Full text data of THTPA
THTPA
[Confidence: low (only semi-automatic identification from reviews)]
Thiamine-triphosphatase; ThTPase; 3.6.1.28
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Thiamine-triphosphatase; ThTPase; 3.6.1.28
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q9BU02
ID THTPA_HUMAN Reviewed; 230 AA.
AC Q9BU02; D3DS50; G3V4J3;
DT 03-OCT-2003, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 3.
DT 22-JAN-2014, entry version 114.
DE RecName: Full=Thiamine-triphosphatase;
DE Short=ThTPase;
DE EC=3.6.1.28;
GN Name=THTPA;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=11827967; DOI=10.1074/jbc.M111241200;
RA Lakaye B., Makarchikov A.F., Antunes A.F., Zorzi W., Coumans B.,
RA De Pauw E., Wins P., Grisar T., Bettendorff L.;
RT "Molecular characterization of a specific thiamine triphosphatase
RT widely expressed in mammalian tissues.";
RL J. Biol. Chem. 277:13771-13777(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Trachea;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Placenta;
RA Li W.B., Gruber C., Jessee J., Polayes D.;
RT "Full-length cDNA libraries and normalization.";
RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12508121; DOI=10.1038/nature01348;
RA Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
RA Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
RA Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S.,
RA Sun H., Du H., Pepin K., Artiguenave F., Robert C., Cruaud C.,
RA Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P.,
RA Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N.,
RA Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C.,
RA Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S.,
RA Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B.,
RA Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M.,
RA Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S.,
RA Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D.,
RA Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A.,
RA Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
RA Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
RA Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L.,
RA Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J.,
RA Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W.,
RA Quetier F., Waterston R., Hood L., Weissenbach J.;
RT "The DNA sequence and analysis of human chromosome 14.";
RL Nature 421:601-607(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lung;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Hydrolase highly specific for thiamine triphosphate
CC (ThTP).
CC -!- CATALYTIC ACTIVITY: Thiamine triphosphate + H(2)O = thiamine
CC diphosphate + phosphate.
CC -!- SUBUNIT: Monomer (By similarity).
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9BU02-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9BU02-2; Sequence=VSP_047213, VSP_047214;
CC Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Widely expressed but at a low level.
CC -!- SIMILARITY: Belongs to the ThTPase family.
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DR EMBL; AF432862; AAM22403.1; -; mRNA.
DR EMBL; AK057691; BAB71546.1; -; mRNA.
DR EMBL; BX161435; CAD61907.1; -; mRNA.
DR EMBL; BX378775; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AL135999; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471078; EAW66140.1; -; Genomic_DNA.
DR EMBL; CH471078; EAW66141.1; -; Genomic_DNA.
DR EMBL; BC002984; AAH02984.1; -; mRNA.
DR RefSeq; NP_001119811.1; NM_001126339.3.
DR RefSeq; NP_001242991.1; NM_001256062.2.
DR RefSeq; NP_001243250.1; NM_001256321.2.
DR RefSeq; NP_001243251.1; NM_001256322.2.
DR RefSeq; NP_001243252.1; NM_001256323.2.
DR RefSeq; NP_077304.1; NM_024328.5.
DR UniGene; Hs.655179; -.
DR UniGene; Hs.732304; -.
DR UniGene; Hs.736905; -.
DR PDB; 3BHD; X-ray; 1.50 A; A/B=1-215.
DR PDB; 3TVL; X-ray; 2.30 A; A/B=1-230.
DR PDBsum; 3BHD; -.
DR PDBsum; 3TVL; -.
DR ProteinModelPortal; Q9BU02; -.
DR SMR; Q9BU02; 3-208.
DR IntAct; Q9BU02; 1.
DR STRING; 9606.ENSP00000288014; -.
DR DrugBank; DB00152; Thiamine.
DR PhosphoSite; Q9BU02; -.
DR DMDM; 37538018; -.
DR PaxDb; Q9BU02; -.
DR PeptideAtlas; Q9BU02; -.
DR PRIDE; Q9BU02; -.
DR DNASU; 79178; -.
DR Ensembl; ENST00000288014; ENSP00000288014; ENSG00000259431.
DR Ensembl; ENST00000404535; ENSP00000384580; ENSG00000259431.
DR Ensembl; ENST00000554789; ENSP00000450459; ENSG00000259431.
DR Ensembl; ENST00000556015; ENSP00000451835; ENSG00000259431.
DR GeneID; 79178; -.
DR KEGG; hsa:79178; -.
DR UCSC; uc031qnv.1; human.
DR CTD; 79178; -.
DR GeneCards; GC14P024025; -.
