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Q9BY32

- ITPA_HUMAN

UniProt

Q9BY32 - ITPA_HUMAN

Protein

Inosine triphosphate pyrophosphatase

Gene

ITPA

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 132 (01 Oct 2014)
      Sequence version 2 (23 Apr 2003)
      Previous versions | rss
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    Functioni

    Pyrophosphatase that hydrolyzes the non-canonical purine nucleotides inosine triphosphate (ITP), deoxyinosine triphosphate (dITP) as well as 2'-deoxy-N-6-hydroxylaminopurine triposphate (dHAPTP) and xanthosine 5'-triphosphate (XTP) to their respective monophosphate derivatives. The enzyme does not distinguish between the deoxy- and ribose forms. Probably excludes non-canonical purines from RNA and DNA precursor pools, thus preventing their incorporation into RNA and DNA and avoiding chromosomal lesions.1 PublicationUniRule annotation

    Catalytic activityi

    A nucleoside triphosphate + H2O = a nucleotide + diphosphate.UniRule annotation

    Cofactori

    Binds 1 magnesium ion per subunit.1 Publication

    Kineticsi

    Vmax values are similar for dITP, dHAPTP and dGTP.

    1. KM=0.51 mM for ITP2 Publications
    2. KM=0.31 mM for dITP2 Publications
    3. KM=0.57 mM for XTP2 Publications
    4. KM=40.7 µM for dHAPTP2 Publications
    5. KM=933 µM for dGTP2 Publications

    Vmax=1520 µmol/min/mg enzyme for ITP2 Publications

    Vmax=940 µmol/min/mg enzyme for dITP2 Publications

    Vmax=1680 µmol/min/mg enzyme for XTP2 Publications

    pH dependencei

    Optimum pH is 10.2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi44 – 441Magnesium
    Binding sitei56 – 561Substrate
    Metal bindingi72 – 721MagnesiumBy similarity
    Binding sitei172 – 1721Substrate

    GO - Molecular functioni

    1. dITP diphosphatase activity Source: Reactome
    2. ITP diphosphatase activity Source: Reactome
    3. metal ion binding Source: UniProtKB-KW
    4. nucleotide binding Source: UniProtKB-KW
    5. XTP diphosphatase activity Source: Reactome

    GO - Biological processi

    1. chromosome organization Source: Ensembl
    2. deoxyribonucleoside triphosphate catabolic process Source: UniProtKB-HAMAP
    3. ITP catabolic process Source: Ensembl
    4. nucleobase-containing small molecule metabolic process Source: Reactome
    5. small molecule metabolic process Source: Reactome

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    Nucleotide metabolism

    Keywords - Ligandi

    Magnesium, Metal-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_1698. Metabolism of nucleotides.
    SABIO-RKQ9BY32.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Inosine triphosphate pyrophosphataseUniRule annotation (EC:3.6.1.19UniRule annotation)
    Short name:
    ITPaseUniRule annotation
    Short name:
    Inosine triphosphataseUniRule annotation
    Alternative name(s):
    Non-canonical purine NTP pyrophosphataseUniRule annotation
    Non-standard purine NTP pyrophosphataseUniRule annotation
    Nucleoside-triphosphate diphosphataseUniRule annotation
    Nucleoside-triphosphate pyrophosphataseUniRule annotation
    Short name:
    NTPaseUniRule annotation
    Putative oncogene protein hlc14-06-p
    Gene namesi
    Name:ITPAUniRule annotation
    Synonyms:C20orf37
    ORF Names:My049, OK/SW-cl.9
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 20

    Organism-specific databases

    HGNCiHGNC:6176. ITPA.

