P04075 (ALDOA_HUMAN) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 149.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Fructose-bisphosphate aldolase A EC=4.1.2.13 Alternative name(s): Lung cancer antigen NY-LU-1 Muscle-type aldolase | ||||
| Gene names |
| ||||
| Organism | Homo sapiens (Human) | ||||
| Taxonomic identifier | 9606 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Protein attributes
| Sequence length | 364 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | Plays a key role in glycolysis and gluconeogenesis. In addition, may also function as scaffolding protein By similarity. |
| Catalytic activity | D-fructose 1,6-bisphosphate = glycerone phosphate + D-glyceraldehyde 3-phosphate. |
| Pathway | |
| Subunit structure | Homotetramer. Interacts with SNX9 and WAS By similarity. |
| Involvement in disease | Defects in ALDOA are the cause of glycogen storage disease type 12 (GSD12) [MIM:611881]; also known as red cell aldolase deficiency. A metabolic disorder associated with increased hepatic glycogen and hemolytic anemia. It may lead to myopathy with exercise intolerance and rhabdomyolysis. Ref.30 Ref.31 Ref.32 Ref.33 Ref.34 |
| Miscellaneous | In vertebrates, three forms of this ubiquitous glycolytic enzyme are found, aldolase A in muscle, aldolase B in liver and aldolase C in brain. |
| Sequence similarities | Belongs to the class I fructose-bisphosphate aldolase family. |
| Biophysicochemical properties | Kinetic parameters: KM=52 µM for fructose 1,6-bisphosphate (at 30 degrees Celsius) Ref.34 Temperature dependence: Thermal denaturation midpoint (Tm) is 54.4 degrees Celsius. |
| Sequence caution | The sequence BAG63399.1 differs from that shown. Reason: Erroneous initiation. |
Ontologies
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | |||||||||||||||||||||||||||||||||||||||||||||||||||||||
Molecule processing | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Initiator methionine | 1 | 1 | Removed Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Chain | 2 – 364 | 363 | Fructose-bisphosphate aldolase A | PRO_0000216936 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Sites | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Active site | 188 | 1 | Proton acceptor By similarity | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Active site | 230 | 1 | Schiff-base intermediate with dihydroxyacetone-P | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Binding site | 56 | 1 | Substrate | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Binding site | 147 | 1 | Substrate | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Site | 364 | 1 | Necessary for preference for fructose 1,6-bisphosphate over fructose 1-phosphate | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Amino acid modifications | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Modified residue | 3 | 1 | Phosphotyrosine Ref.20 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Modified residue | 5 | 1 | Phosphotyrosine Ref.20 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Modified residue | 9 | 1 | Phosphothreonine Ref.22 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Modified residue | 13 | 1 | N6-acetyllysine Ref.19 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Modified residue | 36 | 1 | Phosphoserine Ref.22 Ref.24 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Modified residue | 37 | 1 | Phosphothreonine Ref.22 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Modified residue | 39 | 1 | Phosphoserine Ref.24 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Modified residue | 42 | 1 | N6-acetyllysine Ref.19 Ref.25 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Modified residue | 46 | 1 | Phosphoserine Ref.18 Ref.22 Ref.24 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Modified residue | 65 | 1 | Phosphothreonine Ref.17 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Modified residue | 108 | 1 | N6-acetyllysine Ref.25 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Modified residue | 204 | 1 | Phosphotyrosine Ref.16 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Modified residue | 223 | 1 | Phosphotyrosine Ref.20 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Modified residue | 235 | 1 | Phosphothreonine Ref.21 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Modified residue | 241 | 1 | Phosphothreonine Ref.21 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Modified residue | 330 | 1 | N6-acetyllysine Ref.25 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Modified residue | 354 | 1 | Phosphoserine Ref.21 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Modified residue | 356 | 