DR HGNC; HGNC:18987; THTPA.
DR HPA; HPA028876; -.
DR MIM; 611612; gene.
DR neXtProt; NX_Q9BU02; -.
DR PharmGKB; PA38774; -.
DR eggNOG; NOG42323; -.
DR HOGENOM; HOG000154571; -.
DR HOVERGEN; HBG057173; -.
DR InParanoid; Q9BU02; -.
DR KO; K05307; -.
DR OMA; RDTYYDT; -.
DR OrthoDB; EOG7288SN; -.
DR PhylomeDB; Q9BU02; -.
DR BRENDA; 3.6.1.28; 2681.
DR Reactome; REACT_111217; Metabolism.
DR Reactome; REACT_116125; Disease.
DR EvolutionaryTrace; Q9BU02; -.
DR GenomeRNAi; 79178; -.
DR NextBio; 68161; -.
DR PRO; PR:Q9BU02; -.
DR ArrayExpress; Q9BU02; -.
DR Bgee; Q9BU02; -.
DR CleanEx; HS_THTPA; -.
DR Genevestigator; Q9BU02; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0050333; F:thiamin-triphosphatase activity; IDA:UniProtKB.
DR GO; GO:0016311; P:dephosphorylation; IDA:UniProtKB.
DR GO; GO:0006091; P:generation of precursor metabolites and energy; NAS:UniProtKB.
DR GO; GO:0006772; P:thiamine metabolic process; TAS:UniProtKB.
DR Gene3D; 2.40.320.10; -; 1.
DR InterPro; IPR023577; CYTH-like_domain.
DR InterPro; IPR012177; ThTPase.
DR PANTHER; PTHR14586; PTHR14586; 1.
DR Pfam; PF01928; CYTH; 1.
DR PIRSF; PIRSF036561; ThTPase; 1.
DR SUPFAM; SSF55154; SSF55154; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Complete proteome;
KW Cytoplasm; Hydrolase; Magnesium; Metal-binding; Polymorphism;
KW Reference proteome.
FT INIT_MET 1 1 Removed (By similarity).
FT CHAIN 2 230 Thiamine-triphosphatase.
FT /FTId=PRO_0000221490.
FT METAL 7 7 Magnesium (By similarity).
FT METAL 9 9 Magnesium (By similarity).
FT METAL 145 145 Magnesium (By similarity).
FT METAL 157 157 Magnesium (By similarity).
FT METAL 159 159 Magnesium (By similarity).
FT BINDING 11 11 Substrate (By similarity).
FT BINDING 55 55 Substrate (By similarity).
FT BINDING 57 57 Substrate (By similarity).
FT BINDING 65 65 Substrate (By similarity).
FT BINDING 125 125 Substrate (By similarity).
FT BINDING 193 193 Substrate (By similarity).
FT MOD_RES 2 2 N-acetylalanine.
FT VAR_SEQ 96 105 LRADGLGAGD -> CLHRRQHQPS (in isoform 2).
FT /FTId=VSP_047213.
FT VAR_SEQ 106 230 Missing (in isoform 2).
FT /FTId=VSP_047214.
FT VARIANT 176 176 H -> R (in dbSNP:rs34015250).
FT /FTId=VAR_062152.
FT STRAND 5 12
FT HELIX 18 24
FT STRAND 28 41
FT HELIX 46 49
FT STRAND 53 57
FT TURN 58 60
FT STRAND 61 70
FT STRAND 77 82
FT HELIX 85 96
FT HELIX 106 113
FT STRAND 116 131
FT HELIX 132 135
FT STRAND 137 139
FT STRAND 141 149
FT STRAND 154 164
FT HELIX 165 167
FT HELIX 168 181
FT HELIX 193 201
FT HELIX 203 213
SQ SEQUENCE 230 AA; 25566 MW; 49B79C6C1D19D91D CRC64;
MAQGLIEVER KFLPGPGTEE RLQELGGTLE YRVTFRDTYY DTPELSLMQA DHWLRRREDS
GWELKCPGAA GVLGPHTEYK ELTAEPTIVA QLCKVLRADG LGAGDVAAVL GPLGLQEVAS
FVTKRSAWKL VLLGADEEEP QLRVDLDTAD FGYAVGEVEA LVHEEAEVPT ALEKIHRLSS
MLGVPAQETA PAKLIVYLQR FRPQDYQRLL EVNSSRERPQ ETEDPDHCLG
//
ID THTPA_HUMAN Reviewed; 230 AA.
AC Q9BU02; D3DS50; G3V4J3;
DT 03-OCT-2003, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 3.
