [Contig view]
GeneID4860.
KEGGhsa:4860.

Organism-specific databases

GeneCardsGC14P020007.
HGNCHGNC:7892. NP.
HPAHPA001625.
MIM164050. gene+phenotype.
Orphanet760. Purine nucleoside phosphorylase deficiency.
PharmGKBPA24582.
GenAtlasSearch...

Phylogenomic databases

HOVERGENP00491.

Enzyme and pathway databases

BioCycMetaCyc:MON-10501.
BRENDA2.4.2.1. 247.
ReactomeREACT_1698. Nucleotide metabolism.

Gene expression databases

ArrayExpressP00491.
BgeeP00491.
CleanExHS_NP.
GermOnlineENSG00000198805. Homo sapiens.

Family and domain databases

InterProIPR000845. Nucleoside_phosphorylase.
IPR011268. PNPHPUNA_XAPA.
IPR011270. Pur_Nuc_Pase_Ino/Guo-sp.
IPR001369. Purine_phosphorylase-2.
IPR018099. Purine_phosphorylase-2_CS.
[Graphical view]
PANTHERPTHR11904. Mtap_PNP. 1 hit.
PTHR11904:SF9. PNPHPUNA_XAPA. 1 hit.
PfamPF01048. PNP_UDP_1. 1 hit.
[Graphical view]
TIGRFAMsTIGR01700. PNPH. 1 hit.
TIGR01697. PNPH-PUNA-XAPA. 1 hit.
PROSITEPS01240. PNP_MTAP_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

BindingDBP00491.
DrugBankDB00787. Aciclovir.
DB00242. Cladribine.
DB01033. Mercaptopurine.
NextBio18722.
SOURCESearch...

Entry information

Entry namePNPH_HUMAN
AccessionPrimary (citable) accession number: P00491
Secondary accession number(s): B2R8S5, Q15160, Q5PZ03
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: May 30, 2006
Last modified: June 16, 2009
This is version 108 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

Human chromosome 14

Human chromosome 14: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents