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P17751

- TPIS_MOUSE

UniProt

P17751 - TPIS_MOUSE

Protein

Triosephosphate isomerase

Gene

Tpi1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 136 (01 Oct 2014)
      Sequence version 4 (19 Oct 2011)
      Previous versions | rss
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    Functioni

    Catalytic activityi

    D-glyceraldehyde 3-phosphate = glycerone phosphate.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei62 – 621SubstrateBy similarity
    Binding sitei64 – 641SubstrateBy similarity
    Active sitei146 – 1461ElectrophileBy similarity
    Active sitei216 – 2161Proton acceptorBy similarity

    GO - Molecular functioni

    1. isomerase activity Source: MGI
    2. triose-phosphate isomerase activity Source: MGI

    GO - Biological processi

    1. gluconeogenesis Source: UniProtKB-UniPathway
    2. glucose metabolic process Source: MGI
    3. glyceraldehyde-3-phosphate metabolic process Source: UniProtKB
    4. glycolytic process Source: MGI
    5. multicellular organismal development Source: MGI
    6. pentose-phosphate shunt Source: UniProtKB-KW

    Keywords - Molecular functioni

    Isomerase

    Keywords - Biological processi

    Gluconeogenesis, Glycolysis, Pentose shunt

    Enzyme and pathway databases

    SABIO-RKP17751.
    UniPathwayiUPA00109; UER00189.
    UPA00138.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Triosephosphate isomerase (EC:5.3.1.1)
    Short name:
    TIM
    Alternative name(s):
    Triose-phosphate isomerase
    Gene namesi
    Name:Tpi1
    Synonyms:Tpi
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 6

    Organism-specific databases

    MGIiMGI:98797. Tpi1.

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi213 – 2131L → Q: 50% reduced activity. 1 Publication
    Mutagenesisi243 – 2431L → Q: 50% reduced activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 299299Triosephosphate isomerasePRO_0000090116Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei64 – 641N6-acetyllysineBy similarity
    Modified residuei118 – 1181Nitrated tyrosine1 Publication
    Modified residuei130 – 1301PhosphoserineBy similarity
    Modified residuei199 – 1991N6-succinyllysine1 Publication
    Modified residuei206 – 2061N6-acetyllysine; alternate1 Publication
    Modified residuei206 – 2061N6-succinyllysine; alternate1 Publication
    Modified residuei244 – 2441N6-acetyllysine; alternate1 Publication
    Modified residuei244 – 2441N6-succinyllysine; alternate1 Publication
    Modified residuei259 – 2591Nitrated tyrosine1 Publication
    Modified residuei262 – 2621Phosphoserine1 Publication
    Modified residuei288 – 2881N6-acetyllysineBy similarity

    Keywords - PTMi

    Acetylation, Nitration, Phosphoprotein

    Proteomic databases

    MaxQBiP17751.
    PaxDbiP17751.
    PRIDEiP17751.

    2D gel databases

    COMPLUYEAST-2DPAGEP17751.
    REPRODUCTION-2DPAGEIPI00467833.
    P17751.
    SWISS-2DPAGEP17751.
    UCD-2DPAGEP17751.

    PTM databases

    PhosphoSiteiP17751.

    Expressioni

    Gene expression databases

    ArrayExpressiP17751.
    BgeeiP17751.
    CleanExiMM_TPI1.
    GenevestigatoriP17751.

    Interactioni

    Subunit structurei

    Homodimer.

    Protein-protein interaction databases

    BioGridi204290. 5 interactions.
    IntActiP17751. 11 interactions.
    MINTiMINT-1869495.

    Structurei

    3D structure databases

    ProteinModelPortaliP17751.
    SMRiP17751. Positions 55-299.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the triosephosphate isomerase family.Curated

    Phylogenomic databases

    eggNOGiCOG0149.
    GeneTreeiENSGT00390000013354.
    HOVERGENiHBG002599.
    InParanoidiP17751.
    KOiK01803.
    OMAiCVGGNWK.
    OrthoDBiEOG76DTT8.
    TreeFamiTF300829.

