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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)DescriptionActionsGraphical viewLength
Active sitei149Charge relay system1 Publication1
Active sitei226Charge relay system1 Publication1
Active sitei260Charge relay system1 Publication1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Serine esterase

Enzyme and pathway databases

BioCyciZFISH:G66-33951-MONOMER.
ReactomeiR-HSA-156590. Glutathione conjugation.

Protein family/group databases

ESTHERihuman-ESD. A85-EsteraseD-FGH.
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
Proteomesi
  • UP000005640 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)DescriptionActionsGraphical viewLength
Mutagenesisi54L → A: 83% of wild-type activity. 1 Publication1
Mutagenesisi149S → A: Loss of activity. 1 Publication1
Mutagenesisi149S → T: 1.3% of wild-type activity. 1 Publication1
Mutagenesisi150M → A: 62% increase in activity. 1 Publication1
Mutagenesisi226D → A: 4.3% of wild-type activity. 1 Publication1
Mutagenesisi226D → N: 9% of wild-type activity. 1 Publication1
Mutagenesisi260H → A: 3% of wild-type activity. 1 Publication1
Mutagenesisi260H → Q: 1.3% of wild-type activity. 1 Publication1

Organism-specific databases

DisGeNETi2098.
OpenTargetsiENSG00000139684.
PharmGKBiPA27882.

Chemistry databases

ChEMBLiCHEMBL2189130.
DrugBankiDB00143. Glutathione.

Polymorphism and mutation databases

BioMutaiESD.
DMDMi544254.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00002103392 – 282S-formylglutathione hydrolaseAdd BLAST281

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineBy similarity1
Modified residuei4N6-succinyllysineBy similarity1
Modified residuei200N6-acetyllysineCombined sources1

Keywords - PTMi

Acetylation

Proteomic databases

EPDiP10768.
MaxQBiP10768.
PaxDbiP10768.
PeptideAtlasiP10768.
PRIDEiP10768.
TopDownProteomicsiP10768.

2D gel databases

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

PTM databases

iPTMnetiP10768.
PhosphoSitePlusiP10768.
SwissPalmiP10768.

Expressioni

Gene expression databases

BgeeiENSG00000139684.
CleanExiHS_ESD.
ExpressionAtlasiP10768. baseline and differential.
GenevisibleiP10768. HS.

Organism-specific databases

HPAiHPA039700.

Interactioni

Subunit structurei

Homodimer.

Binary interactionsi

WithEntry#Exp.IntActNotes
itself3EBI-1052334,EBI-1052334
FSD2A1L4K15EBI-1052334,EBI-5661036

Protein-protein interaction databases

BioGridi108402. 31 interactors.
IntActiP10768. 8 interactors.
MINTiMINT-5002423.
STRINGi9606.ENSP00000367992.

Structurei

Secondary structure

1282
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi4 – 11Combined sources8
Beta strandi14 – 23Combined sources10
Turni24 – 27Combined sources4
Beta strandi28 – 36Combined sources9
Helixi38 – 41Combined sources4
Beta strandi45 – 51Combined sources7
Helixi59 – 64Combined sources6
Helixi68 – 74Combined sources7
Beta strandi77 – 81Combined sources5
Beta strandi93 – 95Combined sources3
Helixi114 – 117Combined sources4
Helixi120 – 125Combined sources6
Helixi127 – 135Combined sources9
Beta strandi136 – 148Combined sources13
Helixi150 – 160Combined sources11
Turni163 – 165Combined sources3
Beta strandi169 – 173Combined sources5
Helixi178 – 180Combined sources3
Helixi182 – 192Combined sources11
Helixi199 – 202Combined sources4
Helixi204 – 208Combined sources5
Beta strandi218 – 223Combined sources6
Helixi227 – 230Combined sources4
Helixi236 – 245Combined sources10
Beta strandi250 – 255Combined sources6
Helixi262 – 279Combined sources18

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP10768.

Family & Domainsi

Sequence similaritiesi

Belongs to the esterase D family.Curated

Phylogenomic databases

eggNOGiKOG3101. Eukaryota.
COG0627. LUCA.
GeneTreeiENSGT00390000011864.
HOGENOMiHOG000263929.
HOVERGENiHBG001326.
InParanoidiP10768.
KOiK01070.
OMAiHIKHHAK.
OrthoDBiEOG091G0FIA.
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 differs from that shown. Reason: Erroneous gene model prediction.Curated
The sequence CAI12226 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 (PubMed:12721789, PubMed:7907313).2 Publications

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_005202190G → E in allele ESD*2. 2 PublicationsCorresponds to variant rs9778dbSNPEnsembl.1
Natural variantiVAR_022275257G → D.2 PublicationsCorresponds to variant rs15303dbSNPEnsembl.1

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_005266278.2.
XP_011533256.1. XM_011534954.1.
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_005266278.2.
XP_011533256.1. XM_011534954.1.
UniGeneiHs.432491.

3D structure databases

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

Protein-protein interaction databases

BioGridi108402. 31 interactors.
IntActiP10768. 8 interactors.
MINTiMINT-5002423.
STRINGi9606.ENSP00000367992.

Chemistry databases

ChEMBLiCHEMBL2189130.
DrugBankiDB00143. Glutathione.

Protein family/group databases

ESTHERihuman-ESD. A85-EsteraseD-FGH.
MEROPSiS09.990.

PTM databases

iPTMnetiP10768.
PhosphoSitePlusiP10768.
SwissPalmiP10768.

Polymorphism and mutation databases

BioMutaiESD.
DMDMi544254.

2D gel databases

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

Proteomic databases

EPDiP10768.
MaxQBiP10768.
PaxDbiP10768.
PeptideAtlasiP10768.
PRIDEiP10768.
TopDownProteomicsiP10768.

Protocols and materials databases

DNASUi2098.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi2098.
DisGeNETi2098.
GeneCardsiESD.
HGNCiHGNC:3465. ESD.
HPAiHPA039700.
MIMi133280. gene.
neXtProtiNX_P10768.
OpenTargetsiENSG00000139684.
PharmGKBiPA27882.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3101. Eukaryota.
COG0627. LUCA.
GeneTreeiENSGT00390000011864.
HOGENOMiHOG000263929.
HOVERGENiHBG001326.
InParanoidiP10768.
KOiK01070.
OMAiHIKHHAK.
OrthoDBiEOG091G0FIA.
PhylomeDBiP10768.
TreeFamiTF300793.

Enzyme and pathway databases

BioCyciZFISH:G66-33951-MONOMER.
ReactomeiR-HSA-156590. Glutathione conjugation.

Miscellaneous databases

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

Gene expression databases

BgeeiENSG00000139684.
CleanExiHS_ESD.
ExpressionAtlasiP10768. baseline and differential.
GenevisibleiP10768. HS.

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...

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: November 30, 2016
This is version 168 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

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 one 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.