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P00491

- PNPH_HUMAN

UniProt

P00491 - PNPH_HUMAN

Protein

Purine nucleoside phosphorylase

Gene

PNP

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 164 (01 Oct 2014)
      Sequence version 2 (30 May 2006)
      Previous versions | rss
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    Functioni

    The purine nucleoside phosphorylases catalyze the phosphorolytic breakdown of the N-glycosidic bond in the beta-(deoxy)ribonucleoside molecules, with the formation of the corresponding free purine bases and pentose-1-phosphate.1 Publication

    Catalytic activityi

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

    Pathwayi

    GO - Molecular functioni

    1. drug binding Source: UniProtKB
    2. nucleoside binding Source: UniProtKB
    3. phosphate ion binding Source: UniProtKB
    4. purine nucleobase binding Source: UniProtKB
    5. purine-nucleoside phosphorylase activity Source: UniProtKB

    GO - Biological processi

    1. immune response Source: UniProtKB
    2. inosine catabolic process Source: MGI
    3. interleukin-2 secretion Source: UniProtKB
    4. NAD biosynthesis via nicotinamide riboside salvage pathway Source: UniProtKB
    5. nicotinamide riboside catabolic process Source: UniProtKB
    6. nucleobase-containing compound metabolic process Source: UniProtKB
    7. nucleobase-containing small molecule metabolic process Source: Reactome
    8. positive regulation of alpha-beta T cell differentiation Source: MGI
    9. positive regulation of T cell proliferation Source: MGI
    10. purine-containing compound salvage Source: Reactome
    11. purine nucleobase metabolic process Source: Reactome
    12. purine nucleotide catabolic process Source: Reactome
    13. response to drug Source: UniProtKB
    14. small molecule metabolic process Source: Reactome
    15. urate biosynthetic process Source: MGI

    Keywords - Molecular functioni

    Glycosyltransferase, Transferase

    Enzyme and pathway databases

    BioCyciMetaCyc:HS02151-MONOMER.
    BRENDAi2.4.2.1. 2681.
    ReactomeiREACT_1923. Purine salvage.
    REACT_2086. Purine catabolism.
    SABIO-RKP00491.
    SignaLinkiP00491.
    UniPathwayiUPA00606.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Purine nucleoside phosphorylase (EC:2.4.2.1)
    Short name:
    PNP
    Alternative name(s):
    Inosine phosphorylase
    Inosine-guanosine phosphorylase
    Gene namesi
    Name:PNP
    Synonyms:NP
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 14

    Organism-specific databases

    HGNCiHGNC:7892. PNP.

    Subcellular locationi

    Cytoplasmcytoskeleton By similarity. Cytoplasm 1 Publication

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. cytoskeleton Source: UniProtKB-SubCell
    3. cytosol Source: Reactome
    4. extracellular vesicular exosome Source: UniProt
    5. intracellular Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton

    Pathology & Biotechi

    Involvement in diseasei

    Purine nucleoside phosphorylase deficiency (PNPD) [MIM:613179]: A disorder that interrupts both the catabolism of inosine into hypoxanthine and guanosine into guanine, and leads to the accumulation of guanosine, inosine, and their deoxified by-products. The main clinical presentation is recurrent infections due to severe T-cell immunodeficiency. Some patients also have neurologic impairment.3 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti89 – 891E → K in PNPD. 1 Publication
    VAR_002244
    Natural varianti128 – 1281D → G in PNPD. 1 Publication
    VAR_002245
    Natural varianti174 – 1741A → P in PNPD.
    VAR_002246
    Natural varianti192 – 1921Y → C in PNPD. 1 Publication
    VAR_010653
    Natural varianti234 – 2341R → P in PNPD. 1 Publication
    VAR_002247

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi613179. phenotype.
    Orphaneti760. Purine nucleoside phosphorylase deficiency.
    PharmGKBiPA31694.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 289289Purine nucleoside phosphorylasePRO_0000184536Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine2 Publications

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiP00491.
    PaxDbiP00491.
    PRIDEiP00491.

    2D gel databases

    OGPiP00491.

    PTM databases

    PhosphoSiteiP00491.

    Expressioni

    Tissue specificityi

    Expressed in red blood cells; overexpressed in red blood cells (cytoplasm) of patients with hereditary non-spherocytic hemolytic anemia of unknown etiology.1 Publication

    Gene expression databases

    ArrayExpressiP00491.
    BgeeiP00491.
    CleanExiHS_NP.
    GenevestigatoriP00491.

