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Q9BU02

- THTPA_HUMAN

UniProt

Q9BU02 - THTPA_HUMAN

Protein

Thiamine-triphosphatase

Gene

THTPA

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 121 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Hydrolase highly specific for thiamine triphosphate (ThTP).2 Publications

    Catalytic activityi

    Thiamine triphosphate + H2O = thiamine diphosphate + phosphate.1 Publication

    Cofactori

    Binds 1 Mg2+ ion per subunit.1 Publication

    Kineticsi

    1. KM=8 µM for thiamine triphosphate1 Publication

    Vmax=59 µmol/min/mg enzyme1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi7 – 71MagnesiumBy similarity
    Metal bindingi9 – 91MagnesiumBy similarity
    Binding sitei11 – 111Substrate
    Binding sitei55 – 551Substrate
    Binding sitei57 – 571Substrate
    Binding sitei65 – 651Substrate
    Binding sitei125 – 1251Substrate
    Metal bindingi145 – 1451MagnesiumBy similarity
    Metal bindingi157 – 1571MagnesiumBy similarity
    Binding sitei157 – 1571Substrate
    Metal bindingi159 – 1591MagnesiumBy similarity
    Binding sitei193 – 1931SubstrateCurated

    GO - Molecular functioni

    1. hydrolase activity Source: UniProtKB
    2. magnesium ion binding Source: UniProtKB
    3. thiamin-triphosphatase activity Source: UniProtKB

    GO - Biological processi

    1. dephosphorylation Source: UniProtKB
    2. generation of precursor metabolites and energy Source: UniProtKB
    3. small molecule metabolic process Source: Reactome
    4. thiamine-containing compound metabolic process Source: Reactome
    5. thiamine diphosphate metabolic process Source: UniProtKB
    6. thiamine metabolic process Source: UniProtKB
    7. vitamin metabolic process Source: Reactome
    8. water-soluble vitamin metabolic process Source: Reactome

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Ligandi

    Magnesium, Metal-binding

    Enzyme and pathway databases

    BRENDAi3.6.1.28. 2681.
    ReactomeiREACT_11117. Vitamin B1 (thiamin) metabolism.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Thiamine-triphosphatase (EC:3.6.1.28)
    Short name:
    ThTPase
    Gene namesi
    Name:THTPA
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 14

    Organism-specific databases

    HGNCiHGNC:18987. THTPA.

    Subcellular locationi

    Cytoplasm 1 Publication

    GO - Cellular componenti

    1. cytosol Source: Reactome

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi11 – 111K → A: Mildly decreases enzyme activity. 1 Publication
    Mutagenesisi37 – 371D → A: Strongly decreases affinity for thiamine triphosphate and enzyme activity. 1 Publication
    Mutagenesisi39 – 391Y → A: Strongly decreases affinity for thiamine triphosphate and enzyme activity. 1 Publication
    Mutagenesisi53 – 531W → A: Strongly decreases affinity for thiamine triphosphate and enzyme activity. 1 Publication
    Mutagenesisi65 – 651K → A: Strongly decreases enzyme activity. No effect on affinity for thiamine triphosphate. 1 Publication
    Mutagenesisi79 – 791Y → A: Decreases enzyme activity. 1 Publication
    Mutagenesisi81 – 811E → A: Mildly decreases enzyme activity. 1 Publication
    Mutagenesisi147 – 1471D → A: Strongly decreases affinity for thiamine triphosphate and enzyme activity. 1 Publication
    Mutagenesisi193 – 1931K → A: Strongly decreases affinity for thiamine triphosphate and enzyme activity. 1 Publication

    Organism-specific databases

    PharmGKBiPA38774.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 230229Thiamine-triphosphatasePRO_0000221490Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine2 Publications

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiQ9BU02.
    PaxDbiQ9BU02.
    PeptideAtlasiQ9BU02.
    PRIDEiQ9BU02.

    PTM databases

    PhosphoSiteiQ9BU02.

    Expressioni

    Tissue specificityi

    Widely expressed but at a low level.1 Publication

    Gene expression databases

    BgeeiQ9BU02.
    CleanExiHS_THTPA.
    GenevestigatoriQ9BU02.

    Organism-specific databases

    HPAiHPA028876.

    Interactioni

    Subunit structurei

    Monomer.1 Publication

    Protein-protein interaction databases

    BioGridi122595. 6 interactions.
    IntActiQ9BU02. 1 interaction.
    STRINGi9606.ENSP00000288014.