DT 22-JAN-2014, entry version 114.
DE RecName: Full=Thiamine-triphosphatase;
DE Short=ThTPase;
DE EC=3.6.1.28;
GN Name=THTPA;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=11827967; DOI=10.1074/jbc.M111241200;
RA Lakaye B., Makarchikov A.F., Antunes A.F., Zorzi W., Coumans B.,
RA De Pauw E., Wins P., Grisar T., Bettendorff L.;
RT "Molecular characterization of a specific thiamine triphosphatase
RT widely expressed in mammalian tissues.";
RL J. Biol. Chem. 277:13771-13777(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Trachea;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Placenta;
RA Li W.B., Gruber C., Jessee J., Polayes D.;
RT "Full-length cDNA libraries and normalization.";
RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12508121; DOI=10.1038/nature01348;
RA Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
RA Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
RA Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S.,
RA Sun H., Du H., Pepin K., Artiguenave F., Robert C., Cruaud C.,
RA Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P.,
RA Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N.,
RA Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C.,
RA Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S.,
RA Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B.,
RA Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M.,
RA Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S.,
RA Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D.,
RA Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A.,
RA Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
RA Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
RA Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L.,
RA Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J.,
RA Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W.,
RA Quetier F., Waterston R., Hood L., Weissenbach J.;
RT "The DNA sequence and analysis of human chromosome 14.";
RL Nature 421:601-607(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lung;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Hydrolase highly specific for thiamine triphosphate
CC (ThTP).
CC -!- CATALYTIC ACTIVITY: Thiamine triphosphate + H(2)O = thiamine
CC diphosphate + phosphate.
CC -!- SUBUNIT: Monomer (By similarity).
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9BU02-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9BU02-2; Sequence=VSP_047213, VSP_047214;
CC Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Widely expressed but at a low level.
CC -!- SIMILARITY: Belongs to the ThTPase family.
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DR EMBL; AF432862; AAM22403.1; -; mRNA.
DR EMBL; AK057691; BAB71546.1; -; mRNA.
DR EMBL; BX161435; CAD61907.1; -; mRNA.
DR EMBL; BX378775; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AL135999; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471078; EAW66140.1; -; Genomic_DNA.
DR EMBL; CH471078; EAW66141.1; -; Genomic_DNA.
DR EMBL; BC002984; AAH02984.1; -; mRNA.
DR RefSeq; NP_001119811.1; NM_001126339.3.
DR RefSeq; NP_001242991.1; NM_001256062.2.
DR RefSeq; NP_001243250.1; NM_001256321.2.
DR RefSeq; NP_001243251.1; NM_001256322.2.
DR RefSeq; NP_001243252.1; NM_001256323.2.
DR RefSeq; NP_077304.1; NM_024328.5.
DR UniGene; Hs.655179; -.
DR UniGene; Hs.732304; -.
DR UniGene; Hs.736905; -.
DR PDB; 3BHD; X-ray; 1.50 A; A/B=1-215.
DR PDB; 3TVL; X-ray; 2.30 A; A/B=1-230.
DR PDBsum; 3BHD; -.
DR PDBsum; 3TVL; -.
DR ProteinModelPortal; Q9BU02; -.
DR SMR; Q9BU02; 3-208.
DR IntAct; Q9BU02; 1.
DR STRING; 9606.ENSP00000288014; -.
DR DrugBank; DB00152; Thiamine.
DR PhosphoSite; Q9BU02; -.
DR DMDM; 37538018; -.
DR PaxDb; Q9BU02; -.
DR PeptideAtlas; Q9BU02; -.
DR PRIDE; Q9BU02; -.
DR DNASU; 79178; -.
DR Ensembl; ENST00000288014; ENSP00000288014; ENSG00000259431.
DR Ensembl; ENST00000404535; ENSP00000384580; ENSG00000259431.
DR Ensembl; ENST00000554789; ENSP00000450459; ENSG00000259431.
DR Ensembl; ENST00000556015; ENSP00000451835; ENSG00000259431.
DR GeneID; 79178; -.
DR KEGG; hsa:79178; -.
DR UCSC; uc031qnv.1; human.
DR CTD; 79178; -.
DR GeneCards; GC14P024025; -.
DR HGNC; HGNC:18987; THTPA.
DR HPA; HPA028876; -.
DR MIM; 611612; gene.
DR neXtProt; NX_Q9BU02; -.
DR PharmGKB; PA38774; -.
DR eggNOG; NOG42323; -.
DR HOGENOM; HOG000154571; -.
DR HOVERGEN; HBG057173; -.
