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Protein

Fructose-bisphosphate aldolase C

Gene

ALDOC

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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-phosphate1 Publication

    Pathway: glycolysis

    This protein is involved in step 4 of the subpathway that synthesizes D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose.
    Proteins known to be involved in the 4 steps of the subpathway in this organism are:
    1. no protein annotated in this organism
    2. Glucose-6-phosphate isomerase, Glucose-6-phosphate isomerase (GPI), Glucose-6-phosphate isomerase (GPI), Glucose-6-phosphate isomerase (GPI), Glucose-6-phosphate isomerase
    3. ATP-dependent 6-phosphofructokinase (PFKM), ATP-dependent 6-phosphofructokinase, liver type (PFKL), ATP-dependent 6-phosphofructokinase, muscle type (PFKM), ATP-dependent 6-phosphofructokinase, platelet type (PFKP)
    4. Fructose-bisphosphate aldolase, Fructose-bisphosphate aldolase, Fructose-bisphosphate aldolase (ALDOC), Fructose-bisphosphate aldolase (ALDOB), Fructose-bisphosphate aldolase (ALDOB), Fructose-bisphosphate aldolase, Fructose-bisphosphate aldolase, Fructose-bisphosphate aldolase, Fructose-bisphosphate aldolase, Fructose-bisphosphate aldolase, Fructose-bisphosphate aldolase, Fructose-bisphosphate aldolase, Fructose-bisphosphate aldolase (ALDOC), Fructose-bisphosphate aldolase, Fructose-bisphosphate aldolase, Fructose-bisphosphate aldolase (ALDOA), Fructose-bisphosphate aldolase (ALDOA), Fructose-bisphosphate aldolase C (ALDOC), Fructose-bisphosphate aldolase (HEL-S-87p), Fructose-bisphosphate aldolase, Fructose-bisphosphate aldolase, Fructose-bisphosphate aldolase (ALDOC), Fructose-bisphosphate aldolase (ALDOC), Fructose-bisphosphate aldolase, Fructose-bisphosphate aldolase, Fructose-bisphosphate aldolase, Fructose-bisphosphate aldolase, Fructose-bisphosphate aldolase (ALDOA), Fructose-bisphosphate aldolase (ALDOB), Fructose-bisphosphate aldolase (ALDOB), Fructose-bisphosphate aldolase (ALDOA), Fructose-bisphosphate aldolase (ALDOA), Fructose-bisphosphate aldolase, Fructose-bisphosphate aldolase (ALDOC), Fructose-bisphosphate aldolase (ALDOC), Fructose-bisphosphate aldolase (ALDOA), Fructose-bisphosphate aldolase (ALDOA), Fructose-bisphosphate aldolase (ALDOA), Fructose-bisphosphate aldolase B (ALDOB), Fructose-bisphosphate aldolase (ALDOA), Fructose-bisphosphate aldolase (ALDOA), Fructose-bisphosphate aldolase A (ALDOA), Fructose-bisphosphate aldolase, Fructose-bisphosphate aldolase, Fructose-bisphosphate aldolase (ALDOC), Fructose-bisphosphate aldolase (ALDOC), Fructose-bisphosphate aldolase (ALDOC)
    This subpathway is part of the pathway glycolysis, which is itself part of Carbohydrate degradation.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose, the pathway glycolysis and in Carbohydrate degradation.

    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

    • cytoskeletal protein binding Source: BHF-UCL
    • fructose-bisphosphate aldolase activity Source: UniProtKB

    GO - Biological processi

    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 Componenti: Chromosome 17

    Organism-specific databases

    HGNCiHGNC:418. ALDOC.

    Subcellular locationi

    GO - Cellular componenti

    • axon Source: Ensembl
    • cytoskeleton Source: BHF-UCL
    • cytosol Source: Reactome
    • extracellular exosome Source: UniProtKB
    • mitochondrion Source: Ensembl
    Complete GO annotation...

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA24711.

    Polymorphism and mutation databases

    BioMutaiALDOC.
    DMDMi113613.

    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 residuei13 – 131N6-succinyllysineBy similarity
    Modified residuei36 – 361Phosphoserine1 Publication
    Modified residuei39 – 391Phosphoserine1 Publication
    Modified residuei45 – 451Phosphoserine1 Publication
    Modified residuei111 – 1111N6-acetyllysine1 Publication
    Modified residuei119 – 1191PhosphothreonineBy similarity
    Modified residuei132 – 1321PhosphoserineBy similarity
    Modified residuei272 – 2721PhosphoserineBy similarity
    Modified residuei276 – 2761PhosphoserineBy similarity
    Modified residuei309 – 3091PhosphoserineBy similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP09972.
    PaxDbiP09972.
    PRIDEiP09972.

