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P00491

- PNPH_HUMAN

UniProt

P00491 - PNPH_HUMAN

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Protein

Purine nucleoside phosphorylase

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

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
Complete GO annotation...

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
Complete GO annotation...

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.
Note: The disease is caused by mutations affecting the gene represented in this entry.3 Publications
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.

Miscellaneous databases

EvolutionaryTraceiP00491.

Family & Domainsi

Sequence similaritiesi

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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 163 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

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