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Q8JZL3

- THTPA_MOUSE

UniProt

Q8JZL3 - THTPA_MOUSE

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Protein

Thiamine-triphosphatase

Gene

Thtpa

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Hydrolase highly specific for thiamine triphosphate (ThTP).1 Publication

Catalytic activityi

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

Cofactori

Mg2+1 PublicationNote: Binds 1 Mg(2+) ion per subunit.1 Publication

pH dependencei

Optimum pH is 7.5-9.5.1 Publication

Sites

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

GO - Molecular functioni

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

GO - Biological processi

  1. dephosphorylation Source: Ensembl
  2. thiamine diphosphate metabolic process Source: UniProtKB
  3. thiamine metabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_223427. Vitamin B1 (thiamin) metabolism.

Names & Taxonomyi

Protein namesi
Recommended name:
Thiamine-triphosphatase (EC:3.6.1.28)
Short name:
ThTPase
Gene namesi
Name:Thtpa
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 14

Organism-specific databases

MGIiMGI:2446078. Thtpa.

Subcellular locationi

Cytoplasm By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 224223Thiamine-triphosphatasePRO_0000221492Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ8JZL3.
PaxDbiQ8JZL3.
PRIDEiQ8JZL3.

PTM databases

PhosphoSiteiQ8JZL3.

Expressioni

Gene expression databases

BgeeiQ8JZL3.
CleanExiMM_THTPA.
GenevestigatoriQ8JZL3.

Interactioni

Subunit structurei

Monomer.1 Publication

Protein-protein interaction databases

IntActiQ8JZL3. 1 interaction.
MINTiMINT-4137740.

Structurei

Secondary structure

1
224
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 1412Combined sources
Helixi18 – 258Combined sources
Beta strandi28 – 4114Combined sources
Helixi46 – 494Combined sources
Beta strandi53 – 575Combined sources
Turni58 – 603Combined sources
Beta strandi61 – 666Combined sources
Beta strandi80 – 823Combined sources
Helixi85 – 9612Combined sources
Helixi106 – 1138Combined sources
Beta strandi116 – 13116Combined sources
Beta strandi141 – 1499Combined sources
Turni150 – 1523Combined sources
Beta strandi153 – 16311Combined sources
Helixi165 – 1673Combined sources
Helixi168 – 18215Combined sources
Beta strandi183 – 1853Combined sources
Helixi193 – 2019Combined sources
Helixi203 – 21210Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2JMUNMR-A2-224[»]
ProteinModelPortaliQ8JZL3.
SMRiQ8JZL3. Positions 2-224.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8JZL3.

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.
GeneTreeiENSGT00390000005996.
HOGENOMiHOG000154571.
HOVERGENiHBG057173.
InParanoidiQ8JZL3.
KOiK05307.
OMAiRDTYYDT.
OrthoDBiEOG7288SN.
PhylomeDBiQ8JZL3.
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]

Sequencei

Sequence statusi: Complete.

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

Q8JZL3-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAQGLIEVER KFAPGPDTEE RLQELGATLE HRVTFRDTYY DTSELSLMLS
60 70 80 90 100
DHWLRQREGS GWELKCPGVT GVSGPHNEYV EVTSEAAIVA QLFELLGSGE
110 120 130 140 150
QKPAGVAAVL GSLKLQEVAS FITTRSSWKL ALSGAHGQEP QLTIDLDSAD
160 170 180 190 200
FGYAVGEVEA MVHEKAEVPA ALEKIITVSS MLGVPAQEEA PAKLMVYLQR
210 220
FRPLDYQRLL EAASSGEATG DSAS
Length:224
Mass (Da):24,264
Last modified:January 23, 2007 - v3
Checksum:iD33C844FDA8277D9
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF432864 mRNA. Translation: AAM22405.1.
AK132479 mRNA. Translation: BAE21189.1.
BC025562 mRNA. Translation: AAH25562.1.
CCDSiCCDS27108.1.
RefSeqiNP_694723.1. NM_153083.5.
UniGeneiMm.319204.

Genome annotation databases

EnsembliENSMUST00000050575; ENSMUSP00000056026; ENSMUSG00000045691.
GeneIDi105663.
KEGGimmu:105663.
UCSCiuc007tyb.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF432864 mRNA. Translation: AAM22405.1 .
AK132479 mRNA. Translation: BAE21189.1 .
BC025562 mRNA. Translation: AAH25562.1 .
CCDSi CCDS27108.1.
RefSeqi NP_694723.1. NM_153083.5.
UniGenei Mm.319204.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2JMU NMR - A 2-224 [» ]
ProteinModelPortali Q8JZL3.
SMRi Q8JZL3. Positions 2-224.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi Q8JZL3. 1 interaction.
MINTi MINT-4137740.

PTM databases

PhosphoSitei Q8JZL3.

Proteomic databases

MaxQBi Q8JZL3.
PaxDbi Q8JZL3.
PRIDEi Q8JZL3.

Protocols and materials databases

DNASUi 105663.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000050575 ; ENSMUSP00000056026 ; ENSMUSG00000045691 .
GeneIDi 105663.
KEGGi mmu:105663.
UCSCi uc007tyb.2. mouse.

Organism-specific databases

CTDi 79178.
MGIi MGI:2446078. Thtpa.

Phylogenomic databases

eggNOGi NOG42323.
GeneTreei ENSGT00390000005996.
HOGENOMi HOG000154571.
HOVERGENi HBG057173.
InParanoidi Q8JZL3.
KOi K05307.
OMAi RDTYYDT.
OrthoDBi EOG7288SN.
PhylomeDBi Q8JZL3.
TreeFami TF333398.

Enzyme and pathway databases

Reactomei REACT_223427. Vitamin B1 (thiamin) metabolism.

Miscellaneous databases

EvolutionaryTracei Q8JZL3.
NextBioi 357818.
PROi Q8JZL3.
SOURCEi Search...

Gene expression databases

Bgeei Q8JZL3.
CleanExi MM_THTPA.
Genevestigatori Q8JZL3.

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

« Hide 'large scale' publications
  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.
    , 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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: FVB/N.
    Tissue: Mammary gland.
  4. "Structural basis for the catalytic mechanism of mammalian 25-kDa thiamine triphosphatase."
    Song J., Bettendorff L., Tonelli M., Markley J.L.
    J. Biol. Chem. 283:10939-10948(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 2-223, SUBUNIT, MAGNESIUM-BINDING SITES, SUBSTRATE-BINDING SITES, CATALYTIC ACTIVITY, FUNCTION, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES.

Entry informationi

Entry nameiTHTPA_MOUSE
AccessioniPrimary (citable) accession number: Q8JZL3
Secondary accession number(s): Q3V1G2, Q8C3P9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 3, 2003
Last sequence update: January 23, 2007
Last modified: November 26, 2014
This is version 101 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3