Hmdb loader
Identification
HMDB Protein ID HMDBP01584
Secondary Accession Numbers
  • 6880
  • HMDBP06615
Name Triosephosphate isomerase
Synonyms
  1. TIM
  2. Triose-phosphate isomerase
Gene Name TPI1
Protein Type Enzyme
Biological Properties
General Function Involved in catalytic activity
Specific Function Not Available
Pathways
  • Fanconi-bickel syndrome
  • Fructose and mannose metabolism
  • Fructose and mannose metabolism
  • Fructose intolerance, hereditary
  • Fructose-1,6-diphosphatase deficiency
  • Fructosuria
  • gluconeogenesis
  • Gluconeogenesis
  • Glycogen Storage Disease Type 1A (GSD1A) or Von Gierke Disease
  • Glycogenosis, Type IA. Von gierke disease
  • Glycogenosis, Type IB
  • Glycogenosis, Type IC
  • Glycogenosis, Type VII. Tarui disease
  • glycolysis
  • Glycolysis
  • Glycolysis / Gluconeogenesis
  • Inositol phosphate metabolism
  • Phosphoenolpyruvate carboxykinase deficiency 1 (PEPCK1)
  • Triosephosphate isomerase
Reactions
Glyceraldehyde 3-phosphate → Dihydroxyacetone phosphate details
GO Classification
Biological Process
small molecule metabolic process
embryo development
pentose-phosphate shunt
glycolysis
gluconeogenesis
glyceraldehyde-3-phosphate metabolic process
Cellular Component
cytosol
nucleus
Function
catalytic activity
isomerase activity
intramolecular oxidoreductase activity
intramolecular oxidoreductase activity, interconverting aldoses and ketoses
triose-phosphate isomerase activity
Molecular Function
triose-phosphate isomerase activity
Process
metabolic process
Cellular Location Not Available
Gene Properties
Chromosome Location 12
Locus 12p13
SNPs TPI1
Gene Sequence
>750 bp
ATGGCGCCCTCCAGGAAGTTCTTCGTTGGGGGAAACTGGAAGATGAACGGGCGGAAGCAG
AGTCTGGGGGAGCTCATCGGCACTCTGAACGCGGCCAAGGTGCCGGCCGACACCGAGGTG
GTTTGTGCTCCCCCTACTGCCTATATCGACTTCGCCCGGCAGAAGCTAGATCCCAAGATT
GCTGTGGCTGCGCAGAACTGCTACAAAGTGACTAATGGGGCTTTTACTGGGGAGATCAGC
CCTGGCATGATCAAAGACTGCGGAGCCACGTGGGTGGTCCTGGGACACTCAGAGAGAAGG
CATGTCTTTGGGGAGTCAGATGAGCTGATTGGGCAGAAAGTGGCCCATGCTCTGGCAGAG
GGACTCGGAGTAATCGCCTGCATTGGGGAGAAGCTAGATGAAAGGGAAGCTGGCATCACT
GAGAAGGTTGTTTTCGAGCAGACAAAGGTCATCGCAGATAACGTGAAGGACTGGAGCAAG
GTCGTCCTCGCCTATGAGCCTGTGTGGGCCATTGGTACTGGCAAGACTGCAACACCCCAA
CAGGCCCAGGAAGTACACGAGAAGCTCCGAGGATGGCTGAAGTCCAACGTCTCTGATGCG
GTGGCTCAGAGCACCCGTATCATTTATGGAGGCTCTGTGACTGGGGCAACCTGCAAGGAG
CTGGCCAGCCAGCCTGATGTGGATGGCTTCCTTGTGGGTGGTGCTTCCCTCAAGCCCGAA
TTCGTGGACATCATCAATGCCAAACAATGA
Protein Properties
Number of Residues 249
Molecular Weight 26669.33
Theoretical pI 6.906
Pfam Domain Function
Signals Not Available
Transmembrane Regions Not Available
Protein Sequence
>Triosephosphate isomerase
MAPSRKFFVGGNWKMNGRKQSLGELIGTLNAAKVPADTEVVCAPPTAYIDFARQKLDPKI
AVAAQNCYKVTNGAFTGEISPGMIKDCGATWVVLGHSERRHVFGESDELIGQKVAHALAE
GLGVIACIGEKLDEREAGITEKVVFEQTKVIADNVKDWSKVVLAYEPVWAIGTGKTATPQ
QAQEVHEKLRGWLKSNVSDAVAQSTRIIYGGSVTGATCKELASQPDVDGFLVGGASLKPE
FVDIINAKQ
GenBank ID Protein 339841
UniProtKB/Swiss-Prot ID P60174
UniProtKB/Swiss-Prot Entry Name TPIS_HUMAN
