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Q9R0M5

- TPK1_MOUSE

UniProt

Q9R0M5 - TPK1_MOUSE

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Protein
Thiamin pyrophosphokinase 1
Gene
Tpk1
Organism
Mus musculus (Mouse)
Status
Reviewed - 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

  1. ATP binding Source: UniProtKB-KW
  2. kinase activity Source: UniProtKB-KW
  3. thiamine diphosphokinase activity Source: MGI

GO - Biological processi

  1. thiamine diphosphate biosynthetic process Source: UniProtKB-UniPathway
  2. thiamine metabolic process Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_223427. 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: Chromosome 6

Organism-specific databases

MGIiMGI:1352500. Tpk1.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: Ensembl
Complete GO annotation...

Pathology & Biotechi

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 243243Thiamin pyrophosphokinase 1
PRO_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.2 Publications

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000065631.

Structurei

Secondary structure

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

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiQ9R0M5.

Family & Domainsi

Sequence similaritiesi

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. Align

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

MEHAFTPLEP LLPTGNLKYC LVVLNQPLDA RFRHLWKKAL LRACADGGAN    50
HLYDLTEGER ESFLPEFVSG DFDSIRPEVK EYYTKKGCDL ISTPDQDHTD 100
FTKCLQVLQR KIEEKELQVD VIVTLGGLGG RFDQIMASVN TLFQATHITP 150
VPIIIIQKDS LIYLLQPGKH RLHVDTGMEG SWCGLIPVGQ PCNQVTTTGL 200
KWNLTNDVLG FGTLVSTSNT YDGSGLVTVE TDHPLLWTMA IKS 243
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

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei39 – 6325ALLRA…ERESF → VLGKKSQEVLAERRLIEPLG IQSSL in isoform 3.
VSP_009595Add
BLAST
Alternative sequencei64 – 243180Missing in isoform 3.
VSP_009596Add
BLAST
Alternative sequencei119 – 16749Missing in isoform 2.
VSP_009597Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti20 – 201C → W in BAC25948. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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_006506220.1. [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:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS39474.1. [Q9R0M5-1 ]
RefSeqi NP_038889.1. NM_013861.3. [Q9R0M5-1 ]
XP_006506283.1. XM_006506220.1. [Q9R0M5-2 ]
UniGenei Mm.320979.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1IG3 X-ray 1.90 A/B 1-243 [» ]
2F17 X-ray 2.50 A/B 1-243 [» ]
ProteinModelPortali Q9R0M5.
SMRi Q9R0M5. Positions 1-243.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 10090.ENSMUSP00000065631.

Chemistry

DrugBanki DB00152. Thiamine.

PTM databases

PhosphoSitei Q9R0M5.

Proteomic databases

MaxQBi Q9R0M5.
PaxDbi Q9R0M5.
PRIDEi Q9R0M5.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000067888 ; ENSMUSP00000065631 ; ENSMUSG00000029735 . [Q9R0M5-1 ]
ENSMUST00000114644 ; ENSMUSP00000110291 ; ENSMUSG00000029735 . [Q9R0M5-2 ]
ENSMUST00000150599 ; ENSMUSP00000121115 ; ENSMUSG00000029735 . [Q9R0M5-3 ]
GeneIDi 29807.
KEGGi mmu:29807.
UCSCi uc009bsq.1. mouse. [Q9R0M5-1 ]
uc009bsr.1. mouse. [Q9R0M5-2 ]

Organism-specific databases

CTDi 27010.
MGIi MGI:1352500. Tpk1.

Phylogenomic databases

eggNOGi COG1564.
GeneTreei ENSGT00390000016016.
HOGENOMi HOG000180834.
HOVERGENi HBG003568.
InParanoidi Q9R0M5.
KOi K00949.
OMAi NYFRHLW.
OrthoDBi EOG76HQ2J.
PhylomeDBi Q9R0M5.
TreeFami TF313224.

Enzyme and pathway databases

UniPathwayi UPA00060 ; UER00597 .
Reactomei REACT_223427. Vitamin B1 (thiamin) metabolism.

Miscellaneous databases

EvolutionaryTracei Q9R0M5.
NextBioi 306944.
PROi Q9R0M5.
SOURCEi Search...

Gene expression databases

Bgeei Q9R0M5.
CleanExi MM_TPK1.
Genevestigatori Q9R0M5.

Family and domain databases

Gene3Di 2.60.120.320. 1 hit.
3.40.50.10240. 1 hit.
InterProi IPR006282. Thi_PPkinase.
IPR016966. Thiamin_pyrophosphokinase_euk.
IPR007373. Thiamin_PyroPKinase_B1-bd.
IPR007371. TPK_catalytic.
[Graphical view ]
Pfami PF04265. TPK_B1_binding. 1 hit.
PF04263. TPK_catalytic. 1 hit.
[Graphical view ]
PIRSFi PIRSF031057. Thiamin_pyrophosphokinase. 1 hit.
SMARTi SM00983. TPK_B1_binding. 1 hit.
[Graphical view ]
SUPFAMi SSF63862. SSF63862. 1 hit.
SSF63999. SSF63999. 1 hit.
TIGRFAMsi TIGR01378. thi_PPkinase. 1 hit.
ProtoNeti Search...

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: September 3, 2014
This is version 110 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

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