ALDOA_HUMAN
ID ALDOA_HUMAN Reviewed; 364 AA.
AC P04075; B4DXI7; Q6FH76; Q6FI10; Q96B15; Q9BWD9; Q9UCN2;
DT 01-NOV-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 248.
DE RecName: Full=Fructose-bisphosphate aldolase A {ECO:0000305};
DE EC=4.1.2.13 {ECO:0000269|PubMed:14766013};
DE AltName: Full=Lung cancer antigen NY-LU-1;
DE AltName: Full=Muscle-type aldolase;
GN Name=ALDOA {ECO:0000312|HGNC:HGNC:414}; Synonyms=ALDA;
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).
RC TISSUE=Liver;
RX PubMed=3840020; DOI=10.1016/0006-291x(85)91818-2;
RA Sakakibara M., Mukai T., Hori K.;
RT "Nucleotide sequence of a cDNA clone for human aldolase: a messenger RNA in
RT the liver.";
RL Biochem. Biophys. Res. Commun. 131:413-420(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Fibroblast;
RX PubMed=3030757; DOI=10.1111/j.1432-1033.1987.tb10984.x;
RA Izzo P., Costanzo P., Lupo A., Rippa E., Borghese A.M., Paolella G.,
RA Salvatore F.;
RT "A new human species of aldolase A mRNA from fibroblasts.";
RL Eur. J. Biochem. 164:9-13(1987).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=3391172; DOI=10.1111/j.1432-1033.1988.tb14136.x;
RA Izzo P., Costanzo P., Lupo A., Rippa E., Paolella G., Salvatore F.;
RT "Human aldolase A gene. Structural organization and tissue-specific
RT expression by multiple promoters and alternate mRNA processing.";
RL Eur. J. Biochem. 174:569-578(1988).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=1999195; DOI=10.1111/j.1432-1033.1991.tb15766.x;
RA Mukai T., Arai Y., Yatsuki H., Joh K., Hori K.;
RT "An additional promoter functions in the human aldolase A gene, but not in
RT rat.";
RL Eur. J. Biochem. 195:781-787(1991).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Testis;
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 MRNA] (ISOFORM 1).
RA Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P.,
RA Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y.,
RA LaBaer J.;
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15616553; DOI=10.1038/nature03187;
RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA Myers R.M., Rubin E.M., Pennacchio L.A.;
RT "The sequence and analysis of duplication-rich human chromosome 16.";
RL Nature 432:988-994(2004).
RN [8]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Cervix, Eye, Lung, Testis, and 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 [GENOMIC DNA] OF 1-108 (ISOFORM 1).
RX PubMed=3441006; DOI=10.1016/0022-2836(87)90556-0;
RA Maire P., Gautron S., Hakim V., Gregori C., Mennecier F., Kahn A.;
RT "Characterization of three optional promoters in the 5' region of the human
RT aldolase A gene.";
RL J. Mol. Biol. 197:425-438(1987).
RN [11]
RP PROTEIN SEQUENCE OF 2-364.
RX PubMed=3355497; DOI=10.1042/bj2490779;
RA Freemont P.S., Dunbar B., Fothergill-Gilmore L.A.;
RT "The complete amino acid sequence of human skeletal-muscle fructose-
RT bisphosphate aldolase.";
RL Biochem. J. 249:779-788(1988).
RN [12]
RP PROTEIN SEQUENCE OF 2-63 AND 148-358.
RX PubMed=6696436; DOI=10.1016/0003-9861(84)90075-4;
RA Freemont P.S., Dunbar B., Fothergill L.A.;
RT "Human skeletal-muscle aldolase: N-terminal sequence analysis of CNBr- and
RT o-iodosobenzoic acid-cleavage fragments.";
RL Arch. Biochem. Biophys. 228:342-352(1984).
RN [13]
RP PROTEIN SEQUENCE OF 2-22.
RC TISSUE=Platelet;
RX PubMed=12665801; DOI=10.1038/nbt810;
RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R.,
RA Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass spectrometric
RT identification of sorted N-terminal peptides.";
RL Nat. Biotechnol. 21:566-569(2003).
RN [14]
RP PROTEIN SEQUENCE OF 2-16.
RC TISSUE=Colon carcinoma;
RX PubMed=1353685; DOI=10.1016/0167-4889(92)90078-p;
RA Lee K.N., Maxwell M.D., Patterson M.K. Jr., Birckbichler P.J., Conway E.;
RT "Identification of transglutaminase substrates in HT29 colon cancer cells:
RT use of 5-(biotinamido)pentylamine as a transglutaminase-specific probe.";
RL Biochim. Biophys. Acta 1136:12-16(1992).
RN [15]
RP PROTEIN SEQUENCE OF 2-13; 29-42; 44-56; 61-69; 88-99; 154-173; 244-258 AND
RP 332-342, AND 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 [16]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 139-364 (ISOFORM 1/2).
RX PubMed=3674018;
RA Tolan D.R., Niclas J., Bruce B.D., Lebo R.V.;
RT "Evolutionary implications of the human aldolase-A, -B, -C, and
RT - pseudogene chromosome locations.";
RL Am. J. Hum. Genet. 41:907-924(1987).
RN [17]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Lymphoblast;
RX PubMed=14654843; DOI=10.1038/nature02166;
RA Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.;
RT "Proteomic characterization of the human centrosome by protein correlation
RT profiling.";
RL Nature 426:570-574(2003).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-46, 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 [19]
RP IDENTIFICATION BY 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 [20]
RP INTERACTION WITH FBP2.
RX PubMed=18214967; DOI=10.1002/prot.21909;
RA Gizak A., Maciaszczyk E., Dzugaj A., Eschrich K., Rakus D.;
RT "Evolutionary conserved N-terminal region of human muscle fructose 1,6-
RT bisphosphatase regulates its activity and the interaction with aldolase.";
RL Proteins 72:209-216(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-36 AND SER-39, 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-42; LYS-108 AND LYS-330, 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-36 AND SER-39, AND
RP IDENTIFICATION BY 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 MALONYLATION AT LYS-111 AND LYS-312.
RX PubMed=21908771; DOI=10.1074/mcp.m111.012658;
RA Peng C., Lu Z., Xie Z., Cheng Z., Chen Y., Tan M., Luo H., Zhang Y., He W.,
RA Yang K., Zwaans B.M., Tishkoff D., Ho L., Lombard D., He T.C., Dai J.,
RA Verdin E., Ye Y., Zhao Y.;
RT "The first identification of lysine malonylation substrates and its
RT regulatory enzyme.";
RL Mol. Cell. Proteomics 10:M111.012658.01-M111.012658.12(2011).
RN [27]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-39 AND SER-46, AND
RP IDENTIFICATION BY 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 [28]
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 [29]
RP CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [30]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [31]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-9; SER-36; SER-39 AND SER-46,
RP AND 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 [32]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-39; SER-46 AND SER-272, AND
RP 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 [33]
RP IDENTIFICATION BY MASS 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 [34]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-42, 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 [35]
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 [36]
RP HYDROXYBUTYRYLATION AT LYS-147.
RX PubMed=29192674; DOI=10.1038/cr.2017.149;
RA Huang H., Luo Z., Qi S., Huang J., Xu P., Wang X., Gao L., Li F., Wang J.,
RA Zhao W., Gu W., Chen Z., Dai L., Dai J., Zhao Y.;
RT "Landscape of the regulatory elements for lysine 2-hydroxyisobutyrylation
RT pathway.";
RL Cell Res. 28:111-125(2018).
RN [37]
RP HYDROXYBUTYRYLATION AT LYS-99.
RX PubMed=29775581; DOI=10.1016/j.molcel.2018.04.011;
RA Huang H., Tang S., Ji M., Tang Z., Shimada M., Liu X., Qi S.,
RA Locasale J.W., Roeder R.G., Zhao Y., Li X.;
RT "p300-mediated lysine 2-hydroxyisobutyrylation regulates glycolysis.";
RL Mol. Cell 70:663-678(2018).
RN [38]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
RX PubMed=2335208; DOI=10.1016/0014-5793(90)80211-z;
RA Gamblin S.J., Cooper B., Millar J.R., Davies G.J., Littlechild J.A.,
RA Watson H.C.;
RT "The crystal structure of human muscle aldolase at 3.0-A resolution.";
RL FEBS Lett. 262:282-286(1990).
