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P09972

- ALDOC_HUMAN

UniProt

P09972 - ALDOC_HUMAN

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Protein
Fructose-bisphosphate aldolase C
Gene
ALDOC, ALDC
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Kineticsi

  1. KM=10.7 µM for fructose 1,6-bisphosphate1 Publication
  2. KM=16 mM for fructose 1-phosphate

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei56 – 561Substrate
Binding sitei147 – 1471Substrate
Active sitei188 – 1881Proton acceptor By 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. cytoskeletal protein binding Source: BHF-UCL
  2. fructose-bisphosphate aldolase activity Source: UniProtKB
  3. protein binding Source: UniProtKB

GO - Biological processi

  1. aging Source: Ensembl
  2. apoptotic process Source: Ensembl
  3. carbohydrate metabolic process Source: Reactome
  4. epithelial cell differentiation Source: UniProt
  5. fructose 1,6-bisphosphate metabolic process Source: UniProtKB
  6. fructose metabolic process Source: ProtInc
  7. gluconeogenesis Source: Reactome
  8. glucose metabolic process Source: Reactome
  9. glycolytic process Source: Reactome
  10. organ regeneration Source: Ensembl
  11. protein heterotetramerization Source: Ensembl
  12. protein homotetramerization Source: Ensembl
  13. response to hypoxia Source: Ensembl
  14. response to organic cyclic compound Source: Ensembl
  15. response to organonitrogen compound Source: Ensembl
  16. small molecule metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Glycolysis

Keywords - Ligandi

Schiff base

Enzyme and pathway databases

BioCyciMetaCyc:HS03200-MONOMER.
ReactomeiREACT_1383. Glycolysis.
REACT_1520. Gluconeogenesis.
SABIO-RKP09972.
UniPathwayiUPA00109; UER00183.

Names & Taxonomyi

Protein namesi
Recommended name:
Fructose-bisphosphate aldolase C (EC:4.1.2.13)
Alternative name(s):
Brain-type aldolase
Gene namesi
Name:ALDOC
Synonyms:ALDC
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 17

Organism-specific databases

HGNCiHGNC:418. ALDOC.

Subcellular locationi

GO - Cellular componenti

  1. axon Source: Ensembl
  2. cytoskeleton Source: BHF-UCL
  3. cytosol Source: Reactome
  4. extracellular vesicular exosome Source: UniProt
  5. mitochondrion Source: Ensembl
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA24711.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed By similarity
Chaini2 – 364363Fructose-bisphosphate aldolase C
PRO_0000216947Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei111 – 1111N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP09972.
PaxDbiP09972.
PRIDEiP09972.

2D gel databases

UCD-2DPAGEP09972.

PTM databases

PhosphoSiteiP09972.

Expressioni

Gene expression databases

ArrayExpressiP09972.
BgeeiP09972.
CleanExiHS_ALDOC.
GenevestigatoriP09972.

Organism-specific databases

HPAiCAB020828.
HPA003282.

Interactioni

Subunit structurei

Homotetramer. Interacts with ATP6V1E1. May interact with PLD2.2 Publications

Protein-protein interaction databases

BioGridi106731. 15 interactions.
IntActiP09972. 4 interactions.
STRINGi9606.ENSP00000226253.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi10 – 2314
Beta strandi29 – 335
Helixi37 – 459
Helixi53 – 6412
Helixi68 – 703
Turni71 – 733
Beta strandi74 – 796
Helixi82 – 854
Helixi94 – 1007
Beta strandi104 – 1085
Beta strandi113 – 1153
Beta strandi119 – 1213
Beta strandi123 – 1253
Helixi131 – 14010
Beta strandi145 – 1528
Helixi161 – 17919
Turni180 – 1823
Beta strandi184 – 1918
Helixi199 – 21921
Helixi224 – 2263
Helixi246 – 25712
Turni258 – 2603
Beta strandi267 – 2715
Helixi277 – 28812
Beta strandi295 – 3039
Helixi304 – 31411
Helixi321 – 33818
Turni339 – 3413

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1XFBX-ray3.00A/B/C/D/E/F/G/H/I/J/K/L1-364[»]
ProteinModelPortaliP09972.
SMRiP09972. Positions 3-344.