1 | Phosphoserine Ref.21 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Modified residue | 364 | 1 | Phosphotyrosine Ref.23 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Natural variations | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Natural variant | 82 | 1 | E → Q. Corresponds to variant rs11553107 [ dbSNP | Ensembl ]. | VAR_048219 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Natural variant | 129 | 1 | D → G in GSD12; thermolabile. Ref.30 Ref.31 | VAR_000550 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Natural variant | 142 | 1 | G → V. Corresponds to variant rs11553108 [ dbSNP | Ensembl ]. | VAR_048220 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Natural variant | 207 | 1 | E → K in GSD12; reduces thermal stability; 3-fold decrease in catalytic efficiency mostly due to reduced substrate affinity. Ref.32 Ref.34 | VAR_044142 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Natural variant | 339 | 1 | C → Y in GSD12. Ref.33 | VAR_044143 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Natural variant | 347 | 1 | G → S in GSD12; does not affect thermal stability; 4-fold decrease in catalytic efficiency due to reduced enzyme activity. Ref.34 | VAR_044144 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Experimental info | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Sequence conflict | 180 | 1 | Q → R in CAG46678. Ref.6 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Secondary structure | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Helix Strand Turn | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 10 – 23 | 14 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 29 – 33 | 5 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 37 – 46 | 10 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 53 – 64 | 12 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 68 – 73 | 6 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 74 – 79 | 6 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 83 – 85 | 3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 94 – 100 | 7 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 104 – 108 | 5 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 113 – 115 | 3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 119 – 121 | 3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 123 – 125 | 3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 131 – 140 | 10 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 145 – 152 | 8 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 161 – 179 | 19 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Turn | 180 – 182 | 3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 184 – 191 | 8 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 199 – 219 | 21 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 224 – 226 | 3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 246 – 258 | 13 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 267 – 270 | 4 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 277 – 289 | 13 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 296 – 303 | 8 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 304 – 314 | 11 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 318 – 320 | 3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Helix | 321 – 338 | 18 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Turn | 339 – 341 | 3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 348 – 350 | 3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Sequences
| ||||||||||||||||||
References
| « Hide 'large scale' references | |
| [1] | "Nucleotide sequence of a cDNA clone for human aldolase: a messenger RNA in the liver." Sakakibara M., Mukai T., Hori K. Biochem. Biophys. Res. Commun. 131:413-420(1985) [PubMed: 3840020] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Liver. |
| [2] | "A new human species of aldolase A mRNA from fibroblasts." Izzo P., Costanzo P., Lupo A., Rippa E., Borghese A.M., Paolella G., Salvatore F. Eur. J. Biochem. 164:9-13(1987) [PubMed: 3030757] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Fibroblast. |
| [3] | "Human aldolase A gene. Structural organization and tissue-specific expression by multiple promoters and alternate mRNA processing." Izzo P., Costanzo P., Lupo A., Rippa E., Paolella G., Salvatore F. Eur. J. Biochem. 174:569-578(1988) [PubMed: 3391172] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. |
| [4] | "An additional promoter functions in the human aldolase A gene, but not in rat." Mukai T., Arai Y., Yatsuki H., Joh K., Hori K. Eur. J. Biochem. 195:781-787(1991) [PubMed: 1999195] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. |