    Subcellular locationi

    Cytoplasm 1 PublicationUniRule annotation

    GO - Cellular componenti

    1. cytosol Source: Reactome

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Involvement in diseasei

    Inosine triphosphate pyrophosphohydrolase deficiency (ITPAD) [MIM:613850]: A common inherited condition characterized by the abnormal accumulation of inosine triphosphate in erythrocytes. It might have pharmacogenomic implications and be related to increased drug toxicity of purine analog drugs.3 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry. Three different human populations have been reported with respect to their ITPase activity: high, mean (25% of high) and low activity. The variant Thr-32 is associated with complete loss of enzyme activity, may be by altering the local secondary structure of the protein. Heterozygotes for this polymorphism have 22.5% of the control activity: this is consistent with a dimeric structure of the enzyme.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti32 – 321P → T in ITPAD; complete loss of enzymatic activity at homozygosity; partial loss of activity without ITP accumulation in heterozygous individuals. 3 Publications
    Corresponds to variant rs1127354 [ dbSNP | Ensembl ].
    VAR_015576

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi613850. phenotype.
    Orphaneti319684. Inosine triphosphatase deficiency.
    284113. Susceptibility to adverse reaction due to mercaptopurine.
    PharmGKBiPA29973.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 PublicationUniRule annotation
    Chaini2 – 194193Inosine triphosphate pyrophosphatasePRO_0000178280Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine1 PublicationUniRule annotation

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiQ9BY32.
    PaxDbiQ9BY32.
    PeptideAtlasiQ9BY32.
    PRIDEiQ9BY32.

    PTM databases

    PhosphoSiteiQ9BY32.

    Expressioni

    Tissue specificityi

    Ubiquitous. Highly expressed in heart, liver, sex glands, thyroid and adrenal gland.

    Gene expression databases

    ArrayExpressiQ9BY32.
    BgeeiQ9BY32.
    CleanExiHS_ITPA.
    GenevestigatoriQ9BY32.

    Organism-specific databases

    HPAiHPA022824.

    Interactioni

    Subunit structurei

    Homodimer.2 PublicationsUniRule annotation

    Protein-protein interaction databases

    BioGridi109909. 3 interactions.
    IntActiQ9BY32. 1 interaction.
    MINTiMINT-5006578.
    STRINGi9606.ENSP00000369456.

    Structurei

    Secondary structure

    1
    194
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi2 – 54
    Beta strandi9 – 135
    Helixi17 – 2711
    Beta strandi33 – 386
    Beta strandi45 – 473
    Helixi49 – 6416
    Beta strandi68 – 7710
    Helixi78 – 803
    Helixi88 – 10215
    Turni103 – 1064
    Beta strandi111 – 12111
    Beta strandi130 – 14011
    Helixi152 – 1543
    Beta strandi155 – 1573
    Turni164 – 1663
    Helixi169 – 1757
    Helixi177 – 18913

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2CARX-ray1.09A/B1-194[»]
    2I5DX-ray1.63A1-194[»]
    2J4EX-ray2.80A/B/C/D/E/F/G/H1-194[»]
    4F95X-ray2.07A1-194[»]
    ProteinModelPortaliQ9BY32.
    SMRiQ9BY32. Positions 1-194.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9BY32.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni14 – 196Substrate binding
    Regioni72 – 732Substrate binding
    Regioni149 – 1524Substrate binding
    Regioni177 – 1782Substrate binding

    Sequence similaritiesi

    Belongs to the HAM1 NTPase family.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG0127.
    HOGENOMiHOG000293320.
    HOVERGENiHBG039521.
    InParanoidiQ9BY32.
    KOiK01519.
    OMAiPGAYIKW.
    OrthoDBiEOG7X0VJG.
    PhylomeDBiQ9BY32.
    TreeFamiTF105614.

    Family and domain databases

    Gene3Di3.90.950.10. 1 hit.
    HAMAPiMF_03148. HAM1_NTPase.
    InterProiIPR002637. Ham1p-like.
    IPR027502. ITPase.
    IPR029001. ITPase-like_fam.
    [Graphical view]
    PANTHERiPTHR11067. PTHR11067. 1 hit.
    PfamiPF01725. Ham1p_like. 1 hit.
    [Graphical view]
    SUPFAMiSSF52972. SSF52972. 1 hit.
    TIGRFAMsiTIGR00042. TIGR00042. 1 hit.