PDB IDs
GenBank Gene ID M10036
GeneCard ID TPI1
GenAtlas ID TPI1
HGNC ID HGNC:12009
References
General References
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  3. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. doi: 10.1126/science.1175371. Epub 2009 Jul 16. [PubMed:19608861 ]
  4. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. doi: 10.1073/pnas.0805139105. Epub 2008 Jul 31. [PubMed:18669648 ]
  5. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. doi: 10.1126/scisignal.2000007. [PubMed:19690332 ]
  6. Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed:17081983 ]
  7. Yu LR, Zhu Z, Chan KC, Issaq HJ, Dimitrov DS, Veenstra TD: Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra. J Proteome Res. 2007 Nov;6(11):4150-62. Epub 2007 Oct 9. [PubMed:17924679 ]
  8. Imami K, Sugiyama N, Kyono Y, Tomita M, Ishihama Y: Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column. Anal Sci. 2008 Jan;24(1):161-6. [PubMed:18187866 ]
  9. Kim SC, Sprung R, Chen Y, Xu Y, Ball H, Pei J, Cheng T, Kho Y, Xiao H, Xiao L, Grishin NV, White M, Yang XJ, Zhao Y: Substrate and functional diversity of lysine acetylation revealed by a proteomics survey. Mol Cell. 2006 Aug;23(4):607-18. [PubMed:16916647 ]
  10. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. doi: 10.1021/ac9004309. [PubMed:19413330 ]
  11. Tang LY, Deng N, Wang LS, Dai J, Wang ZL, Jiang XS, Li SJ, Li L, Sheng QH, Wu DQ, Li L, Zeng R: Quantitative phosphoproteome profiling of Wnt3a-mediated signaling network: indicating the involvement of ribonucleoside-diphosphate reductase M2 subunit phosphorylation at residue serine 20 in canonical Wnt signal transduction. Mol Cell Proteomics. 2007 Nov;6(11):1952-67. Epub 2007 Aug 12. [PubMed:17693683 ]
  12. Rasmussen RK, Ji H, Eddes JS, Moritz RL, Reid GE, Simpson RJ, Dorow DS: Two-dimensional electrophoretic analysis of human breast carcinoma proteins: mapping of proteins that bind to the SH3 domain of mixed lineage kinase MLK2. Electrophoresis. 1997 Mar-Apr;18(3-4):588-98. [PubMed:9150946 ]
  13. Ji H, Reid GE, Moritz RL, Eddes JS, Burgess AW, Simpson RJ: A two-dimensional gel database of human colon carcinoma proteins. Electrophoresis. 1997 Mar-Apr;18(3-4):605-13. [PubMed:9150948 ]
  14. Ansari-Lari MA, Shen Y, Muzny DM, Lee W, Gibbs RA: Large-scale sequencing in human chromosome 12p13: experimental and computational gene structure determination. Genome Res. 1997 Mar;7(3):268-80. [PubMed:9074930 ]
  15. Carrascal M, Ovelleiro D, Casas V, Gay M, Abian J: Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment. J Proteome Res. 2008 Dec;7(12):5167-76. [PubMed:19367720 ]
  16. Beranova-Giorgianni S, Zhao Y, Desiderio DM, Giorgianni F: Phosphoproteomic analysis of the human pituitary. Pituitary. 2006;9(2):109-20. [PubMed:16807684 ]
  17. Lu HS, Yuan PM, Gracy RW: Primary structure of human triosephosphate isomerase. J Biol Chem. 1984 Oct 10;259(19):11958-68. [PubMed:6434534 ]
  18. Maquat LE, Chilcote R, Ryan PM: Human triosephosphate isomerase cDNA and protein structure. Studies of triosephosphate isomerase deficiency in man. J Biol Chem. 1985 Mar 25;260(6):3748-53. [PubMed:2579079 ]
  19. Brown JR, Daar IO, Krug JR, Maquat LE: Characterization of the functional gene and several processed pseudogenes in the human triosephosphate isomerase gene family. Mol Cell Biol. 1985 Jul;5(7):1694-706. [PubMed:4022011 ]
  20. Ansari-Lari MA, Muzny DM, Lu J, Lu F, Lilley CE, Spanos S, Malley T, Gibbs RA: A gene-rich cluster between the CD4 and triosephosphate isomerase genes at human chromosome 12p13. Genome Res. 1996 Apr;6(4):314-26. [PubMed:8723724 ]
  21. Boyer TG, Krug JR, Maquat LE: Transcriptional regulatory sequences of the housekeeping gene for human triosephosphate isomerase. J Biol Chem. 1989 Mar 25;264(9):5177-87. [PubMed:2925688 ]
  22. Mande SC, Mainfroid V, Kalk KH, Goraj K, Martial JA, Hol WG: Crystal structure of recombinant human triosephosphate isomerase at 2.8 A resolution. Triosephosphate isomerase-related human genetic disorders and comparison with the trypanosomal enzyme. Protein Sci. 1994 May;3(5):810-21. [PubMed:8061610 ]
  23. Kinoshita T, Maruki R, Warizaya M, Nakajima H, Nishimura S: Structure of a high-resolution crystal form of human triosephosphate isomerase: improvement of crystals using the gel-tube method. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2005 Apr 1;61(Pt 4):346-9. Epub 2005 Mar 24. [PubMed:16511037 ]
  24. Rodriguez-Almazan C, Arreola R, Rodriguez-Larrea D, Aguirre-Lopez B, de Gomez-Puyou MT, Perez-Montfort R, Costas M, Gomez-Puyou A, Torres-Larios A: Structural basis of human triosephosphate isomerase deficiency: mutation E104D is related to alterations of a conserved water network at the dimer interface. J Biol Chem. 2008 Aug 22;283(34):23254-63. doi: 10.1074/jbc.M802145200. Epub 2008 Jun 18. [PubMed:18562316 ]
  25. Daar IO, Artymiuk PJ, Phillips DC, Maquat LE: Human triose-phosphate isomerase deficiency: a single amino acid substitution results in a thermolabile enzyme. Proc Natl Acad Sci U S A. 1986 Oct;83(20):7903-7. [PubMed:2876430 ]
  26. Perry BA, Mohrenweiser HW: Human triosephosphate isomerase: substitution of Arg for Gly at position 122 in a thermolabile electromorph variant, TPI-Manchester. Hum Genet. 1992 Mar;88(6):634-8. [PubMed:1339398 ]
  27. Chang ML, Artymiuk PJ, Wu X, Hollan S, Lammi A, Maquat LE: Human triosephosphate isomerase deficiency resulting from mutation of Phe-240. Am J Hum Genet. 1993 Jun;52(6):1260-9. [PubMed:8503454 ]
  28. Watanabe M, Zingg BC, Mohrenweiser HW: Molecular analysis of a series of alleles in humans with reduced activity at the triosephosphate isomerase locus. Am J Hum Genet. 1996 Feb;58(2):308-16. [PubMed:8571957 ]
  29. Arya R, Lalloz MR, Bellingham AJ, Layton DM: Evidence for founder effect of the Glu104Asp substitution and identification of new mutations in triosephosphate isomerase deficiency. Hum Mutat. 1997;10(4):290-4. [PubMed:9338582 ]