| [5] | "Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. Sugano S.Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Testis. |
| [6] | "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)." Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., LaBaer J. Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. |
| [7] | Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. Venter J.C.Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
| [8] | "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Cervix, Eye, Lung, Testis and Uterus. |
| [9] | "Characterization of three optional promoters in the 5' region of the human aldolase A gene." Maire P., Gautron S., Hakim V., Gregori C., Mennecier F., Kahn A. J. Mol. Biol. 197:425-438(1987) [PubMed: 3441006] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-108. |
| [10] | "The complete amino acid sequence of human skeletal-muscle fructose-bisphosphate aldolase." Freemont P.S., Dunbar B., Fothergill-Gilmore L.A. Biochem. J. 249:779-788(1988) [PubMed: 3355497] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-364. |
| [11] | "Human skeletal-muscle aldolase: N-terminal sequence analysis of CNBr- and o-iodosobenzoic acid-cleavage fragments." Freemont P.S., Dunbar B., Fothergill L.A. Arch. Biochem. Biophys. 228:342-352(1984) [PubMed: 6696436] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-63 AND 148-358. |
| [12] | "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides." Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J. Nat. Biotechnol. 21:566-569(2003) [PubMed: 12665801] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-22. Tissue: Platelet. |
| [13] | "Identification of transglutaminase substrates in HT29 colon cancer cells: use of 5-(biotinamido)pentylamine as a transglutaminase-specific probe." Lee K.N., Maxwell M.D., Patterson M.K. Jr., Birckbichler P.J., Conway E. Biochim. Biophys. Acta 1136:12-16(1992) [PubMed: 1353685] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-16. Tissue: Colon carcinoma. |
| [14] | Lubec G., Vishwanath V., Chen W.-Q., Sun Y. Submitted (DEC-2008) to UniProtKB Cited for: PROTEIN SEQUENCE OF 2-13; 29-42; 44-56; 61-69; 88-99; 154-173; 244-258 AND 332-342, MASS SPECTROMETRY. Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex. |
| [15] | "Evolutionary implications of the human aldolase-A, -B, -C, and - pseudogene chromosome locations." Tolan D.R., Niclas J., Bruce B.D., Lebo R.V. Am. J. Hum. Genet. 41:907-924(1987) [PubMed: 3674018] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 139-364. |
| [16] | "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells." Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J. Nat. Biotechnol. 23:94-101(2005) [PubMed: 15592455] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-204, MASS SPECTROMETRY. Tissue: Epithelium. |
| [17] | "Global phosphoproteome analysis on human HepG2 hepatocytes using reversed-phase diagonal LC." Gevaert K., Staes A., Van Damme J., De Groot S., Hugelier K., Demol H., Martens L., Goethals M., Vandekerckhove J. Proteomics 5:3589-3599(2005) [PubMed: 16097034] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-65, MASS SPECTROMETRY. Tissue: Hepatoma. |
| [18] | "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-46, MASS SPECTROMETRY. Tissue: Cervix carcinoma. |
| [19] | "Substrate and functional diversity of lysine acetylation revealed by a proteomics survey." Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T., Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y. Mol. Cell 23:607-618(2006) [PubMed: 16916647] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-13 AND LYS-42, MASS SPECTROMETRY. Tissue: Cervix carcinoma. |
| [20] | "Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer." Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M. Comb M.J.Cell 131:1190-1203(2007) [PubMed: 18083107] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-3; TYR-5 AND TYR-223, MASS SPECTROMETRY. Tissue: Lung carcinoma. |
| [21] | "Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry." Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A. Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007) [PubMed: 17287340] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-235; THR-241; SER-354 AND SER-356, MASS SPECTROMETRY. Tissue: Embryonic kidney. |
| [22] | "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach." Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S. Anal. Chem. 81:4493-4501(2009) [PubMed: 19413330] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-9; SER-36; THR-37 AND SER-46, MASS SPECTROMETRY. Tissue: Embryonic kidney. |