    Sequences (3)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9BY32-1) [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

    MAASLVGKKI VFVTGNAKKL EEVVQILGDK FPCTLVAQKI DLPEYQGEPD    50
    EISIQKCQEA VRQVQGPVLV EDTCLCFNAL GGLPGPYIKW FLEKLKPEGL 100
    HQLLAGFEDK SAYALCTFAL STGDPSQPVR LFRGRTSGRI VAPRGCQDFG 150
    WDPCFQPDGY EQTYAEMPKA EKNAVSHRFR ALLELQEYFG SLAA 194
    Length:194
    Mass (Da):21,446
    Last modified:April 23, 2003 - v2
    Checksum:iF0EC6A523722DF05
    GO
    Isoform 2 (identifier: Q9BY32-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         7-23: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:177
    Mass (Da):19,603
    Checksum:iAAE9E3F8713D476D
    GO
    Isoform 3 (identifier: Q9BY32-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         23-63: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:153
    Mass (Da):16,833
    Checksum:iDDC0D289C0158A76
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti33 – 331C → R in AAK21848. (PubMed:11278832)Curated
    Sequence conflicti41 – 411D → G in AAG43165. 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti32 – 321P → T in ITPAD; complete loss of enzymatic activity at homozygosity; partial loss of activity without ITP accumulation in heterozygous individuals. 3 Publications
    Corresponds to variant rs1127354 [ dbSNP | Ensembl ].
    VAR_015576

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei7 – 2317Missing in isoform 2. 1 PublicationVSP_042548Add
    BLAST
    Alternative sequencei23 – 6341Missing in isoform 3. 1 PublicationVSP_045545Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF219116 mRNA. Translation: AAK21848.1.
    AF063607 mRNA. Translation: AAG43165.1.
    AF026816 mRNA. Translation: AAB82608.2.
    EF199841 mRNA. Translation: ABP01354.1.
    EF213026 mRNA. Translation: ABO70316.1.
    AB062127 mRNA. Translation: BAB93459.1.
    AL109976 Genomic DNA. Translation: CAC16798.3.
    AL121891, AL109976 Genomic DNA. Translation: CAI19399.1.
    AL121891, AL109976 Genomic DNA. Translation: CAM27676.1.
    AL109976, AL121891 Genomic DNA. Translation: CAM28311.1.
    CH471133 Genomic DNA. Translation: EAX10541.1.
    BC010138 mRNA. Translation: AAH10138.1.
    BI115811 mRNA. No translation available.
    CCDSiCCDS13051.1. [Q9BY32-1]
    CCDS46576.1. [Q9BY32-2]
    CCDS58762.1. [Q9BY32-3]
    RefSeqiNP_001254552.1. NM_001267623.1. [Q9BY32-3]
    NP_258412.1. NM_033453.3. [Q9BY32-1]
    NP_852470.1. NM_181493.2. [Q9BY32-2]
    UniGeneiHs.415299.

    Genome annotation databases

    EnsembliENST00000380113; ENSP00000369456; ENSG00000125877. [Q9BY32-1]
    ENST00000399838; ENSP00000382732; ENSG00000125877. [Q9BY32-3]
    ENST00000455664; ENSP00000413282; ENSG00000125877. [Q9BY32-2]
    GeneIDi3704.
    KEGGihsa:3704.
    UCSCiuc002wid.4. human. [Q9BY32-1]
    uc002wie.4. human. [Q9BY32-2]
    uc031rsg.1. human.