DR InParanoid; Q9BU02; -.
DR KO; K05307; -.
DR OMA; RDTYYDT; -.
DR OrthoDB; EOG7288SN; -.
DR PhylomeDB; Q9BU02; -.
DR BRENDA; 3.6.1.28; 2681.
DR Reactome; REACT_111217; Metabolism.
DR Reactome; REACT_116125; Disease.
DR EvolutionaryTrace; Q9BU02; -.
DR GenomeRNAi; 79178; -.
DR NextBio; 68161; -.
DR PRO; PR:Q9BU02; -.
DR ArrayExpress; Q9BU02; -.
DR Bgee; Q9BU02; -.
DR CleanEx; HS_THTPA; -.
DR Genevestigator; Q9BU02; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0050333; F:thiamin-triphosphatase activity; IDA:UniProtKB.
DR GO; GO:0016311; P:dephosphorylation; IDA:UniProtKB.
DR GO; GO:0006091; P:generation of precursor metabolites and energy; NAS:UniProtKB.
DR GO; GO:0006772; P:thiamine metabolic process; TAS:UniProtKB.
DR Gene3D; 2.40.320.10; -; 1.
DR InterPro; IPR023577; CYTH-like_domain.
DR InterPro; IPR012177; ThTPase.
DR PANTHER; PTHR14586; PTHR14586; 1.
DR Pfam; PF01928; CYTH; 1.
DR PIRSF; PIRSF036561; ThTPase; 1.
DR SUPFAM; SSF55154; SSF55154; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Complete proteome;
KW Cytoplasm; Hydrolase; Magnesium; Metal-binding; Polymorphism;
KW Reference proteome.
FT INIT_MET 1 1 Removed (By similarity).
FT CHAIN 2 230 Thiamine-triphosphatase.
FT /FTId=PRO_0000221490.
FT METAL 7 7 Magnesium (By similarity).
FT METAL 9 9 Magnesium (By similarity).
FT METAL 145 145 Magnesium (By similarity).
FT METAL 157 157 Magnesium (By similarity).
FT METAL 159 159 Magnesium (By similarity).
FT BINDING 11 11 Substrate (By similarity).
FT BINDING 55 55 Substrate (By similarity).
FT BINDING 57 57 Substrate (By similarity).
FT BINDING 65 65 Substrate (By similarity).
FT BINDING 125 125 Substrate (By similarity).
FT BINDING 193 193 Substrate (By similarity).
FT MOD_RES 2 2 N-acetylalanine.
FT VAR_SEQ 96 105 LRADGLGAGD -> CLHRRQHQPS (in isoform 2).
FT /FTId=VSP_047213.
FT VAR_SEQ 106 230 Missing (in isoform 2).
FT /FTId=VSP_047214.
FT VARIANT 176 176 H -> R (in dbSNP:rs34015250).
FT /FTId=VAR_062152.
FT STRAND 5 12
FT HELIX 18 24
FT STRAND 28 41
FT HELIX 46 49
FT STRAND 53 57
FT TURN 58 60
FT STRAND 61 70
FT STRAND 77 82
FT HELIX 85 96
FT HELIX 106 113
FT STRAND 116 131
FT HELIX 132 135
FT STRAND 137 139
FT STRAND 141 149
FT STRAND 154 164
FT HELIX 165 167
FT HELIX 168 181
FT HELIX 193 201
FT HELIX 203 213
SQ SEQUENCE 230 AA; 25566 MW; 49B79C6C1D19D91D CRC64;
MAQGLIEVER KFLPGPGTEE RLQELGGTLE YRVTFRDTYY DTPELSLMQA DHWLRRREDS
GWELKCPGAA GVLGPHTEYK ELTAEPTIVA QLCKVLRADG LGAGDVAAVL GPLGLQEVAS
FVTKRSAWKL VLLGADEEEP QLRVDLDTAD FGYAVGEVEA LVHEEAEVPT ALEKIHRLSS
MLGVPAQETA PAKLIVYLQR FRPQDYQRLL EVNSSRERPQ ETEDPDHCLG
//
MIM
611612
*RECORD*
*FIELD* NO
611612
*FIELD* TI
*611612 THIAMINE TRIPHOSPHATASE; THTPA
;;THTPase
*FIELD* TX
DESCRIPTION
Thiamine triphosphatase (THTPA) catalyzes the hydrolysis of thiamine
read moretriphosphate (THTP) to thiamine diphosphate (THDP), which is the major
cellular form of thiamine (vitamin B1) (Lakaye et al., 2002).
