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P04075 (ALDOA_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 177. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Fructose-bisphosphate aldolase A

EC=4.1.2.13
Alternative name(s):
Lung cancer antigen NY-LU-1
Muscle-type aldolase
Gene names
Name:ALDOA
Synonyms:ALDA
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length364 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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

Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 4/4.

Subunit structure

Homotetramer. Interacts with SNX9 and WAS By similarity. Interacts with FBP2; the interaction blocks FBP2 inhibition by physiological concentrations of AMP and reduces inhibition by Ca2+. Ref.19

Subcellular location

CytoplasmmyofibrilsarcomereI band. CytoplasmmyofibrilsarcomereM line. Note: In skeletal muscle, accumulates around the M line and within the I band, colocalizing with FBP2 on both sides of the Z line in the absence of Ca2+ By similarity.

Involvement in disease

Glycogen storage disease 12 (GSD12) [MIM:611881]: A metabolic disorder associated with increased hepatic glycogen and hemolytic anemia. It may lead to myopathy with exercise intolerance and rhabdomyolysis.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.31 Ref.32 Ref.33 Ref.34 Ref.35

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.35

Temperature dependence:

Thermal denaturation midpoint (Tm) is 54.4 degrees Celsius.

Ontologies

Keywords
   Biological processGlycolysis
   Cellular componentCytoplasm
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDisease mutation
Glycogen storage disease
Hereditary hemolytic anemia
   LigandSchiff base
   Molecular functionLyase
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processATP biosynthetic process

Inferred from mutant phenotype Ref.34. Source: BHF-UCL

actin filament organization

Traceable author statement PubMed 1008835. Source: BHF-UCL

blood coagulation

Traceable author statement. Source: Reactome

carbohydrate metabolic process

Traceable author statement. Source: Reactome

fructose 1,6-bisphosphate metabolic process

Inferred from direct assay Ref.35PubMed 9244396. Source: BHF-UCL

fructose metabolic process

Inferred from mutant phenotype Ref.34. Source: BHF-UCL

gluconeogenesis

Traceable author statement. Source: Reactome

glucose metabolic process

Traceable author statement. Source: Reactome

glycolytic process

Inferred from mutant phenotype Ref.34. Source: BHF-UCL

muscle cell cellular homeostasis

Inferred from mutant phenotype Ref.34. Source: BHF-UCL

platelet activation

Traceable author statement. Source: Reactome

platelet degranulation

Traceable author statement. Source: Reactome

protein homotetramerization

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of cell shape

Inferred from direct assay PubMed 9244396. Source: BHF-UCL

small molecule metabolic process

Traceable author statement. Source: Reactome

striated muscle contraction

Inferred from mutant phenotype Ref.34. Source: BHF-UCL

   Cellular_componentI band

Traceable author statement PubMed 1008835. Source: BHF-UCL

M band

Inferred from electronic annotation. Source: UniProtKB-SubCell

actin cytoskeleton

Inferred from direct assay PubMed 9244396. Source: BHF-UCL

cytosol

Traceable author statement. Source: Reactome

extracellular region

Traceable author statement. Source: Reactome

extracellular space

Inferred from direct assay PubMed 23580065. Source: UniProt

extracellular vesicular exosome

Inferred from direct assay PubMed 17641064. Source: BHF-UCL

nucleus

Inferred from direct assay PubMed 21630459. Source: UniProt

platelet alpha granule lumen

Traceable author statement. Source: Reactome

   Molecular_functionactin binding

Traceable author statement PubMed 1008835. Source: BHF-UCL

cytoskeletal protein binding

Inferred from direct assay PubMed 9244396. Source: BHF-UCL

fructose binding

Inferred from direct assay Ref.30Ref.35. Source: BHF-UCL

fructose-bisphosphate aldolase activity

Inferred from direct assay Ref.35PubMed 9244396. Source: BHF-UCL

identical protein binding

Traceable author statement Ref.35. Source: BHF-UCL

poly(A) RNA binding

Inferred from direct assay PubMed 22681889. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 20849852. Source: IntAct

tubulin binding

Traceable author statement PubMed 17329259. Source: BHF-UCL

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

PCNAP120043EBI-709613,EBI-358311

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P04075-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P04075-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MARRKPEGSSFNMTHLSMAMAFSFPPVASGQLHPQLGNTQHQTELGKELATTSTM

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.11 Ref.12 Ref.13 Ref.14 Ref.15
Chain2 – 364363Fructose-bisphosphate aldolase A
PRO_0000216936

Sites

Active site1881Proton acceptor By similarity
Active site2301Schiff-base intermediate with dihydroxyacetone-P
Binding site561Substrate
Binding site1471Substrate
Site3641Necessary for preference for fructose 1,6-bisphosphate over fructose 1-phosphate

Amino acid modifications

Modified residue361Phosphoserine Ref.21 Ref.23
Modified residue391Phosphoserine Ref.21 Ref.23 Ref.26
Modified residue421N6-acetyllysine Ref.22
Modified residue461Phosphoserine Ref.17 Ref.26
Modified residue1081N6-acetyllysine Ref.22
Modified residue1111N6-malonyllysine Ref.25
Modified residue3121N6-malonyllysine Ref.25
Modified residue3301N6-acetyllysine Ref.22

Natural variations

Alternative sequence11M → MARRKPEGSSFNMTHLSMAM AFSFPPVASGQLHPQLGNTQ HQTELGKELATTSTM in isoform 2.
VSP_047261
Natural variant821E → Q.
Corresponds to variant rs11553107 [ dbSNP | Ensembl ].
VAR_048219
Natural variant1291D → G in GSD12; thermolabile. Ref.31 Ref.32
VAR_000550
Natural variant1421G → V.
Corresponds to variant rs11553108 [ dbSNP | Ensembl ].
VAR_048220
Natural variant2071E → K in GSD12; reduces thermal stability; 3-fold decrease in catalytic efficiency mostly due to reduced substrate affinity. Ref.33 Ref.35
VAR_044142
Natural variant3391C → Y in GSD12. Ref.34
VAR_044143
Natural variant3471G → S in GSD12; does not affect thermal stability; 4-fold decrease in catalytic efficiency due to reduced enzyme activity. Ref.35
Corresponds to variant rs138824667 [ dbSNP | Ensembl ].
VAR_044144

Experimental info

Sequence conflict731C → G in CAA30979. Ref.3
Sequence conflict1801Q → R in CAG46678. Ref.6
Sequence conflict1961D → A in CAA30979. Ref.3
Sequence conflict2301K → N in CAA30979. Ref.3
Sequence conflict2801A → S in CAA30979. Ref.3

Secondary structure

...................................................... 364
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 0AAED80F755A7BE8

FASTA36439,420
        10         20         30         40         50         60 
MPYQYPALTP EQKKELSDIA HRIVAPGKGI LAADESTGSI AKRLQSIGTE NTEENRRFYR 

        70         80         90        100        110        120 
QLLLTADDRV NPCIGGVILF HETLYQKADD GRPFPQVIKS KGGVVGIKVD KGVVPLAGTN 

       130        140        150        160        170        180 
GETTTQGLDG LSERCAQYKK DGADFAKWRC VLKIGEHTPS ALAIMENANV LARYASICQQ 

       190        200        210        220        230        240 
NGIVPIVEPE ILPDGDHDLK RCQYVTEKVL AAVYKALSDH HIYLEGTLLK PNMVTPGHAC 

       250        260        270        280        290        300 
TQKFSHEEIA MATVTALRRT VPPAVTGITF LSGGQSEEEA SINLNAINKC PLLKPWALTF 

       310        320        330        340        350        360 
SYGRALQASA LKAWGGKKEN LKAAQEEYVK RALANSLACQ GKYTPSGQAG AAASESLFVS 


NHAY 

« Hide

Isoform 2 [UniParc].

Checksum: FAE6E6CA84022A8A
Show »

FASTA41845,261

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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[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. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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] (ISOFORM 1).
[7]"The sequence and analysis of duplication-rich human chromosome 16."
Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J. expand/collapse author list , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]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. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Cervix, Eye, Lung, Testis and Uterus.
[10]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-108 (ISOFORM 1).
[11]"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] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-364.
[12]"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] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-63 AND 148-358.
[13]"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] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-22.
Tissue: Platelet.
[14]"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] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-16.
Tissue: Colon carcinoma.
[15]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, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
[16]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 139-364 (ISOFORM 1/2).
[17]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-46, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[18]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[19]"Evolutionary conserved N-terminal region of human muscle fructose 1,6-bisphosphatase regulates its activity and the interaction with aldolase."
Gizak A., Maciaszczyk E., Dzugaj A., Eschrich K., Rakus D.
Proteins 72:209-216(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH FBP2.
[20]"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] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[21]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36 AND SER-39, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[22]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-42; LYS-108 AND LYS-330, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[23]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36 AND SER-39, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[24]"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] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[25]"The first identification of lysine malonylation substrates and its regulatory enzyme."
Peng C., Lu Z., Xie Z., Cheng Z., Chen Y., Tan M., Luo H., Zhang Y., He W., Yang K., Zwaans B.M., Tishkoff D., Ho L., Lombard D., He T.C., Dai J., Verdin E., Ye Y., Zhao Y.
Mol. Cell. Proteomics 10:M111.012658.01-M111.012658.12(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: MALONYLATION AT LYS-111 AND LYS-312.
[26]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-39 AND SER-46, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[27]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[28]"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] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
[29]"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] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
[30]"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] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
[31]"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] [Europe PMC] [Abstract]
Cited for: VARIANT GSD12 GLY-129, CHARACTERIZATION OF VARIANT GSD12 GLY-129.
[32]"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] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION OF VARIANT GSD12 GLY-129.
[33]"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] [Europe PMC] [Abstract]
Cited for: VARIANT GSD12 LYS-207.
[34]"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] [Europe PMC] [Abstract]
Cited for: VARIANT GSD12 TYR-339.
[35]"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] [Europe PMC] [Abstract]
Cited for: VARIANT GSD12 SER-347, BIOPHYSICOCHEMICAL PROPERTIES, CHARACTERIZATION OF VARIANTS GSD12 LYS-207 AND SER-347.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M11560 mRNA. Translation: AAA51690.1.
X05236 mRNA. Translation: CAA28861.1.
X12447 Genomic DNA. Translation: CAA30979.1.
AK301993 mRNA. Translation: BAG63399.1.
CR536528 mRNA. Translation: CAG38765.1.
CR541880 mRNA. Translation: CAG46678.1.
AC093512 Genomic DNA. No translation available.
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.
CCDSCCDS10668.1. [P04075-1]
CCDS58450.1. [P04075-2]
PIRADHUA. S14084.
RefSeqNP_000025.1. NM_000034.3. [P04075-1]
NP_001121089.1. NM_001127617.2. [P04075-1]
NP_001230106.1. NM_001243177.1. [P04075-2]
NP_908930.1. NM_184041.2. [P04075-1]
NP_908932.1. NM_184043.2. [P04075-1]
UniGeneHs.513490.
Hs.732822.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1ALDX-ray2.00A2-364[»]
2ALDX-ray2.10A2-364[»]
4ALDX-ray2.80A2-364[»]
ProteinModelPortalP04075.
SMRP04075. Positions 2-364.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid106728. 51 interactions.
IntActP04075. 25 interactions.
MINTMINT-4998828.
STRING9606.ENSP00000336927.

Chemistry

ChEMBLCHEMBL2106.

PTM databases

PhosphoSiteP04075.

Polymorphism databases

DMDM113606.

2D gel databases

DOSAC-COBS-2DPAGEP04075.
OGPP04075.
REPRODUCTION-2DPAGEIPI00465439.
P04075.
SWISS-2DPAGEP04075.
UCD-2DPAGEP04075.

Proteomic databases

MaxQBP04075.
PaxDbP04075.
PRIDEP04075.

Protocols and materials databases

DNASU226.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000338110; ENSP00000336927; ENSG00000149925. [P04075-1]
ENST00000395248; ENSP00000378669; ENSG00000149925. [P04075-2]
ENST00000412304; ENSP00000400452; ENSG00000149925. [P04075-1]
ENST00000563060; ENSP00000455800; ENSG00000149925. [P04075-1]
ENST00000564546; ENSP00000455917; ENSG00000149925. [P04075-1]
ENST00000564595; ENSP00000457468; ENSG00000149925. [P04075-2]
ENST00000566897; ENSP00000455724; ENSG00000149925. [P04075-1]
ENST00000569545; ENSP00000455700; ENSG00000149925. [P04075-1]
GeneID226.
KEGGhsa:226.
UCSCuc002dvw.3. human. [P04075-1]

Organism-specific databases

CTD226.
GeneCardsGC16P030064.
HGNCHGNC:414. ALDOA.
HPACAB006252.
HPA004177.
MIM103850. gene.
611881. phenotype.
neXtProtNX_P04075.
Orphanet57. Glycogen storage disease due to aldolase A deficiency.
PharmGKBPA24707.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG3588.
HOVERGENHBG002386.
InParanoidP04075.
KOK01623.
OMAWRAVIAI.
OrthoDBEOG744T94.
PhylomeDBP04075.
TreeFamTF314203.

Enzyme and pathway databases

BioCycMetaCyc:HS07647-MONOMER.
ReactomeREACT_111217. Metabolism.
REACT_116125. Disease.
REACT_604. Hemostasis.
SABIO-RKP04075.
UniPathwayUPA00109; UER00183.

Gene expression databases

ArrayExpressP04075.
BgeeP04075.
CleanExHS_ALDOA.
GenevestigatorP04075.

Family and domain databases

Gene3D3.20.20.70. 1 hit.
InterProIPR000741. Aldolase_I.
IPR013785. Aldolase_TIM.
[Graphical view]
PANTHERPTHR11627. PTHR11627. 1 hit.
PfamPF00274. Glycolytic. 1 hit.
[Graphical view]
PROSITEPS00158. ALDOLASE_CLASS_I. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP04075.
GeneWikiAldolase_A.
GenomeRNAi226.
NextBio920.
PROP04075.
SOURCESearch...

Entry information

Entry nameALDOA_HUMAN
AccessionPrimary (citable) accession number: P04075
Secondary accession number(s): B4DXI7 expand/collapse secondary AC list , Q6FH76, Q6FI10, Q96B15, Q9BWD9, Q9UCN2
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1986
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 177 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 16

Human chromosome 16: entries, gene names and cross-references to MIM