Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q9R0M5

- TPK1_MOUSE

UniProt

Q9R0M5 - TPK1_MOUSE

Protein

Thiamin pyrophosphokinase 1

Gene

Tpk1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 111 (01 Oct 2014)
      Sequence version 1 (01 May 2000)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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

    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

    Pathology & Biotechi

    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 – 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.
    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. 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

    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:
    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

    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: October 1, 2014
    This is version 111 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