    Polymorphism databases

    DMDMi30173120.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF219116 mRNA. Translation: AAK21848.1 .
    AF063607 mRNA. Translation: AAG43165.1 .
    AF026816 mRNA. Translation: AAB82608.2 .
    EF199841 mRNA. Translation: ABP01354.1 .
    EF213026 mRNA. Translation: ABO70316.1 .
    AB062127 mRNA. Translation: BAB93459.1 .
    AL109976 Genomic DNA. Translation: CAC16798.3 .
    AL121891 , AL109976 Genomic DNA. Translation: CAI19399.1 .
    AL121891 , AL109976 Genomic DNA. Translation: CAM27676.1 .
    AL109976 , AL121891 Genomic DNA. Translation: CAM28311.1 .
    CH471133 Genomic DNA. Translation: EAX10541.1 .
    BC010138 mRNA. Translation: AAH10138.1 .
    BI115811 mRNA. No translation available.
    CCDSi CCDS13051.1. [Q9BY32-1 ]
    CCDS46576.1. [Q9BY32-2 ]
    CCDS58762.1. [Q9BY32-3 ]
    RefSeqi NP_001254552.1. NM_001267623.1. [Q9BY32-3 ]
    NP_258412.1. NM_033453.3. [Q9BY32-1 ]
    NP_852470.1. NM_181493.2. [Q9BY32-2 ]
    UniGenei Hs.415299.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2CAR X-ray 1.09 A/B 1-194 [» ]
    2I5D X-ray 1.63 A 1-194 [» ]
    2J4E X-ray 2.80 A/B/C/D/E/F/G/H 1-194 [» ]
    4F95 X-ray 2.07 A 1-194 [» ]
    ProteinModelPortali Q9BY32.
    SMRi Q9BY32. Positions 1-194.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109909. 3 interactions.
    IntActi Q9BY32. 1 interaction.
    MINTi MINT-5006578.
    STRINGi 9606.ENSP00000369456.

    PTM databases

    PhosphoSitei Q9BY32.

    Polymorphism databases

    DMDMi 30173120.

    Proteomic databases

    MaxQBi Q9BY32.
    PaxDbi Q9BY32.
    PeptideAtlasi Q9BY32.
    PRIDEi Q9BY32.

    Protocols and materials databases

    DNASUi 3704.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000380113 ; ENSP00000369456 ; ENSG00000125877 . [Q9BY32-1 ]
    ENST00000399838 ; ENSP00000382732 ; ENSG00000125877 . [Q9BY32-3 ]
    ENST00000455664 ; ENSP00000413282 ; ENSG00000125877 . [Q9BY32-2 ]
    GeneIDi 3704.
    KEGGi hsa:3704.
    UCSCi uc002wid.4. human. [Q9BY32-1 ]
    uc002wie.4. human. [Q9BY32-2 ]
    uc031rsg.1. human.

    Organism-specific databases

    CTDi 3704.
    GeneCardsi GC20P003189.
    HGNCi HGNC:6176. ITPA.
    HPAi HPA022824.
    MIMi 147520. gene.
    613850. phenotype.
    neXtProti NX_Q9BY32.
    Orphaneti 319684. Inosine triphosphatase deficiency.
    284113. Susceptibility to adverse reaction due to mercaptopurine.
    PharmGKBi PA29973.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0127.
    HOGENOMi HOG000293320.
    HOVERGENi HBG039521.
    InParanoidi Q9BY32.
    KOi K01519.
    OMAi PGAYIKW.
    OrthoDBi EOG7X0VJG.
    PhylomeDBi Q9BY32.
    TreeFami TF105614.

    Enzyme and pathway databases

    Reactomei REACT_1698. Metabolism of nucleotides.
    SABIO-RK Q9BY32.

    Miscellaneous databases

    EvolutionaryTracei Q9BY32.
    GeneWikii ITPA.
    GenomeRNAii 3704.
    NextBioi 14515.
    PROi Q9BY32.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9BY32.
    Bgeei Q9BY32.
    CleanExi HS_ITPA.
    Genevestigatori Q9BY32.