RN [39]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RX PubMed=2056525; DOI=10.1016/0022-2836(91)90650-u;
RA Gamblin S.J., Davies G.J., Grimes J.M., Jackson R.M., Littlechild J.A.,
RA Watson H.C.;
RT "Activity and specificity of human aldolases.";
RL J. Mol. Biol. 219:573-576(1991).
RN [40]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
RX PubMed=10048322; DOI=10.1110/ps.8.2.291;
RA Dalby A., Dauter Z., Littlechild J.A.;
RT "Crystal structure of human muscle aldolase complexed with fructose 1,6-
RT bisphosphate: mechanistic implications.";
RL Protein Sci. 8:291-297(1999).
RN [41]
RP VARIANT GSD12 GLY-129, AND CHARACTERIZATION OF VARIANT GSD12 GLY-129.
RX PubMed=2825199; DOI=10.1073/pnas.84.23.8623;
RA Kishi H., Mukai T., Hirono A., Fujii H., Miwa S., Hori K.;
RT "Human aldolase A deficiency associated with a hemolytic anemia:
RT thermolabile aldolase due to a single base mutation.";
RL Proc. Natl. Acad. Sci. U.S.A. 84:8623-8627(1987).
RN [42]
RP CHARACTERIZATION OF VARIANT GSD12 GLY-129.
RX PubMed=2229018; DOI=10.1093/oxfordjournals.jbchem.a123174;
RA Takasaki Y., Takahashi I., Mukai T., Hori K.;
RT "Human aldolase A of a hemolytic anemia patient with Asp-128-->Gly
RT substitution: characteristics of an enzyme generated in E. coli transfected
RT with the expression plasmid pHAAD128G.";
RL J. Biochem. 108:153-157(1990).
RN [43]
RP VARIANT GSD12 LYS-207.
RX PubMed=8598869; DOI=10.1056/nejm199604253341705;
RA Kreuder J., Borkhardt A., Repp R., Pekrun A., Goettsche B., Gottschalk U.,
RA Reichmann H., Schachenmayr W., Schlegel K., Lampert F.;
RT "Brief report: inherited metabolic myopathy and hemolysis due to a mutation
RT in aldolase A.";
RL N. Engl. J. Med. 334:1100-1104(1996).
RN [44]
RP VARIANTS GSD12 303-GLY--TYR-364 DEL AND TYR-339.
RX PubMed=14615364; DOI=10.1182/blood-2003-09-3160;
RA Yao D.C., Tolan D.R., Murray M.F., Harris D.J., Darras B.T., Geva A.,
RA Neufeld E.J.;
RT "Hemolytic anemia and severe rhabdomyolysis caused by compound heterozygous
RT mutations of the gene for erythrocyte/muscle isozyme of aldolase,
RT ALDOA(Arg303X/Cys338Tyr).";
RL Blood 103:2401-2403(2004).
RN [45]
RP VARIANT GSD12 SER-347, BIOPHYSICOCHEMICAL PROPERTIES, CHARACTERIZATION OF
RP VARIANTS GSD12 LYS-207 AND SER-347, CATALYTIC ACTIVITY, AND FUNCTION.
RX PubMed=14766013; DOI=10.1042/bj20031941;
RA Esposito G., Vitagliano L., Costanzo P., Borrelli L., Barone R., Pavone L.,
RA Izzo P., Zagari A., Salvatore F.;
RT "Human aldolase A natural mutants: relationship between flexibility of the
RT C-terminal region and enzyme function.";
RL Biochem. J. 380:51-56(2004).
CC -!- FUNCTION: Catalyzes the reversible conversion of beta-D-fructose 1,6-
CC bisphosphate (FBP) into two triose phosphate and plays a key role in
CC glycolysis and gluconeogenesis (PubMed:14766013). In addition, may also
CC function as scaffolding protein (By similarity). {ECO:0000250,
CC ECO:0000269|PubMed:14766013}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=beta-D-fructose 1,6-bisphosphate = D-glyceraldehyde 3-
CC phosphate + dihydroxyacetone phosphate; Xref=Rhea:RHEA:14729,
CC ChEBI:CHEBI:32966, ChEBI:CHEBI:57642, ChEBI:CHEBI:59776; EC=4.1.2.13;
CC Evidence={ECO:0000269|PubMed:14766013};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14730;
CC Evidence={ECO:0000305|PubMed:14766013};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=52 uM for fructose 1,6-bisphosphate (at 30 degrees Celsius)
CC {ECO:0000269|PubMed:14766013};
CC Temperature dependence:
CC Thermal denaturation midpoint (Tm) is 54.4 degrees Celsius.
