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P37837

- TALDO_HUMAN

UniProt

P37837 - TALDO_HUMAN

Protein

Transaldolase

Gene

TALDO1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 160 (01 Oct 2014)
      Sequence version 2 (30 May 2000)
      Previous versions | rss
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    Functioni

    Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway.

    Catalytic activityi

    Sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate = D-erythrose 4-phosphate + D-fructose 6-phosphate.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei142 – 1421Schiff-base intermediate with substrate1 Publication

    GO - Molecular functioni

    1. monosaccharide binding Source: Ensembl
    2. sedoheptulose-7-phosphate:D-glyceraldehyde-3-phosphate glyceronetransferase activity Source: ProtInc

    GO - Biological processi

    1. carbohydrate metabolic process Source: Reactome
    2. energy reserve metabolic process Source: Reactome
    3. fructose 6-phosphate metabolic process Source: Ensembl
    4. glyceraldehyde-3-phosphate metabolic process Source: Ensembl
    5. pentose-phosphate shunt Source: Reactome
    6. pentose-phosphate shunt, non-oxidative branch Source: Ensembl
    7. small molecule metabolic process Source: Reactome
    8. xylulose biosynthetic process Source: Reactome

    Keywords - Molecular functioni

    Transferase

    Keywords - Biological processi

    Pentose shunt

    Keywords - Ligandi

    Schiff base

    Enzyme and pathway databases

    ReactomeiREACT_1859. Pentose phosphate pathway (hexose monophosphate shunt).
    REACT_939. Insulin effects increased synthesis of Xylulose-5-Phosphate.
    UniPathwayiUPA00115; UER00414.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Transaldolase (EC:2.2.1.2)
    Gene namesi
    Name:TALDO1
    Synonyms:TAL, TALDO, TALDOR
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 11

    Organism-specific databases

    HGNCiHGNC:11559. TALDO1.

    Subcellular locationi

    Cytoplasm Curated

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. cytosol Source: Reactome
    3. extracellular vesicular exosome Source: UniProt
    4. nucleus Source: UniProt

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Involvement in diseasei

    Transaldolase 1 deficiency (TALDO1 deficiency) [MIM:606003]: Results in telangiectases of the skin, hepatosplenomegaly, and enlarged clitoris.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti171 – 1711Missing in TALDO1 deficiency. 1 Publication
    VAR_011511

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi606003. phenotype.
    Orphaneti101028. Transaldolase deficiency.
    PharmGKBiPA36328.

    Protein family/group databases

    Allergomei9551. Hom s Transaldolase.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 337337TransaldolasePRO_0000173564Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei115 – 1151N6-acetyllysineBy similarity
    Modified residuei219 – 2191N6-acetyllysine1 Publication
    Modified residuei269 – 2691N6-acetyllysine1 Publication
    Modified residuei286 – 2861N6-acetyllysine1 Publication
    Modified residuei321 – 3211N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiP37837.
    PaxDbiP37837.
    PeptideAtlasiP37837.
    PRIDEiP37837.

    2D gel databases

    OGPiP37837.
    REPRODUCTION-2DPAGEIPI00744692.

    PTM databases

    PhosphoSiteiP37837.

    Expressioni

    Gene expression databases

    ArrayExpressiP37837.
    BgeeiP37837.
    CleanExiHS_TALDO1.
    GenevestigatoriP37837.

    Organism-specific databases

    HPAiHPA040373.
    HPA048089.

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Protein-protein interaction databases

    BioGridi112751. 27 interactions.
    IntActiP37837. 4 interactions.
    MINTiMINT-4999914.
    STRINGi9606.ENSP00000321259.

    Structurei

    Secondary structure

    1
    337
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi14 – 218
    Beta strandi22 – 276
    Turni31 – 344
    Helixi35 – 373
    Beta strandi40 – 434
    Helixi46 – 538
    Helixi56 – 583
    Helixi59 – 7214
    Helixi76 – 9823
    Beta strandi103 – 1064
    Helixi109 – 1113
    Helixi115 – 13117
    Helixi136 – 1383
    Beta strandi139 – 1446
    Helixi147 – 16014
    Beta strandi164 – 1696
    Helixi172 – 1809
    Beta strandi184 – 1907
    Helixi191 – 20010
    Helixi208 – 2103
    Helixi212 – 22615
    Beta strandi232 – 2365
    Helixi241 – 2455
    Turni246 – 2494
    Beta strandi250 – 2556
    Helixi257 – 2659
    Helixi276 – 2816
    Helixi291 – 2999
    Helixi302 – 33029

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1F05X-ray2.45A/B1-337[»]
    ProteinModelPortaliP37837.
    SMRiP37837. Positions 11-332.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP37837.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the transaldolase family. Type 1 subfamily.Curated

    Phylogenomic databases

    eggNOGiCOG0176.
    HOGENOMiHOG000281234.
    HOVERGENiHBG054014.
    InParanoidiP37837.
    KOiK00616.
    OMAiEAKFRWA.
    OrthoDBiEOG7MD4QF.
    PhylomeDBiP37837.
    TreeFamiTF300757.

