TPIS_HUMAN
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 03-AUG-2022, entry version 193.
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 ---------------------------------------------------------------------------
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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 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 AlphaFoldDB; P60174; -.
DR SMR; P60174; -.
DR BioGRID; 113020; 210.
DR IntAct; P60174; 52.
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 SWISS-2DPAGE; P60174; -.
DR UCD-2DPAGE; P60174; -.
DR EPD; P60174; -.
DR jPOST; P60174; -.
DR MassIVE; P60174; -.
DR MaxQB; P60174; -.
DR PaxDb; P60174; -.
DR PeptideAtlas; P60174; -.
DR PRIDE; P60174; -.
DR ProteomicsDB; 57186; -. [P60174-3]
DR ProteomicsDB; 57187; -. [P60174-1]
DR ProteomicsDB; 6680; -.
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; 479 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 CTD; 7167; -.
DR DisGeNET; 7167; -.
DR GeneCards; TPI1; -.
DR HGNC; HGNC:12009; TPI1.
DR HPA; ENSG00000111669; Tissue enhanced (skeletal muscle, tongue).
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; 540689at2759; -.
DR PhylomeDB; P60174; -.
DR TreeFam; TF300829; -.
DR BioCyc; MetaCyc:HS03441-MON; -.
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; 544 hits in 1088 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 209 other tissues.
DR ExpressionAtlas; P60174; baseline and differential.
DR Genevisible; P60174; HS.
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; -; 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 PANTHER; PTHR21139; PTHR21139; 1.
DR Pfam; PF00121; TIM; 1.
DR SUPFAM; SSF51351; SSF51351; 1.
DR TIGRFAMs; TIGR00419; tim; 1.
DR PROSITE; PS00171; TIM_1; 1.
DR PROSITE; PS51440; TIM_2; 1.
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:4UNL"
FT HELIX 19..31
FT /evidence="ECO:0007829|PDB:4UNL"
FT STRAND 38..43
FT /evidence="ECO:0007829|PDB:4UNL"
FT HELIX 46..48
FT /evidence="ECO:0007829|PDB:4UNL"
FT HELIX 49..55
FT /evidence="ECO:0007829|PDB:4UNL"
FT STRAND 60..65
FT /evidence="ECO:0007829|PDB:4UNL"
FT STRAND 69..74
FT /evidence="ECO:0007829|PDB:4UNL"
FT HELIX 81..86
FT /evidence="ECO:0007829|PDB:4UNL"
FT STRAND 91..95
FT /evidence="ECO:0007829|PDB:4UNL"
FT HELIX 97..101
FT /evidence="ECO:0007829|PDB:4UNL"
FT HELIX 107..119
FT /evidence="ECO:0007829|PDB:4UNL"
FT STRAND 123..128
FT /evidence="ECO:0007829|PDB:4UNL"
FT HELIX 132..136
FT /evidence="ECO:0007829|PDB:4UNL"
FT TURN 137..139
FT /evidence="ECO:0007829|PDB:6UP8"
FT HELIX 140..153
FT /evidence="ECO:0007829|PDB:4UNL"
FT HELIX 158..160
FT /evidence="ECO:0007829|PDB:4UNL"
FT STRAND 161..165
FT /evidence="ECO:0007829|PDB:4UNL"
FT HELIX 168..170
FT /evidence="ECO:0007829|PDB:4UNL"
FT TURN 171..173
FT /evidence="ECO:0007829|PDB:4UNL"
FT HELIX 179..196
FT /evidence="ECO:0007829|PDB:4UNL"
FT HELIX 199..204
FT /evidence="ECO:0007829|PDB:4UNL"
FT STRAND 207..209
FT /evidence="ECO:0007829|PDB:4UNL"
FT TURN 215..217
FT /evidence="ECO:0007829|PDB:4UNL"
FT HELIX 218..223
FT /evidence="ECO:0007829|PDB:4UNL"
FT STRAND 229..232
FT /evidence="ECO:0007829|PDB:4UNL"
FT HELIX 234..237
FT /evidence="ECO:0007829|PDB:4UNL"
FT HELIX 240..245
FT /evidence="ECO:0007829|PDB:4UNL"
FT TURN 246..248
FT /evidence="ECO:0007829|PDB:4UNL"
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
