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P10768

- ESTD_HUMAN

UniProt

P10768 - ESTD_HUMAN

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Protein

S-formylglutathione hydrolase

Gene

ESD

Organism
Homo sapiens (Human)
Status
Reviewed - 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

  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
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: Chromosome 13

Organism-specific databases

HGNCiHGNC:3465. ESD.

Subcellular locationi

GO - Cellular componenti

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

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.

Protein-protein interaction databases

BioGridi108402. 7 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.
GeneTreeiENSGT00390000011864.
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

        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.
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. 7 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.
GeneTreei ENSGT00390000011864.
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.
ExpressionAtlasi P10768. baseline and differential.
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

« 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. "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 29, 2014
This is version 146 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