ID TPIS_HUMAN Reviewed; 249 AA. AC P60174; B7Z5D8; D3DUS9; P00938; Q6FHP9; Q6IS07; Q8WWD0; Q96AG5; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 07-OCT-2020, sequence version 4. DT 27-MAR-2024, entry version 202. DE RecName: Full=Triosephosphate isomerase {ECO:0000305|PubMed:18562316}; DE Short=TIM; DE EC=5.3.1.1 {ECO:0000269|PubMed:18562316}; DE AltName: Full=Methylglyoxal synthase {ECO:0000250|UniProtKB:P00939}; DE EC=4.2.3.3 {ECO:0000250|UniProtKB:P00939}; DE AltName: Full=Triose-phosphate isomerase; GN Name=TPI1; Synonyms=TPI; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RX PubMed=2579079; DOI=10.1016/s0021-9258(19)83687-6; RA Maquat L.E., Chilcote R., Ryan P.M.; RT "Human triosephosphate isomerase cDNA and protein structure. Studies of RT triosephosphate isomerase deficiency in man."; RL J. Biol. Chem. 260:3748-3753(1985). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=4022011; DOI=10.1128/mcb.5.7.1694-1706.1985; RA Brown J.R., Daar I.O., Krug J.R., Maquat L.E.; RT "Characterization of the functional gene and several processed pseudogenes RT in the human triosephosphate isomerase gene family."; RL Mol. Cell. Biol. 5:1694-1706(1985). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=8723724; DOI=10.1101/gr.6.4.314; RA Ansari-Lari M.A., Muzny D.M., Lu J., Lu F., Lilley C.E., Spanos S., RA Malley T., Gibbs R.A.; RT "A gene-rich cluster between the CD4 and triosephosphate isomerase genes at RT human chromosome 12p13."; RL Genome Res. 6:314-326(1996). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=9074930; DOI=10.1101/gr.7.3.268; RA Ansari-Lari M.A., Shen Y., Muzny D.M., Lee W., Gibbs R.A.; RT "Large-scale sequencing in human chromosome 12p13: experimental and RT computational gene structure determination."; RL Genome Res. 7:268-280(1997). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3). RC TISSUE=Skeletal muscle; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16541075; DOI=10.1038/nature04569; RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., RA Gibbs R.A.; RT "The finished DNA sequence of human chromosome 12."; RL Nature 440:346-351(2006). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [8] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-5. RX PubMed=2925688; DOI=10.1016/s0021-9258(18)83716-4; RA Boyer T.G., Krug J.R., Maquat L.E.; RT "Transcriptional regulatory sequences of the housekeeping gene for human RT triosephosphate isomerase."; RL J. Biol. Chem. 264:5177-5187(1989). RN [9] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Brain, Kidney, Placenta, Prostate, Skeletal muscle, Skin, and RC Uterus; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [10] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.; RT "Cloning of human full open reading frames in Gateway(TM) system entry RT vector (pDONR201)."; RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases. RN [11] RP PROTEIN SEQUENCE OF 2-249. RX PubMed=6434534; DOI=10.1016/s0021-9258(20)71304-9; RA Lu H.S., Yuan P.M., Gracy R.W.; RT "Primary structure of human triosephosphate isomerase."; RL J. Biol. Chem. 259:11958-11968(1984). RN [12] RP PROTEIN SEQUENCE OF 2-20. RC TISSUE=Mammary carcinoma; RX PubMed=9150946; DOI=10.1002/elps.1150180342; RA Rasmussen R.K., Ji H., Eddes J.S., Moritz R.L., Reid G.E., Simpson R.J., RA Dorow D.S.; RT "Two-dimensional electrophoretic analysis of human breast carcinoma RT proteins: mapping of proteins that bind to the SH3 domain of mixed lineage RT kinase MLK2."; RL Electrophoresis 18:588-598(1997). RN [13] RP PROTEIN SEQUENCE OF 2-20. RC TISSUE=Colon carcinoma; RX PubMed=9150948; DOI=10.1002/elps.1150180344; RA Ji H., Reid G.E., Moritz R.L., Eddes J.S., Burgess A.W., Simpson R.J.; RT "A two-dimensional gel database of human colon carcinoma proteins."; RL Electrophoresis 18:605-613(1997). RN [14] RP PROTEIN SEQUENCE OF 6-14; 56-90; 60-131; 143-156; 161-175 AND 195-219, AND RP IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex; RA Lubec G., Vishwanath V., Chen W.-Q., Sun Y.; RL Submitted (DEC-2008) to UniProtKB. RN [15] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026; RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling RT networks."; RL Cell 127:635-648(2006). RN [16] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Pituitary; RX PubMed=16807684; DOI=10.1007/s11102-006-8916-x; RA Beranova-Giorgianni S., Zhao Y., Desiderio D.M., Giorgianni F.; RT "Phosphoproteomic analysis of the human pituitary."; RL Pituitary 9:109-120(2006). RN [17] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=17924679; DOI=10.1021/pr070152u; RA Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.; RT "Improved titanium dioxide enrichment of phosphopeptides from HeLa cells RT and high confident phosphopeptide identification by cross-validation of RT MS/MS and MS/MS/MS spectra."; RL J. Proteome Res. 6:4150-4162(2007). RN [18] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Embryonic kidney; RX PubMed=17693683; DOI=10.1074/mcp.m700120-mcp200; RA Tang L.-Y., Deng N., Wang L.-S., Dai J., Wang Z.-L., Jiang X.-S., Li S.-J., RA Li L., Sheng Q.-H., Wu D.-Q., Li L., Zeng R.; RT "Quantitative phosphoproteome profiling of Wnt3a-mediated signaling RT network: indicating the involvement of ribonucleoside-diphosphate reductase RT M2 subunit phosphorylation at residue serine 20 in canonical Wnt signal RT transduction."; RL Mol. Cell. Proteomics 6:1952-1967(2007). RN [19] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=T-cell; RX PubMed=19367720; DOI=10.1021/pr800500r; RA Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.; RT "Phosphorylation analysis of primary human T lymphocytes using sequential RT IMAC and titanium oxide enrichment."; RL J. Proteome Res. 7:5167-5176(2008). RN [20] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [21] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [22] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21 AND SER-80, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [23] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-14; LYS-194 AND LYS-238, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., RA Olsen J.V., Mann M.; RT "Lysine acetylation targets protein complexes and co-regulates major RT cellular functions."; RL Science 325:834-840(2009). RN [24] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [25] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [26] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [27] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22905912; DOI=10.1021/pr300539b; RA Rosenow A., Noben J.P., Jocken J., Kallendrusch S., Fischer-Posovszky P., RA Mariman E.C., Renes J.; RT "Resveratrol-induced changes of the human adipocyte secretion profile."; RL J. Proteome Res. 11:4733-4743(2012). RN [28] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21; SER-80 AND SER-212, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [29] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21; SER-212; THR-214 AND RP SER-223, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [30] RP METHYLATION [LARGE SCALE ANALYSIS] AT LYS-194, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Colon carcinoma; RX PubMed=24129315; DOI=10.1074/mcp.o113.027870; RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M., RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V., RA