CLONING
By database analysis using peptide sequence from purified bovine soluble
thiamine triphosphate as probe, followed by RT-PCR of human brain
poly(A+) RNA, Lakaye et al. (2002) cloned THTPA. The deduced 230-amino
acid protein has a predicted molecular mass of 25.55 kD and contains a
high percentage of negatively-charged residues (17.4% glutamic acid and
aspartic acid). THTPA shares 80% and 70% sequence identity with the
bovine and macaque Thtpa enzymes, respectively. All 3 enzyme homologs
contain several potential phosphorylation sites. Dot-blot hybridization
of multiple human tissues detected widespread THTPA expression, but only
at low levels. The highest hybridization signals were observed in
uterus, testis, and prostate, followed by bladder, kidney, lung, and
thyroid gland. Lower signals were detected in various brain regions with
no detectable signal in cerebellum. Expression was particularly low in
the digestive system, fetal tissues, and transformed cell lines.
GENE FUNCTION
Lakaye et al. (2002) determined that both recombinant THTPA and native
THTPA enzyme purified from human cerebellar cortex catalyzed the highly
specific hydrolysis of thiamine triphosphate to thiamine diphosphate.
THTPA displayed an optimal pH of 8.5, similar to that observed in the
bovine enzyme, although the human enzyme had a broader pH spectrum.
Lakaye et al. (2002) noted that human THTPA displayed remarkable
insensitivity to chemical denaturation and proteolysis.
MAPPING
By genomic sequence analysis, Lakaye et al. (2002) mapped the THTPA gene
to chromosome 14.
*FIELD* RF
1. Lakaye, B.; Makarchikov, A. F.; Antunes, A. F.; Zorzi, W.; Coumans,
B.; De Pauw, E.; Wins, P.; Grisar, T.; Bettendorff, L.: Molecular
characterization of a specific thiamine triphosphatase widely expressed
in mammalian tissues. J. Biol. Chem. 277: 13771-13777, 2002.
*FIELD* CD
Dorothy S. Reilly: 11/21/2007
*FIELD* ED
carol: 11/26/2007
*RECORD*
*FIELD* NO
611612
*FIELD* TI
*611612 THIAMINE TRIPHOSPHATASE; THTPA
;;THTPase
*FIELD* TX
DESCRIPTION
Thiamine triphosphatase (THTPA) catalyzes the hydrolysis of thiamine
read moretriphosphate (THTP) to thiamine diphosphate (THDP), which is the major
cellular form of thiamine (vitamin B1) (Lakaye et al., 2002).
CLONING
By database analysis using peptide sequence from purified bovine soluble
thiamine triphosphate as probe, followed by RT-PCR of human brain
poly(A+) RNA, Lakaye et al. (2002) cloned THTPA. The deduced 230-amino
acid protein has a predicted molecular mass of 25.55 kD and contains a
high percentage of negatively-charged residues (17.4% glutamic acid and
aspartic acid). THTPA shares 80% and 70% sequence identity with the
bovine and macaque Thtpa enzymes, respectively. All 3 enzyme homologs
contain several potential phosphorylation sites. Dot-blot hybridization
of multiple human tissues detected widespread THTPA expression, but only
at low levels. The highest hybridization signals were observed in
uterus, testis, and prostate, followed by bladder, kidney, lung, and
thyroid gland. Lower signals were detected in various brain regions with
no detectable signal in cerebellum. Expression was particularly low in
the digestive system, fetal tissues, and transformed cell lines.
GENE FUNCTION
Lakaye et al. (2002) determined that both recombinant THTPA and native
THTPA enzyme purified from human cerebellar cortex catalyzed the highly
specific hydrolysis of thiamine triphosphate to thiamine diphosphate.
THTPA displayed an optimal pH of 8.5, similar to that observed in the
bovine enzyme, although the human enzyme had a broader pH spectrum.
Lakaye et al. (2002) noted that human THTPA displayed remarkable
insensitivity to chemical denaturation and proteolysis.
MAPPING
By genomic sequence analysis, Lakaye et al. (2002) mapped the THTPA gene
to chromosome 14.
*FIELD* RF
1. Lakaye, B.; Makarchikov, A. F.; Antunes, A. F.; Zorzi, W.; Coumans,
B.; De Pauw, E.; Wins, P.; Grisar, T.; Bettendorff, L.: Molecular
characterization of a specific thiamine triphosphatase widely expressed
in mammalian tissues. J. Biol. Chem. 277: 13771-13777, 2002.
*FIELD* CD
Dorothy S. Reilly: 11/21/2007
*FIELD* ED
carol: 11/26/2007