    Family and domain databases

    Gene3Di 3.90.950.10. 1 hit.
    HAMAPi MF_03148. HAM1_NTPase.
    InterProi IPR002637. Ham1p-like.
    IPR027502. ITPase.
    IPR029001. ITPase-like_fam.
    [Graphical view ]
    PANTHERi PTHR11067. PTHR11067. 1 hit.
    Pfami PF01725. Ham1p_like. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52972. SSF52972. 1 hit.
    TIGRFAMsi TIGR00042. TIGR00042. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Cloning, expression, and characterization of a human inosine triphosphate pyrophosphatase encoded by the ITPA gene."
      Lin S., McLennan A.G., Ying K., Wang Z., Gu S., Jin H., Wu C., Lu W., Yuan Y., Tang R., Xie Y., Mao Y.
      J. Biol. Chem. 276:18695-18701(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBUNIT, SUBCELLULAR LOCATION, BIOPHYSICOCHEMICAL PROPERTIES.
      Tissue: Fetal brain.
    2. Mao Y.M., Xie Y., Zheng Z.H.
      Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT ITPAD THR-32.
      Tissue: Fetal brain.
    3. "Molecular cloning of cDNA associated with human lung cancer antigen and study on its functions."
      Fan M.-Z., Chen Z., Cao Z.-M.
      Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Lung carcinoma.
    4. Danaei Y., Behmanesh M., Sadeghi Zadeh M.
      Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
    5. "Identification of immuno-peptidmics that are recognized by tumor-reactive CTL generated from TIL of colon cancer patients."
      Shichijo S., Itoh K.
      Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Colon adenocarcinoma.
    6. "The DNA sequence and comparative analysis of human chromosome 20."
      Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E.
      , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
      Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. "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] (ISOFORMS 1 AND 3).
      Tissue: Lung carcinoma and Neuroblastoma.
    9. Bienvenut W.V., Waridel P., Quadroni M.
      Submitted (MAR-2009) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 2-9; 40-56; 95-110 AND 181-194, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Embryonic kidney.
    10. Lubec G., Afjehi-Sadat L., Chen W.-Q., Sun Y.
      Submitted (DEC-2008) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 10-56 AND 95-130, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
    11. "Substrate specificity of RdgB protein, a deoxyribonucleoside triphosphate pyrophosphohydrolase."
      Burgis N.E., Cunningham R.P.
      J. Biol. Chem. 282:3531-3538(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBSTRATE SPECIFICITY, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES.
    12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "Structure of the orthorhombic form of human inosine triphosphate pyrophosphatase."
      Porta J., Kolar C., Kozmin S.G., Pavlov Y.I., Borgstahl G.E.
      Acta Crystallogr. F 62:1076-1081(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.63 ANGSTROMS).
    14. "Crystal structure of human inosine triphosphatase. Substrate binding and implication of the inosine triphosphatase deficiency mutation P32T."
      Stenmark P., Kursula P., Flodin S., Graslund S., Landry R., Nordlund P., Schueler H.
      J. Biol. Chem. 282:3182-3187(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.1 ANGSTROMS) ALONE AND IN COMPLEX WITH ITP, COFACTOR, MAGNESIUM-BINDING SITES, SUBSTRATE-BINDING SITES.
    15. Cited for: VARIANT ITPAD THR-32.
    16. "DNA polymorphisms in ITPA including basis of inosine triphosphatase deficiency."
      Cao H., Hegele R.A.
      J. Hum. Genet. 47:620-622(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT ITPAD THR-32.

    Entry informationi

    Entry nameiITPA_HUMAN
    AccessioniPrimary (citable) accession number: Q9BY32
    Secondary accession number(s): A2A2N2
    , A4UIM5, B2BCH7, O14878, Q5JWH4, Q9BYN1, Q9BYX0, Q9H3H8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 23, 2003
    Last sequence update: April 23, 2003
    Last modified: October 1, 2014
    This is version 132 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 20
      Human chromosome 20: 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3