    Family and domain databases

    Gene3Di3.20.20.70. 1 hit.
    HAMAPiMF_00492. Transaldolase_1.
    InterProiIPR013785. Aldolase_TIM.
    IPR001585. Transaldolase.
    IPR004730. Transaldolase_1.
    IPR018225. Transaldolase_AS.
    [Graphical view]
    PANTHERiPTHR10683. PTHR10683. 1 hit.
    PfamiPF00923. Transaldolase. 1 hit.
    [Graphical view]
    TIGRFAMsiTIGR00874. talAB. 1 hit.
    PROSITEiPS01054. TRANSALDOLASE_1. 1 hit.
    PS00958. TRANSALDOLASE_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P37837-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSSSPVKRQR MESALDQLKQ FTTVVADTGD FHAIDEYKPQ DATTNPSLIL    50
    AAAQMPAYQE LVEEAIAYGR KLGGSQEDQI KNAIDKLFVL FGAEILKKIP 100
    GRVSTEVDAR LSFDKDAMVA RARRLIELYK EAGISKDRIL IKLSSTWEGI 150
    QAGKELEEQH GIHCNMTLLF SFAQAVACAE AGVTLISPFV GRILDWHVAN 200
    TDKKSYEPLE DPGVKSVTKI YNYYKKFSYK TIVMGASFRN TGEIKALAGC 250
    DFLTISPKLL GELLQDNAKL VPVLSAKAAQ ASDLEKIHLD EKSFRWLHNE 300
    DQMAVEKLSD GIRKFAADAV KLERMLTERM FNAENGK 337
    Length:337
    Mass (Da):37,540
    Last modified:May 30, 2000 - v2
    Checksum:i8CB4992AEF364E64
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti171 – 1711Missing in TALDO1 deficiency. 1 Publication
    VAR_011511

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L19437 mRNA. Translation: AAB53943.1.
    AF010400, AF010398, AF010399 Genomic DNA. Translation: AAC52068.1.
    AF058913 Genomic DNA. Translation: AAF40478.1.
    AK313427 mRNA. Translation: BAG36219.1.
    BC010103 mRNA. Translation: AAH10103.1.
    BC018847 mRNA. Translation: AAH18847.2.
    L27346 Genomic DNA. Translation: AAL31313.1.
    CCDSiCCDS7712.1.
    PIRiA49985.
    RefSeqiNP_006746.1. NM_006755.1.
    UniGeneiHs.438678.

    Genome annotation databases

    EnsembliENST00000319006; ENSP00000321259; ENSG00000177156.
    GeneIDi6888.
    KEGGihsa:6888.
    UCSCiuc001lqz.3. human.

    Polymorphism databases

    DMDMi6648092.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L19437 mRNA. Translation: AAB53943.1 .
    AF010400 , AF010398 , AF010399 Genomic DNA. Translation: AAC52068.1 .
    AF058913 Genomic DNA. Translation: AAF40478.1 .
    AK313427 mRNA. Translation: BAG36219.1 .
    BC010103 mRNA. Translation: AAH10103.1 .
    BC018847 mRNA. Translation: AAH18847.2 .
    L27346 Genomic DNA. Translation: AAL31313.1 .
    CCDSi CCDS7712.1.
    PIRi A49985.
    RefSeqi NP_006746.1. NM_006755.1.
    UniGenei Hs.438678.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1F05 X-ray 2.45 A/B 1-337 [» ]
    ProteinModelPortali P37837.
    SMRi P37837. Positions 11-332.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112751. 27 interactions.
    IntActi P37837. 4 interactions.
    MINTi MINT-4999914.
    STRINGi 9606.ENSP00000321259.

    Protein family/group databases

    Allergomei 9551. Hom s Transaldolase.

    PTM databases

    PhosphoSitei P37837.

    Polymorphism databases

    DMDMi 6648092.

    2D gel databases

    OGPi P37837.
    REPRODUCTION-2DPAGE IPI00744692.

    Proteomic databases

    MaxQBi P37837.
    PaxDbi P37837.
    PeptideAtlasi P37837.
    PRIDEi P37837.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000319006 ; ENSP00000321259 ; ENSG00000177156 .
    GeneIDi 6888.
    KEGGi hsa:6888.
    UCSCi uc001lqz.3. human.

    Organism-specific databases

    CTDi 6888.
    GeneCardsi GC11P000737.
    HGNCi HGNC:11559. TALDO1.
    HPAi HPA040373.
    HPA048089.
    MIMi 602063. gene.
    606003. phenotype.
    neXtProti NX_P37837.
    Orphaneti 101028. Transaldolase deficiency.
    PharmGKBi PA36328.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0176.
    HOGENOMi HOG000281234.
    HOVERGENi HBG054014.
    InParanoidi P37837.
    KOi K00616.
    OMAi EAKFRWA.
    OrthoDBi EOG7MD4QF.
    PhylomeDBi P37837.
    TreeFami TF300757.

    Enzyme and pathway databases

    UniPathwayi UPA00115 ; UER00414 .
    Reactomei REACT_1859. Pentose phosphate pathway (hexose monophosphate shunt).
    REACT_939. Insulin effects increased synthesis of Xylulose-5-Phosphate.

    Miscellaneous databases

    ChiTaRSi TALDO1. human.
    EvolutionaryTracei P37837.
    GenomeRNAii 6888.
    NextBioi 26917.
    PROi P37837.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P37837.
    Bgeei P37837.
    CleanExi HS_TALDO1.
    Genevestigatori P37837.

    Family and domain databases

    Gene3Di 3.20.20.70. 1 hit.
    HAMAPi MF_00492. Transaldolase_1.
    InterProi IPR013785. Aldolase_TIM.
    IPR001585. Transaldolase.
    IPR004730. Transaldolase_1.
    IPR018225. Transaldolase_AS.
    [Graphical view ]
    PANTHERi PTHR10683. PTHR10683. 1 hit.
    Pfami PF00923. Transaldolase. 1 hit.
    [Graphical view ]
    TIGRFAMsi TIGR00874. talAB. 1 hit.
    PROSITEi PS01054. TRANSALDOLASE_1. 1 hit.
    PS00958. TRANSALDOLASE_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and expression of the human gene for transaldolase. A novel highly repetitive element constitutes an integral part of the coding sequence."
      Banki K., Halladay D.L., Perl A.
      J. Biol. Chem. 269:2847-2851(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "The human transaldolase gene (TALDO1) is located on chromosome 11 at p15.4-p15.5."
      Banki K., Eddy R.L., Shows T.B., Halladay D.L., Bullrich F., Croce C.M., Jurecic V., Baldini A., Perl A.
      Genomics 45:233-238(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: SEQUENCE REVISION.
    3. "Cloning and chromosomal localization of a paralog and a mouse homolog of the human transaldolase gene."
      Kusuda J., Hirai M., Toyoda A., Tanuma R., Nomura-Kitabayashi A., Hashimoto K.
      Gene 209:13-21(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    4. "Human transaldolase-associated repetitive elements are transcribed by RNA polymerase III."
      Perl A., Colombo E., Samoilova E., Butler M.C., Banki K.
      J. Biol. Chem. 275:7261-7272(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    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].
      Tissue: Cerebellum.
    6. "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: Lung and Ovary.
    7. "Family of active retrotransposons carry two exons of the transaldolase gene and shows evidence of reverse splicing in human DNA."
      Perl A.
      Submitted (NOV-2001) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 33-110.
    8. "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].
    9. "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-219; LYS-269; LYS-286 AND LYS-321, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. "The three-dimensional structure of human transaldolase."
      Thorell S., Gergely P. Jr., Banki K., Perl A., Schneider G.
      FEBS Lett. 475:205-208(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS), SUBUNIT, ACTIVE SITE.
    12. "Transaldolase deficiency: liver cirrhosis associated with a new inborn error in the pentose phosphate pathway."
      Verhoeven N.M., Huck J.H.J., Roos B., Struys E.A., Salomons G.S., Douwes A.C., van der Knaap M.S., Jakobs C.
      Am. J. Hum. Genet. 68:1086-1092(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT TALDO1 DEFICIENCY SER-171 DEL.

    Entry informationi

    Entry nameiTALDO_HUMAN
    AccessioniPrimary (citable) accession number: P37837
    Secondary accession number(s): B2R8M2
    , O00751, Q8WV32, Q8WZ45
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1994
    Last sequence update: May 30, 2000
    Last modified: October 1, 2014
    This is version 160 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

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 11
      Human chromosome 11: 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. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    4. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3