Bedford M.T., Comb M.J.; RT "Immunoaffinity enrichment and mass spectrometry analysis of protein RT methylation."; RL Mol. Cell. Proteomics 13:372-387(2014). RN [31] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-142, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25114211; DOI=10.1073/pnas.1413825111; RA Impens F., Radoshevich L., Cossart P., Ribet D.; RT "Mapping of SUMO sites and analysis of SUMOylation changes induced by RT external stimuli."; RL Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014). RN [32] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). RN [33] RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 2-249 IN COMPLEX WITH SUBSTRATE RP ANALOG, HOMODIMERIZATION, ACTIVE SITE, AND SUBSTRATE BINDING-SITE. RX PubMed=8061610; DOI=10.1002/pro.5560030510; RA Mande S.C., Mainfroid V., Kalk K.H., Goraj K., Martial J.A., Hol W.G.J.; RT "Crystal structure of recombinant human triosephosphate isomerase at 2.8-A RT resolution. Triosephosphate isomerase-related human genetic disorders and RT comparison with the trypanosomal enzyme."; RL Protein Sci. 3:810-821(1994). RN [34] RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 2-249. RX PubMed=16511037; DOI=10.1107/s1744309105008341; RA Kinoshita T., Maruki R., Warizaya M., Nakajima H., Nishimura S.; RT "Structure of a high-resolution crystal form of human triosephosphate RT isomerase: improvement of crystals using the gel-tube method."; RL Acta Crystallogr. F 61:346-349(2005). RN [35] RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 39-289 OF MUTANT ASP-105, RP FUNCTION, SUBUNIT, CHARACTERIZATION OF VARIANT ASP-105, CATALYTIC ACTIVITY, RP BIOPHYSICOCHEMICAL PROPERTIES, AND PATHWAY. RX PubMed=18562316; DOI=10.1074/jbc.m802145200; RA Rodriguez-Almazan C., Arreola R., Rodriguez-Larrea D., Aguirre-Lopez B., RA de Gomez-Puyou M.T., Perez-Montfort R., Costas M., Gomez-Puyou A., RA Torres-Larios A.; RT "Structural basis of human triosephosphate isomerase deficiency: mutation RT E104D is related to alterations of a conserved water network at the dimer RT interface."; RL J. Biol. Chem. 283:23254-23263(2008). RN [36] RP VARIANT TPID ASP-105. RX PubMed=2876430; DOI=10.1073/pnas.83.20.7903; RA Daar I.O., Artymiuk P.J., Phillips D.C., Maquat L.E.; RT "Human triose-phosphate isomerase deficiency: a single amino acid RT substitution results in a thermolabile enzyme."; RL Proc. Natl. Acad. Sci. U.S.A. 83:7903-7907(1986). RN [37] RP VARIANTS TPID ASP-105 AND MET-232. RA Neubauer B.A., Pekrun A., Eber S.W., Lakomek M., Schroeter W.; RT "Relation between genetic defect, altered protein structure, and enzyme RT function in triose-phosphate isomerase (TPI) deficiency."; RL Eur. J. Pediatr. Suppl. 151:232-232(1992). RN [38] RP VARIANT MANCHESTER ARG-123. RX PubMed=1339398; DOI=10.1007/bf02265287; RA Perry B.A., Mohrenweiser H.W.; RT "Human triosephosphate isomerase: substitution of Arg for Gly at position RT 122 in a thermolabile electromorph variant, TPI-Manchester."; RL Hum. Genet. 88:634-638(1992). RN [39] RP VARIANT TPID HUNGARY LEU-241. RX PubMed=8503454; RA Chang M.-L., Artymiuk P.J., Wu X., Hollan S., Lammi A., Maquat L.E.; RT "Human triosephosphate isomerase deficiency resulting from mutation of Phe- RT 240."; RL Am. J. Hum. Genet. 52:1260-1269(1993). RN [40] RP VARIANTS TPID ALA-73; ASP-105 AND MET-155. RX PubMed=8571957; RA Watanabe M., Zingg B.C., Mohrenweiser H.W.; RT "Molecular analysis of a series of alleles in humans with reduced activity RT at the triosephosphate isomerase locus."; RL Am. J. Hum. Genet. 