CC {ECO:0000269|PubMed:14766013};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC phosphate and glycerone phosphate from D-glucose: step 4/4.
CC -!- SUBUNIT: Homotetramer. Interacts with SNX9 and WAS (By similarity).
CC Interacts with FBP2; the interaction blocks FBP2 inhibition by
CC physiological concentrations of AMP and reduces inhibition by Ca(2+).
CC {ECO:0000250, ECO:0000269|PubMed:18214967}.
CC -!- INTERACTION:
CC P04075; P04075: ALDOA; NbExp=2; IntAct=EBI-709613, EBI-709613;
CC P04075; P09972: ALDOC; NbExp=3; IntAct=EBI-709613, EBI-2952751;
CC P04075; P12004: PCNA; NbExp=3; IntAct=EBI-709613, EBI-358311;
CC P04075-2; P04075-2: ALDOA; NbExp=4; IntAct=EBI-10194102, EBI-10194102;
CC P04075-2; P09972: ALDOC; NbExp=6; IntAct=EBI-10194102, EBI-2952751;
CC P04075-2; P42858: HTT; NbExp=6; IntAct=EBI-10194102, EBI-466029;
CC P04075-2; P05014: IFNA4; NbExp=3; IntAct=EBI-10194102, EBI-10194381;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, myofibril, sarcomere, I band
CC {ECO:0000250|UniProtKB:P00883}. Cytoplasm, myofibril, sarcomere, M line
CC {ECO:0000250|UniProtKB:P00883}. Note=In skeletal muscle, accumulates
CC around the M line and within the I band, colocalizing with FBP2 on both
CC sides of the Z line in the absence of Ca(2+).
CC {ECO:0000250|UniProtKB:P00883}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P04075-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P04075-2; Sequence=VSP_047261;
CC -!- DISEASE: Glycogen storage disease 12 (GSD12) [MIM:611881]: A metabolic
CC disorder associated with increased hepatic glycogen and hemolytic
CC anemia. It may lead to myopathy with exercise intolerance and
CC rhabdomyolysis. {ECO:0000269|PubMed:14615364,
CC ECO:0000269|PubMed:14766013, ECO:0000269|PubMed:2229018,
CC ECO:0000269|PubMed:2825199, ECO:0000269|PubMed:8598869}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- MISCELLANEOUS: In vertebrates, three forms of this ubiquitous
CC glycolytic enzyme are found, aldolase A in muscle, aldolase B in liver
CC and aldolase C in brain.
CC -!- SIMILARITY: Belongs to the class I fructose-bisphosphate aldolase
CC family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
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DR EMBL; M11560; AAA51690.1; -; mRNA.
DR EMBL; X05236; CAA28861.1; -; mRNA.
DR EMBL; X12447; CAA30979.1; -; Genomic_DNA.
DR EMBL; AK301993; BAG63399.1; -; mRNA.
DR EMBL; CR536528; CAG38765.1; -; mRNA.
DR EMBL; CR541880; CAG46678.1; -; mRNA.
DR EMBL; AC093512; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471238; EAW79933.1; -; Genomic_DNA.
DR EMBL; BC000367; AAH00367.2; -; mRNA.
DR EMBL; BC004333; AAH04333.1; -; mRNA.
DR EMBL; BC010660; AAH10660.1; -; mRNA.
DR EMBL; BC012880; AAH12880.1; -; mRNA.
DR EMBL; BC013614; AAH13614.1; -; mRNA.
DR EMBL; BC015888; AAH15888.1; -; mRNA.
DR EMBL; BC016170; AAH16170.1; -; mRNA.
DR EMBL; BC016800; AAH16800.1; -; mRNA.
DR EMBL; M21190; AAA51697.1; -; mRNA.
DR CCDS; CCDS10668.1; -. [P04075-1]
DR CCDS; CCDS58450.1; -. [P04075-2]
DR PIR; S14084; ADHUA.
DR RefSeq; NP_000025.1; NM_000034.3.