| [23] | "An extensive survey of tyrosine phosphorylation revealing new sites in human mammary epithelial cells." Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A., Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D., Wiley H.S., Qian W.-J. J. Proteome Res. 8:3852-3861(2009) [PubMed: 19534553] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-364, MASS SPECTROMETRY. Tissue: Mammary epithelium. |
| [24] | "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36; SER-39 AND SER-46, MASS SPECTROMETRY. Tissue: Leukemic T-cell. |
| [25] | "Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-42; LYS-108 AND LYS-330, MASS SPECTROMETRY. |
| [26] | "Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. |
| [27] | "The crystal structure of human muscle aldolase at 3.0-A resolution." Gamblin S.J., Cooper B., Millar J.R., Davies G.J., Littlechild J.A., Watson H.C. FEBS Lett. 262:282-286(1990) [PubMed: 2335208] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS). |
| [28] | "Activity and specificity of human aldolases." Gamblin S.J., Davies G.J., Grimes J.M., Jackson R.M., Littlechild J.A., Watson H.C. J. Mol. Biol. 219:573-576(1991) [PubMed: 2056525] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS). |
| [29] | "Crystal structure of human muscle aldolase complexed with fructose 1,6-bisphosphate: mechanistic implications." Dalby A., Dauter Z., Littlechild J.A. Protein Sci. 8:291-297(1999) [PubMed: 10048322] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS). |
| [30] | "Human aldolase A deficiency associated with a hemolytic anemia: thermolabile aldolase due to a single base mutation." Kishi H., Mukai T., Hirono A., Fujii H., Miwa S., Hori K. Proc. Natl. Acad. Sci. U.S.A. 84:8623-8627(1987) [PubMed: 2825199] [Abstract] Cited for: VARIANT GSD12 GLY-129, CHARACTERIZATION OF VARIANT GSD12 GLY-129. |
| [31] | "Human aldolase A of a hemolytic anemia patient with Asp-128-->Gly substitution: characteristics of an enzyme generated in E. coli transfected with the expression plasmid pHAAD128G." Takasaki Y., Takahashi I., Mukai T., Hori K. J. Biochem. 108:153-157(1990) [PubMed: 2229018] [Abstract] Cited for: CHARACTERIZATION OF VARIANT GSD12 GLY-129. |
| [32] | "Brief report: inherited metabolic myopathy and hemolysis due to a mutation in aldolase A." Kreuder J., Borkhardt A., Repp R., Pekrun A., Goettsche B., Gottschalk U., Reichmann H., Schachenmayr W., Schlegel K., Lampert F. N. Engl. J. Med. 334:1100-1104(1996) [PubMed: 8598869] [Abstract] Cited for: VARIANT GSD12 LYS-207. |
| [33] | "Hemolytic anemia and severe rhabdomyolysis caused by compound heterozygous mutations of the gene for erythrocyte/muscle isozyme of aldolase, ALDOA(Arg303X/Cys338Tyr)." Yao D.C., Tolan D.R., Murray M.F., Harris D.J., Darras B.T., Geva A., Neufeld E.J. Blood 103:2401-2403(2004) [PubMed: 14615364] [Abstract] Cited for: VARIANT GSD12 TYR-339. |
| [34] | "Human aldolase A natural mutants: relationship between flexibility of the C-terminal region and enzyme function." Esposito G., Vitagliano L., Costanzo P., Borrelli L., Barone R., Pavone L., Izzo P., Zagari A., Salvatore F. Biochem. J. 380:51-56(2004) [PubMed: 14766013] [Abstract] Cited for: VARIANT GSD12 SER-347, BIOPHYSICOCHEMICAL PROPERTIES, CHARACTERIZATION OF VARIANTS GSD12 LYS-207 AND SER-347. |
| + | Additional computationally mapped references. |
Web resources
Cross-references
Sequence databases | |||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| EMBL GenBank DDBJ | M11560 mRNA. Translation: AAA51690.1. X05236 mRNA. Translation: CAA28861.1. X12447 Genomic DNA. Translation: CAA30979.1. Sequence problems. AK301993 mRNA. Translation: BAG63399.1. Different initiation. CR536528 mRNA. Translation: CAG38765.1. CR541880 mRNA. Translation: CAG46678.1. CH471238 Genomic DNA. Translation: EAW79933.1. BC000367 mRNA. Translation: AAH00367.2. BC004333 mRNA. Translation: AAH04333.1. BC010660 mRNA. Translation: AAH10660.1. BC012880 mRNA. Translation: AAH12880.1. BC013614 mRNA. Translation: AAH13614.1. BC015888 mRNA. Translation: AAH15888.1. BC016170 mRNA. Translation: AAH16170.1. BC016800 mRNA. Translation: AAH16800.1. M21190 mRNA. Translation: AAA51697.1. | ||||||||||||||||||||||||
| IPI | IPI00465439. | ||||||||||||||||||||||||
| PIR | ADHUA. S14084. | ||||||||||||||||||||||||
| RefSeq | NP_000025.1. NM_000034.3. NP_001121089.1. NM_001127617.2. NP_001230106.1. NM_001243177.1. NP_908930.1. NM_184041.2. NP_908932.1. NM_184043.2. | ||||||||||||||||||||||||
| UniGene | Hs.513490. | ||||||||||||||||||||||||
3D structure databases | |||||||||||||||||||||||||
| PDBe RCSB PDB PDBj |
| ||||||||||||||||||||||||
| ProteinModelPortal | P04075. | ||||||||||||||||||||||||
| SMR | P04075. Positions 2-364. | ||||||||||||||||||||||||