    Organism-specific databases

    HPAiHPA001625.

    Interactioni

    Subunit structurei

    Homotrimer.

    Protein-protein interaction databases

    BioGridi110921. 26 interactions.
    DIPiDIP-50406N.
    IntActiP00491. 7 interactions.
    MINTiMINT-1375849.
    STRINGi9606.ENSP00000354532.

    Structurei

    Secondary structure

    1
    289
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi7 – 2014
    Beta strandi26 – 316
    Helixi36 – 416
    Beta strandi43 – 497
    Helixi50 – 523
    Beta strandi53 – 553
    Helixi62 – 654
    Beta strandi67 – 737
    Beta strandi76 – 838
    Helixi87 – 893
    Helixi93 – 964
    Helixi98 – 1069
    Beta strandi110 – 11910
    Beta strandi121 – 1233
    Beta strandi129 – 1379
    Helixi138 – 1414
    Turni153 – 1553
    Turni163 – 1664
    Helixi168 – 17912
    Turni180 – 1823
    Beta strandi188 – 1947
    Beta strandi197 – 1993
    Helixi203 – 2119
    Beta strandi215 – 2217
    Helixi222 – 2309
    Beta strandi234 – 24411
    Beta strandi248 – 2503
    Helixi257 – 26610
    Helixi268 – 28013
    Turni285 – 2873

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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[»]
    3D1VX-ray2.70A1-289[»]
    3GB9X-ray2.30A/B/C1-289[»]
    3GGSX-ray2.52A/B/C1-289[»]
    3INYX-ray2.75A1-289[»]
    3K8OX-ray2.40E/Q/S/T/U/Y1-289[»]
    3K8QX-ray2.50A1-289[»]
    3PHBX-ray2.30E/Q/S/T/U/Y1-289[»]
    4EARX-ray1.70A/B/C1-289[»]
    4EB8X-ray2.30A/B/C1-289[»]
    4ECEX-ray2.60A/B/C/D/E/F1-289[»]
    4GKAX-ray2.20A/B/C/D/E/F1-289[»]
    ProteinModelPortaliP00491.
    SMRiP00491. Positions 2-289.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP00491.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the PNP/MTAP phosphorylase family.Curated

    Phylogenomic databases

    eggNOGiCOG0005.
    HOVERGENiHBG002460.
    KOiK03783.
    OMAiGDIMFIR.
    PhylomeDBiP00491.
    TreeFamiTF300049.

    Family and domain databases

    Gene3Di3.40.50.1580. 1 hit.
    InterProiIPR000845. Nucleoside_phosphorylase_d.
    IPR001369. PNP/MTAP.
    IPR011270. Pur_Nuc_Pase_Ino/Guo-sp.
    IPR011268. Purine_phosphorylase.
    IPR018099. Purine_phosphorylase-2_CS.
    [Graphical view]
    PANTHERiPTHR11904. PTHR11904. 1 hit.
    PfamiPF01048. PNP_UDP_1. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000477. PurNPase. 1 hit.
    SUPFAMiSSF53167. SSF53167. 1 hit.
    TIGRFAMsiTIGR01700. PNPH. 1 hit.
    TIGR01697. PNPH-PUNA-XAPA. 1 hit.
    PROSITEiPS01240. PNP_MTAP_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P00491-1 [UniParc]FASTAAdd to Basket

    « Hide

    MENGYTYEDY KNTAEWLLSH TKHRPQVAII CGSGLGGLTD KLTQAQIFDY    50
    GEIPNFPRST VPGHAGRLVF GFLNGRACVM MQGRFHMYEG YPLWKVTFPV 100
    RVFHLLGVDT LVVTNAAGGL NPKFEVGDIM LIRDHINLPG FSGQNPLRGP 150
    NDERFGDRFP AMSDAYDRTM RQRALSTWKQ MGEQRELQEG TYVMVAGPSF 200
    ETVAECRVLQ KLGADAVGMS TVPEVIVARH CGLRVFGFSL ITNKVIMDYE 250
    SLEKANHEEV LAAGKQAAQK LEQFVSILMA SIPLPDKAS 289
    Length:289
    Mass (Da):32,118
    Last modified:May 30, 2006 - v2
    Checksum:i91622FB1D26479D3
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti51 – 511G → S.5 Publications
    Corresponds to variant rs1049564 [ dbSNP | Ensembl ].
    VAR_002243
    Natural varianti89 – 891E → K in PNPD. 1 Publication
    VAR_002244
    Natural varianti128 – 1281D → G in PNPD. 1 Publication
    VAR_002245
    Natural varianti174 – 1741A → P in PNPD.
    VAR_002246
    Natural varianti192 – 1921Y → C in PNPD. 1 Publication
    VAR_010653
    Natural varianti234 – 2341R → P in PNPD. 1 Publication
    VAR_002247