DR RefSeq; NP_001121089.1; NM_001127617.2. [P04075-1]
DR RefSeq; NP_001230106.1; NM_001243177.1. [P04075-2]
DR RefSeq; NP_908930.1; NM_184041.2. [P04075-1]
DR RefSeq; NP_908932.1; NM_184043.2. [P04075-1]
DR RefSeq; XP_011544070.1; XM_011545768.2.
DR PDB; 1ALD; X-ray; 2.00 A; A=2-364.
DR PDB; 2ALD; X-ray; 2.10 A; A=2-364.
DR PDB; 4ALD; X-ray; 2.80 A; A=2-364.
DR PDB; 5KY6; X-ray; 1.94 A; A/B/C/D=2-364.
DR PDB; 6XMH; X-ray; 1.95 A; A/B=1-364.
DR PDB; 6XML; X-ray; 1.88 A; A/B=1-364.
DR PDB; 6XMM; X-ray; 2.11 A; A/B=1-364.
DR PDB; 6XMO; X-ray; 2.60 A; A/B=1-364.
DR PDBsum; 1ALD; -.
DR PDBsum; 2ALD; -.
DR PDBsum; 4ALD; -.
DR PDBsum; 5KY6; -.
DR PDBsum; 6XMH; -.
DR PDBsum; 6XML; -.
DR PDBsum; 6XMM; -.
DR PDBsum; 6XMO; -.
DR AlphaFoldDB; P04075; -.
DR SMR; P04075; -.
DR BioGRID; 106728; 232.
DR IntAct; P04075; 82.
DR MINT; P04075; -.
DR STRING; 9606.ENSP00000378669; -.
DR ChEMBL; CHEMBL2106; -.
DR DrugBank; DB04733; 1,6-DI-O-PHOSPHONO-D-MANNITOL.
DR DrugBank; DB02512; 1,6-Fructose Diphosphate (Linear Form).
DR DrugBank; DB11638; Artenimol.
DR DrugBank; DB04326; Dihydroxyacetone phosphate.
DR DrugBank; DB08240; N-(4-CHLOROPHENYL)-3-(PHOSPHONOOXY)NAPHTHALENE-2-CARBOXAMIDE.
DR DrugBank; DB01593; Zinc.
DR DrugBank; DB14487; Zinc acetate.
DR DrugBank; DB14533; Zinc chloride.
DR DrugBank; DB14548; Zinc sulfate, unspecified form.
DR MoonProt; P04075; -.
DR CarbonylDB; P04075; -.
DR GlyGen; P04075; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P04075; -.
DR MetOSite; P04075; -.
DR PhosphoSitePlus; P04075; -.
DR SwissPalm; P04075; -.
DR BioMuta; ALDOA; -.
DR DMDM; 113606; -.
DR DOSAC-COBS-2DPAGE; P04075; -.
DR OGP; P04075; -.
DR REPRODUCTION-2DPAGE; IPI00465439; -.
DR REPRODUCTION-2DPAGE; P04075; -.
DR SWISS-2DPAGE; P04075; -.
DR UCD-2DPAGE; P04075; -.
DR CPTAC; CPTAC-459; -.
DR EPD; P04075; -.
DR jPOST; P04075; -.
DR MassIVE; P04075; -.
DR MaxQB; P04075; -.
DR PaxDb; P04075; -.
DR PeptideAtlas; P04075; -.
DR PRIDE; P04075; -.
DR ProteomicsDB; 51647; -. [P04075-1]
DR TopDownProteomics; P04075-1; -. [P04075-1]
DR Antibodypedia; 1031; 711 antibodies from 38 providers.
DR DNASU; 226; -.
DR Ensembl; ENST00000412304.6; ENSP00000400452.2; ENSG00000149925.22. [P04075-1]
DR Ensembl; ENST00000563060.6; ENSP00000455800.2; ENSG00000149925.22. [P04075-1]
DR Ensembl; ENST00000569545.5; ENSP00000455700.1; ENSG00000149925.22. [P04075-1]
DR Ensembl; ENST00000642816.3; ENSP00000496166.1; ENSG00000149925.22. [P04075-2]
DR Ensembl; ENST00000643777.4; ENSP00000494188.2; ENSG00000149925.22. [P04075-1]
DR GeneID; 226; -.
DR KEGG; hsa:226; -.
DR MANE-Select; ENST00000642816.3; ENSP00000496166.1; NM_001243177.4; NP_001230106.1. [P04075-2]
DR UCSC; uc010veg.3; human. [P04075-1]
DR CTD; 226; -.
