Details for: ALDOA

Gene ID: 226

Symbol: ALDOA

Ensembl ID: ENSG00000149925

Description: aldolase, fructose-bisphosphate A

Associated with

Other Information

Genular Protein ID: 556857321

Symbol: ALDOA_HUMAN

Name: Lung cancer antigen NY-LU-1

UniProtKB Accession Codes:

Database IDs:

Citations:

PubMed ID: 3840020

Title: Nucleotide sequence of a cDNA clone for human aldolase: a messenger RNA in the liver.

PubMed ID: 3840020

DOI: 10.1016/0006-291x(85)91818-2

PubMed ID: 3030757

Title: A new human species of aldolase A mRNA from fibroblasts.

PubMed ID: 3030757

DOI: 10.1111/j.1432-1033.1987.tb10984.x

PubMed ID: 3391172

Title: Human aldolase A gene. Structural organization and tissue-specific expression by multiple promoters and alternate mRNA processing.

PubMed ID: 3391172

DOI: 10.1111/j.1432-1033.1988.tb14136.x

PubMed ID: 1999195

Title: An additional promoter functions in the human aldolase A gene, but not in rat.

PubMed ID: 1999195

DOI: 10.1111/j.1432-1033.1991.tb15766.x

PubMed ID: 14702039

Title: Complete sequencing and characterization of 21,243 full-length human cDNAs.

PubMed ID: 14702039

DOI: 10.1038/ng1285

PubMed ID: 15616553

Title: The sequence and analysis of duplication-rich human chromosome 16.

PubMed ID: 15616553

DOI: 10.1038/nature03187

PubMed ID: 15489334

Title: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).

PubMed ID: 15489334

DOI: 10.1101/gr.2596504

PubMed ID: 3441006

Title: Characterization of three optional promoters in the 5' region of the human aldolase A gene.

PubMed ID: 3441006

DOI: 10.1016/0022-2836(87)90556-0

PubMed ID: 3355497

Title: The complete amino acid sequence of human skeletal-muscle fructose-bisphosphate aldolase.

PubMed ID: 3355497

DOI: 10.1042/bj2490779

PubMed ID: 6696436

Title: Human skeletal-muscle aldolase: N-terminal sequence analysis of CNBr- and o-iodosobenzoic acid-cleavage fragments.

PubMed ID: 6696436

DOI: 10.1016/0003-9861(84)90075-4

PubMed ID: 12665801

Title: Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides.

PubMed ID: 12665801

DOI: 10.1038/nbt810

PubMed ID: 1353685

Title: Identification of transglutaminase substrates in HT29 colon cancer cells: use of 5-(biotinamido)pentylamine as a transglutaminase-specific probe.

PubMed ID: 1353685

DOI: 10.1016/0167-4889(92)90078-p

PubMed ID: 3674018

Title: Evolutionary implications of the human aldolase-A, -B, -C, and - pseudogene chromosome locations.

PubMed ID: 3674018

PubMed ID: 14654843

Title: Proteomic characterization of the human centrosome by protein correlation profiling.

PubMed ID: 14654843

DOI: 10.1038/nature02166

PubMed ID: 17081983

Title: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.

PubMed ID: 17081983

DOI: 10.1016/j.cell.2006.09.026

PubMed ID: 18669648

Title: A quantitative atlas of mitotic phosphorylation.

PubMed ID: 18669648

DOI: 10.1073/pnas.0805139105

PubMed ID: 18214967

Title: Evolutionary conserved N-terminal region of human muscle fructose 1,6-bisphosphatase regulates its activity and the interaction with aldolase.

PubMed ID: 18214967

DOI: 10.1002/prot.21909

PubMed ID: 19413330

Title: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach.

PubMed ID: 19413330

DOI: 10.1021/ac9004309

PubMed ID: 19690332

Title: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions.

PubMed ID: 19690332

DOI: 10.1126/scisignal.2000007

PubMed ID: 19608861

Title: Lysine acetylation targets protein complexes and co-regulates major cellular functions.

PubMed ID: 19608861

DOI: 10.1126/science.1175371

PubMed ID: 20068231

Title: Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis.

PubMed ID: 20068231

DOI: 10.1126/scisignal.2000475

PubMed ID: 21269460

Title: Initial characterization of the human central proteome.