Miscellaneous databases

EvolutionaryTraceiP09972.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG3588.
HOVERGENiHBG002386.
InParanoidiP09972.
KOiK01623.
OMAiRGQQDNA.
PhylomeDBiP09972.
TreeFamiTF314203.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR000741. FBA_I.
[Graphical view]
PfamiPF00274. Glycolytic. 1 hit.
[Graphical view]
PROSITEiPS00158. ALDOLASE_CLASS_I. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P09972-1 [UniParc]FASTAAdd to Basket

« Hide

MPHSYPALSA EQKKELSDIA LRIVAPGKGI LAADESVGSM AKRLSQIGVE    50
NTEENRRLYR QVLFSADDRV KKCIGGVIFF HETLYQKDDN GVPFVRTIQD 100
KGIVVGIKVD KGVVPLAGTD GETTTQGLDG LSERCAQYKK DGADFAKWRC 150
VLKISERTPS ALAILENANV LARYASICQQ NGIVPIVEPE ILPDGDHDLK 200
RCQYVTEKVL AAVYKALSDH HVYLEGTLLK PNMVTPGHAC PIKYTPEEIA 250
MATVTALRRT VPPAVPGVTF LSGGQSEEEA SFNLNAINRC PLPRPWALTF 300
SYGRALQASA LNAWRGQRDN AGAATEEFIK RAEVNGLAAQ GKYEGSGEDG 350
GAAAQSLYIA NHAY 364
Length:364
Mass (Da):39,456
Last modified:January 23, 2007 - v2
Checksum:i506A570B3E507971
GO

Sequence cautioni

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

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti311 – 3111L → V in CAA30270. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS11236.1.
PIRiA25861. ADHUC.
RefSeqiNP_005156.1. NM_005165.2.
XP_005258006.1. XM_005257949.1.
UniGeneiHs.155247.

Genome annotation databases

EnsembliENST00000226253; ENSP00000226253; ENSG00000109107.
ENST00000395321; ENSP00000378731; ENSG00000109107.
GeneIDi230.
KEGGihsa:230.
UCSCiuc002hbp.3. human.

Polymorphism databases

DMDMi113613.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS11236.1.
PIRi A25861. ADHUC.
RefSeqi NP_005156.1. NM_005165.2.
XP_005258006.1. XM_005257949.1.
UniGenei Hs.155247.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1XFB X-ray 3.00 A/B/C/D/E/F/G/H/I/J/K/L 1-364 [» ]
ProteinModelPortali P09972.
SMRi P09972. Positions 3-344.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 106731. 15 interactions.
IntActi P09972. 4 interactions.
STRINGi 9606.ENSP00000226253.

PTM databases

PhosphoSitei P09972.

Polymorphism databases

DMDMi 113613.

2D gel databases

UCD-2DPAGE P09972.

Proteomic databases

MaxQBi P09972.
PaxDbi P09972.
PRIDEi P09972.

Protocols and materials databases

DNASUi 230.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000226253 ; ENSP00000226253 ; ENSG00000109107 .
ENST00000395321 ; ENSP00000378731 ; ENSG00000109107 .
GeneIDi 230.
KEGGi hsa:230.
UCSCi uc002hbp.3. human.

Organism-specific databases

CTDi 230.
GeneCardsi GC17M026900.
HGNCi HGNC:418. ALDOC.
HPAi CAB020828.
HPA003282.
MIMi 103870. gene.
neXtProti NX_P09972.
PharmGKBi PA24711.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG3588.
HOVERGENi HBG002386.
InParanoidi P09972.
KOi K01623.
OMAi RGQQDNA.
PhylomeDBi P09972.
TreeFami TF314203.

Enzyme and pathway databases

UniPathwayi UPA00109 ; UER00183 .
BioCyci MetaCyc:HS03200-MONOMER.
Reactomei REACT_1383. Glycolysis.
REACT_1520. Gluconeogenesis.
SABIO-RK P09972.

Miscellaneous databases

ChiTaRSi ALDOC. human.
EvolutionaryTracei P09972.
GeneWikii Aldolase_C.
GenomeRNAii 230.
NextBioi 934.
PROi P09972.
SOURCEi Search...

Gene expression databases

ArrayExpressi P09972.
Bgeei P09972.
CleanExi HS_ALDOC.
Genevestigatori P09972.

Family and domain databases

Gene3Di 3.20.20.70. 1 hit.
InterProi IPR013785. Aldolase_TIM.
IPR000741. FBA_I.
[Graphical view ]
Pfami PF00274. Glycolytic. 1 hit.
[Graphical view ]
PROSITEi PS00158. ALDOLASE_CLASS_I. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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. 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.

Entry informationi

Entry nameiALDOC_HUMAN
AccessioniPrimary (citable) accession number: P09972
Secondary accession number(s): B2R5R3
, Q3SYL3, Q6FH94, Q6P0L5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: January 23, 2007
Last modified: September 3, 2014
This is version 153 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, Reference proteome

Documents

  1. Human chromosome 17
    Human chromosome 17: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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