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Protein

S-formylglutathione hydrolase

Gene

ESD

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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

GO - Biological processi

Complete GO annotation...

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 Componenti: Chromosome 13

Organism-specific databases

HGNCiHGNC:3465. ESD.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

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.

Chemistry

DrugBankiDB00143. Glutathione.

Polymorphism and mutation databases

BioMutaiESD.
DMDMi544254.

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.
ExpressionAtlasiP10768. baseline and differential.
GenevestigatoriP10768.

Organism-specific databases

HPAiHPA039700.
HPA052854.

Interactioni

Subunit structurei

Homodimer.

Binary interactionsi

WithEntry#Exp.IntActNotes
FSD2A1L4K13EBI-1052334,EBI-5661036

Protein-protein interaction databases

BioGridi108402. 9 interactions.
IntActiP10768. 7 interactions.
MINTiMINT-5002423.
STRINGi9606.ENSP00000367992.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00390000011864.
HOGENOMiHOG000263929.
HOVERGENiHBG001326.
InParanoidiP10768.
KOiK01070.
OMAiCTHANVT.
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

        10         20         30         40         50
MALKQISSNK CFGGLQKVFE HDSVELNCKM KFAVYLPPKA ETGKCPALYW
60 70 80 90 100
LSGLTCTEQN FISKSGYHQS ASEHGLVVIA PDTSPRGCNI KGEDESWDFG
110 120 130 140 150
TGAGFYVDAT EDPWKTNYRM YSYVTEELPQ LINANFPVDP QRMSIFGHSM
160 170 180 190 200
GGHGALICAL KNPGKYKSVS AFAPICNPVL CPWGKKAFSG YLGTDQSKWK
210 220 230 240 250
AYDATHLVKS YPGSQLDILI DQGKDDQFLL DGQLLPDNFI AACTEKKIPV
260 270 280
VFRLQEGYDH SYYFIATFIT DHIRHHAKYL NA
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. Curated
The sequence CAI12226.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

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:
EMBLi
GenBanki
DDBJi
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.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

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

Protein-protein interaction databases

BioGridi108402. 9 interactions.
IntActiP10768. 7 interactions.
MINTiMINT-5002423.
STRINGi9606.ENSP00000367992.

Chemistry

ChEMBLiCHEMBL2189130.
DrugBankiDB00143. Glutathione.

Protein family/group databases

MEROPSiS09.990.

PTM databases

PhosphoSiteiP10768.

Polymorphism and mutation databases

BioMutaiESD.
DMDMi544254.

2D gel databases

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

Proteomic databases

MaxQBiP10768.
PaxDbiP10768.
PeptideAtlasiP10768.
PRIDEiP10768.

Protocols and materials databases

DNASUi2098.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi2098.
GeneCardsiGC13M047345.
HGNCiHGNC:3465. ESD.
HPAiHPA039700.
HPA052854.
MIMi133280. gene.
neXtProtiNX_P10768.
PharmGKBiPA27882.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0627.
GeneTreeiENSGT00390000011864.
HOGENOMiHOG000263929.
HOVERGENiHBG001326.
InParanoidiP10768.
KOiK01070.
OMAiCTHANVT.
OrthoDBiEOG7TF79G.
PhylomeDBiP10768.
TreeFamiTF300793.

Enzyme and pathway databases

BioCyciRETL1328306-WGS:GSTH-4746-MONOMER.

Miscellaneous databases

ChiTaRSiESD. human.
EvolutionaryTraceiP10768.
GeneWikiiESD_(gene).
GenomeRNAii2098.
NextBioi8487.
PROiP10768.
SOURCEiSearch...

Gene expression databases

BgeeiP10768.
CleanExiHS_ESD.
ExpressionAtlasiP10768. baseline and differential.
GenevestigatoriP10768.

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.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  15. "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.
  16. "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.
  17. "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: May 27, 2015
This is version 152 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

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.