P04075 (ALDOA_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names 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

Name:	ALDOA
Synonyms:	ALDA

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › 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	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.
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.27 Ref.28 Ref.29 Ref.30 Ref.31
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.31 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

Keywords
Biological process	Glycolysis
Coding sequence diversity	Polymorphism
Disease	Disease mutation Glycogen storage disease Hereditary hemolytic anemia
Ligand	Schiff base
Molecular function	Lyase
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	ATP biosynthetic process Inferred from mutant phenotype Ref.30. Source: BHF-UCL actin filament organization Traceable author statement PubMed 1008835. Source: BHF-UCL fructose 1,6-bisphosphate metabolic process Inferred from direct assay Ref.31PubMed 9244396. Source: BHF-UCL fructose metabolic process Inferred from mutant phenotype Ref.30. Source: BHF-UCL gluconeogenesis Traceable author statement. Source: Reactome glycolysis Inferred from mutant phenotype Ref.30. Source: BHF-UCL muscle cell homeostasis Inferred from mutant phenotype Ref.30. 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 striated muscle contraction Inferred from mutant phenotype Ref.30. Source: BHF-UCL
Cellular_component	I band Traceable author statement PubMed 1008835. Source: BHF-UCL actin cytoskeleton Inferred from direct assay PubMed 9244396. Source: BHF-UCL cytosol Traceable author statement. Source: Reactome extracellular vesicular exosome Inferred from direct assay PubMed 17641064. Source: BHF-UCL platelet alpha granule lumen Traceable author statement. Source: Reactome
Molecular_function	actin binding Traceable author statement PubMed 1008835. Source: BHF-UCL fructose binding Inferred from direct assay Ref.26Ref.31. Source: BHF-UCL fructose-bisphosphate aldolase activity Inferred from direct assay Ref.31PubMed 9244396. Source: BHF-UCL identical protein binding Traceable author statement Ref.31. Source: BHF-UCL tubulin binding Traceable author statement PubMed 17329259. Source: BHF-UCL
Complete GO annotation...

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

36

1

Phosphoserine Ref.18 Ref.20

Modified residue

39

1

Phosphoserine Ref.18 Ref.20 Ref.23

Modified residue

42

1

N6-acetyllysine Ref.19

Modified residue

46

1

Phosphoserine Ref.16 Ref.23

Modified residue

108

1

N6-acetyllysine Ref.19

Modified residue

111

1

N6-malonyllysine Ref.22

Modified residue

312

1

N6-malonyllysine Ref.22

Modified residue

330

1

N6-acetyllysine Ref.19

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.27 Ref.28

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.29 Ref.31

VAR_044142

Natural variant

339

1

C → Y in GSD12. Ref.30

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.31

VAR_044144

Experimental info

Sequence conflict

180

1

Q → R in CAG46678. Ref.6

Secondary structure

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364

Helix Strand Turn

Details...

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

Beta strand

155 – 157

3

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

	Sequence		Length	Mass (Da)
	P04075 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: 0AAED80F755A7BE8	FASTA	364	39,420
	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

References

	« Hide 'large scale' referencesShow '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]. 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]. 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].
[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].
[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. , 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]. 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. , 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].
[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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 139-364.
[16]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[17]	"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.
[18]	"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, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[19]	"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, MASS SPECTROMETRY.
[20]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[21]	"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].
[22]	"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.
[23]	"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, MASS SPECTROMETRY.
[24]	"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).
[25]	"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).
[26]	"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).
[27]	"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.
[28]	"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.
[29]	"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.
[30]	"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.
[31]	"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.

Web resources

GeneReviews

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.
Hs.732822.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1ALD	X-ray	2.00	A	2-364	[»]
2ALD	X-ray	2.10	A	2-364	[»]
4ALD	X-ray	2.80	A	2-364	[»]

ProteinModelPortal

P04075.

ModBase

Search...

Protein-protein interaction databases

IntAct

P04075. 24 interactions.

MINT

MINT-4998828.

STRING

9606.ENSP00000336927.

PTM databases

PhosphoSite

P04075.

Polymorphism databases

DMDM

113606.

2D gel databases

DOSAC-COBS-2DPAGE

P04075.

OGP

P04075.

REPRODUCTION-2DPAGE

IPI00465439.
P04075.

SWISS-2DPAGE

P04075.

UCD-2DPAGE

P04075.

Proteomic databases

PaxDb

P04075.

PRIDE

P04075.

Protocols and materials databases

DNASU

226.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000338110; ENSP00000336927; ENSG00000149925.
ENST00000395248; ENSP00000378669; ENSG00000149925.
ENST00000412304; ENSP00000400452; ENSG00000149925.
ENST00000563060; ENSP00000455800; ENSG00000149925.
ENST00000564546; ENSP00000455917; ENSG00000149925.
ENST00000564595; ENSP00000457468; ENSG00000149925.
ENST00000566897; ENSP00000455724; ENSG00000149925.
ENST00000569545; ENSP00000455700; ENSG00000149925.

GeneID

226.

KEGG

hsa:226.

UCSC

uc002dvw.3. human.

Organism-specific databases

CTD

226.

GeneCards

GC16P030064.

HGNC

HGNC:414. ALDOA.

HPA

CAB006252.
HPA004177.

MIM

103850. gene.
611881. phenotype.

neXtProt

NX_P04075.

Orphanet

57. Glycogen storage disease due to aldolase A deficiency.

PharmGKB

PA24707.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG3588.

HOVERGEN

HBG002386.

InParanoid

P04075.

KO

K01623.

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_111217. Metabolism.
REACT_604. Hemostasis.

SABIO-RK

P04075.

UniPathway

UPA00109; UER00183.

Gene expression databases

ArrayExpress

P04075.

Bgee

P04075.

CleanEx

HS_ALDOA.

Genevestigator

P04075.

GermOnline

ENSG00000149925. Homo sapiens.

Family and domain databases

Gene3D

3.20.20.70. 1 hit.

InterPro

IPR000741. Aldolase_I.
IPR013785. Aldolase_TIM.
[Graphical view]

PANTHER

PTHR11627. PTHR11627. 1 hit.

Pfam

PF00274. Glycolytic. 1 hit.
[Graphical view]

PROSITE

PS00158. ALDOLASE_CLASS_I. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChEMBL

CHEMBL2106.

EvolutionaryTrace

P04075.

GenomeRNAi

226.

NextBio

920.

SOURCE

Search...

Entry information

Entry name

ALDOA_HUMAN

Accession

Primary (citable) accession number: P04075
Secondary accession number(s): B4DXI7 , Q6FH76, Q6FI10, Q96B15, Q9BWD9, Q9UCN2

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1986
Last sequence update:	January 23, 2007
Last modified:	May 29, 2013
This is version 164 of the entry and version 2 of the sequence. [Complete 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.