DR DisGeNET; 226; -.
DR GeneCards; ALDOA; -.
DR HGNC; HGNC:414; ALDOA.
DR HPA; ENSG00000149925; Group enriched (skeletal muscle, tongue).
DR MalaCards; ALDOA; -.
DR MIM; 103850; gene.
DR MIM; 611881; phenotype.
DR neXtProt; NX_P04075; -.
DR OpenTargets; ENSG00000149925; -.
DR Orphanet; 57; Glycogen storage disease due to aldolase A deficiency.
DR PharmGKB; PA24707; -.
DR VEuPathDB; HostDB:ENSG00000149925; -.
DR eggNOG; KOG1557; Eukaryota.
DR GeneTree; ENSGT00950000182987; -.
DR HOGENOM; CLU_031243_0_0_1; -.
DR InParanoid; P04075; -.
DR OMA; DYREMLF; -.
DR OrthoDB; 799973at2759; -.
DR PhylomeDB; P04075; -.
DR TreeFam; TF314203; -.
DR BioCyc; MetaCyc:HS07647-MON; -.
DR BRENDA; 4.1.2.13; 2681.
DR PathwayCommons; P04075; -.
DR Reactome; R-HSA-114608; Platelet degranulation.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR Reactome; R-HSA-70171; Glycolysis.
DR Reactome; R-HSA-70263; Gluconeogenesis.
DR SABIO-RK; P04075; -.
DR SignaLink; P04075; -.
DR SIGNOR; P04075; -.
DR UniPathway; UPA00109; UER00183.
DR BioGRID-ORCS; 226; 760 hits in 1085 CRISPR screens.
DR ChiTaRS; ALDOA; human.
DR EvolutionaryTrace; P04075; -.
DR GeneWiki; Aldolase_A; -.
DR GenomeRNAi; 226; -.
DR Pharos; P04075; Tbio.
DR PRO; PR:P04075; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; P04075; protein.
DR Bgee; ENSG00000149925; Expressed in gastrocnemius and 94 other tissues.
DR ExpressionAtlas; P04075; baseline and differential.
DR Genevisible; P04075; HS.
DR GO; GO:0015629; C:actin cytoskeleton; IDA:BHF-UCL.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0070062; C:extracellular exosome; IDA:BHF-UCL.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; HDA:UniProtKB.
DR GO; GO:1904813; C:ficolin-1-rich granule lumen; TAS:Reactome.
DR GO; GO:0031674; C:I band; TAS:BHF-UCL.
DR GO; GO:0031430; C:M band; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; HDA:UniProtKB.
DR GO; GO:0031093; C:platelet alpha granule lumen; TAS:Reactome.
DR GO; GO:0034774; C:secretory granule lumen; TAS:Reactome.
DR GO; GO:0061827; C:sperm head; IDA:CAFA.
DR GO; GO:1904724; C:tertiary granule lumen; TAS:Reactome.
DR GO; GO:0003779; F:actin binding; TAS:BHF-UCL.
DR GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL.
DR GO; GO:0008092; F:cytoskeletal protein binding; IDA:BHF-UCL.
DR GO; GO:0070061; F:fructose binding; IDA:BHF-UCL.
DR GO; GO:0004332; F:fructose-bisphosphate aldolase activity; IDA:BHF-UCL.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0015631; F:tubulin binding; TAS:BHF-UCL.
DR GO; GO:0007015; P:actin filament organization; TAS:BHF-UCL.
DR GO; GO:0006754; P:ATP biosynthetic process; IMP:BHF-UCL.
DR GO; GO:0007339; P:binding of sperm to zona pellucida; IMP:CAFA.
DR GO; GO:0030388; P:fructose 1,6-bisphosphate metabolic process; IDA:BHF-UCL.
DR GO; GO:0006000; P:fructose metabolic process; IMP:BHF-UCL.
DR GO; GO:0006096; P:glycolytic process; IMP:BHF-UCL.
DR GO; GO:0046716; P:muscle cell cellular homeostasis; IMP:BHF-UCL.
DR GO; GO:0051289; P:protein homotetramerization; ISS:UniProtKB.
DR GO; GO:0008360; P:regulation of cell shape; IDA:BHF-UCL.
DR GO; GO:0006941; P:striated muscle contraction; IMP:BHF-UCL.
DR Gene3D; 3.20.20.70; -; 1.
DR InterPro; IPR029768; Aldolase_I_AS.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR000741; FBA_I.
DR PANTHER; PTHR11627; PTHR11627; 1.
DR Pfam; PF00274; Glycolytic; 1.
DR PROSITE; PS00158; ALDOLASE_CLASS_I; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cytoplasm;
KW Direct protein sequencing; Disease variant; Glycogen storage disease;
KW Glycolysis; Hereditary hemolytic anemia; Hydroxylation; Isopeptide bond;
KW Lyase; Phosphoprotein; Reference proteome; Schiff base; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:12665801,
FT ECO:0000269|PubMed:1353685, ECO:0000269|PubMed:3355497,
FT ECO:0000269|PubMed:6696436, ECO:0000269|Ref.15,
FT ECO:0007744|PubMed:22223895"
FT CHAIN 2..364
FT /note="Fructose-bisphosphate aldolase A"
FT /id="PRO_0000216936"
FT ACT_SITE 188
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT ACT_SITE 230
FT /note="Schiff-base intermediate with dihydroxyacetone-P"
FT BINDING 56
FT /ligand="substrate"
FT BINDING 147
FT /ligand="substrate"
FT SITE 364
FT /note="Necessary for preference for fructose 1,6-
FT bisphosphate over fructose 1-phosphate"
FT MOD_RES 5
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P05065"
FT MOD_RES 9
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 36
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 39
FT /note="Phosphoserine"
FT /evidence="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 42
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 46
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 99
FT /note="N6-(2-hydroxyisobutyryl)lysine"
FT /evidence="ECO:0000269|PubMed:29775581"
FT MOD_RES 108
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 111
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P09972"
FT MOD_RES 111
FT /note="N6-malonyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:21908771"
FT MOD_RES 132
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P05065"
FT MOD_RES 147
FT /note="N6-(2-hydroxyisobutyryl)lysine"
FT /evidence="ECO:0000269|PubMed:29192674"
FT MOD_RES 272
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 312
FT /note="N6-malonyllysine"
FT /evidence="ECO:0000269|PubMed:21908771"
FT MOD_RES 330
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT CROSSLNK 42
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0007744|PubMed:25114211"
FT CROSSLNK 42
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:25114211"
FT VAR_SEQ 1
FT /note="M -> MARRKPEGSSFNMTHLSMAMAFSFPPVASGQLHPQLGNTQHQTELGK
FT ELATTSTM (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_047261"
FT VARIANT 82
FT /note="E -> Q (in dbSNP:rs11553107)"
FT /id="VAR_048219"
FT VARIANT 129
FT /note="D -> G (in GSD12; thermolabile; dbSNP:rs121909533)"
FT /evidence="ECO:0000269|PubMed:2229018,
FT ECO:0000269|PubMed:2825199"
FT /id="VAR_000550"
FT VARIANT 142
FT /note="G -> V (in dbSNP:rs11553108)"
FT /id="VAR_048220"
FT VARIANT 207
FT /note="E -> K (in GSD12; reduces thermal stability; 3-fold
FT decrease in catalytic efficiency mostly due to reduced
FT substrate affinity; dbSNP:rs121909534)"
FT /evidence="ECO:0000269|PubMed:14766013,
FT ECO:0000269|PubMed:8598869"
