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Q9R0M5 (TPK1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 109. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Thiamin pyrophosphokinase 1

Short name=mTPK1
EC=2.7.6.2
Alternative name(s):
Thiamine pyrophosphokinase 1
Gene names
Name:Tpk1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length243 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the phosphorylation of thiamine to thiamine pyrophosphate. Can also catalyze the phosphorylation of pyrithiamine to pyrithiamine pyrophosphate. Ref.1 Ref.5

Catalytic activity

ATP + thiamine = AMP + thiamine diphosphate.

Pathway

Cofactor biosynthesis; thiamine diphosphate biosynthesis; thiamine diphosphate from thiamine: step 1/1.

Subunit structure

Homodimer. Ref.1 Ref.4

Tissue specificity

Detected in kidney and liver, and at lower levels in heart, brain and testis. Ref.1

Sequence similarities

Belongs to the thiamine pyrophosphokinase family.

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9R0M5-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q9R0M5-2)

The sequence of this isoform differs from the canonical sequence as follows:
     119-167: Missing.
Isoform 3 (identifier: Q9R0M5-3)

The sequence of this isoform differs from the canonical sequence as follows:
     39-63: ALLRACADGGANHLYDLTEGERESF → VLGKKSQEVLAERRLIEPLGIQSSL
     64-243: Missing.
Note: May be due to intron retention. No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 243243Thiamin pyrophosphokinase 1
PRO_0000072648

Natural variations

Alternative sequence39 – 6325ALLRA…ERESF → VLGKKSQEVLAERRLIEPLG IQSSL in isoform 3.
VSP_009595
Alternative sequence64 – 243180Missing in isoform 3.
VSP_009596
Alternative sequence119 – 16749Missing in isoform 2.
VSP_009597

Experimental info

Sequence conflict201C → W in BAC25948. Ref.2

Secondary structure

.................................................... 243
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 946896D2493F44EA

FASTA24327,068
        10         20         30         40         50         60 
MEHAFTPLEP LLPTGNLKYC LVVLNQPLDA RFRHLWKKAL LRACADGGAN HLYDLTEGER 

        70         80         90        100        110        120 
ESFLPEFVSG DFDSIRPEVK EYYTKKGCDL ISTPDQDHTD FTKCLQVLQR KIEEKELQVD 

       130        140        150        160        170        180 
VIVTLGGLGG RFDQIMASVN TLFQATHITP VPIIIIQKDS LIYLLQPGKH RLHVDTGMEG 

       190        200        210        220        230        240 
SWCGLIPVGQ PCNQVTTTGL KWNLTNDVLG FGTLVSTSNT YDGSGLVTVE TDHPLLWTMA 


IKS 

« Hide

Isoform 2 [UniParc].

Checksum: 58E61181F8A33A9B
Show »

FASTA19421,766
Isoform 3 [UniParc].

Checksum: 1AEFBAE8B507EC14
Show »

