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Q9BY32

- ITPA_HUMAN

UniProt

Q9BY32 - ITPA_HUMAN

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Protein

Inosine triphosphate pyrophosphatase

Gene

ITPA

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

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

Mg2+1 PublicationNote: Binds 1 Mg(2+) 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
Complete GO annotation...

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
Complete GO annotation...

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

BgeeiQ9BY32.
CleanExiHS_ITPA.
ExpressionAtlasiQ9BY32. baseline and differential.
GenevestigatoriQ9BY32.

Organism-specific databases

HPAiHPA022824.

Interactioni

Subunit structurei

Homodimer.2 PublicationsUniRule annotation

Protein-protein interaction databases

BioGridi109909. 7 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 – 54Combined sources
Beta strandi9 – 135Combined sources
Helixi17 – 2711Combined sources
Beta strandi33 – 386Combined sources
Beta strandi45 – 473Combined sources
Helixi49 – 6416Combined sources
Beta strandi68 – 7710Combined sources
Helixi78 – 803Combined sources
Helixi88 – 10215Combined sources
Turni103 – 1064Combined sources
Beta strandi111 – 12111Combined sources
Beta strandi130 – 14011Combined sources
Helixi152 – 1543Combined sources
Beta strandi155 – 1573Combined sources
Turni164 – 1663Combined sources
Helixi169 – 1757Combined sources
Helixi177 – 18913Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00390000015399.
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

        10         20         30         40         50
MAASLVGKKI VFVTGNAKKL EEVVQILGDK FPCTLVAQKI DLPEYQGEPD
60 70 80 90 100
EISIQKCQEA VRQVQGPVLV EDTCLCFNAL GGLPGPYIKW FLEKLKPEGL
110 120 130 140 150
HQLLAGFEDK SAYALCTFAL STGDPSQPVR LFRGRTSGRI VAPRGCQDFG
160 170 180 190
WDPCFQPDGY EQTYAEMPKA EKNAVSHRFR ALLELQEYFG SLAA
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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. 7 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.
GeneTreei ENSGT00390000015399.
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

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

Gene expression databases

Bgeei Q9BY32.
CleanExi HS_ITPA.
ExpressionAtlasi Q9BY32. baseline and differential.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 134 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

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