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Protein

Thiamin pyrophosphokinase 1

Gene

Tpk1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the phosphorylation of thiamine to thiamine pyrophosphate. Can also catalyze the phosphorylation of pyrithiamine to pyrithiamine pyrophosphate.2 Publications

Catalytic activityi

ATP + thiamine = AMP + thiamine diphosphate.

Pathwayi

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • kinase activity Source: UniProtKB-KW
  • thiamine binding Source: InterPro
  • thiamine diphosphokinase activity Source: MGI

GO - Biological processi

  • thiamine diphosphate biosynthetic process Source: GO_Central
  • thiamine metabolic process Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_295805. Vitamin B1 (thiamin) metabolism.
UniPathwayiUPA00060; UER00597.

Names & Taxonomyi

Protein namesi
Recommended name:
Thiamin pyrophosphokinase 1 (EC:2.7.6.2)
Short name:
mTPK1
Alternative name(s):
Thiamine pyrophosphokinase 1
Gene namesi
Name:Tpk1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 6

Organism-specific databases

MGIiMGI:1352500. Tpk1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 243243Thiamin pyrophosphokinase 1PRO_0000072648Add
BLAST

Proteomic databases

MaxQBiQ9R0M5.
PaxDbiQ9R0M5.
PRIDEiQ9R0M5.

PTM databases

PhosphoSiteiQ9R0M5.

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiQ9R0M5.
CleanExiMM_TPK1.
GenevestigatoriQ9R0M5.

Interactioni

Subunit structurei

Homodimer.3 Publications

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000065631.

Structurei

Secondary structure

1
243
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 53Combined sources
Helixi9 – 113Combined sources
Beta strandi12 – 143Combined sources
Beta strandi19 – 235Combined sources
Helixi32 – 387Combined sources
Beta strandi40 – 456Combined sources
Helixi48 – 547Combined sources
Helixi60 – 623Combined sources
Beta strandi66 – 705Combined sources
Beta strandi72 – 754Combined sources
Helixi77 – 859Combined sources
Beta strandi89 – 924Combined sources
Helixi100 – 11415Combined sources
Beta strandi120 – 1256Combined sources
Beta strandi128 – 1303Combined sources
Helixi132 – 14413Combined sources
Helixi145 – 1473Combined sources
Beta strandi153 – 1575Combined sources
Beta strandi160 – 1656Combined sources
Beta strandi167 – 1737Combined sources
Beta strandi179 – 1868Combined sources
Beta strandi192 – 20211Combined sources
Beta strandi205 – 2106Combined sources
Turni211 – 2133Combined sources
Beta strandi216 – 2194Combined sources
Beta strandi223 – 23311Combined sources
Beta strandi235 – 2417Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1IG3X-ray1.90A/B1-243[»]
2F17X-ray2.50A/B1-243[»]
ProteinModelPortaliQ9R0M5.
SMRiQ9R0M5. Positions 1-243.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9R0M5.

Family & Domainsi

Sequence similaritiesi

Belongs to the thiamine pyrophosphokinase family.Curated

Phylogenomic databases

eggNOGiCOG1564.
GeneTreeiENSGT00390000016016.
HOGENOMiHOG000180834.
HOVERGENiHBG003568.
InParanoidiQ9R0M5.
KOiK00949.
OMAiNYFRHLW.
OrthoDBiEOG76HQ2J.
PhylomeDBiQ9R0M5.
TreeFamiTF313224.

Family and domain databases

Gene3Di2.60.120.320. 1 hit.
3.40.50.10240. 1 hit.
InterProiIPR006282. Thi_PPkinase.
IPR016966. Thiamin_pyrophosphokinase_euk.
IPR007373. Thiamin_PyroPKinase_B1-bd.
IPR007371. TPK_catalytic.
[Graphical view]
PfamiPF04265. TPK_B1_binding. 1 hit.
PF04263. TPK_catalytic. 1 hit.
[Graphical view]
PIRSFiPIRSF031057. Thiamin_pyrophosphokinase. 1 hit.
SMARTiSM00983. TPK_B1_binding. 1 hit.
[Graphical view]
SUPFAMiSSF63862. SSF63862. 1 hit.
SSF63999. SSF63999. 1 hit.
TIGRFAMsiTIGR01378. thi_PPkinase. 1 hit.

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9R0M5-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MEHAFTPLEP LLPTGNLKYC LVVLNQPLDA RFRHLWKKAL LRACADGGAN
60 70 80 90 100
HLYDLTEGER ESFLPEFVSG DFDSIRPEVK EYYTKKGCDL ISTPDQDHTD
110 120 130 140 150
FTKCLQVLQR KIEEKELQVD VIVTLGGLGG RFDQIMASVN TLFQATHITP
160 170 180 190 200
VPIIIIQKDS LIYLLQPGKH RLHVDTGMEG SWCGLIPVGQ PCNQVTTTGL
210 220 230 240
KWNLTNDVLG FGTLVSTSNT YDGSGLVTVE TDHPLLWTMA IKS
Length:243
Mass (Da):27,068
Last modified:May 1, 2000 - v1
Checksum:i946896D2493F44EA
GO
Isoform 2 (identifier: Q9R0M5-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     119-167: Missing.

