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P04075

- ALDOA_HUMAN

UniProt

P04075 - ALDOA_HUMAN

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Protein

Fructose-bisphosphate aldolase A

Gene

ALDOA

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Plays a key role in glycolysis and gluconeogenesis. In addition, may also function as scaffolding protein (By similarity).By similarity

Catalytic activityi

D-fructose 1,6-bisphosphate = glycerone phosphate + D-glyceraldehyde 3-phosphate.

Kineticsi

  1. KM=52 µM for fructose 1,6-bisphosphate (at 30 degrees Celsius)1 Publication

Temperature dependencei

Thermal denaturation midpoint (Tm) is 54.4 degrees Celsius.1 Publication

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei56 – 561Substrate
Binding sitei147 – 1471Substrate
Active sitei188 – 1881Proton acceptorBy similarity
Active sitei230 – 2301Schiff-base intermediate with dihydroxyacetone-P
Sitei364 – 3641Necessary for preference for fructose 1,6-bisphosphate over fructose 1-phosphate

GO - Molecular functioni

  1. actin binding Source: BHF-UCL
  2. cytoskeletal protein binding Source: BHF-UCL
  3. fructose binding Source: BHF-UCL
  4. fructose-bisphosphate aldolase activity Source: BHF-UCL
  5. identical protein binding Source: BHF-UCL
  6. poly(A) RNA binding Source: UniProtKB
  7. tubulin binding Source: BHF-UCL

GO - Biological processi

  1. actin filament organization Source: BHF-UCL
  2. ATP biosynthetic process Source: BHF-UCL
  3. blood coagulation Source: Reactome
  4. carbohydrate metabolic process Source: Reactome
  5. fructose 1,6-bisphosphate metabolic process Source: BHF-UCL
  6. fructose metabolic process Source: BHF-UCL
  7. gluconeogenesis Source: Reactome
  8. glucose metabolic process Source: Reactome
  9. glycolytic process Source: BHF-UCL
  10. muscle cell cellular homeostasis Source: BHF-UCL
  11. platelet activation Source: Reactome
  12. platelet degranulation Source: Reactome
  13. protein homotetramerization Source: UniProtKB
  14. regulation of cell shape Source: BHF-UCL
  15. small molecule metabolic process Source: Reactome
  16. striated muscle contraction Source: BHF-UCL
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Glycolysis

Keywords - Ligandi

Schiff base

Enzyme and pathway databases

BioCyciMetaCyc:HS07647-MONOMER.
ReactomeiREACT_1383. Glycolysis.
REACT_1520. Gluconeogenesis.
SABIO-RKP04075.
UniPathwayiUPA00109; UER00183.

Names & Taxonomyi

Protein namesi
Recommended name:
Fructose-bisphosphate aldolase A (EC:4.1.2.13)
Alternative name(s):
Lung cancer antigen NY-LU-1
Muscle-type aldolase
Gene namesi
Name:ALDOA
Synonyms:ALDA
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 16

Organism-specific databases

HGNCiHGNC:414. ALDOA.

Subcellular locationi

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

GO - Cellular componenti

  1. actin cytoskeleton Source: BHF-UCL
  2. cytosol Source: Reactome
  3. extracellular region Source: Reactome
  4. extracellular space Source: UniProt
  5. extracellular vesicular exosome Source: UniProtKB
  6. I band Source: BHF-UCL
  7. membrane Source: UniProtKB
  8. nucleus Source: UniProt
  9. platelet alpha granule lumen Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Involvement in diseasei

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.4 Publications
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti129 – 1291D → G in GSD12; thermolabile. 1 Publication
VAR_000550
Natural varianti207 – 2071E → K in GSD12; reduces thermal stability; 3-fold decrease in catalytic efficiency mostly due to reduced substrate affinity. 1 Publication
VAR_044142
Natural varianti339 – 3391C → Y in GSD12. 1 Publication
VAR_044143
Natural varianti347 – 3471G → S in GSD12; does not affect thermal stability; 4-fold decrease in catalytic efficiency due to reduced enzyme activity. 1 Publication
Corresponds to variant rs138824667 [ dbSNP | Ensembl ].
VAR_044144

Keywords - Diseasei

Disease mutation, Glycogen storage disease, Hereditary hemolytic anemia

Organism-specific databases

MIMi611881. phenotype.
Orphaneti57. Glycogen storage disease due to aldolase A deficiency.
PharmGKBiPA24707.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed5 Publications
Chaini2 – 364363Fructose-bisphosphate aldolase APRO_0000216936Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei36 – 361Phosphoserine2 Publications
Modified residuei39 – 391Phosphoserine3 Publications
Modified residuei42 – 421N6-acetyllysine1 Publication
Modified residuei46 – 461Phosphoserine2 Publications
Modified residuei108 – 1081N6-acetyllysine1 Publication
Modified residuei111 – 1111N6-malonyllysine1 Publication
Modified residuei312 – 3121N6-malonyllysine1 Publication
Modified residuei330 – 3301N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP04075.
PaxDbiP04075.
PRIDEiP04075.

2D gel databases

DOSAC-COBS-2DPAGEP04075.
OGPiP04075.
REPRODUCTION-2DPAGEIPI00465439.
P04075.
SWISS-2DPAGEP04075.
UCD-2DPAGEP04075.

PTM databases

PhosphoSiteiP04075.

Expressioni

Gene expression databases

BgeeiP04075.
CleanExiHS_ALDOA.
ExpressionAtlasiP04075. baseline and differential.
GenevestigatoriP04075.

Organism-specific databases

HPAiCAB006252.
HPA004177.

Interactioni

Subunit structurei

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+.By similarity1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
PCNAP120043EBI-709613,EBI-358311

Protein-protein interaction databases

BioGridi106728. 54 interactions.
IntActiP04075. 26 interactions.
MINTiMINT-4998828.
STRINGi9606.ENSP00000336927.

Structurei

Secondary structure

1
364
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi10 – 2314Combined sources
Beta strandi29 – 335Combined sources
Helixi37 – 4610Combined sources
Helixi53 – 6412Combined sources
Helixi68 – 736Combined sources
Beta strandi74 – 796Combined sources
Helixi83 – 853Combined sources
Helixi94 – 1007Combined sources
Beta strandi104 – 1085Combined sources
Beta strandi113 – 1153Combined sources
Beta strandi119 – 1213Combined sources
Beta strandi123 – 1253Combined sources
Helixi131 – 14010Combined sources
Beta strandi145 – 1528Combined sources
Beta strandi155 – 1573Combined sources
Helixi161 – 17919Combined sources
Turni180 – 1823Combined sources
Beta strandi184 – 1918Combined sources
Helixi199 – 21921Combined sources
Helixi224 – 2263Combined sources
Helixi246 – 25813Combined sources
Beta strandi267 – 2704Combined sources
Helixi277 – 28913Combined sources
Beta strandi296 – 3038Combined sources
Helixi304 – 31411Combined sources
Helixi318 – 3203Combined sources
Helixi321 – 33818Combined sources
Turni339 – 3413Combined sources
Beta strandi348 – 3503Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ALDX-ray2.00A2-364[»]
2ALDX-ray2.10A2-364[»]
4ALDX-ray2.80A2-364[»]
ProteinModelPortaliP04075.
SMRiP04075. Positions 2-364.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP04075.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG3588.
GeneTreeiENSGT00390000010235.
HOVERGENiHBG002386.
InParanoidiP04075.
KOiK01623.
OMAiWRAVIAI.
OrthoDBiEOG744T94.
PhylomeDBiP04075.
TreeFamiTF314203.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
InterProiIPR029768. Aldolase_I_AS.
IPR013785. Aldolase_TIM.
IPR029769. FBA_euk-type.
IPR000741. FBA_I.
[Graphical view]
PANTHERiPTHR11627. PTHR11627. 1 hit.
PfamiPF00274. Glycolytic. 1 hit.
[Graphical view]
PROSITEiPS00158. ALDOLASE_CLASS_I. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P04075-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MPYQYPALTP EQKKELSDIA HRIVAPGKGI LAADESTGSI AKRLQSIGTE
60 70 80 90 100
NTEENRRFYR QLLLTADDRV NPCIGGVILF HETLYQKADD GRPFPQVIKS
110 120 130 140 150
KGGVVGIKVD KGVVPLAGTN GETTTQGLDG LSERCAQYKK DGADFAKWRC
160 170 180 190 200
VLKIGEHTPS ALAIMENANV LARYASICQQ NGIVPIVEPE ILPDGDHDLK
210 220 230 240 250
RCQYVTEKVL AAVYKALSDH HIYLEGTLLK PNMVTPGHAC TQKFSHEEIA
260 270 280 290 300
MATVTALRRT VPPAVTGITF LSGGQSEEEA SINLNAINKC PLLKPWALTF
310 320 330 340 350
SYGRALQASA LKAWGGKKEN LKAAQEEYVK RALANSLACQ GKYTPSGQAG
360
AAASESLFVS NHAY
Length:364
Mass (Da):39,420
Last modified:January 23, 2007 - v2
Checksum:i0AAED80F755A7BE8
GO
Isoform 2 (identifier: P04075-2) [UniParc]FASTAAdd to Basket

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

Show »
Length:418
Mass (Da):45,261
Checksum:iFAE6E6CA84022A8A
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti73 – 731C → G in CAA30979. (PubMed:3391172)Curated
Sequence conflicti180 – 1801Q → R in CAG46678. 1 PublicationCurated
Sequence conflicti196 – 1961D → A in CAA30979. (PubMed:3391172)Curated
Sequence conflicti230 – 2301K → N in CAA30979. (PubMed:3391172)Curated
Sequence conflicti280 – 2801A → S in CAA30979. (PubMed:3391172)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti82 – 821E → Q.
Corresponds to variant rs11553107 [ dbSNP | Ensembl ].
VAR_048219
Natural varianti129 – 1291D → G in GSD12; thermolabile. 1 Publication
VAR_000550
Natural varianti142 – 1421G → V.
Corresponds to variant rs11553108 [ dbSNP | Ensembl ].
VAR_048220
Natural varianti207 – 2071E → K in GSD12; reduces thermal stability; 3-fold decrease in catalytic efficiency mostly due to reduced substrate affinity. 1 Publication
VAR_044142
Natural varianti339 – 3391C → Y in GSD12. 1 Publication
VAR_044143
Natural varianti347 – 3471G → S in GSD12; does not affect thermal stability; 4-fold decrease in catalytic efficiency due to reduced enzyme activity. 1 Publication
Corresponds to variant rs138824667 [ dbSNP | Ensembl ].
VAR_044144

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 11M → MARRKPEGSSFNMTHLSMAM AFSFPPVASGQLHPQLGNTQ HQTELGKELATTSTM in isoform 2. 1 PublicationVSP_047261

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS10668.1. [P04075-1]
CCDS58450.1. [P04075-2]
PIRiS14084. ADHUA.
RefSeqiNP_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]
UniGeneiHs.513490.
Hs.732822.

Genome annotation databases

EnsembliENST00000338110; 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]
GeneIDi226.
KEGGihsa:226.
UCSCiuc002dvw.3. human. [P04075-1]

Polymorphism databases

DMDMi113606.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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 .
CCDSi CCDS10668.1. [P04075-1 ]
CCDS58450.1. [P04075-2 ]
PIRi S14084. ADHUA.
RefSeqi NP_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 ]
UniGenei Hs.513490.
Hs.732822.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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 [» ]
ProteinModelPortali P04075.
SMRi P04075. Positions 2-364.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 106728. 54 interactions.
IntActi P04075. 26 interactions.
MINTi MINT-4998828.
STRINGi 9606.ENSP00000336927.

Chemistry

ChEMBLi CHEMBL2106.

PTM databases

PhosphoSitei P04075.

Polymorphism databases

DMDMi 113606.

2D gel databases

DOSAC-COBS-2DPAGE P04075.
OGPi P04075.
REPRODUCTION-2DPAGE IPI00465439.
P04075.
SWISS-2DPAGE P04075.
UCD-2DPAGE P04075.

Proteomic databases

MaxQBi P04075.
PaxDbi P04075.
PRIDEi P04075.

Protocols and materials databases

DNASUi 226.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000338110 ; 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 ]
GeneIDi 226.
KEGGi hsa:226.
UCSCi uc002dvw.3. human. [P04075-1 ]

Organism-specific databases

CTDi 226.
GeneCardsi GC16P030064.
HGNCi HGNC:414. ALDOA.
HPAi CAB006252.
HPA004177.
MIMi 103850. gene.
611881. phenotype.
neXtProti NX_P04075.
Orphaneti 57. Glycogen storage disease due to aldolase A deficiency.
PharmGKBi PA24707.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG3588.
GeneTreei ENSGT00390000010235.
HOVERGENi HBG002386.
InParanoidi P04075.
KOi K01623.
OMAi WRAVIAI.
OrthoDBi EOG744T94.
PhylomeDBi P04075.
TreeFami TF314203.

Enzyme and pathway databases

UniPathwayi UPA00109 ; UER00183 .
BioCyci MetaCyc:HS07647-MONOMER.
Reactomei REACT_1383. Glycolysis.
REACT_1520. Gluconeogenesis.
SABIO-RK P04075.

Miscellaneous databases

EvolutionaryTracei P04075.
GeneWikii Aldolase_A.
GenomeRNAii 226.
NextBioi 920.
PROi P04075.
SOURCEi Search...

Gene expression databases

Bgeei P04075.
CleanExi HS_ALDOA.
ExpressionAtlasi P04075. baseline and differential.
Genevestigatori P04075.

Family and domain databases

Gene3Di 3.20.20.70. 1 hit.
InterProi IPR029768. Aldolase_I_AS.
IPR013785. Aldolase_TIM.
IPR029769. FBA_euk-type.
IPR000741. FBA_I.
[Graphical view ]
PANTHERi PTHR11627. PTHR11627. 1 hit.
Pfami PF00274. Glycolytic. 1 hit.
[Graphical view ]
PROSITEi PS00158. ALDOLASE_CLASS_I. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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.
    , 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.
    , 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. 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. 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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  25. 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. 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. 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.

Entry informationi

Entry nameiALDOA_HUMAN
AccessioniPrimary (citable) accession number: P04075
Secondary accession number(s): B4DXI7
, Q6FH76, Q6FI10, Q96B15, Q9BWD9, Q9UCN2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1986
Last sequence update: January 23, 2007
Last modified: November 26, 2014
This is version 181 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

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.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 16
    Human chromosome 16: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3