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X00737 mRNA. Translation: CAA25320.1.
    M13953
    , J02672, M13951, M13952 Genomic DNA. Translation: AAA36460.1.
    AY817667 Genomic DNA. Translation: AAV68044.1.
    AK313490 mRNA. Translation: BAG36272.1.
    CR407607 mRNA. Translation: CAG28535.1.
    CH471078 Genomic DNA. Translation: EAW66458.1.
    CH471078 Genomic DNA. Translation: EAW66459.1.
    BC104206 mRNA. Translation: AAI04207.1.
    BC104207 mRNA. Translation: AAI04208.1.
    BC106074 mRNA. Translation: AAI06075.1.
    CCDSiCCDS9552.1.
    PIRiA00578. PHHUPN.
    RefSeqiNP_000261.2. NM_000270.3.
    UniGeneiHs.75514.

    Genome annotation databases

    EnsembliENST00000361505; ENSP00000354532; ENSG00000198805.
    GeneIDi4860.
    KEGGihsa:4860.
    UCSCiuc001vxo.4. human.

    Polymorphism databases

    DMDMi108935929.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    NPbase

    NP mutation db

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X00737 mRNA. Translation: CAA25320.1 .
    M13953
    , J02672 , M13951 , M13952 Genomic DNA. Translation: AAA36460.1 .
    AY817667 Genomic DNA. Translation: AAV68044.1 .
    AK313490 mRNA. Translation: BAG36272.1 .
    CR407607 mRNA. Translation: CAG28535.1 .
    CH471078 Genomic DNA. Translation: EAW66458.1 .
    CH471078 Genomic DNA. Translation: EAW66459.1 .
    BC104206 mRNA. Translation: AAI04207.1 .
    BC104207 mRNA. Translation: AAI04208.1 .
    BC106074 mRNA. Translation: AAI06075.1 .
    CCDSi CCDS9552.1.
    PIRi A00578. PHHUPN.
    RefSeqi NP_000261.2. NM_000270.3.
    UniGenei Hs.75514.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1M73 X-ray 2.30 E 2-289 [» ]
    1PF7 X-ray 2.60 E 1-289 [» ]
    1PWY X-ray 2.80 E 2-289 [» ]
    1RCT X-ray 2.80 E 2-289 [» ]
    1RFG X-ray 2.90 E 2-289 [» ]
    1RR6 X-ray 2.50 A 1-289 [» ]
    1RSZ X-ray 2.20 A 1-289 [» ]
    1RT9 X-ray 2.30 A 1-289 [» ]
    1ULA X-ray 2.75 A 1-289 [» ]
    1ULB X-ray 2.75 A 1-289 [» ]
    1V2H X-ray 2.70 E 2-289 [» ]
    1V3Q X-ray 2.80 E 2-289 [» ]
    1V41 X-ray 2.85 E 2-289 [» ]
    1V45 X-ray 2.86 E 2-289 [» ]
    1YRY X-ray 2.80 E 1-289 [» ]
    2A0W X-ray 2.28 A 1-289 [» ]
    2A0X X-ray 2.28 A 1-289 [» ]
    2A0Y X-ray 2.28 A 1-289 [» ]
    2OC4 X-ray 2.59 A 1-289 [» ]
    2OC9 X-ray 2.59 A 1-289 [» ]
    2ON6 X-ray 2.50 A 1-289 [» ]
    2Q7O X-ray 2.90 E 1-289 [» ]
    3BGS X-ray 2.10 A 1-289 [» ]
    3D1V X-ray 2.70 A 1-289 [» ]
    3GB9 X-ray 2.30 A/B/C 1-289 [» ]
    3GGS X-ray 2.52 A/B/C 1-289 [» ]
    3INY X-ray 2.75 A 1-289 [» ]
    3K8O X-ray 2.40 E/Q/S/T/U/Y 1-289 [» ]
    3K8Q X-ray 2.50 A 1-289 [» ]
    3PHB X-ray 2.30 E/Q/S/T/U/Y 1-289 [» ]
    4EAR X-ray 1.70 A/B/C 1-289 [» ]
    4EB8 X-ray 2.30 A/B/C 1-289 [» ]
    4ECE X-ray 2.60 A/B/C/D/E/F 1-289 [» ]
    4GKA X-ray 2.20 A/B/C/D/E/F 1-289 [» ]
    ProteinModelPortali P00491.
    SMRi P00491. Positions 2-289.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 110921. 26 interactions.
    DIPi DIP-50406N.
    IntActi P00491. 7 interactions.
    MINTi MINT-1375849.
    STRINGi 9606.ENSP00000354532.