Show »
Length:194
Mass (Da):21,766
Checksum:i58E61181F8A33A9B
GO
Isoform 3 (identifier: Q9R0M5-3) [UniParc]FASTAAdd to basket

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.

Show »
Length:63
Mass (Da):7,237
Checksum:i1AEFBAE8B507EC14
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti20 – 201C → W in BAC25948 (PubMed:16141072).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei39 – 6325ALLRA…ERESF → VLGKKSQEVLAERRLIEPLG IQSSL in isoform 3. 1 PublicationVSP_009595Add
BLAST
Alternative sequencei64 – 243180Missing in isoform 3. 1 PublicationVSP_009596Add
BLAST
Alternative sequencei119 – 16749Missing in isoform 2. 2 PublicationsVSP_009597Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS39474.1. [Q9R0M5-1]
RefSeqiNP_038889.1. NM_013861.3. [Q9R0M5-1]
XP_006506283.1. XM_006506220.2. [Q9R0M5-2]
UniGeneiMm.320979.

Genome annotation databases

EnsembliENSMUST00000067888; ENSMUSP00000065631; ENSMUSG00000029735. [Q9R0M5-1]
ENSMUST00000114644; ENSMUSP00000110291; ENSMUSG00000029735. [Q9R0M5-2]
ENSMUST00000150599; ENSMUSP00000121115; ENSMUSG00000029735. [Q9R0M5-3]
GeneIDi29807.
KEGGimmu:29807.
UCSCiuc009bsq.1. mouse. [Q9R0M5-1]
uc009bsr.1. mouse. [Q9R0M5-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS39474.1. [Q9R0M5-1]
RefSeqiNP_038889.1. NM_013861.3. [Q9R0M5-1]
XP_006506283.1. XM_006506220.2. [Q9R0M5-2]
UniGeneiMm.320979.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1IG3X-ray1.90A/B1-243[»]
2F17X-ray2.50A/B1-243[»]
ProteinModelPortaliQ9R0M5.
SMRiQ9R0M5. Positions 1-243.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000065631.

PTM databases

PhosphoSiteiQ9R0M5.

Proteomic databases

MaxQBiQ9R0M5.
PaxDbiQ9R0M5.
PRIDEiQ9R0M5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000067888; ENSMUSP00000065631; ENSMUSG00000029735. [Q9R0M5-1]
ENSMUST00000114644; ENSMUSP00000110291; ENSMUSG00000029735. [Q9R0M5-2]
ENSMUST00000150599; ENSMUSP00000121115; ENSMUSG00000029735. [Q9R0M5-3]
GeneIDi29807.
KEGGimmu:29807.
UCSCiuc009bsq.1. mouse. [Q9R0M5-1]
uc009bsr.1. mouse. [Q9R0M5-2]

Organism-specific databases

CTDi27010.
MGIiMGI:1352500. Tpk1.

Phylogenomic databases

eggNOGiCOG1564.
GeneTreeiENSGT00390000016016.
HOGENOMiHOG000180834.
HOVERGENiHBG003568.
InParanoidiQ9R0M5.
KOiK00949.
OMAiNYFRHLW.
OrthoDBiEOG76HQ2J.
PhylomeDBiQ9R0M5.
TreeFamiTF313224.

Enzyme and pathway databases

UniPathwayiUPA00060; UER00597.
ReactomeiREACT_295805. Vitamin B1 (thiamin) metabolism.

Miscellaneous databases

EvolutionaryTraceiQ9R0M5.
NextBioi306944.
PROiQ9R0M5.
SOURCEiSearch...

Gene expression databases

BgeeiQ9R0M5.
CleanExiMM_TPK1.
GenevestigatoriQ9R0M5.

Family and domain databases

Gene3Di2.60.120.320. 1 hit.
3.40.50.10240. 1 hit.
InterProiIPR006282. Thi_PPkinase.
IPR016966. Thiamin_pyrophosphokinase_euk.
IPR007373. Thiamin_PyroPKinase_B1-bd.
IPR007371. TPK_catalytic.
[Graphical view]
PfamiPF04265. TPK_B1_binding. 1 hit.
PF04263. TPK_catalytic. 1 hit.
[Graphical view]
PIRSFiPIRSF031057. Thiamin_pyrophosphokinase. 1 hit.
SMARTiSM00983. TPK_B1_binding. 1 hit.
[Graphical view]
SUPFAMiSSF63862. SSF63862. 1 hit.
SSF63999. SSF63999. 1 hit.
TIGRFAMsiTIGR01378. thi_PPkinase. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry nameiTPK1_MOUSE
AccessioniPrimary (citable) accession number: Q9R0M5
Secondary accession number(s): Q3UWB5
, Q8CAB5, Q8CEE8, Q8R1Q6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 1, 2004
Last sequence update: May 1, 2000
Last modified: May 27, 2015
This is version 115 of the entry and version 1 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.