Reviewed, UniProtKB/Swiss-Prot P04075 (ALDOA_HUMAN)

Names and origin

Protein names

Recommended name:
    Fructose-bisphosphate aldolase A
    EC=4.1.2.13
Alternative name(s):
    Muscle-type aldolase
    Lung cancer antigen NY-LU-1

Gene names

Name:	ALDOA
Synonyms:	ALDA

Organism

Homo sapiens (Human) [Complete proteome]

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)

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.
Involvement in disease	Defects in ALDOA are the cause of aldolase A deficiency (ALDOA deficiency) [MIM:611881]; also known as red cell aldolase deficiency. ALDOA deficiency is an autosomal recessive disorder associated with hereditary hemolytic anemia.
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) Temperature dependence: Thermal denaturation midpoint (Tm) is 54.4 degrees Celsius.

Ontologies

Keywords
Biological process	Glycolysis
Coding sequence diversity	Polymorphism
Disease	Disease mutation Hereditary hemolytic anemia
Ligand	Schiff base
Molecular function	Lyase
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	ATP biosynthetic process Ref.31 Inferred from mutant phenotype. Source: UniProtKB actin filament organization Traceable author statement. Source: UniProtKB fructose 1,6-bisphosphate metabolic process Ref.32 Inferred from direct assay. Source: UniProtKB glycolysis Ref.31 Inferred from mutant phenotype. Source: UniProtKB muscle homeostasis Ref.31 Inferred from mutant phenotype. Source: UniProtKB regulation of cell shape Inferred from direct assay. Source: UniProtKB striated muscle contraction Ref.31 Inferred from mutant phenotype. Source: UniProtKB
Cellular component	I band Traceable author statement. Source: UniProtKB actin cytoskeleton Inferred from direct assay. Source: UniProtKB extracellular vesicular exosome Inferred from direct assay. Source: UniProtKB
Molecular function	actin binding Traceable author statement. Source: UniProtKB fructose binding Ref.27 Ref.32 Inferred from direct assay. Source: UniProtKB fructose-bisphosphate aldolase activity Ref.32 Inferred from direct assay. Source: UniProtKB identical protein binding Ref.32 Traceable author statement. Source: UniProtKB tubulin binding Traceable author statement. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
XRN1	Q8IZH2	1	EBI-709613,EBI-372406

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

13

1

N6-acetyllysine Ref.19

Modified residue

36

1

Phosphoserine By similarity

Modified residue

39

1

Phosphoserine By similarity

Modified residue

42

1

N6-acetyllysine Ref.19 Ref.24

Modified residue

46

1

Phosphoserine Ref.18

Modified residue

65

1

Phosphothreonine Ref.17

Modified residue

108

1

N6-acetyllysine Ref.24

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.24

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: dbSNP rs11553107.

VAR_048219

Natural variant

129

1

D → G in ALDOA deficiency; thermolabile. Ref.28 Ref.29

VAR_000550

Natural variant

142

1

G → V: dbSNP rs11553108.

VAR_048220

Natural variant

207

1

E → K in ALDOA deficiency; reduces thermal stability; 3-fold decrease in catalytic efficiency mostly due to reduced substrate affinity. Ref.30 Ref.32

VAR_044142

Natural variant

339

1

C → Y in ALDOA deficiency. Ref.31

VAR_044143

Natural variant

347

1

G → S in ALDOA deficiency; does not affect thermal stability; 4-fold decrease in catalytic efficiency due to reduced enzyme activity. Ref.32

VAR_044144

Experimental info

Sequence conflict

180

1

Q → R in CAG46678. Ref.6

Secondary structure

1

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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

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)
	P04075-1 [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: 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. , 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: 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. , 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: 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: Hepatocyte.
[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: Epithelium.
[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.
[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. , Yuan J., Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., 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.
[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.
[22]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[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]	"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.
[25]	"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).
[26]	"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).
[27]	"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).
[28]	"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 ALDOA DEFICIENCY GLY-129, CHARACTERIZATION OF VARIANT ALDOA DEFICIENCY GLY-129.
[29]	"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 ALDOA DEFICIENCY GLY-129.
[30]	"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 ALDOA DEFICIENCY LYS-207.
[31]	"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 ALDOA DEFICIENCY TYR-339.
[32]	"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 ALDOA DEFICIENCY SER-347, BIOPHYSICOCHEMICAL PROPERTIES, CHARACTERIZATION OF VARIANTS ALDOA DEFICIENCY LYS-207 AND SER-347.
+	Additional computationally mapped references.

Web resources

GeneReviews

Cross-references

Sequence databases

EMBLGenBankDDBJ

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.
NP_001121089.1.
NP_908930.1.
NP_908932.1.

UniGene

Hs.513490

3D structure databases

PDBPDBe

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	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

P04075. 5 interactions.

STRING

P04075.

PTM databases

PhosphoSite

P04075.

2-D gel databases

SWISS-2DPAGE

P04075.

Aarhus/Ghent-2DPAGE

1302. NEPHGE.

DOSAC-COBS-2DPAGE

P04075.

OGP

P04075.

REPRODUCTION-2DPAGE

IPI00465439.
P04075.

Siena-2DPAGE

P04075.

Proteomic databases

PRIDE

P04075.

Genome annotation databases

Ensembl

ENST00000338110; ENSP00000336927; ENSG00000149925; Homo sapiens. [Genome view]
ENST00000395240; ENSP00000378661; ENSG00000149925; Homo sapiens. [Genome view]
ENST00000395248; ENSP00000378669; ENSG00000149925; Homo sapiens. [Genome view]
ENST00000412304; ENSP00000400452; ENSG00000149925; Homo sapiens. [Genome view]
ENST00000436540; ENSP00000387793; ENSG00000149925; Homo sapiens. [Genome view]

GeneID

226.

KEGG

hsa:226.

UCSC

uc002dvw.1. human.
uc002dwb.1. human.

Organism-specific databases

CTD

226.

GeneCards

GC16P029971.

H-InvDB

HIX0012935.

HGNC

HGNC:414. ALDOA.

HPA

CAB006252.
HPA004177.

MIM

103850. gene.
611881. phenotype.

Orphanet

57. Aldolase A deficiency.

PharmGKB

PA24707.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

P04075.

HOVERGEN

P04075.

Enzyme and pathway databases

BRENDA

4.1.2.13. 247.

Pathway_Interaction_DB

hif1_tfpathway. HIF-1-alpha transcription factor network.

Reactome

REACT_1505. Integration of energy metabolism.
REACT_15380. Diabetes pathways.
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.

PANTHER

PTHR11627. Aldolase_I. 1 hit.

Pfam

PF00274. Glycolytic. 1 hit.
[Graphical view]

ProDom

PD001128. Aldolase_I. 1 hit.
[Graphical view] [Entries sharing at least one domain]

PROSITE

PS00158. ALDOLASE_CLASS_I. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

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:	November 3, 2009
This is version 128 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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.