    Chemistry

    BindingDBi P00491.
    ChEMBLi CHEMBL4338.
    DrugBanki DB00787. Aciclovir.
    DB00242. Cladribine.
    DB01033. Mercaptopurine.

    PTM databases

    PhosphoSitei P00491.

    Polymorphism databases

    DMDMi 108935929.

    2D gel databases

    OGPi P00491.

    Proteomic databases

    MaxQBi P00491.
    PaxDbi P00491.
    PRIDEi P00491.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000361505 ; ENSP00000354532 ; ENSG00000198805 .
    GeneIDi 4860.
    KEGGi hsa:4860.
    UCSCi uc001vxo.4. human.

    Organism-specific databases

    CTDi 4860.
    GeneCardsi GC14P021021.
    HGNCi HGNC:7892. PNP.
    HPAi HPA001625.
    MIMi 164050. gene.
    613179. phenotype.
    neXtProti NX_P00491.
    Orphaneti 760. Purine nucleoside phosphorylase deficiency.
    PharmGKBi PA31694.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0005.
    HOVERGENi HBG002460.
    KOi K03783.
    OMAi GDIMFIR.
    PhylomeDBi P00491.
    TreeFami TF300049.

    Enzyme and pathway databases

    UniPathwayi UPA00606 .
    BioCyci MetaCyc:HS02151-MONOMER.
    BRENDAi 2.4.2.1. 2681.
    Reactomei REACT_1923. Purine salvage.
    REACT_2086. Purine catabolism.
    SABIO-RK P00491.
    SignaLinki P00491.

    Miscellaneous databases

    ChiTaRSi PNP. human.
    EvolutionaryTracei P00491.
    GeneWikii Purine_nucleoside_phosphorylase.
    GenomeRNAii 4860.
    NextBioi 18722.
    PROi P00491.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P00491.
    Bgeei P00491.
    CleanExi HS_NP.
    Genevestigatori P00491.

    Family and domain databases

    Gene3Di 3.40.50.1580. 1 hit.
    InterProi IPR000845. Nucleoside_phosphorylase_d.
    IPR001369. PNP/MTAP.
    IPR011270. Pur_Nuc_Pase_Ino/Guo-sp.
    IPR011268. Purine_phosphorylase.
    IPR018099. Purine_phosphorylase-2_CS.
    [Graphical view ]
    PANTHERi PTHR11904. PTHR11904. 1 hit.
    Pfami PF01048. PNP_UDP_1. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000477. PurNPase. 1 hit.
    SUPFAMi SSF53167. SSF53167. 1 hit.
    TIGRFAMsi TIGR01700. PNPH. 1 hit.
    TIGR01697. PNPH-PUNA-XAPA. 1 hit.
    PROSITEi PS01240. PNP_MTAP_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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] [Europe PMC] [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] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT PNPD 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] [Europe PMC] [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.
      , 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] [Europe PMC] [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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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].
      Tissue: Ovary.
    8. 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, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Platelet.
    9. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
      Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
      Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. "Assessment of the red cell proteome of young patients with unexplained hemolytic anemia by two-dimensional differential in-gel electrophoresis (DIGE)."
      von Lohneysen K., Scott T.M., Soldau K., Xu X., Friedman J.S.
      PLoS ONE 7:E34237-E34237(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
    13. "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] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS), FUNCTION.
    14. "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] [Europe PMC] [Abstract]
      Cited for: VARIANT SER-51, VARIANTS PNPD GLY-128 AND PRO-234.
    15. "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] [Europe PMC] [Abstract]
      Cited for: VARIANT PNPD CYS-192.

    Entry informationi

    Entry nameiPNPH_HUMAN
    AccessioniPrimary (citable) accession number: P00491
    Secondary accession number(s): B2R8S5
    , D3DS00, Q15160, Q5PZ03
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: May 30, 2006
    Last modified: October 1, 2014
    This is version 164 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

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 14
      Human chromosome 14: 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3