    Structurei

    Secondary structure

    1
    230
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi5 – 128
    Helixi18 – 247
    Beta strandi28 – 4114
    Helixi46 – 494
    Beta strandi53 – 575
    Turni58 – 603
    Beta strandi61 – 7010
    Beta strandi77 – 826
    Helixi85 – 9612
    Helixi106 – 1138
    Beta strandi116 – 13116
    Helixi132 – 1354
    Beta strandi137 – 1393
    Beta strandi141 – 1499
    Beta strandi154 – 16411
    Helixi165 – 1673
    Helixi168 – 18114
    Helixi193 – 2019
    Helixi203 – 21311

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3BHDX-ray1.50A/B1-215[»]
    3TVLX-ray2.30A/B1-230[»]
    ProteinModelPortaliQ9BU02.
    SMRiQ9BU02. Positions 3-208.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9BU02.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini5 – 201197CYTHPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the ThTPase family.Curated
    Contains 1 CYTH domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiNOG42323.
    HOGENOMiHOG000154571.
    HOVERGENiHBG057173.
    InParanoidiQ9BU02.
    KOiK05307.
    OMAiRDTYYDT.
    OrthoDBiEOG7288SN.
    PhylomeDBiQ9BU02.
    TreeFamiTF333398.

    Family and domain databases

    Gene3Di2.40.320.10. 1 hit.
    InterProiIPR023577. CYTH-like_domain.
    IPR012177. ThTPase.
    [Graphical view]
    PANTHERiPTHR14586. PTHR14586. 1 hit.
    PfamiPF01928. CYTH. 1 hit.
    [Graphical view]
    PIRSFiPIRSF036561. ThTPase. 1 hit.
    SUPFAMiSSF55154. SSF55154. 1 hit.
    PROSITEiPS51707. CYTH. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9BU02-1) [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

    MAQGLIEVER KFLPGPGTEE RLQELGGTLE YRVTFRDTYY DTPELSLMQA    50
    DHWLRRREDS GWELKCPGAA GVLGPHTEYK ELTAEPTIVA QLCKVLRADG 100
    LGAGDVAAVL GPLGLQEVAS FVTKRSAWKL VLLGADEEEP QLRVDLDTAD 150
    FGYAVGEVEA LVHEEAEVPT ALEKIHRLSS MLGVPAQETA PAKLIVYLQR 200
    FRPQDYQRLL EVNSSRERPQ ETEDPDHCLG 230
    Length:230
    Mass (Da):25,566
    Last modified:January 23, 2007 - v3
    Checksum:i49B79C6C1D19D91D
    GO
    Isoform 2 (identifier: Q9BU02-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         96-105: LRADGLGAGD → CLHRRQHQPS
         106-230: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:105
    Mass (Da):12,038
    Checksum:iD326E9A8991B8A1F
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti176 – 1761H → R.
    Corresponds to variant rs34015250 [ dbSNP | Ensembl ].
    VAR_062152

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei96 – 10510LRADGLGAGD → CLHRRQHQPS in isoform 2. 1 PublicationVSP_047213
    Alternative sequencei106 – 230125Missing in isoform 2. 1 PublicationVSP_047214Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF432862 mRNA. Translation: AAM22403.1.
    AK057691 mRNA. Translation: BAB71546.1.
    BX161435 mRNA. Translation: CAD61907.1.
    BX378775 mRNA. No translation available.
    AL135999 Genomic DNA. No translation available.
    CH471078 Genomic DNA. Translation: EAW66140.1.
    CH471078 Genomic DNA. Translation: EAW66141.1.
    BC002984 mRNA. Translation: AAH02984.1.
    CCDSiCCDS32053.1. [Q9BU02-1]
    CCDS58307.1. [Q9BU02-2]
    RefSeqiNP_001119811.1. NM_001126339.3. [Q9BU02-1]
    NP_001242991.1. NM_001256062.2. [Q9BU02-2]
    NP_001243250.1. NM_001256321.2. [Q9BU02-2]
    NP_001243251.1. NM_001256322.2.
    NP_001243252.1. NM_001256323.2.
    NP_077304.1. NM_024328.5. [Q9BU02-1]
    UniGeneiHs.655179.
    Hs.732304.
    Hs.736905.

    Genome annotation databases

    EnsembliENST00000288014; ENSP00000288014; ENSG00000259431. [Q9BU02-1]
    ENST00000404535; ENSP00000384580; ENSG00000259431. [Q9BU02-1]
    ENST00000554789; ENSP00000450459; ENSG00000259431. [Q9BU02-2]
    ENST00000556015; ENSP00000451835; ENSG00000259431. [Q9BU02-2]
    GeneIDi79178.
    KEGGihsa:79178.
    UCSCiuc001wkg.5. human. [Q9BU02-1]
    uc031qnv.1. human.

    Polymorphism databases

    DMDMi37538018.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF432862 mRNA. Translation: AAM22403.1 .
    AK057691 mRNA. Translation: BAB71546.1 .
    BX161435 mRNA. Translation: CAD61907.1 .
    BX378775 mRNA. No translation available.
    AL135999 Genomic DNA. No translation available.
    CH471078 Genomic DNA. Translation: EAW66140.1 .
    CH471078 Genomic DNA. Translation: EAW66141.1 .
    BC002984 mRNA. Translation: AAH02984.1 .
    CCDSi CCDS32053.1. [Q9BU02-1 ]
    CCDS58307.1. [Q9BU02-2 ]
    RefSeqi NP_001119811.1. NM_001126339.3. [Q9BU02-1 ]
    NP_001242991.1. NM_001256062.2. [Q9BU02-2 ]
    NP_001243250.1. NM_001256321.2. [Q9BU02-2 ]
    NP_001243251.1. NM_001256322.2.
    NP_001243252.1. NM_001256323.2.
    NP_077304.1. NM_024328.5. [Q9BU02-1 ]
    UniGenei Hs.655179.
    Hs.732304.
    Hs.736905.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3BHD X-ray 1.50 A/B 1-215 [» ]
    3TVL X-ray 2.30 A/B 1-230 [» ]
    ProteinModelPortali Q9BU02.
    SMRi Q9BU02. Positions 3-208.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 122595. 6 interactions.
    IntActi Q9BU02. 1 interaction.
    STRINGi 9606.ENSP00000288014.

    Chemistry

    DrugBanki DB00152. Thiamine.

    PTM databases

    PhosphoSitei Q9BU02.

    Polymorphism databases

    DMDMi 37538018.

    Proteomic databases

    MaxQBi Q9BU02.
    PaxDbi Q9BU02.
    PeptideAtlasi Q9BU02.
    PRIDEi Q9BU02.

    Protocols and materials databases

    DNASUi 79178.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000288014 ; ENSP00000288014 ; ENSG00000259431 . [Q9BU02-1 ]
    ENST00000404535 ; ENSP00000384580 ; ENSG00000259431 . [Q9BU02-1 ]
    ENST00000554789 ; ENSP00000450459 ; ENSG00000259431 . [Q9BU02-2 ]
    ENST00000556015 ; ENSP00000451835 ; ENSG00000259431 . [Q9BU02-2 ]
    GeneIDi 79178.
    KEGGi hsa:79178.
    UCSCi uc001wkg.5. human. [Q9BU02-1 ]
    uc031qnv.1. human.

    Organism-specific databases

    CTDi 79178.
    GeneCardsi GC14P024025.
    HGNCi HGNC:18987. THTPA.
    HPAi HPA028876.
    MIMi 611612. gene.
    neXtProti NX_Q9BU02.
    PharmGKBi PA38774.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG42323.
    HOGENOMi HOG000154571.
    HOVERGENi HBG057173.
    InParanoidi Q9BU02.
    KOi K05307.
    OMAi RDTYYDT.
    OrthoDBi EOG7288SN.
    PhylomeDBi Q9BU02.
    TreeFami TF333398.

    Enzyme and pathway databases

    BRENDAi 3.6.1.28. 2681.
    Reactomei REACT_11117. Vitamin B1 (thiamin) metabolism.

    Miscellaneous databases

    EvolutionaryTracei Q9BU02.
    GenomeRNAii 79178.
    NextBioi 68161.
    PROi Q9BU02.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q9BU02.
    CleanExi HS_THTPA.
    Genevestigatori Q9BU02.

    Family and domain databases

    Gene3Di 2.40.320.10. 1 hit.
    InterProi IPR023577. CYTH-like_domain.
    IPR012177. ThTPase.
    [Graphical view ]
    PANTHERi PTHR14586. PTHR14586. 1 hit.
    Pfami PF01928. CYTH. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF036561. ThTPase. 1 hit.
    SUPFAMi SSF55154. SSF55154. 1 hit.
    PROSITEi PS51707. CYTH. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular characterization of a specific thiamine triphosphatase widely expressed in mammalian tissues."
      Lakaye B., Makarchikov A.F., Antunes A.F., Zorzi W., Coumans B., De Pauw E., Wins P., Grisar T., Bettendorff L.
      J. Biol. Chem. 277:13771-13777(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
      Tissue: Brain.
    2. "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] (ISOFORM 1).
      Tissue: Trachea.
    3. "Full-length cDNA libraries and normalization."
      Li W.B., Gruber C., Jessee J., Polayes D.
      Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
      Tissue: Placenta.
    4. "The DNA sequence and analysis of human chromosome 14."
      Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., Du H.
      , Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., Waterston R., Hood L., Weissenbach J.
      Nature 421:601-607(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    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] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Lung.
    7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    8. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    9. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    10. "Structural determinants of specificity and catalytic mechanism in mammalian 25-kDa thiamine triphosphatase."
      Delvaux D., Kerff F., Murty M.R., Lakaye B., Czerniecki J., Kohn G., Wins P., Herman R., Gabelica V., Heuze F., Tordoir X., Maree R., Matagne A., Charlier P., De Pauw E., Bettendorff L.
      Biochim. Biophys. Acta 1830:4513-4523(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) IN COMPLEX WITH TRIPHOSPHATE, CATALYTIC ACTIVITY, FUNCTION, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, MUTAGENESIS OF LYS-11; ASP-37; TYR-39; TRP-53; LYS-65; TYR-79; GLU-81; ASP-147 AND LYS-193.

    Entry informationi

    Entry nameiTHTPA_HUMAN
    AccessioniPrimary (citable) accession number: Q9BU02
    Secondary accession number(s): D3DS50, G3V4J3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 3, 2003
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 121 of the entry and version 3 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, 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3