58:308-316(1996). RN [41] RP VARIANTS TPID TYR-42; ASP-105 AND VAL-171. RX PubMed=9338582; RX DOI=10.1002/(sici)1098-1004(1997)10:4<290::aid-humu4>3.0.co;2-l; RA Arya R., Lalloz M.R.A., Bellingham A.J., Layton D.M.; RT "Evidence for founder effect of the Glu104Asp substitution and RT identification of new mutations in triosephosphate isomerase deficiency."; RL Hum. Mutat. 10:290-294(1997). CC -!- FUNCTION: Triosephosphate isomerase is an extremely efficient metabolic CC enzyme that catalyzes the interconversion between dihydroxyacetone CC phosphate (DHAP) and D-glyceraldehyde-3-phosphate (G3P) in glycolysis CC and gluconeogenesis. {ECO:0000269|PubMed:18562316}. CC -!- FUNCTION: It is also responsible for the non-negligible production of CC methylglyoxal a reactive cytotoxic side-product that modifies and can CC alter proteins, DNA and lipids. {ECO:0000250|UniProtKB:P00939}. CC -!- CATALYTIC ACTIVITY: CC Reaction=D-glyceraldehyde 3-phosphate = dihydroxyacetone phosphate; CC Xref=Rhea:RHEA:18585, ChEBI:CHEBI:57642, ChEBI:CHEBI:59776; CC EC=5.3.1.1; Evidence={ECO:0000269|PubMed:18562316}; CC -!- CATALYTIC ACTIVITY: CC Reaction=dihydroxyacetone phosphate = methylglyoxal + phosphate; CC Xref=Rhea:RHEA:17937, ChEBI:CHEBI:17158, ChEBI:CHEBI:43474, CC ChEBI:CHEBI:57642; EC=4.2.3.3; CC Evidence={ECO:0000250|UniProtKB:P00939}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=0.74 mM for D-glyceraldehyde 3-phosphate (at pH 7.4 and 25 degrees CC Celsius) {ECO:0000269|PubMed:18562316}; CC Vmax=7.1 mmol/min/mg enzyme {ECO:0000269|PubMed:18562316}; CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3- CC phosphate from glycerone phosphate: step 1/1. {ECO:0000255|PROSITE- CC ProRule:PRU10127}. CC -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis. CC {ECO:0000255|PROSITE-ProRule:PRU10127}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|PROSITE-ProRule:PRU10127, CC ECO:0000269|PubMed:18562316, ECO:0000269|PubMed:8061610}. CC -!- INTERACTION: CC P60174; P42858: HTT; NbExp=6; IntAct=EBI-717475, EBI-466029; CC P60174; P12004: PCNA; NbExp=2; IntAct=EBI-717475, EBI-358311; CC P60174; P54274: TERF1; NbExp=2; IntAct=EBI-717475, EBI-710997; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|PROSITE-ProRule:PRU10127}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative promoter usage, Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=P60174-1; Sequence=Displayed; CC Name=2; CC IsoId=P60174-3; Sequence=VSP_060722; CC Name=3; CC IsoId=P60174-4; Sequence=VSP_060721; CC -!- DISEASE: Triosephosphate isomerase deficiency (TPID) [MIM:615512]: An CC autosomal recessive multisystem disorder characterized by congenital CC hemolytic anemia, progressive neuromuscular dysfunction, susceptibility CC to bacterial infection, and cardiomyopathy. CC {ECO:0000269|PubMed:2876430, ECO:0000269|PubMed:8503454, CC ECO:0000269|PubMed:8571957, ECO:0000269|PubMed:9338582, CC ECO:0000269|Ref.37}. Note=The disease is caused by variants affecting CC the gene represented in this entry. CC -!- MISCELLANEOUS: [Isoform 3]: Produced by alternative splicing. CC {ECO:0000305}. CC -!- SIMILARITY: Belongs to the triosephosphate isomerase family. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAH70129.1; Type=Miscellaneous discrepancy; Note=Sequence differs at the C-terminus.; Evidence={ECO:0000305}; CC -!- WEB RESOURCE: Name=Wikipedia; Note=Triosephosphate isomerase entry; CC URL="https://en.wikipedia.org/wiki/Triosephosphate_isomerase"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; M10036; AAB59511.1; -; mRNA. DR EMBL; X69723; CAA49379.1; -; Genomic_DNA. DR EMBL; AK298809; BAH12874.1; -; mRNA. DR EMBL; U47924; AAB51316.1; -; Genomic_DNA. DR EMBL; CH471116; EAW88722.1; -; Genomic_DNA. DR EMBL; CH471116; EAW88723.1; -; Genomic_DNA. DR EMBL; J04603; AAN86636.1; -; Genomic_DNA. DR EMBL; BC007086; AAH07086.1; -; mRNA. DR EMBL; BC007812; AAH07812.1; -; mRNA. DR EMBL; BC009329; AAH09329.1; -; mRNA. DR EMBL; BC011611; AAH11611.1; -; mRNA. DR EMBL; BC015100; AAH15100.1; -; mRNA. DR EMBL; BC017165; AAH17165.1; -; mRNA. DR EMBL; BC017917; AAH17917.1; -; mRNA. DR EMBL; BC070129; AAH70129.1; ALT_SEQ; mRNA. DR EMBL; AK313282; BAG36090.1; -; mRNA. DR EMBL; CR541702; CAG46503.1; -; mRNA. DR CCDS; CCDS53740.1; -. [P60174-3] DR CCDS; CCDS58206.1; -. [P60174-4] DR CCDS; CCDS8566.1; -. [P60174-1] DR PIR; S29743; ISHUT. DR RefSeq; NP_000356.1; NM_000365.5. [P60174-1] DR RefSeq; NP_001152759.1; NM_001159287.1. [P60174-3] DR RefSeq; NP_001244955.1; NM_001258026.1. [P60174-4] DR PDB; 1HTI; X-ray; 2.80 A; A/B=2-249. DR PDB; 1KLG; X-ray; 2.40 A; C=23-37. DR PDB; 1KLU; X-ray; 1.93 A; C=23-37. DR PDB; 1WYI; X-ray; 2.20 A; A/B=2-249. DR PDB; 2IAM; X-ray; 2.80 A; P=23-37. DR PDB; 2IAN; X-ray; 2.80 A; C/H/M/R=23-37. DR PDB; 2JK2; X-ray; 1.70 A; A/B=2-249. DR PDB; 2VOM; X-ray; 1.85 A; A/B/C/D=2-249. DR PDB; 4BR1; X-ray; 1.90 A; A/B=4-249. DR PDB; 4E41; X-ray; 2.60 A; C/H=23-37. DR PDB; 4POC; X-ray; 1.60 A; A/B=1-249. DR PDB; 4POD; X-ray; 1.99 A; A/B=1-249. DR PDB; 4UNK; X-ray; 2.00 A; A/B=2-249. DR PDB; 4UNL; X-ray; 1.50 A; A/B=2-249. DR PDB; 4ZVJ; X-ray; 1.70 A; A/B=1-249. DR PDB; 6C2G; X-ray; 2.30 A; A/B/C/D=1-249. DR PDB; 6D43; X-ray; 2.04 A; A/B=4-249. DR PDB; 6NLH; X-ray; 2.20 A; A/B/C/D/E/F/G/H=5-249. DR PDB; 6UP1; X-ray; 1.83 A; A/B=1-249. DR PDB; 6UP5; X-ray; 1.92 A; A/B=1-249. DR PDB; 6UP8; X-ray; 2.00 A; A/B=1-249. DR PDB; 6UPF; X-ray; 1.65 A; A/B=1-249. DR PDB; 7RDE; X-ray; 1.31 A; A/B=1-249. DR PDB; 7SX1; X-ray; 2.23 A; A/B=1-249. DR PDB; 7T0Q; X-ray; 2.00 A; A/B=2-249. DR PDB; 7UXB; X-ray; 2.00 A; A/B=1-249. DR PDB; 7UXV; X-ray; 2.15 A; A/B=1-249. DR PDBsum; 1HTI; -. DR PDBsum; 1KLG; -. DR PDBsum; 1KLU; -. DR PDBsum; 1WYI; -. DR PDBsum; 2IAM; -. DR PDBsum; 2IAN; -. DR PDBsum; 2JK2; -. DR PDBsum; 2VOM; -. DR PDBsum; 4BR1; -. DR PDBsum; 4E41; -. DR PDBsum; 4POC; -. DR PDBsum; 4POD; -. DR PDBsum; 4UNK; -. DR PDBsum; 4UNL; -. DR PDBsum; 4ZVJ; -. DR PDBsum; 6C2G; -. DR PDBsum; 6D43; -. DR PDBsum; 6NLH; -. DR PDBsum; 6UP1; -. DR PDBsum; 6UP5; -. DR PDBsum; 6UP8; -. DR PDBsum; 6UPF; -. DR PDBsum; 7RDE; -. DR PDBsum; 7SX1; -. DR PDBsum; 7T0Q; -. DR PDBsum; 7UXB; -. DR PDBsum; 7UXV; -. DR AlphaFoldDB; P60174; -. DR SMR; P60174; -. DR BioGRID; 113020; 257. DR IntAct; P60174; 55. DR MINT; P60174; -. DR STRING; 9606.ENSP00000229270; -. DR BindingDB; P60174; -. DR ChEMBL; CHEMBL4880; -. DR DrugBank; DB04447; 1,4-Dithiothreitol. DR DrugBank; DB03379; 2-Carboxyethylphosphonic Acid. DR DrugBank; DB02726; 2-Phosphoglycolic Acid. DR DrugBank; DB03132; 3-(2-Benzothiazolylthio)-1-Propanesulfonic Acid. DR DrugBank; DB07387; 3-(BUTYLSULPHONYL)-PROPANOIC ACID. DR DrugBank; DB04510; 3-phospho-D-glyceric acid. DR DrugBank; DB03314; 5-fluorotryptophan. DR DrugBank; DB03135; [2(Formyl-Hydroxy-Amino)-Ethyl]-Phosphonic Acid. DR DrugBank; DB11638; Artenimol. DR DrugBank; DB04326; Dihydroxyacetone phosphate. DR DrugBank; DB01695; N-Hydroxy-4-phosphonobutanamide. DR DrugBank; DB03026; Phosphoglycolohydroxamic Acid. DR DrugBank; DB03900; tert-butanol. DR DrugBank; DB01593; Zinc. DR DrugBank; DB14487; Zinc acetate. DR DrugBank; DB14533; Zinc chloride. DR DrugBank; DB14548; Zinc sulfate, unspecified form. DR MoonProt; P60174; -. DR GlyGen; P60174; 1 site. DR iPTMnet; P60174; -. DR MetOSite; P60174; -. DR PhosphoSitePlus; P60174; -. DR SwissPalm; P60174; -. DR BioMuta; TPI1; -. DR DMDM; 