| ModBase | Search... | ||||||||||||||||||||||||
Protein-protein interaction databases | |||||||||||||||||||||||||
| IntAct | P04075. 19 interactions. | ||||||||||||||||||||||||
| MINT | MINT-4998828. | ||||||||||||||||||||||||
| STRING | P04075. | ||||||||||||||||||||||||
PTM databases | |||||||||||||||||||||||||
| PhosphoSite | P04075. | ||||||||||||||||||||||||
Polymorphism databases | |||||||||||||||||||||||||
| DMDM | 113606. | ||||||||||||||||||||||||
2D gel databases | |||||||||||||||||||||||||
| SWISS-2DPAGE | P04075. | ||||||||||||||||||||||||
| Aarhus/Ghent-2DPAGE | 1302. NEPHGE. | ||||||||||||||||||||||||
| DOSAC-COBS-2DPAGE | P04075. | ||||||||||||||||||||||||
| OGP | P04075. | ||||||||||||||||||||||||
| REPRODUCTION-2DPAGE | IPI00465439. P04075. | ||||||||||||||||||||||||
| Siena-2DPAGE | P04075. | ||||||||||||||||||||||||
| UCD-2DPAGE | P04075. | ||||||||||||||||||||||||
Proteomic databases | |||||||||||||||||||||||||
| PRIDE | P04075. | ||||||||||||||||||||||||
Protocols and materials databases | |||||||||||||||||||||||||
| StructuralBiologyKnowledgebase | Search... | ||||||||||||||||||||||||
Genome annotation databases | |||||||||||||||||||||||||
| Ensembl | ENST00000338110; ENSP00000336927; ENSG00000149925. ENST00000395240; ENSP00000378661; ENSG00000149925. ENST00000395248; ENSP00000378669; ENSG00000149925. ENST00000412304; ENSP00000400452; ENSG00000149925. ENST00000436540; ENSP00000387793; ENSG00000149925. | ||||||||||||||||||||||||
| GeneID | 226. | ||||||||||||||||||||||||
| KEGG | hsa:226. | ||||||||||||||||||||||||
| UCSC | uc002dvw.1. human. | ||||||||||||||||||||||||
Organism-specific databases | |||||||||||||||||||||||||
| CTD | 226. | ||||||||||||||||||||||||
| GeneCards | GC16P030064. | ||||||||||||||||||||||||
| H-InvDB | HIX0012935. | ||||||||||||||||||||||||
| HGNC | HGNC:414. ALDOA. | ||||||||||||||||||||||||
| HPA | CAB006252. HPA004177. | ||||||||||||||||||||||||
| MIM | 103850. gene. 611881. phenotype. | ||||||||||||||||||||||||
| neXtProt | NX_P04075. | ||||||||||||||||||||||||
| Orphanet | 57. Aldolase A deficiency. | ||||||||||||||||||||||||
| PharmGKB | PA24707. | ||||||||||||||||||||||||
| GenAtlas | Search... | ||||||||||||||||||||||||
Phylogenomic databases | |||||||||||||||||||||||||
| eggNOG | prNOG06512. | ||||||||||||||||||||||||
| GeneTree | ENSGT00390000010235. | ||||||||||||||||||||||||
| HOVERGEN | HBG002386. | ||||||||||||||||||||||||
| InParanoid | P04075. | ||||||||||||||||||||||||
| OrthoDB | EOG4X3H1J. | ||||||||||||||||||||||||
| PhylomeDB | P04075. | ||||||||||||||||||||||||
Enzyme and pathway databases | |||||||||||||||||||||||||
| BioCyc | MetaCyc:HS07647-MONOMER. | ||||||||||||||||||||||||
| Pathway_Interaction_DB | hif1_tfpathway. HIF-1-alpha transcription factor network. | ||||||||||||||||||||||||
| Reactome | REACT_474. Metabolism of carbohydrates. REACT_604. Hemostasis. | ||||||||||||||||||||||||
Gene expression databases | |||||||||||||||||||||||||
| ArrayExpress | P04075. | ||||||||||||||||||||||||
| Bgee | P04075. | ||||||||||||||||||||||||
| CleanEx | HS_ALDOA. | ||||||||||||||||||||||||
| Genevestigator | P04075. | ||||||||||||||||||||||||
| GermOnline | ENSG00000149925. Homo sapiens. | ||||||||||||||||||||||||
Family and domain databases | |||||||||||||||||||||||||
| InterPro | IPR000741. Aldolase_I. IPR013785. Aldolase_TIM. [Graphical view] | ||||||||||||||||||||||||
| Gene3D | G3DSA:3.20.20.70. Aldolase_TIM. 1 hit. | ||||||||||||||||||||||||
| KO | K01623. | ||||||||||||||||||||||||
| PANTHER | PTHR11627. Aldolase_I. 1 hit. | ||||||||||||||||||||||||
| Pfam | PF00274. Glycolytic. 1 hit. [Graphical view] | ||||||||||||||||||||||||
| PROSITE | PS00158. ALDOLASE_CLASS_I. 1 hit. [Graphical view] | ||||||||||||||||||||||||
| ProtoNet | Search... | ||||||||||||||||||||||||
Other | |||||||||||||||||||||||||
| NextBio | 920. | ||||||||||||||||||||||||
| SOURCE | Search... | ||||||||||||||||||||||||
Entry information
| Entry name | ALDOA_HUMAN | ||||||||
| Accession | Primary (citable) accession number: P04075 Secondary accession number(s): B4DXI7 Q9UCN2 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
| Disclaimer | Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. | ||||||||
Relevant documents
| Human chromosome 16 Human chromosome 16: entries, gene names and cross-references to MIM |
| Human entries with polymorphisms or disease mutations List of human entries with polymorphisms or disease mutations |
| Human polymorphisms and disease mutations Index of human polymorphisms and disease mutations |
| MIM cross-references Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot |
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with