FASTA637,237

References

« Hide 'large scale' references
[1]"Molecular cloning and expression of a mouse thiamin pyrophosphokinase cDNA."
Nosaka K., Onozuka M., Nishino H., Nishimura H., Kawasaki Y., Ueyama H.
J. Biol. Chem. 274:34129-34133(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBUNIT, TISSUE SPECIFICITY.
Tissue: Embryo.
[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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
Strain: C57BL/6J.
Tissue: Colon, Embryo, Embryonic liver and Hypothalamus.
[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] (ISOFORMS 1 AND 2).
Tissue: Kidney.
[4]"Crystal structure of thiamin pyrophosphokinase."
Timm D.E., Liu J., Baker L.-J., Harris R.A.
J. Mol. Biol. 310:195-204(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF ISOFORM 1 IN COMPLEX WITH THIAMINE, HOMODIMERIZATION.
[5]"Pyrithiamine as a substrate for thiamine pyrophosphokinase."
Liu J.Y., Timm D.E., Hurley T.D.
J. Biol. Chem. 281:6601-6607(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF ISOFORM 2 IN COMPLEX WITH PYRITHIAMINE PYROPHOSPHATE AND AMP, FUNCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB027568 mRNA. Translation: BAA87040.1.
AK028431 mRNA. Translation: BAC25948.1.
AK035044 mRNA. Translation: BAC28923.1.
AK039131 mRNA. Translation: BAC30248.1.
AK136486 mRNA. Translation: BAE23001.1.
BC015246 mRNA. Translation: AAH15246.1.
BC023354 mRNA. Translation: AAH23354.1.
CCDSCCDS39474.1. [Q9R0M5-1]
RefSeqNP_038889.1. NM_013861.3. [Q9R0M5-1]
XP_006506283.1. XM_006506220.1. [Q9R0M5-2]
UniGeneMm.320979.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1IG3X-ray1.90A/B1-243[»]
2F17X-ray2.50A/B1-243[»]
ProteinModelPortalQ9R0M5.
SMRQ9R0M5. Positions 1-243.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10090.ENSMUSP00000065631.

Chemistry

DrugBankDB00152. Thiamine.

PTM databases

PhosphoSiteQ9R0M5.

Proteomic databases

MaxQBQ9R0M5.
PaxDbQ9R0M5.
PRIDEQ9R0M5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000067888; ENSMUSP00000065631; ENSMUSG00000029735. [Q9R0M5-1]
ENSMUST00000114644; ENSMUSP00000110291; ENSMUSG00000029735. [Q9R0M5-2]
ENSMUST00000150599; ENSMUSP00000121115; ENSMUSG00000029735. [Q9R0M5-3]
GeneID29807.
KEGGmmu:29807.
UCSCuc009bsq.1. mouse. [Q9R0M5-1]
uc009bsr.1. mouse. [Q9R0M5-2]

Organism-specific databases

CTD27010.
MGIMGI:1352500. Tpk1.

Phylogenomic databases

eggNOGCOG1564.
GeneTreeENSGT00390000016016.
HOGENOMHOG000180834.
HOVERGENHBG003568.
InParanoidQ9R0M5.
KOK00949.
OMANYFRHLW.
OrthoDBEOG76HQ2J.
PhylomeDBQ9R0M5.
TreeFamTF313224.

Enzyme and pathway databases

UniPathwayUPA00060; UER00597.

Gene expression databases

BgeeQ9R0M5.
CleanExMM_TPK1.
GenevestigatorQ9R0M5.

Family and domain databases

Gene3D2.60.120.320. 1 hit.
3.40.50.10240. 1 hit.
InterProIPR006282. Thi_PPkinase.
IPR016966. Thiamin_pyrophosphokinase_euk.
IPR007373. Thiamin_PyroPKinase_B1-bd.
IPR007371. TPK_catalytic.
[Graphical view]
PfamPF04265. TPK_B1_binding. 1 hit.
PF04263. TPK_catalytic. 1 hit.
[Graphical view]
PIRSFPIRSF031057. Thiamin_pyrophosphokinase. 1 hit.
SMARTSM00983. TPK_B1_binding. 1 hit.
[Graphical view]
SUPFAMSSF63862. SSF63862. 1 hit.
SSF63999. SSF63999. 1 hit.
TIGRFAMsTIGR01378. thi_PPkinase. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceQ9R0M5.
NextBio306944.
PROQ9R0M5.
SOURCESearch...

Entry information

Entry nameTPK1_MOUSE
AccessionPrimary (citable) accession number: Q9R0M5
Secondary accession number(s): Q3UWB5 expand/collapse secondary AC list , Q8CAB5, Q8CEE8, Q8R1Q6
Entry history
Integrated into UniProtKB/Swiss-Prot: March 1, 2004
Last sequence update: May 1, 2000
Last modified: July 9, 2014
This is version 109 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

MGD cross-references

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