Q9BU02 (THTPA_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Thiamine-triphosphatase
Short name=ThTPase
EC=3.6.1.28

Gene names

Name:

THTPA

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	230 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Hydrolase highly specific for thiamine triphosphate (ThTP). Ref.1
Catalytic activity	Thiamine triphosphate + H2O = thiamine diphosphate + phosphate.
Subunit structure	Monomer By similarity.
Subcellular location	Cytoplasm Ref.1.
Tissue specificity	Widely expressed but at a low level. Ref.1
Sequence similarities	Belongs to the ThTPase family.

Ontologies

Keywords
Cellular component	Cytoplasm
Coding sequence diversity	Polymorphism
Ligand	Magnesium Metal-binding
Molecular function	Hydrolase
PTM	Acetylation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	dephosphorylation Inferred from direct assay Ref.1. Source: UniProtKB generation of precursor metabolites and energy Non-traceable author statement Ref.1. Source: UniProtKB thiamine metabolic process Traceable author statement Ref.1. Source: UniProtKB
Cellular_component	cytosol Traceable author statement. Source: Reactome nucleolus Inferred from direct assay. Source: HPA
Molecular_function	metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW thiamin-triphosphatase activity Inferred from direct assay Ref.1. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed By similarity

Chain

2 – 230

229

Thiamine-triphosphatase

PRO_0000221490

Sites

Metal binding

7

1

Magnesium By similarity

Metal binding

9

1

Magnesium By similarity

Metal binding

145

1

Magnesium By similarity

Metal binding

157

1

Magnesium By similarity

Metal binding

159

1

Magnesium By similarity

Binding site

11

1

Substrate By similarity

Binding site

55

1

Substrate By similarity

Binding site

57

1

Substrate By similarity

Binding site

65

1

Substrate By similarity

Binding site

125

1

Substrate By similarity

Binding site

193

1

Substrate By similarity

Amino acid modifications

Modified residue

2

1

N-acetylalanine By similarity

Natural variations

Natural variant

176

1

H → R.
Corresponds to variant rs34015250 [ dbSNP | Ensembl ].

VAR_062152

Secondary structure

1

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230

Helix Strand Turn

Details...

Beta strand

5 – 12

8

Helix

18 – 24

7

Beta strand

28 – 41

14

Helix

46 – 49

4

Beta strand

53 – 57

5

Turn

58 – 60

3

Beta strand

61 – 70

10

Beta strand

77 – 82

6

Helix

85 – 96

12

Helix

106 – 113

8

Beta strand

116 – 131

16

Helix

132 – 135

4

Beta strand

137 – 139

3

Beta strand

141 – 149

9

Beta strand

154 – 164

11

Helix

165 – 167

3

Helix

168 – 181

14

Helix

193 – 201

9

Helix

203 – 213

11

Sequences

	Sequence		Length	Mass (Da)
	Q9BU02 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 49B79C6C1D19D91D	FASTA	230	25,566
	10 20 30 40 50 60 MAQGLIEVER KFLPGPGTEE RLQELGGTLE YRVTFRDTYY DTPELSLMQA DHWLRRREDS 70 80 90 100 110 120 GWELKCPGAA GVLGPHTEYK ELTAEPTIVA QLCKVLRADG LGAGDVAAVL GPLGLQEVAS 130 140 150 160 170 180 FVTKRSAWKL VLLGADEEEP QLRVDLDTAD FGYAVGEVEA LVHEEAEVPT ALEKIHRLSS 190 200 210 220 230 MLGVPAQETA PAKLIVYLQR FRPQDYQRLL EVNSSRERPQ ETEDPDHCLG

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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], 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]. 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]. 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]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases 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]. Tissue: Lung.
[7]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF432862 mRNA. Translation: AAM22403.1.
AK057691 mRNA. Translation: BAB71546.1.
BX161435 mRNA. Translation: CAD61907.1.
AL135999 Genomic DNA. No translation available.
CH471078 Genomic DNA. Translation: EAW66140.1.
CH471078 Genomic DNA. Translation: EAW66141.1.
BC002984 mRNA. Translation: AAH02984.1.

IPI

IPI00013621.

RefSeq

NP_001119811.1. NM_001126339.2.
NP_001243250.1. NM_001256321.1.
NP_001243251.1. NM_001256322.1.
NP_001243252.1. NM_001256323.1.
NP_077304.1. NM_024328.4.

UniGene

Hs.655179.
Hs.732304.
Hs.736905.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

Q9BU02.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q9BU02. 1 interaction.

STRING

9606.ENSP00000288014.

PTM databases

PhosphoSite

Q9BU02.

Polymorphism databases

DMDM

37538018.

Proteomic databases

PaxDb

Q9BU02.

PeptideAtlas

Q9BU02.

PRIDE

Q9BU02.

Protocols and materials databases

DNASU

79178.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000288014; ENSP00000288014; ENSG00000259431.
ENST00000404535; ENSP00000384580; ENSG00000259431.

GeneID

79178.

KEGG

hsa:79178.

UCSC

uc001wkg.4. human.

Organism-specific databases

CTD

79178.

GeneCards

GC14P024025.

HGNC

HGNC:18987. THTPA.

HPA

HPA028876.

MIM

611612. gene.

neXtProt

NX_Q9BU02.

PharmGKB

PA38774.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG42323.

HOGENOM

HOG000154571.

HOVERGEN

HBG057173.

InParanoid

Q9BU02.

KO

K05307.

OMA

RDTYYDT.

OrthoDB

EOG4Z62PN.

PhylomeDB

Q9BU02.

Enzyme and pathway databases

BRENDA

3.6.1.28. 2681.

Reactome

REACT_111217. Metabolism.

Gene expression databases

ArrayExpress

Q9BU02.

Bgee

Q9BU02.

CleanEx

HS_THTPA.

Genevestigator

Q9BU02.

GermOnline

ENSG00000157306. Homo sapiens.

Family and domain databases

Gene3D

2.40.320.10. 1 hit.

InterPro

IPR023577. CYTH-like_domain.
IPR012177. ThTPase.
[Graphical view]

PANTHER

PTHR14586. PTHR14586. 1 hit.

Pfam

PF01928. CYTH. 1 hit.
[Graphical view]

PIRSF

PIRSF036561. ThTPase. 1 hit.

SUPFAM

SSF55154. mRNA_capping_enz_bsu. 1 hit.

ProtoNet

Search...

Other

DrugBank

DB00152. Thiamine.

EvolutionaryTrace

Q9BU02.

GenomeRNAi

79178.

NextBio

68161.

SOURCE

Search...

Entry information

Entry name

THTPA_HUMAN

Accession

Primary (citable) accession number: Q9BU02
Secondary accession number(s): D3DS50

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 3, 2003
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 107 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.