    2D gel databases

    UCD-2DPAGEP09972.

    PTM databases

    PhosphoSiteiP09972.

    Expressioni

    Gene expression databases

    BgeeiP09972.
    CleanExiHS_ALDOC.
    ExpressionAtlasiP09972. baseline and differential.
    GenevisibleiP09972. HS.

    Organism-specific databases

    HPAiCAB020828.
    HPA003282.

    Interactioni

    Subunit structurei

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

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ALDOAP04075-23EBI-2952751,EBI-10194102
    LNX1Q8TBB13EBI-2952751,EBI-739832

    Protein-protein interaction databases

    BioGridi106731. 19 interactions.
    IntActiP09972. 7 interactions.
    STRINGi9606.ENSP00000226253.

    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 – 459Combined sources
    Helixi53 – 6412Combined sources
    Helixi68 – 703Combined sources
    Turni71 – 733Combined sources
    Beta strandi74 – 796Combined sources
    Helixi82 – 854Combined 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
    Helixi161 – 17919Combined sources
    Turni180 – 1823Combined sources
    Beta strandi184 – 1918Combined sources
    Helixi199 – 21921Combined sources
    Helixi224 – 2263Combined sources
    Helixi246 – 25712Combined sources
    Turni258 – 2603Combined sources
    Beta strandi267 – 2715Combined sources
    Helixi277 – 28812Combined sources
    Beta strandi295 – 3039Combined sources
    Helixi304 – 31411Combined sources
    Helixi321 – 33818Combined sources
    Turni339 – 3413Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    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.
    GeneTreeiENSGT00390000010235.
    HOVERGENiHBG002386.
    InParanoidiP09972.
    KOiK01623.
    OMAiWRGQQDN.
    PhylomeDBiP09972.
    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]

    Sequencei

    Sequence statusi: Complete.

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

    P09972-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MPHSYPALSA EQKKELSDIA LRIVAPGKGI LAADESVGSM AKRLSQIGVE
    60 70 80 90 100
    NTEENRRLYR QVLFSADDRV KKCIGGVIFF HETLYQKDDN GVPFVRTIQD
    110 120 130 140 150
    KGIVVGIKVD KGVVPLAGTD GETTTQGLDG LSERCAQYKK DGADFAKWRC
    160 170 180 190 200
    VLKISERTPS ALAILENANV LARYASICQQ NGIVPIVEPE ILPDGDHDLK
    210 220 230 240 250
    RCQYVTEKVL AAVYKALSDH HVYLEGTLLK PNMVTPGHAC PIKYTPEEIA
    260 270 280 290 300
    MATVTALRRT VPPAVPGVTF LSGGQSEEEA SFNLNAINRC PLPRPWALTF
    310 320 330 340 350
    SYGRALQASA LNAWRGQRDN AGAATEEFIK RAEVNGLAAQ GKYEGSGEDG
    360
    GAAAQSLYIA NHAY
    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. Curated

    Experimental Info

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

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    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.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    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.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    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...

    Protein-protein interaction databases

    BioGridi106731. 19 interactions.
    IntActiP09972. 7 interactions.
    STRINGi9606.ENSP00000226253.

    PTM databases

    PhosphoSiteiP09972.

    Polymorphism and mutation databases

    BioMutaiALDOC.
    DMDMi113613.

    2D gel databases

    UCD-2DPAGEP09972.

    Proteomic databases

    MaxQBiP09972.
    PaxDbiP09972.
    PRIDEiP09972.

    Protocols and materials databases

    DNASUi230.
    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

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

    Organism-specific databases

    CTDi230.
    GeneCardsiGC17M026900.
    HGNCiHGNC:418. ALDOC.
    HPAiCAB020828.
    HPA003282.
    MIMi103870. gene.
    neXtProtiNX_P09972.
    PharmGKBiPA24711.
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiCOG3588.
    GeneTreeiENSGT00390000010235.
    HOVERGENiHBG002386.
    InParanoidiP09972.
    KOiK01623.
    OMAiWRGQQDN.
    PhylomeDBiP09972.
    TreeFamiTF314203.

    Enzyme and pathway databases

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

    Miscellaneous databases

    ChiTaRSiALDOC. human.
    EvolutionaryTraceiP09972.
    GeneWikiiAldolase_C.
    GenomeRNAii230.
    NextBioi934.
    PROiP09972.
    SOURCEiSearch...

    Gene expression databases

    BgeeiP09972.
    CleanExiHS_ALDOC.
    ExpressionAtlasiP09972. baseline and differential.
    GenevisibleiP09972. HS.

    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]
    ProtoNetiSearch...

    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. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
      Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
      J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36; SER-39 AND SER-45, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    15. "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: June 24, 2015
    This is version 162 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

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.