353526311; -. DR DOSAC-COBS-2DPAGE; P60174; -. DR REPRODUCTION-2DPAGE; IPI00797687; -. DR REPRODUCTION-2DPAGE; P60174; -. DR CPTAC; CPTAC-2780; -. DR EPD; P60174; -. DR jPOST; P60174; -. DR MassIVE; P60174; -. DR MaxQB; P60174; -. DR PaxDb; 9606-ENSP00000229270; -. DR PeptideAtlas; P60174; -. DR PRIDE; P60174; -. DR ProteomicsDB; 57186; -. [P60174-3] DR ProteomicsDB; 57187; -. [P60174-1] DR ProteomicsDB; 6680; -. DR Pumba; P60174; -. DR TopDownProteomics; P60174-1; -. [P60174-1] DR TopDownProteomics; P60174-3; -. [P60174-3] DR TopDownProteomics; P60174-4; -. [P60174-4] DR ABCD; P60174; 1 sequenced antibody. DR Antibodypedia; 22744; 525 antibodies from 37 providers. DR DNASU; 7167; -. DR Ensembl; ENST00000229270.8; ENSP00000229270.4; ENSG00000111669.15. [P60174-3] DR Ensembl; ENST00000396705.10; ENSP00000379933.4; ENSG00000111669.15. [P60174-1] DR Ensembl; ENST00000488464.6; ENSP00000475620.1; ENSG00000111669.15. [P60174-4] DR Ensembl; ENST00000535434.5; ENSP00000443599.1; ENSG00000111669.15. [P60174-4] DR Ensembl; ENST00000613953.4; ENSP00000484435.1; ENSG00000111669.15. [P60174-3] DR GeneID; 7167; -. DR KEGG; hsa:7167; -. DR MANE-Select; ENST00000396705.10; ENSP00000379933.4; NM_000365.6; NP_000356.1. DR UCSC; uc001qrk.5; human. [P60174-1] DR AGR; HGNC:12009; -. DR CTD; 7167; -. DR DisGeNET; 7167; -. DR GeneCards; TPI1; -. DR HGNC; HGNC:12009; TPI1. DR HPA; ENSG00000111669; Tissue enhanced (skeletal). DR MalaCards; TPI1; -. DR MIM; 190450; gene. DR MIM; 615512; phenotype. DR neXtProt; NX_P60174; -. DR OpenTargets; ENSG00000111669; -. DR Orphanet; 868; Triose phosphate-isomerase deficiency. DR PharmGKB; PA36689; -. DR VEuPathDB; HostDB:ENSG00000111669; -. DR eggNOG; KOG1643; Eukaryota. DR GeneTree; ENSGT00390000013354; -. DR HOGENOM; CLU_024251_2_0_1; -. DR InParanoid; P60174; -. DR OrthoDB; 167479at2759; -. DR PhylomeDB; P60174; -. DR TreeFam; TF300829; -. DR BioCyc; MetaCyc:HS03441-MONOMER; -. DR BRENDA; 5.3.1.1; 2681. DR PathwayCommons; P60174; -. DR Reactome; R-HSA-70171; Glycolysis. DR Reactome; R-HSA-70263; Gluconeogenesis. DR SABIO-RK; P60174; -. DR SignaLink; P60174; -. DR SIGNOR; P60174; -. DR UniPathway; UPA00109; UER00189. DR UniPathway; UPA00138; -. DR BioGRID-ORCS; 7167; 580 hits in 1183 CRISPR screens. DR ChiTaRS; TPI1; human. DR EvolutionaryTrace; P60174; -. DR GeneWiki; TPI1; -. DR GenomeRNAi; 7167; -. DR Pharos; P60174; Tbio. DR PRO; PR:P60174; -. DR Proteomes; UP000005640; Chromosome 12. DR RNAct; P60174; Protein. DR Bgee; ENSG00000111669; Expressed in right frontal lobe and 211 other cell types or tissues. DR ExpressionAtlas; P60174; baseline and differential. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0005615; C:extracellular space; HDA:UniProtKB. DR GO; GO:0005634; C:nucleus; HDA:UniProtKB. DR GO; GO:0008929; F:methylglyoxal synthase activity; ISS:UniProtKB. DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB. DR GO; GO:0004807; F:triose-phosphate isomerase activity; IDA:UniProtKB. DR GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:ParkinsonsUK-UCL. DR GO; GO:0061621; P:canonical glycolysis; IEA:Ensembl. DR GO; GO:0006094; P:gluconeogenesis; IBA:GO_Central. DR GO; GO:0046166; P:glyceraldehyde-3-phosphate biosynthetic process; IDA:UniProtKB. DR GO; GO:0019563; P:glycerol catabolic process; IBA:GO_Central. DR GO; GO:0006096; P:glycolytic process; IBA:GO_Central. DR GO; GO:0019242; P:methylglyoxal biosynthetic process; ISS:UniProtKB. DR CDD; cd00311; TIM; 1. DR Gene3D; 3.20.20.70; Aldolase class I; 1. DR HAMAP; MF_00147_B; TIM_B; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR035990; TIM_sf. DR InterPro; IPR022896; TrioseP_Isoase_bac/euk. DR