PubMed ID: 21269460

DOI: 10.1186/1752-0509-5-17

PubMed ID: 21908771

Title: The first identification of lysine malonylation substrates and its regulatory enzyme.

PubMed ID: 21908771

DOI: 10.1074/mcp.m111.012658

PubMed ID: 21406692

Title: System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation.

PubMed ID: 21406692

DOI: 10.1126/scisignal.2001570

PubMed ID: 22905912

Title: Resveratrol-induced changes of the human adipocyte secretion profile.

PubMed ID: 22905912

DOI: 10.1021/pr300539b

PubMed ID: 22223895

Title: Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features.

PubMed ID: 22223895

DOI: 10.1074/mcp.m111.015131

PubMed ID: 22814378

Title: N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB.

PubMed ID: 22814378

DOI: 10.1073/pnas.1210303109

PubMed ID: 23186163

Title: Toward a comprehensive characterization of a human cancer cell phosphoproteome.

PubMed ID: 23186163

DOI: 10.1021/pr300630k

PubMed ID: 24275569

Title: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.

PubMed ID: 24275569

DOI: 10.1016/j.jprot.2013.11.014

PubMed ID: 24129315

Title: Immunoaffinity enrichment and mass spectrometry analysis of protein methylation.

PubMed ID: 24129315

DOI: 10.1074/mcp.o113.027870

PubMed ID: 25114211

Title: Mapping of SUMO sites and analysis of SUMOylation changes induced by external stimuli.

PubMed ID: 25114211

DOI: 10.1073/pnas.1413825111

PubMed ID: 25944712

Title: N-terminome analysis of the human mitochondrial proteome.

PubMed ID: 25944712

DOI: 10.1002/pmic.201400617

PubMed ID: 29192674

Title: Landscape of the regulatory elements for lysine 2-hydroxyisobutyrylation pathway.

PubMed ID: 29192674

DOI: 10.1038/cr.2017.149

PubMed ID: 29775581

Title: p300-mediated lysine 2-hydroxyisobutyrylation regulates glycolysis.

PubMed ID: 29775581

DOI: 10.1016/j.molcel.2018.04.011

PubMed ID: 2335208

Title: The crystal structure of human muscle aldolase at 3.0-A resolution.

PubMed ID: 2335208

DOI: 10.1016/0014-5793(90)80211-z

PubMed ID: 2056525

Title: Activity and specificity of human aldolases.

PubMed ID: 2056525

DOI: 10.1016/0022-2836(91)90650-u

PubMed ID: 10048322

Title: Crystal structure of human muscle aldolase complexed with fructose 1,6-bisphosphate: mechanistic implications.

PubMed ID: 10048322

DOI: 10.1110/ps.8.2.291

PubMed ID: 2825199

Title: Human aldolase A deficiency associated with a hemolytic anemia: thermolabile aldolase due to a single base mutation.

PubMed ID: 2825199

DOI: 10.1073/pnas.84.23.8623

PubMed ID: 2229018

Title: 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.

PubMed ID: 2229018

DOI: 10.1093/oxfordjournals.jbchem.a123174

PubMed ID: 8598869

Title: Brief report: inherited metabolic myopathy and hemolysis due to a mutation in aldolase A.

PubMed ID: 8598869

DOI: 10.1056/nejm199604253341705

PubMed ID: 14615364

Title: Hemolytic anemia and severe rhabdomyolysis caused by compound heterozygous mutations of the gene for erythrocyte/muscle isozyme of aldolase, ALDOA(Arg303X/Cys338Tyr).

PubMed ID: 14615364

DOI: 10.1182/blood-2003-09-3160

PubMed ID: 14766013

Title: Human aldolase A natural mutants: relationship between flexibility of the C-terminal region and enzyme function.

PubMed ID: 14766013

DOI: 10.1042/bj20031941

Sequence Information:

  • Length: 364
  • Mass: 39420
  • Checksum: 0AAED80F755A7BE8
  • Sequence:
  • 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

Database document:

This is a preview of the gene's schema. Only a few entries are kept for 'singleCellExpressions,' 'mRNAExpressions,' and other large data arrays for visualization purposes. You can zoom in with the mouse wheel for a closer view, and the text will adjust automatically if necessary. For the full schema, download it here.