Thiamine-triphosphatase - Homo sapiens (Human)

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Reviewed, UniProtKB/Swiss-Prot Q9BU02 (THTPA_HUMAN)

Last modified June 16, 2009. Version 67. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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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)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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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.

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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.

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Ontologies

Keywords
Cellular component	Cytoplasm
Molecular function	Hydrolase
PTM	Acetylation
Technical term	3D-structure
Gene Ontology (GO)
Biological process	cAMP biosynthetic process Inferred from electronic annotation. Source: InterPro dephosphorylation Ref.1 Inferred from direct assay. Source: UniProtKB generation of precursor metabolites and energy Ref.1 Non-traceable author statement. Source: UniProtKB thiamin metabolic process Ref.1 Traceable author statement. Source: UniProtKB
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell soluble fraction Ref.1 Non-traceable author statement. Source: UniProtKB
Molecular function	adenylate cyclase activity Inferred from electronic annotation. Source: InterPro thiamin-triphosphatase activity Ref.1 Inferred from direct assay. Source: UniProtKB
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed By similarity

Chain

2 – 230

229

Thiamine-triphosphatase

PRO_0000221490

Amino acid modifications

Modified residue

N-acetylalanine By similarity

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Sequences

Sequence

Length

Mass (Da)

Tools

Q9BU02-1 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 49B79C6C1D19D91D
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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

« Hide

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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: 11827967] [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. Sugano S. Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [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. Weissenbach J. Nature 421:601-607(2003) [PubMed: 12508121] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Lung.
[6]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
+	Additional computationally mapped references.

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Cross-references

Sequence databases

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

IPI

IPI00013621.

RefSeq

NP_001119811.1.
NP_077304.1.

UniGene

Hs.655179

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3BHD	X-ray	1.50	A/B	1-215	[»]

ModBase

Search...

PTM databases

PhosphoSite

Q9BU02.

Proteomic databases

PeptideAtlas

Q9BU02.

PRIDE

Q9BU02.

Genome annotation databases

Ensembl

ENSG00000157306. Homo sapiens. [Contig view]

GeneID

79178.

KEGG

hsa:79178.

Organism-specific databases

GeneCards

GC14P023095.

H-InvDB

HIX0011542.

HGNC

HGNC:18987. THTPA.

MIM

611612. gene.

PharmGKB

PA38774.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

Q9BU02.

HOVERGEN

Q9BU02.

OMA

Q9BU02. EVERKFV.

Enzyme and pathway databases

BRENDA

3.6.1.28. 247.

Gene expression databases

ArrayExpress

Q9BU02.

Bgee

Q9BU02.

CleanEx

HS_THTPA.

GermOnline

ENSG00000157306. Homo sapiens.

Family and domain databases

InterPro

IPR008172. Adenylate_cyclase.
IPR012177. ThTPase.
[Graphical view]

PANTHER

PTHR14586. ThTPase. 1 hit.

Pfam

PF01928. CYTH. 1 hit.
[Graphical view]

PIRSF

PIRSF036561. ThTPase. 1 hit.

ProtoNet

Search...

Other Resources

DrugBank

DB00152. Thiamine.

NextBio

68161.

SOURCE

Search...

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Entry information

Entry name

THTPA_HUMAN

Accession

Primary (citable) accession number: Q9BU02

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 3, 2003
Last sequence update:	January 23, 2007
Last modified:	June 16, 2009
This is version 67 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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