InterPro; IPR000652; Triosephosphate_isomerase. DR InterPro; IPR020861; Triosephosphate_isomerase_AS. DR NCBIfam; TIGR00419; tim; 1. DR PANTHER; PTHR21139; TRIOSEPHOSPHATE ISOMERASE; 1. DR PANTHER; PTHR21139:SF2; TRIOSEPHOSPHATE ISOMERASE; 1. DR Pfam; PF00121; TIM; 1. DR SUPFAM; SSF51351; Triosephosphate isomerase (TIM); 1. DR PROSITE; PS00171; TIM_1; 1. DR PROSITE; PS51440; TIM_2; 1. DR SWISS-2DPAGE; P60174; -. DR UCD-2DPAGE; P60174; -. DR Genevisible; P60174; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative promoter usage; KW Alternative splicing; Cytoplasm; Direct protein sequencing; KW Disease variant; Gluconeogenesis; Glycolysis; Hereditary hemolytic anemia; KW Isomerase; Isopeptide bond; Lyase; Methylation; Nitration; Phosphoprotein; KW Reference proteome; Ubl conjugation. FT INIT_MET 1 FT /note="Removed" FT CHAIN 2..249 FT /note="Triosephosphate isomerase" FT /id="PRO_0000090113" FT ACT_SITE 96 FT /note="Electrophile" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10127, FT ECO:0000269|PubMed:8061610" FT ACT_SITE 166 FT /note="Proton acceptor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10127, FT ECO:0000269|PubMed:8061610" FT BINDING 12 FT /ligand="substrate" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10127, FT ECO:0000269|PubMed:8061610" FT BINDING 14 FT /ligand="substrate" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10127, FT ECO:0000269|PubMed:8061610" FT MOD_RES 14 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 21 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:16807684, FT ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:17693683, FT ECO:0007744|PubMed:17924679, ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19367720, ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569" FT MOD_RES 68 FT /note="3'-nitrotyrosine" FT /evidence="ECO:0000250|UniProtKB:P17751" FT MOD_RES 80 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:23186163" FT MOD_RES 106 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P48500" FT MOD_RES 149 FT /note="N6-succinyllysine" FT /evidence="ECO:0000250|UniProtKB:P17751" FT MOD_RES 156 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P17751" FT MOD_RES 156 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P17751" FT MOD_RES 159 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P17751" FT MOD_RES 173 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P17751" FT MOD_RES 194 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 194 FT /note="N6-methyllysine; alternate" FT /evidence="ECO:0007744|PubMed:24129315" FT MOD_RES 194 FT /note="N6-succinyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P17751" FT MOD_RES 198 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P48500" FT MOD_RES 209 FT /note="3'-nitrotyrosine" FT /evidence="ECO:0000250|UniProtKB:P17751" FT MOD_RES 212 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT MOD_RES 214 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 223 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 238 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT CROSSLNK 142 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO1)" FT /evidence="ECO:0007744|PubMed:25114211" FT VAR_SEQ 1..82 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000305" FT /id="VSP_060721" FT VAR_SEQ 1 FT /note="M -> MAEDGEEAEFHFAALYISGQWPRLRADTDLQRLGSSAM (in FT isoform 2)" FT /evidence="ECO:0000305" FT /id="VSP_060722" FT VARIANT 42 FT /note="C -> Y (in TPID; dbSNP:rs121964848)" FT /evidence="ECO:0000269|PubMed:9338582" FT /id="VAR_007534" FT VARIANT 73 FT /note="G -> A (in TPID)" FT /evidence="ECO:0000269|PubMed:8571957" FT /id="VAR_007535" FT VARIANT 105 FT /note="E -> D (in TPID; no effect on triose-phosphate FT isomerase activity; changed protein homodimerization FT activity; the homodimer stability is temperature-dependent FT and affects the triose-phosphate isomerase activity; FT dbSNP:rs121964845)" FT /evidence="ECO:0000269|PubMed:18562316, FT ECO:0000269|PubMed:2876430, ECO:0000269|PubMed:8571957, FT ECO:0000269|PubMed:9338582, ECO:0000269|Ref.37" FT /id="VAR_007536" FT VARIANT 123 FT /note="G -> R (in Manchester; thermolabile; FT dbSNP:rs121964846)" FT /evidence="ECO:0000269|PubMed:1339398" FT /id="VAR_007537" FT VARIANT 155 FT /note="V -> M (in TPID; dbSNP:rs188138723)" FT /evidence="ECO:0000269|PubMed:8571957" FT /id="VAR_007538" FT VARIANT 171 FT /note="I -> V (in TPID; dbSNP:rs121964849)" FT /evidence="ECO:0000269|PubMed:9338582" FT /id="VAR_007539" FT VARIANT 232 FT /note="V -> M (in TPID; dbSNP:rs1555132614)" FT /evidence="ECO:0000269|Ref.37" FT /id="VAR_007540" FT VARIANT 241 FT /note="F -> L (in TPID; Hungary; thermolabile; FT dbSNP:rs121964847)" FT /evidence="ECO:0000269|PubMed:8503454" FT /id="VAR_007541" FT CONFLICT 20..21 FT /note="QS -> KN (in Ref. 11; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 27 FT /note="G -> S (in Ref. 11; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 30..31 FT /note="NA -> QG (in Ref. 11; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 43..44 FT /note="AP -> IG (in Ref. 11; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 58 FT /note="P -> Q (in Ref. 11; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 155 FT /note="V -> A (in Ref. 9; AAH17917)" FT /evidence="ECO:0000305" FT CONFLICT 167 FT /note="P -> N (in Ref. 11; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 244 FT /note="I -> L (in Ref. 11; AA sequence)" FT /evidence="ECO:0000305" FT STRAND 7..12 FT /evidence="ECO:0007829|PDB:7RDE" FT HELIX 19..32 FT /evidence="ECO:0007829|PDB:7RDE" FT STRAND 38..43 FT /evidence="ECO:0007829|PDB:7RDE" FT HELIX 46..48 FT /evidence="ECO:0007829|PDB:7RDE" FT HELIX 49..55 FT /evidence="ECO:0007829|PDB:7RDE" FT STRAND 60..65 FT /evidence="ECO:0007829|PDB:7RDE" FT STRAND 69..74 FT /evidence="ECO:0007829|PDB:7RDE" FT HELIX 81..86 FT /evidence="ECO:0007829|PDB:7RDE" FT STRAND 91..95 FT /evidence="ECO:0007829|PDB:7RDE" FT HELIX 97..101 FT /evidence="ECO:0007829|PDB:7RDE" FT HELIX 107..119 FT /evidence="ECO:0007829|PDB:7RDE" FT STRAND 123..128 FT /evidence="ECO:0007829|PDB:7RDE" FT HELIX 132..136 FT /evidence="ECO:0007829|PDB:7RDE" FT TURN 137..139 FT /evidence="ECO:0007829|PDB:6UP8" FT HELIX 140..152 FT /evidence="ECO:0007829|PDB:7RDE" FT HELIX 158..160 FT /evidence="ECO:0007829|PDB:7RDE" FT STRAND 161..165 FT /evidence="ECO:0007829|PDB:7RDE" FT HELIX 168..170 FT /evidence="ECO:0007829|PDB:4UNL" FT TURN 171..173 FT /evidence="ECO:0007829|PDB:4UNL" FT HELIX 181..196 FT /evidence="ECO:0007829|PDB:7RDE" FT HELIX 199..204 FT /evidence="ECO:0007829|PDB:7RDE" FT STRAND 207..209 FT /evidence="ECO:0007829|PDB:7RDE" FT TURN 215..217 FT /evidence="ECO:0007829|PDB:7RDE" FT HELIX 218..222 FT /evidence="ECO:0007829|PDB:7RDE" FT STRAND 229..233 FT /evidence="ECO:0007829|PDB:7RDE" FT HELIX 234..237 FT /evidence="ECO:0007829|PDB:7RDE" FT HELIX 241..245 FT /evidence="ECO:0007829|PDB:7RDE" FT TURN 246..248 FT /evidence="ECO:0007829|PDB:7RDE" SQ SEQUENCE 249 AA; 26669 MW; 73844175635F858E CRC64; MAPSRKFFVG GNWKMNGRKQ SLGELIGTLN AAKVPADTEV VCAPPTAYID FARQKLDPKI AVAAQNCYKV TNGAFTGEIS PGMIKDCGAT WVVLGHSERR HVFGESDELI GQKVAHALAE GLGVIACIGE KLDEREAGIT EKVVFEQTKV IADNVKDWSK VVLAYEPVWA IGTGKTATPQ QAQEVHEKLR GWLKSNVSDA VAQSTRIIYG GSVTGATCKE LASQPDVDGF LVGGASLKPE FVDIINAKQ //