FT /id="VAR_044142"
FT VARIANT 303..364
FT /note="Missing (in GSD12)"
FT /evidence="ECO:0000269|PubMed:14615364"
FT /id="VAR_085824"
FT VARIANT 339
FT /note="C -> Y (in GSD12)"
FT /evidence="ECO:0000269|PubMed:14615364"
FT /id="VAR_044143"
FT VARIANT 347
FT /note="G -> S (in GSD12; likely benign variant; does not
FT affect thermal stability; 4-fold decrease in catalytic
FT efficiency due to reduced enzyme activity;
FT dbSNP:rs138824667)"
FT /evidence="ECO:0000269|PubMed:14766013"
FT /id="VAR_044144"
FT CONFLICT 73
FT /note="C -> G (in Ref. 3; CAA30979)"
FT /evidence="ECO:0000305"
FT CONFLICT 180
FT /note="Q -> R (in Ref. 6; CAG46678)"
FT /evidence="ECO:0000305"
FT CONFLICT 196
FT /note="D -> A (in Ref. 3; CAA30979)"
FT /evidence="ECO:0000305"
FT CONFLICT 230
FT /note="K -> N (in Ref. 3; CAA30979)"
FT /evidence="ECO:0000305"
FT CONFLICT 280
FT /note="A -> S (in Ref. 3; CAA30979)"
FT /evidence="ECO:0000305"
FT HELIX 10..23
FT /evidence="ECO:0007829|PDB:6XML"
FT STRAND 29..33
FT /evidence="ECO:0007829|PDB:6XML"
FT TURN 37..39
FT /evidence="ECO:0007829|PDB:6XML"
FT HELIX 40..45
FT /evidence="ECO:0007829|PDB:6XML"
FT TURN 46..48
FT /evidence="ECO:0007829|PDB:6XML"
FT HELIX 53..64
FT /evidence="ECO:0007829|PDB:6XML"
FT HELIX 68..73
FT /evidence="ECO:0007829|PDB:6XML"
FT STRAND 74..79
FT /evidence="ECO:0007829|PDB:6XML"
FT HELIX 81..84
FT /evidence="ECO:0007829|PDB:6XML"
FT HELIX 94..100
FT /evidence="ECO:0007829|PDB:6XML"
FT STRAND 104..108
FT /evidence="ECO:0007829|PDB:6XML"
FT STRAND 113..115
FT /evidence="ECO:0007829|PDB:6XML"
FT STRAND 119..121
FT /evidence="ECO:0007829|PDB:6XML"
FT STRAND 123..125
FT /evidence="ECO:0007829|PDB:6XML"
FT HELIX 131..140
FT /evidence="ECO:0007829|PDB:6XML"
FT STRAND 145..152
FT /evidence="ECO:0007829|PDB:6XML"
FT STRAND 155..157
FT /evidence="ECO:0007829|PDB:5KY6"
FT HELIX 161..180
FT /evidence="ECO:0007829|PDB:6XML"
FT STRAND 184..191
FT /evidence="ECO:0007829|PDB:6XML"
FT HELIX 199..219
FT /evidence="ECO:0007829|PDB:6XML"
FT HELIX 224..226
FT /evidence="ECO:0007829|PDB:6XML"
FT HELIX 246..258
FT /evidence="ECO:0007829|PDB:6XML"
FT STRAND 267..271
FT /evidence="ECO:0007829|PDB:6XML"
FT HELIX 277..289
FT /evidence="ECO:0007829|PDB:6XML"
FT STRAND 296..303
FT /evidence="ECO:0007829|PDB:6XML"
FT HELIX 304..314
FT /evidence="ECO:0007829|PDB:6XML"
FT HELIX 318..320
FT /evidence="ECO:0007829|PDB:6XML"
FT HELIX 321..338
FT /evidence="ECO:0007829|PDB:6XML"
FT TURN 339..341
FT /evidence="ECO:0007829|PDB:6XML"
FT STRAND 348..350
FT /evidence="ECO:0007829|PDB:1ALD"
FT HELIX 351..354
FT /evidence="ECO:0007829|PDB:6XMH"
FT HELIX 357..359
FT /evidence="ECO:0007829|PDB:5KY6"
FT HELIX 361..363
FT /evidence="ECO:0007829|PDB:5KY6"
SQ SEQUENCE 364 AA; 39420 MW; 0AAED80F755A7BE8 CRC64;
MPYQYPALTP EQKKELSDIA HRIVAPGKGI LAADESTGSI AKRLQSIGTE NTEENRRFYR
QLLLTADDRV NPCIGGVILF HETLYQKADD GRPFPQVIKS KGGVVGIKVD KGVVPLAGTN
GETTTQGLDG LSERCAQYKK DGADFAKWRC VLKIGEHTPS ALAIMENANV LARYASICQQ
NGIVPIVEPE ILPDGDHDLK RCQYVTEKVL AAVYKALSDH HIYLEGTLLK PNMVTPGHAC
TQKFSHEEIA MATVTALRRT VPPAVTGITF LSGGQSEEEA SINLNAINKC PLLKPWALTF
SYGRALQASA LKAWGGKKEN LKAAQEEYVK RALANSLACQ GKYTPSGQAG AAASESLFVS
NHAY
