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P10768

- ESTD_HUMAN

UniProt

P10768 - ESTD_HUMAN

Protein

S-formylglutathione hydrolase

Gene

ESD

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 145 (01 Oct 2014)
      Sequence version 2 (01 Jun 1994)
      Previous versions | rss
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    Functioni

    Serine hydrolase involved in the detoxification of formaldehyde.2 Publications

    Catalytic activityi

    S-formylglutathione + H2O = glutathione + formate.1 Publication
    4-methylumbelliferyl acetate + H2O = 4-methylumbelliferone + acetate.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei149 – 1491Charge relay system1 Publication
    Active sitei226 – 2261Charge relay system1 Publication
    Active sitei260 – 2601Charge relay system1 Publication

    GO - Molecular functioni

    1. carboxylic ester hydrolase activity Source: UniProtKB
    2. hydrolase activity, acting on ester bonds Source: UniProt
    3. methylumbelliferyl-acetate deacetylase activity Source: UniProtKB-EC
    4. S-formylglutathione hydrolase activity Source: UniProtKB-EC

    GO - Biological processi

    1. formaldehyde catabolic process Source: InterPro

    Keywords - Molecular functioni

    Hydrolase, Serine esterase

    Enzyme and pathway databases

    BioCyciRETL1328306-WGS:GSTH-4746-MONOMER.

    Protein family/group databases

    MEROPSiS09.990.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    S-formylglutathione hydrolase (EC:3.1.2.12)
    Short name:
    FGH
    Alternative name(s):
    Esterase D
    Methylumbelliferyl-acetate deacetylase (EC:3.1.1.56)
    Gene namesi
    Name:ESD
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 13

    Organism-specific databases

    HGNCiHGNC:3465. ESD.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    2. cytoplasmic membrane-bounded vesicle Source: UniProtKB-SubCell
    3. extracellular vesicular exosome Source: UniProt
    4. Golgi apparatus Source: HPA
    5. nucleus Source: HPA
    6. plasma membrane Source: HPA

    Keywords - Cellular componenti

    Cytoplasm, Cytoplasmic vesicle

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi54 – 541L → A: 83% of wild-type activity. 1 Publication
    Mutagenesisi149 – 1491S → A: Loss of activity. 1 Publication
    Mutagenesisi149 – 1491S → T: 1.3% of wild-type activity. 1 Publication
    Mutagenesisi150 – 1501M → A: 62% increase in activity. 1 Publication
    Mutagenesisi226 – 2261D → A: 4.3% of wild-type activity. 1 Publication
    Mutagenesisi226 – 2261D → N: 9% of wild-type activity. 1 Publication
    Mutagenesisi260 – 2601H → A: 3% of wild-type activity. 1 Publication
    Mutagenesisi260 – 2601H → Q: 1.3% of wild-type activity. 1 Publication

    Organism-specific databases

    PharmGKBiPA27882.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 282281S-formylglutathione hydrolasePRO_0000210339Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanineBy similarity
    Modified residuei4 – 41N6-succinyllysineBy similarity
    Modified residuei200 – 2001N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiP10768.
    PaxDbiP10768.
    PeptideAtlasiP10768.
    PRIDEiP10768.

    2D gel databases

    DOSAC-COBS-2DPAGEP10768.
    OGPiP10768.
    REPRODUCTION-2DPAGEIPI00411706.
    UCD-2DPAGEP10768.

    PTM databases

    PhosphoSiteiP10768.

    Expressioni

    Gene expression databases

    BgeeiP10768.
    CleanExiHS_ESD.
    GenevestigatoriP10768.

    Organism-specific databases

    HPAiHPA039700.
    HPA052854.

    Interactioni

    Subunit structurei

    Homodimer.

    Protein-protein interaction databases

    BioGridi108402. 6 interactions.
    IntActiP10768. 4 interactions.
    MINTiMINT-5002423.
    STRINGi9606.ENSP00000367992.

    Structurei

    Secondary structure

    1
    282
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi4 – 118
    Beta strandi14 – 2310
    Turni24 – 274
    Beta strandi28 – 369
    Helixi38 – 414
    Beta strandi45 – 517
    Helixi59 – 646
    Helixi68 – 747
    Beta strandi77 – 815
    Helixi114 – 1174
    Helixi120 – 1256
    Helixi127 – 1359
    Beta strandi136 – 14813
    Helixi150 – 16011
    Turni163 – 1653
    Beta strandi169 – 1735
    Helixi178 – 1803
    Helixi182 – 19211
    Helixi199 – 2024
    Helixi204 – 2085
    Beta strandi218 – 2236
    Helixi227 – 2304
    Helixi236 – 24510
    Beta strandi250 – 2556
    Helixi262 – 27918

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3FCXX-ray1.50A/B1-282[»]
    ProteinModelPortaliP10768.
    SMRiP10768. Positions 3-281.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP10768.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the esterase D family.Curated

    Phylogenomic databases

    eggNOGiCOG0627.
    HOGENOMiHOG000263929.
    HOVERGENiHBG001326.
    InParanoidiP10768.
    KOiK01070.
    OMAiWAHNAQT.
    OrthoDBiEOG7TF79G.
    PhylomeDBiP10768.
    TreeFamiTF300793.

    Family and domain databases

    Gene3Di3.40.50.1820. 1 hit.
    InterProiIPR029058. AB_hydrolase.
    IPR000801. Esterase_put.
    IPR014186. S-formylglutathione_hydrol.
    [Graphical view]
    PANTHERiPTHR10061. PTHR10061. 1 hit.
    PfamiPF00756. Esterase. 1 hit.
    [Graphical view]
    SUPFAMiSSF53474. SSF53474. 1 hit.
    TIGRFAMsiTIGR02821. fghA_ester_D. 1 hit.

    Sequencei

    Sequence statusi: Complete.

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

    P10768-1 [UniParc]FASTAAdd to Basket

    « Hide

    MALKQISSNK CFGGLQKVFE HDSVELNCKM KFAVYLPPKA ETGKCPALYW    50
    LSGLTCTEQN FISKSGYHQS ASEHGLVVIA PDTSPRGCNI KGEDESWDFG 100
    TGAGFYVDAT EDPWKTNYRM YSYVTEELPQ LINANFPVDP QRMSIFGHSM 150
    GGHGALICAL KNPGKYKSVS AFAPICNPVL CPWGKKAFSG YLGTDQSKWK 200
    AYDATHLVKS YPGSQLDILI DQGKDDQFLL DGQLLPDNFI AACTEKKIPV 250
    VFRLQEGYDH SYYFIATFIT DHIRHHAKYL NA 282
    Length:282
    Mass (Da):31,463
    Last modified:June 1, 1994 - v2
    Checksum:iBFC20D5FA2BB0DCE
    GO

    Sequence cautioni

    The sequence CAI12225.1 differs from that shown. Reason: Erroneous gene model prediction.
    The sequence CAI12226.1 differs from that shown. Reason: Erroneous gene model prediction.

    Polymorphismi

    There are two major electrophoretic isotypes. The sequence of the ESD*1 variant is shown.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti190 – 1901G → E in allele ESD*2. 2 Publications
    Corresponds to variant rs9778 [ dbSNP | Ensembl ].
    VAR_005202
    Natural varianti257 – 2571G → D.2 Publications
    Corresponds to variant rs15303 [ dbSNP | Ensembl ].
    VAR_022275

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M13450 mRNA. Translation: AAA52408.1. Sequence problems.
    AF112219 mRNA. Translation: AAC99788.1.
    BT007059 mRNA. Translation: AAP35708.1.
    AL136958 Genomic DNA. Translation: CAI12225.1. Sequence problems.
    AL136958 Genomic DNA. Translation: CAI12226.1. Sequence problems.
    AL136958 Genomic DNA. Translation: CAI12228.1.
    BC001169 mRNA. Translation: AAH01169.1.
    AF052509 Genomic DNA. Translation: AAC06298.1.
    CCDSiCCDS9404.1.
    PIRiA23543.
    RefSeqiNP_001975.1. NM_001984.1.
    XP_005266335.1. XM_005266278.1.
    UniGeneiHs.432491.

    Genome annotation databases

    EnsembliENST00000378720; ENSP00000367992; ENSG00000139684.
    GeneIDi2098.
    KEGGihsa:2098.
    UCSCiuc001vbn.3. human.

    Polymorphism databases

    DMDMi544254.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M13450 mRNA. Translation: AAA52408.1 . Sequence problems.
    AF112219 mRNA. Translation: AAC99788.1 .
    BT007059 mRNA. Translation: AAP35708.1 .
    AL136958 Genomic DNA. Translation: CAI12225.1 . Sequence problems.
    AL136958 Genomic DNA. Translation: CAI12226.1 . Sequence problems.
    AL136958 Genomic DNA. Translation: CAI12228.1 .
    BC001169 mRNA. Translation: AAH01169.1 .
    AF052509 Genomic DNA. Translation: AAC06298.1 .
    CCDSi CCDS9404.1.
    PIRi A23543.
    RefSeqi NP_001975.1. NM_001984.1.
    XP_005266335.1. XM_005266278.1.
    UniGenei Hs.432491.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3FCX X-ray 1.50 A/B 1-282 [» ]
    ProteinModelPortali P10768.
    SMRi P10768. Positions 3-281.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108402. 6 interactions.
    IntActi P10768. 4 interactions.
    MINTi MINT-5002423.
    STRINGi 9606.ENSP00000367992.

    Chemistry

    ChEMBLi CHEMBL2189130.
    DrugBanki DB00143. Glutathione.

    Protein family/group databases

    MEROPSi S09.990.

    PTM databases

    PhosphoSitei P10768.

    Polymorphism databases

    DMDMi 544254.

    2D gel databases

    DOSAC-COBS-2DPAGE P10768.
    OGPi P10768.
    REPRODUCTION-2DPAGE IPI00411706.
    UCD-2DPAGE P10768.

    Proteomic databases

    MaxQBi P10768.
    PaxDbi P10768.
    PeptideAtlasi P10768.
    PRIDEi P10768.

    Protocols and materials databases

    DNASUi 2098.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000378720 ; ENSP00000367992 ; ENSG00000139684 .
    GeneIDi 2098.
    KEGGi hsa:2098.
    UCSCi uc001vbn.3. human.

    Organism-specific databases

    CTDi 2098.
    GeneCardsi GC13M047345.
    HGNCi HGNC:3465. ESD.
    HPAi HPA039700.
    HPA052854.
    MIMi 133280. gene.
    neXtProti NX_P10768.
    PharmGKBi PA27882.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0627.
    HOGENOMi HOG000263929.
    HOVERGENi HBG001326.
    InParanoidi P10768.
    KOi K01070.
    OMAi WAHNAQT.
    OrthoDBi EOG7TF79G.
    PhylomeDBi P10768.
    TreeFami TF300793.

    Enzyme and pathway databases

    BioCyci RETL1328306-WGS:GSTH-4746-MONOMER.

    Miscellaneous databases

    ChiTaRSi ESD. human.
    EvolutionaryTracei P10768.
    GeneWikii ESD_(gene).
    GenomeRNAii 2098.
    NextBioi 8487.
    PROi P10768.
    SOURCEi Search...

    Gene expression databases

    Bgeei P10768.
    CleanExi HS_ESD.
    Genevestigatori P10768.

    Family and domain databases

    Gene3Di 3.40.50.1820. 1 hit.
    InterProi IPR029058. AB_hydrolase.
    IPR000801. Esterase_put.
    IPR014186. S-formylglutathione_hydrol.
    [Graphical view ]
    PANTHERi PTHR10061. PTHR10061. 1 hit.
    Pfami PF00756. Esterase. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53474. SSF53474. 1 hit.
    TIGRFAMsi TIGR02821. fghA_ester_D. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning of the human esterase D gene, a genetic marker of retinoblastoma."
      Lee E.Y.-H.P., Lee W.-H.
      Proc. Natl. Acad. Sci. U.S.A. 83:6337-6341(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: PRELIMINARY NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
    2. "Human esterase D gene: complete cDNA sequence, genomic structure, and application in the genetic diagnosis of human retinoblastoma."
      Young L.-J.S., Lee E.Y.-H.P., To H., Bookstein R., Shew J.-Y., Donoso L.A., Sery T., Giblin M., Shields J.A., Lee W.-H.
      Hum. Genet. 79:137-141(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Hypothalamus.
    4. "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], VARIANT ASP-257.
    5. "The DNA sequence and analysis of human chromosome 13."
      Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L., Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T.
      , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P., Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L., Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S., Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T.
      Nature 428:522-528(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    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], VARIANT ASP-257.
      Tissue: Muscle.
    7. Lubec G., Vishwanath V.
      Submitted (MAR-2007) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 65-86 AND 254-274, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Brain and Cajal-Retzius cell.
    8. "Cloning of the esterase D gene: a polymorphic gene probe closely linked to the retinoblastoma locus on chromosome 13."
      Squire J., Dryja T.P., Dunn J., Goddard A., Hofmann T., Musarella M., Willard H.F., Becker A.J., Gallie B.L., Phillips R.A.
      Proc. Natl. Acad. Sci. U.S.A. 83:6573-6577(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 150-186, PROTEIN SEQUENCE OF 150-175.
    9. Tuchhida S., Ikemoto S., Kajii E.
      Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 168-200.
    10. Cited for: FUNCTION AS METHYLUMBELLIFERYL-ACETATE DEACETYLASE, CATALYTIC ACTIVITY.
    11. "Identity of the polymorphisms for esterase D and S-formylglutathione hydrolase in red blood cells."
      Eiberg H., Mohr J.
      Hum. Genet. 74:174-175(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    12. "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-200, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. "Crystal structure of human esterase D: a potential genetic marker of retinoblastoma."
      Wu D., Li Y., Song G., Zhang D., Shaw N., Liu Z.-J.
      FASEB J. 23:1441-1446(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS), MUTAGENESIS OF LEU-54; SER-149; MET-150; ASP-226 AND HIS-260, ACTIVE SITE.
    15. "Molecular analysis of esterase D polymorphism."
      Tsuchida S., Fukui E., Ikemoto S.
      Hum. Genet. 93:255-258(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT GLU-190.
    16. "Catalog of 680 variations among eight cytochrome p450 (CYP) genes, nine esterase genes, and two other genes in the Japanese population."
      Saito S., Iida A., Sekine A., Kawauchi S., Higuchi S., Ogawa C., Nakamura Y.
      J. Hum. Genet. 48:249-270(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT GLU-190.

    Entry informationi

    Entry nameiESTD_HUMAN
    AccessioniPrimary (citable) accession number: P10768
    Secondary accession number(s): Q5TBU8
    , Q5TBV0, Q5TBV2, Q9BVJ2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1989
    Last sequence update: June 1, 1994
    Last modified: October 1, 2014
    This is version 145 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, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 13
      Human chromosome 13: 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. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    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