    Family and domain databases

    Gene3Di3.20.20.70. 1 hit.
    HAMAPiMF_00147_B. TIM_B.
    InterProiIPR013785. Aldolase_TIM.
    IPR022896. TrioseP_Isoase_bac/euk.
    IPR000652. Triosephosphate_isomerase.
    IPR020861. Triosephosphate_isomerase_AS.
    [Graphical view]
    PANTHERiPTHR21139. PTHR21139. 1 hit.
    PfamiPF00121. TIM. 1 hit.
    [Graphical view]
    SUPFAMiSSF51351. SSF51351. 1 hit.
    TIGRFAMsiTIGR00419. tim. 1 hit.
    PROSITEiPS00171. TIM_1. 1 hit.
    PS51440. TIM_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P17751-1 [UniParc]FASTAAdd to Basket

    « Hide

    MEGKAEQQGA GLTMAEGGEK EEFCFTAIYI SGQWREPCVC TDLQRLEPGT    50
    MAPTRKFFVG GNWKMNGRKK CLGELICTLN AANVPAGTEV VCAPPTAYID 100
    FARQKLDPKI AVAAQNCYKV TNGAFTGEIS PGMIKDLGAT WVVLGHSERR 150
    HVFGESDELI GQKVSHALAE GLGVIACIGE KLDEREAGIT EKVVFEQTKV 200
    IADNVKDWSK VVLAYEPVWA IGTGKTATPQ QAQEVHEKLR GWLKSNVNDG 250
    VAQSTRIIYG GSVTGATCKE LASQPDVDGF LVGGASLKPE FVDIINAKQ 299
    Length:299
    Mass (Da):32,192
    Last modified:October 19, 2011 - v4
    Checksum:iD465FD57108A3BD4
    GO

    Sequence cautioni

    The sequence AAC36016.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence AAH46761.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence BAB27194.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence BAE26832.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence BAE29073.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence BAE29810.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence BAE35334.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence BAE39523.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence BAE40350.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence BAE40594.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence CAA37420.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti124 – 1241A → P in CAA37420. (PubMed:2377473)Curated
    Sequence conflicti157 – 1571D → G in BAE39523. (PubMed:16141072)Curated
    Sequence conflicti244 – 2441K → R in BAB27194. (PubMed:16141072)Curated
    Sequence conflicti245 – 2451S → P in BAE26832. (PubMed:16141072)Curated
    Sequence conflicti266 – 2661A → G in BAB27194. (PubMed:16141072)Curated
    Sequence conflicti272 – 2721A → Q in BAB27194. (PubMed:16141072)Curated
    Sequence conflicti273 – 2753SQP → TPA in CAA37420. (PubMed:2377473)Curated
    Sequence conflicti277 – 2771V → M in BAB25634. (PubMed:16141072)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AC002397 Genomic DNA. Translation: AAC36016.1. Different initiation.
    AC142254 Genomic DNA. No translation available.
    AK008373 mRNA. Translation: BAB25634.1.
    AK010808 mRNA. Translation: BAB27194.1. Different initiation.
    AK146013 mRNA. Translation: BAE26832.1. Different initiation.
    AK149768 mRNA. Translation: BAE29073.1. Different initiation.
    AK150735 mRNA. Translation: BAE29810.1. Different initiation.
    AK159741 mRNA. Translation: BAE35334.1. Different initiation.
    AK167437 mRNA. Translation: BAE39523.1. Different initiation.
    AK168446 mRNA. Translation: BAE40350.1. Different initiation.
    AK168756 mRNA. Translation: BAE40594.1. Different initiation.
    X53333 mRNA. Translation: CAA37420.1. Different initiation.
    BC046761 mRNA. Translation: AAH46761.1. Different initiation.
    L31777 Genomic DNA. Translation: AAB48543.1.
    CCDSiCCDS20530.2.
    PIRiS10490. ISMST.
    RefSeqiNP_033441.2. NM_009415.2.
    UniGeneiMm.4222.
    Mm.439915.

    Genome annotation databases

    EnsembliENSMUST00000172132; ENSMUSP00000130858; ENSMUSG00000023456.
    GeneIDi21991.
    KEGGimmu:21991.
    UCSCiuc012esp.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AC002397 Genomic DNA. Translation: AAC36016.1 . Different initiation.
    AC142254 Genomic DNA. No translation available.
    AK008373 mRNA. Translation: BAB25634.1 .
    AK010808 mRNA. Translation: BAB27194.1 . Different initiation.
    AK146013 mRNA. Translation: BAE26832.1 . Different initiation.
    AK149768 mRNA. Translation: BAE29073.1 . Different initiation.
    AK150735 mRNA. Translation: BAE29810.1 . Different initiation.
    AK159741 mRNA. Translation: BAE35334.1 . Different initiation.
    AK167437 mRNA. Translation: BAE39523.1 . Different initiation.
    AK168446 mRNA. Translation: BAE40350.1 . Different initiation.
    AK168756 mRNA. Translation: BAE40594.1 . Different initiation.
    X53333 mRNA. Translation: CAA37420.1 . Different initiation.
    BC046761 mRNA. Translation: AAH46761.1 . Different initiation.
    L31777 Genomic DNA. Translation: AAB48543.1 .
    CCDSi CCDS20530.2.
    PIRi S10490. ISMST.
    RefSeqi NP_033441.2. NM_009415.2.
    UniGenei Mm.4222.
    Mm.439915.

    3D structure databases

    ProteinModelPortali P17751.
    SMRi P17751. Positions 55-299.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 204290. 5 interactions.
    IntActi P17751. 11 interactions.
    MINTi MINT-1869495.

    PTM databases

    PhosphoSitei P17751.

    2D gel databases

    COMPLUYEAST-2DPAGE P17751.
    REPRODUCTION-2DPAGE IPI00467833.
    P17751.
    SWISS-2DPAGE P17751.
    UCD-2DPAGE P17751.

    Proteomic databases

    MaxQBi P17751.
    PaxDbi P17751.
    PRIDEi P17751.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000172132 ; ENSMUSP00000130858 ; ENSMUSG00000023456 .
    GeneIDi 21991.
    KEGGi mmu:21991.
    UCSCi uc012esp.1. mouse.

    Organism-specific databases

    CTDi 7167.
    MGIi MGI:98797. Tpi1.

    Phylogenomic databases

    eggNOGi COG0149.
    GeneTreei ENSGT00390000013354.
    HOVERGENi HBG002599.
    InParanoidi P17751.
    KOi K01803.
    OMAi CVGGNWK.
    OrthoDBi EOG76DTT8.
    TreeFami TF300829.

    Enzyme and pathway databases

    UniPathwayi UPA00109 ; UER00189 .
    UPA00138 .
    SABIO-RK P17751.

    Miscellaneous databases

    ChiTaRSi TPI1. mouse.
    NextBioi 301728.
    PROi P17751.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P17751.
    Bgeei P17751.
    CleanExi MM_TPI1.
    Genevestigatori P17751.

    Family and domain databases

    Gene3Di 3.20.20.70. 1 hit.
    HAMAPi MF_00147_B. TIM_B.
    InterProi IPR013785. Aldolase_TIM.
    IPR022896. TrioseP_Isoase_bac/euk.
    IPR000652. Triosephosphate_isomerase.
    IPR020861. Triosephosphate_isomerase_AS.
    [Graphical view ]
    PANTHERi PTHR21139. PTHR21139. 1 hit.
    Pfami PF00121. TIM. 1 hit.
    [Graphical view ]
    SUPFAMi SSF51351. SSF51351. 1 hit.
    TIGRFAMsi TIGR00419. tim. 1 hit.
    PROSITEi PS00171. TIM_1. 1 hit.
    PS51440. TIM_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Comparative sequence analysis of a gene-rich cluster at human chromosome 12p13 and its syntenic region in mouse chromosome 6."
      Ansari-Lari M.A., Oeltjen J.C., Schwartz S., Zhang Z., Muzny D.M., Lu J., Gorrell J.H., Chinault A.C., Belmont J.W., Miller W., Gibbs R.A.
      Genome Res. 8:29-40(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    3. "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] OF 39-299.
      Strain: C57BL/6J.
      Tissue: Bone marrow, Placenta and Stomach.
    4. "Nucleotide sequence of murine triosephosphate isomerase cDNA."
      Cheng J., Mielnicki L.M., Pruitt S.C., Maquat L.E.
      Nucleic Acids Res. 18:4261-4261(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 40-299.
    5. "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] OF 43-299.
      Strain: C57BL/6.
      Tissue: Brain.
    6. Lubec G., Klug S., Yang J.W., Zigmond M., Kang S.U., Sunyer B., Chen W.-Q.
      Submitted (JAN-2009) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 56-64; 71-103; 110-181; 193-206; 211-238; 245-256 AND 270-298, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: C57BL/6 and OF1.
      Tissue: Brain and Hippocampus.
    7. "Molecular analysis of four ENU induced triosephosphate isomerase null mutants in Mus musculus."
      Zingg B.C., Pretsch W., Mohrenweiser H.W.
      Mutat. Res. 328:163-173(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 90-299, MUTAGENESIS OF LEU-213 AND LEU-243.
    8. Cited for: NITRATION [LARGE SCALE ANALYSIS] AT TYR-118 AND TYR-259, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Brain.
    9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-262, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    10. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
      Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
      Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-206 AND LYS-244, SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-199; LYS-206 AND LYS-244, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic fibroblast and Liver.

    Entry informationi

    Entry nameiTPIS_MOUSE
    AccessioniPrimary (citable) accession number: P17751
    Secondary accession number(s): Q3TJH2
    , Q3UC04, Q3UKG9, Q64513, Q9CVF9, Q9CWE7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1990
    Last sequence update: October 19, 2011
    Last modified: October 1, 2014
    This is version 136 of the entry and version 4 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Caution

    It is uncertain if Met-1 or Met-14 is the initiator.Curated

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3