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Q8JZL3 (THTPA_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 78. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Thiamine-triphosphatase
Short name=ThTPase
EC=3.6.1.28
Gene names
Name:Thtpa
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length224 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Hydrolase highly specific for thiamine triphosphate (ThTP) By similarity.

Catalytic activity

Thiamine triphosphate + H2O = thiamine diphosphate + phosphate.

Subunit structure

Monomer By similarity.

Subcellular location

Cytoplasm By similarity.

Sequence similarities

Belongs to the ThTPase family.

Ontologies

Keywords
   Cellular componentCytoplasm
   Molecular functionHydrolase
   PTMAcetylation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological processthiamine metabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionthiamin-triphosphatase activity

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 224223Thiamine-triphosphatase
PRO_0000221492

Amino acid modifications

Modified residue21N-acetylalanine By similarity

Secondary structure

1 ................................. 224
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q8JZL3 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: D33C844FDA8277D9

FASTA22424,264
        10         20         30         40         50         60 
MAQGLIEVER KFAPGPDTEE RLQELGATLE HRVTFRDTYY DTSELSLMLS DHWLRQREGS 

        70         80         90        100        110        120 
GWELKCPGVT GVSGPHNEYV EVTSEAAIVA QLFELLGSGE QKPAGVAAVL GSLKLQEVAS 

       130        140        150        160        170        180 
FITTRSSWKL ALSGAHGQEP QLTIDLDSAD FGYAVGEVEA MVHEKAEVPA ALEKIITVSS 

       190        200        210        220 
MLGVPAQEEA PAKLMVYLQR FRPLDYQRLL EAASSGEATG DSAS

« Hide

References

« Hide 'large scale' references
[1]"Cloning and expression of mouse thiamine triphosphatase cDNA."
Lakaye B., Coumans B., Makarchikov A., Grisar T., Bettendorff L.
Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: C57BL/6.
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Skin.
[3]"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].
Strain: FVB/N.
Tissue: Mammary gland.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF432864 mRNA. Translation: AAM22405.1.
AK132479 mRNA. Translation: BAE21189.1.
BC025562 mRNA. Translation: AAH25562.1.
IPIIPI00128570.
RefSeqNP_694723.1. NM_153083.5.
UniGeneMm.319204.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2JMUNMR-A2-223[»]
ProteinModelPortalQ8JZL3.
SMRQ8JZL3. Positions 2-224.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ8JZL3.

PTM databases

PhosphoSiteQ8JZL3.

Proteomic databases

PRIDEQ8JZL3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000050575; ENSMUSP00000056026; ENSMUSG00000045691.
GeneID105663.
KEGGmmu:105663.
UCSCuc007tyb.2. mouse.

Organism-specific databases

CTD79178.
MGIMGI:2446078. Thtpa.

Phylogenomic databases

eggNOGroNOG08037.
GeneTreeENSGT00390000005996.
HOGENOMHBG716312.
HOVERGENHBG057173.
InParanoidQ8JZL3.
OMAQREGSGW.
OrthoDBEOG4Z62PN.
PhylomeDBQ8JZL3.

Gene expression databases

ArrayExpressQ8JZL3.
BgeeQ8JZL3.
CleanExMM_THTPA.
GenevestigatorQ8JZL3.
GermOnlineENSMUSG00000045691. Mus musculus.

Family and domain databases

InterProIPR023577. CYTH-like_domain.
IPR008172. CYTH_domain.
IPR012177. ThTPase.
[Graphical view]
Gene3DG3DSA:2.40.320.10. G3DSA:2.40.320.10. 1 hit.
KOK05307.
PANTHERPTHR14586. ThTPase. 1 hit.
PfamPF01928. CYTH. 1 hit.
[Graphical view]
PIRSFPIRSF036561. ThTPase. 1 hit.
SUPFAMSSF55154. mRNA_capping_enz_bsu. 1 hit.
ProtoNetSearch...

Other

NextBio357818.
SOURCESearch...

Entry information

Entry nameTHTPA_MOUSE
AccessionPrimary (citable) accession number: Q8JZL3
Secondary accession number(s): Q3V1G2, Q8C3P9
Entry history
Integrated into UniProtKB/Swiss-Prot: October 3, 2003
Last sequence update: January 23, 2007
Last modified: November 16, 2011
This is version 78 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents