Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P09972 (ALDOC_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 149. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Fructose-bisphosphate aldolase C

EC=4.1.2.13
Alternative name(s):
Brain-type aldolase
Gene names
Name:ALDOC
Synonyms:ALDC
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)

Catalytic activity

D-fructose 1,6-bisphosphate = glycerone phosphate + D-glyceraldehyde 3-phosphate. Ref.14

Pathway

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

Subunit structure

Homotetramer. Interacts with ATP6V1E1. May interact with PLD2. Ref.10 Ref.11

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=10.7 µM for fructose 1,6-bisphosphate Ref.14

KM=16 mM for fructose 1-phosphate

Sequence caution

The sequence AAI03761.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processGlycolysis
   LigandSchiff base
   Molecular functionLyase
   PTMAcetylation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processaging

Inferred from electronic annotation. Source: Ensembl

apoptotic process

Inferred from electronic annotation. Source: Ensembl

carbohydrate metabolic process

Traceable author statement. Source: Reactome

epithelial cell differentiation

Inferred from expression pattern PubMed 21492153. Source: UniProt

fructose 1,6-bisphosphate metabolic process

Inferred from direct assay Ref.14. Source: UniProtKB

fructose metabolic process

Traceable author statement Ref.1. Source: ProtInc

gluconeogenesis

Traceable author statement. Source: Reactome

glucose metabolic process

Traceable author statement. Source: Reactome

glycolysis

Traceable author statement. Source: Reactome

organ regeneration

Inferred from electronic annotation. Source: Ensembl

protein heterotetramerization

Inferred from electronic annotation. Source: Ensembl

protein homotetramerization

Inferred from electronic annotation. Source: Ensembl

response to hypoxia

Inferred from electronic annotation. Source: Ensembl

response to organic cyclic compound

Inferred from electronic annotation. Source: Ensembl

response to organonitrogen compound

Inferred from electronic annotation. Source: Ensembl

small molecule metabolic process

Traceable author statement. Source: Reactome

   Cellular_componentaxon

Inferred from electronic annotation. Source: Ensembl

cytoskeleton

Inferred by curator PubMed 9244396. Source: BHF-UCL

cytosol

Traceable author statement. Source: Reactome

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867PubMed 20458337. Source: UniProt

mitochondrion

Inferred from electronic annotation. Source: Ensembl

   Molecular_functioncytoskeletal protein binding

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

fructose-bisphosphate aldolase activity

Inferred from direct assay Ref.14. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 364363Fructose-bisphosphate aldolase C
PRO_0000216947

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 residue1111N6-acetyllysine Ref.12

Experimental info

Sequence conflict3111L → V in CAA30270. Ref.2

Secondary structure

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

Details...

Sequences

Sequence LengthMass (Da)Tools
P09972 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 506A570B3E507971

FASTA36439,456
        10         20         30         40         50         60 
MPHSYPALSA EQKKELSDIA LRIVAPGKGI LAADESVGSM AKRLSQIGVE NTEENRRLYR 

        70         80         90        100        110        120 
QVLFSADDRV KKCIGGVIFF HETLYQKDDN GVPFVRTIQD KGIVVGIKVD KGVVPLAGTD 

       130        140        150        160        170        180 
GETTTQGLDG LSERCAQYKK DGADFAKWRC VLKISERTPS ALAILENANV LARYASICQQ 

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

       250        260        270        280        290        300 
PIKYTPEEIA MATVTALRRT VPPAVPGVTF LSGGQSEEEA SFNLNAINRC PLPRPWALTF 

       310        320        330        340        350        360 
SYGRALQASA LNAWRGQRDN AGAATEEFIK RAEVNGLAAQ GKYEGSGEDG GAAAQSLYIA 


NHAY 

« Hide

References

« Hide 'large scale' references
[1]"The complete amino acid sequence of the human aldolase C isozyme derived from genomic clones."
Rottmann W.H., Deselms K.R., Niclas J., Camerato T., Holman P.S., Green C.J., Tolan D.R.
Biochimie 69:137-145(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"The complete nucleotide sequence of the gene coding for the human aldolase C."
Buono P., Paolella G., Mancini F.P., Izzo P., Salvatore F.
Nucleic Acids Res. 16:4733-4733(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Characterization of the transcription-initiation site and of the promoter region within the 5' flanking region of the human aldolase C gene."
Buono P., Mancini F.P., Izzo P., Salvatore F.
Eur. J. Biochem. 192:805-811(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]Yu W., Gibbs R.A.
Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain.
[5]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[6]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[7]"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].
Tissue: Cerebellum.
[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].
Tissue: Colon, Eye and Uterus.
[10]"Interaction between aldolase and vacuolar H+-ATPase: evidence for direct coupling of glycolysis to the ATP-hydrolyzing proton pump."
Lu M., Holliday L.S., Zhang L., Dunn W.A. Jr., Gluck S.L.
J. Biol. Chem. 276:30407-30413(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ATP6V1E1.
[11]"Phospholipase D2 directly interacts with aldolase via its PH domain."
Kim J.H., Lee S., Kim J.H., Lee T.G., Hirata M., Suh P.-G., Ryu S.H.
Biochemistry 41:3414-3421(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PLD2.
[12]"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: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-111, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"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].
[14]"Structure of human brain fructose 1,6-(bis)phosphate aldolase: linking isozyme structure with function."
Arakaki T.L., Pezza J.A., Cronin M.A., Hopkins C.E., Zimmer D.B., Tolan D.R., Allen K.N.
Protein Sci. 13:3077-3084(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) OF 1-364, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X05196 Genomic DNA. Translation: CAA28825.1.
X07292 Genomic DNA. Translation: CAA30270.1.
AF054987 mRNA. Translation: AAC09348.1.
BT007006 mRNA. Translation: AAP35652.1.
CR541862 mRNA. Translation: CAG46660.1.
CR541881 mRNA. Translation: CAG46679.1.
AK312281 mRNA. Translation: BAG35210.1.
CH471159 Genomic DNA. Translation: EAW51104.1.
BC003613 mRNA. Translation: AAH03613.3.
BC103760 mRNA. Translation: AAI03761.1. Different initiation.
BC065565 mRNA. Translation: AAH65565.2.
BC106925 mRNA. Translation: AAI06926.1.
BC106926 mRNA. Translation: AAI06927.1.
PIRADHUC. A25861.
RefSeqNP_005156.1. NM_005165.2.
XP_005258006.1. XM_005257949.1.
UniGeneHs.155247.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1XFBX-ray3.00A/B/C/D/E/F/G/H/I/J/K/L1-364[»]
ProteinModelPortalP09972.
SMRP09972. Positions 3-344.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid106731. 15 interactions.
IntActP09972. 4 interactions.
STRING9606.ENSP00000226253.

PTM databases

PhosphoSiteP09972.

Polymorphism databases

DMDM113613.

2D gel databases

UCD-2DPAGEP09972.

Proteomic databases

PaxDbP09972.
PRIDEP09972.

Protocols and materials databases

DNASU230.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000226253; ENSP00000226253; ENSG00000109107.
ENST00000395321; ENSP00000378731; ENSG00000109107.
GeneID230.
KEGGhsa:230.
UCSCuc002hbp.3. human.

Organism-specific databases

CTD230.
GeneCardsGC17M026900.
HGNCHGNC:418. ALDOC.
HPACAB020828.
HPA003282.
MIM103870. gene.
neXtProtNX_P09972.
PharmGKBPA24711.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG3588.
HOVERGENHBG002386.
InParanoidP09972.
KOK01623.
OMARGQQDNA.
PhylomeDBP09972.
TreeFamTF314203.

Enzyme and pathway databases

BioCycMetaCyc:HS03200-MONOMER.
ReactomeREACT_111217. Metabolism.
SABIO-RKP09972.
UniPathwayUPA00109; UER00183.

Gene expression databases

ArrayExpressP09972.
BgeeP09972.
CleanExHS_ALDOC.
GenevestigatorP09972.

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

ChiTaRSALDOC. human.
EvolutionaryTraceP09972.
GeneWikiAldolase_C.
GenomeRNAi230.
NextBio934.
PROP09972.
SOURCESearch...

Entry information

Entry nameALDOC_HUMAN
AccessionPrimary (citable) accession number: P09972
Secondary accession number(s): B2R5R3 expand/collapse secondary AC list , Q3SYL3, Q6FH94, Q6P0L5
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 149 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 chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM