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P10768 (ESTD_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 143. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
S-formylglutathione hydrolase

Short name=FGH
EC=3.1.2.12
Alternative name(s):
Esterase D
Methylumbelliferyl-acetate deacetylase
EC=3.1.1.56
Gene names
Name:ESD
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length282 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Serine hydrolase involved in the detoxification of formaldehyde. Ref.10 Ref.11

Catalytic activity

S-formylglutathione + H2O = glutathione + formate. Ref.10

4-methylumbelliferyl acetate + H2O = 4-methylumbelliferone + acetate. Ref.10

Subunit structure

Homodimer.

Subcellular location

Cytoplasm. Cytoplasmic vesicle.

Polymorphism

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

Sequence similarities

Belongs to the esterase D family.

Sequence caution

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 282281S-formylglutathione hydrolase
PRO_0000210339

Sites

Active site1491Charge relay system Ref.14
Active site2261Charge relay system Ref.14
Active site2601Charge relay system Ref.14

Amino acid modifications

Modified residue21N-acetylalanine By similarity
Modified residue41N6-succinyllysine By similarity
Modified residue2001N6-acetyllysine Ref.12

Natural variations

Natural variant1901G → E in allele ESD*2. Ref.15 Ref.16
Corresponds to variant rs9778 [ dbSNP | Ensembl ].
VAR_005202
Natural variant2571G → D. Ref.4 Ref.6
Corresponds to variant rs15303 [ dbSNP | Ensembl ].
VAR_022275

Experimental info

Mutagenesis541L → A: 83% of wild-type activity. Ref.14
Mutagenesis1491S → A: Loss of activity. Ref.14
Mutagenesis1491S → T: 1.3% of wild-type activity. Ref.14
Mutagenesis1501M → A: 62% increase in activity. Ref.14
Mutagenesis2261D → A: 4.3% of wild-type activity. Ref.14
Mutagenesis2261D → N: 9% of wild-type activity. Ref.14
Mutagenesis2601H → A: 3% of wild-type activity. Ref.14
Mutagenesis2601H → Q: 1.3% of wild-type activity. Ref.14

Secondary structure

................................................ 282
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P10768 [UniParc].

Last modified June 1, 1994. Version 2.
Checksum: BFC20D5FA2BB0DCE

FASTA28231,463
        10         20         30         40         50         60 
MALKQISSNK CFGGLQKVFE HDSVELNCKM KFAVYLPPKA ETGKCPALYW LSGLTCTEQN 

        70         80         90        100        110        120 
FISKSGYHQS ASEHGLVVIA PDTSPRGCNI KGEDESWDFG TGAGFYVDAT EDPWKTNYRM 

       130        140        150        160        170        180 
YSYVTEELPQ LINANFPVDP QRMSIFGHSM GGHGALICAL KNPGKYKSVS AFAPICNPVL 

       190        200        210        220        230        240 
CPWGKKAFSG YLGTDQSKWK AYDATHLVKS YPGSQLDILI DQGKDDQFLL DGQLLPDNFI 

       250        260        270        280 
AACTEKKIPV VFRLQEGYDH SYYFIATFIT DHIRHHAKYL NA 

« Hide

References

« Hide 'large scale' references
[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]"Gene expression profiling in the human hypothalamus-pituitary-adrenal axis and full-length cDNA cloning."
Hu R.-M., Han Z.-G., Song H.-D., Peng Y.-D., Huang Q.-H., Ren S.-X., Gu Y.-J., Huang C.-H., Li Y.-B., Jiang C.-L., Fu G., Zhang Q.-H., Gu B.-W., Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M. expand/collapse author list , Zhou J., Xu S.-H., Gu J., Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M., Huang G.-Y., Chen Z., Chen M.-D., Chen J.-L.
Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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]"Esterase D: a new human polymorphism."
Hopkinson D.A., Mestriner M.A., Cortner J., Harris H.
Ann. Hum. Genet. 37:119-137(1973) [PubMed] [Europe PMC] [Abstract]
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS9404.1.
PIRA23543.
RefSeqNP_001975.1. NM_001984.1.
XP_005266335.1. XM_005266278.1.
UniGeneHs.432491.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3FCXX-ray1.50A/B1-282[»]
ProteinModelPortalP10768.
SMRP10768. Positions 3-281.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108402. 6 interactions.
IntActP10768. 4 interactions.
MINTMINT-5002423.
STRING9606.ENSP00000367992.

Chemistry

ChEMBLCHEMBL2189130.
DrugBankDB00143. Glutathione.

Protein family/group databases

MEROPSS09.990.

PTM databases

PhosphoSiteP10768.

Polymorphism databases

DMDM544254.

2D gel databases

DOSAC-COBS-2DPAGEP10768.
OGPP10768.
REPRODUCTION-2DPAGEIPI00411706.
UCD-2DPAGEP10768.

Proteomic databases

MaxQBP10768.
PaxDbP10768.
PeptideAtlasP10768.
PRIDEP10768.

Protocols and materials databases

DNASU2098.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000378720; ENSP00000367992; ENSG00000139684.
GeneID2098.
KEGGhsa:2098.
UCSCuc001vbn.3. human.

Organism-specific databases

CTD2098.
GeneCardsGC13M047345.
HGNCHGNC:3465. ESD.
HPAHPA039700.
HPA052854.
MIM133280. gene.
neXtProtNX_P10768.
PharmGKBPA27882.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0627.
HOGENOMHOG000263929.
HOVERGENHBG001326.
InParanoidP10768.
KOK01070.
OMAWAHNAQT.
OrthoDBEOG7TF79G.
PhylomeDBP10768.
TreeFamTF300793.

Enzyme and pathway databases

BioCycRETL1328306-WGS:GSTH-4746-MONOMER.

Gene expression databases

BgeeP10768.
CleanExHS_ESD.
GenevestigatorP10768.

Family and domain databases

Gene3D3.40.50.1820. 1 hit.
InterProIPR029058. AB_hydrolase.
IPR000801. Esterase_put.
IPR014186. S-formylglutathione_hydrol.
[Graphical view]
PANTHERPTHR10061. PTHR10061. 1 hit.
PfamPF00756. Esterase. 1 hit.
[Graphical view]
SUPFAMSSF53474. SSF53474. 1 hit.
TIGRFAMsTIGR02821. fghA_ester_D. 1 hit.
ProtoNetSearch...

Other

ChiTaRSESD. human.
EvolutionaryTraceP10768.
GeneWikiESD_(gene).
GenomeRNAi2098.
NextBio8487.
PROP10768.
SOURCESearch...

Entry information

Entry nameESTD_HUMAN
AccessionPrimary (citable) accession number: P10768
Secondary accession number(s): Q5TBU8 expand/collapse secondary AC list , Q5TBV0, Q5TBV2, Q9BVJ2
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: June 1, 1994
Last modified: July 9, 2014
This is version 143 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 13

Human chromosome 13: entries, gene names and cross-references to MIM