Triosephosphate isomerase

Details

Name
Triosephosphate isomerase
Synonyms
  • 5.3.1.1
  • TIM
  • TPI
  • Triose-phosphate isomerase
Gene Name
TPI1
Organism
Humans
Amino acid sequence
>lcl|BSEQ0037263|Triosephosphate isomerase
MAEDGEEAEFHFAALYISGQWPRLRADTDLQRLGSSAMAPSRKFFVGGNWKMNGRKQSLG
ELIGTLNAAKVPADTEVVCAPPTAYIDFARQKLDPKIAVAAQNCYKVTNGAFTGEISPGM
IKDCGATWVVLGHSERRHVFGESDELIGQKVAHALAEGLGVIACIGEKLDEREAGITEKV
VFEQTKVIADNVKDWSKVVLAYEPVWAIGTGKTATPQQAQEVHEKLRGWLKSNVSDAVAQ
STRIIYGGSVTGATCKELASQPDVDGFLVGGASLKPEFVDIINAKQ
Number of residues
286
Molecular Weight
30790.785
Theoretical pI
6.91
GO Classification
Functions
triose-phosphate isomerase activity / ubiquitin protein ligase binding
Processes
canonical glycolysis / carbohydrate metabolic process / gluconeogenesis / glucose metabolic process / glyceraldehyde-3-phosphate biosynthetic process / glycerol catabolic process / glycolytic process / multicellular organismal development / pentose-phosphate shunt / small molecule metabolic process
Components
cytosol / extracellular exosome / extracellular space / nucleus
General Function
Ubiquitin protein ligase binding
Specific Function
Not Available
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Not Available
Gene sequence
>lcl|BSEQ0017243|Triosephosphate isomerase (TPI1)
ATGGCGCCCTCCAGGAAGTTCTTCGTTGGGGGAAACTGGAAGATGAACGGGCGGAAGCAG
AGTCTGGGGGAGCTCATCGGCACTCTGAACGCGGCCAAGGTGCCGGCCGACACCGAGGTG
GTTTGTGCTCCCCCTACTGCCTATATCGACTTCGCCCGGCAGAAGCTAGATCCCAAGATT
GCTGTGGCTGCGCAGAACTGCTACAAAGTGACTAATGGGGCTTTTACTGGGGAGATCAGC
CCTGGCATGATCAAAGACTGCGGAGCCACGTGGGTGGTCCTGGGGCACTCAGAGAGAAGG
CATGTCTTTGGGGAGTCAGATGAGCTGATTGGGCAGAAAGTGGCCCATGCTCTGGCAGAG
GGACTCGGAGTAATCGCCTGCATTGGGGAGAAGCTAGATGAAAGGGAAGCTGGCATCACT
GAGAAGGTTGTTTTCGAGCAGACAAAGGTCATCGCAGATAACGTGAAGGACTGGAGCAAG
GTCGTCCTGGCCTATGAGCCTGTGTGGGCCATTGGTACTGGCAAGACTGCAACACCCCAA
CAGGCCCAGGAAGTACACGAGAAGCTCCGAGGATGGCTGAAGTCCAACGTCTCTGATGCG
GTGGCTCAGAGCACCCGTATCATTTATGGAGGCTCTGTGACTGGGGCAACCTGCAAGGAG
CTGGCCAGCCAGCCTGATGTGGATGGCTTCCTTGTGGGTGGTGCTTCCCTCAAGCCCGAA
TTCGTGGACATCATCAATGCCAAACAATGA
Chromosome Location
12
Locus
12p13
External Identifiers
ResourceLink
UniProtKB IDP60174
UniProtKB Entry NameTPIS_HUMAN
GenBank Protein ID339841
GenBank Gene IDM10036
HGNC IDHGNC:12009
General References
  1. 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. [Article]
  2. 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. [Article]
  3. 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. [Article]
  4. 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. [Article]
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  9. Lu HS, Yuan PM, Gracy RW: Primary structure of human triosephosphate isomerase. J Biol Chem. 1984 Oct 10;259(19):11958-68. [Article]
  10. 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. [Article]
  11. 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. [Article]
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  13. Beranova-Giorgianni S, Zhao Y, Desiderio DM, Giorgianni F: Phosphoproteomic analysis of the human pituitary. Pituitary. 2006;9(2):109-20. [Article]
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  15. 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. [Article]
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  27. 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. [Article]
  28. 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. [Article]
  29. 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. [Article]
  30. 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. [Article]
  31. 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. [Article]
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Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB01695N-Hydroxy-4-phosphonobutanamideexperimentalunknownDetails
DB03026Phosphoglycolohydroxamic AcidexperimentalunknownDetails
DB03135[2(Formyl-Hydroxy-Amino)-Ethyl]-Phosphonic AcidexperimentalunknownDetails
DB033145-fluorotryptophanexperimentalunknownDetails
DB033792-Carboxyethylphosphonic AcidexperimentalunknownDetails
DB03900tert-butanolexperimentalunknownDetails
DB04326Dihydroxyacetone phosphateinvestigationalunknownDetails
DB044471,4-DithiothreitolexperimentalunknownDetails
DB045103-phospho-D-glyceric acidexperimentalunknownDetails
DB027262-Phosphoglycolic AcidexperimentalunknownDetails
DB073873-(BUTYLSULPHONYL)-PROPANOIC ACIDexperimentalunknownDetails
DB031323-(2-Benzothiazolylthio)-1-Propanesulfonic AcidexperimentalunknownDetails
DB01593Zincapproved, investigationalunknownDetails
DB11638Artenimolapproved, experimental, investigationalunknownligandDetails
DB14487Zinc acetateapproved, investigationalunknownDetails
DB14533Zinc chlorideapproved, investigationalunknownbinderDetails
DB14548Zinc sulfate, unspecified formapproved, experimentalunknownbinderDetails