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P09972

- ALDOC_HUMAN

UniProt

P09972 - ALDOC_HUMAN

Protein

Fructose-bisphosphate aldolase C

Gene

ALDOC

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 154 (01 Oct 2014)
      Sequence version 2 (23 Jan 2007)
      Previous versions | rss
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    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-phosphate1 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. 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

    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

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA24711.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 364363Fructose-bisphosphate aldolase CPRO_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. 5 interactions.
    STRINGi9606.ENSP00000226253.

    Structurei

    Secondary structure

    1
    364
    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.
    ModBaseiSearch...
    MobiDBiSearch...

    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.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti311 – 3111L → V in CAA30270. (PubMed:3267224)Curated

    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. 5 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

    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: October 1, 2014
    This is version 154 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