Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Prostaglandin E synthase 2

Gene

PTGES2

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

Functioni

Isomerase that catalyzes the conversion of PGH2 into the more stable prostaglandin E2 (PGE2).2 Publications

Catalytic activityi

(5Z,13E)-(15S)-9-alpha,11-alpha-epidioxy-15-hydroxyprosta-5,13-dienoate = (5Z,13E)-(15S)-11-alpha,15-dihydroxy-9-oxoprosta-5,13-dienoate.2 Publications

Enzyme regulationi

Isomerase activity is increased by sulfhydril compounds. Dithiothreitol (DTT) is most effective, followed by dihydrolipoic acid, glutathione (GSH) and 2-mercaptoethanol.1 Publication

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei87 – 882CleavageBy similarity
Binding sitei148 – 1481Glutathione; via amide nitrogen and carbonyl oxygenBy similarity

GO - Molecular functioni

  1. DNA binding Source: Ensembl
  2. electron carrier activity Source: InterPro
  3. glutathione binding Source: UniProtKB
  4. heme binding Source: UniProtKB
  5. lyase activity Source: UniProtKB
  6. prostaglandin-E synthase activity Source: UniProtKB-EC
  7. protein disulfide oxidoreductase activity Source: InterPro

GO - Biological processi

  1. cell redox homeostasis Source: InterPro
  2. positive regulation of transcription, DNA-templated Source: Ensembl
  3. prostaglandin biosynthetic process Source: UniProtKB-UniPathway
  4. secretion Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Biological processi

Fatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism, Prostaglandin biosynthesis, Prostaglandin metabolism

Enzyme and pathway databases

BioCyciMetaCyc:HS07514-MONOMER.
BRENDAi5.3.99.3. 2681.
UniPathwayiUPA00662.

Names & Taxonomyi

Protein namesi
Recommended name:
Prostaglandin E synthase 2
Alternative name(s):
Membrane-associated prostaglandin E synthase-21 Publication
Short name:
mPGE synthase-21 Publication
Microsomal prostaglandin E synthase 2
Short name:
mPGES-2
Prostaglandin-H(2) E-isomerase (EC:5.3.99.32 Publications)
Cleaved into the following chain:
Gene namesi
Name:PTGES2
Synonyms:C9orf15, PGES2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 9

Organism-specific databases

HGNCiHGNC:17822. PTGES2.

Subcellular locationi

  1. Golgi apparatus membrane 1 Publication; Single-pass membrane protein 1 Publication
Chain Prostaglandin E synthase 2 truncated form :
  1. Cytoplasmperinuclear region

  2. Note: Synthesized as a Golgi membrane-bound protein, which is further cleaved into the predominant soluble truncated form. The truncated form is cytoplasmic and is enriched in the perinuclear region.

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 5757LumenalSequence AnalysisAdd
BLAST
Transmembranei58 – 7417HelicalSequence AnalysisAdd
BLAST
Topological domaini75 – 377303CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. cytosol Source: Ensembl
  2. Golgi membrane Source: UniProtKB-SubCell
  3. integral component of membrane Source: UniProtKB-KW
  4. mitochondrion Source: UniProtKB
  5. nucleus Source: Ensembl
  6. perinuclear region of cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Golgi apparatus, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi110 – 1101C → S: Loss of function. 1 Publication
Mutagenesisi113 – 1131C → S: Slightly decreased enzyme activity. 1 Publication

Organism-specific databases

PharmGKBiPA33949.

Polymorphism and mutation databases

BioMutaiPTGES2.
DMDMi73921741.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 377377Prostaglandin E synthase 2PRO_0000013127Add
BLAST
Chaini88 – 377290Prostaglandin E synthase 2 truncated formBy similarityPRO_0000013128Add
BLAST

Proteomic databases

MaxQBiQ9H7Z7.
PaxDbiQ9H7Z7.
PRIDEiQ9H7Z7.

PTM databases

PhosphoSiteiQ9H7Z7.

Expressioni

Tissue specificityi

Widely expressed. Expressed in the heart, including apex, inter-ventricular septum, both atria and ventricles, but not in the aorta. Also expressed in fetal heart. Detected in various regions of the brain: cerebellum; occipital, frontal and parietal lobes. Also expressed in the lymph nodes, skeletal muscle, kidney and trachea, but not in the thymus or lung. Overexpressed in colorectal cancer.1 Publication

Gene expression databases

BgeeiQ9H7Z7.
CleanExiHS_PTGES2.
ExpressionAtlasiQ9H7Z7. baseline and differential.
GenevestigatoriQ9H7Z7.

Organism-specific databases

HPAiHPA020631.

Interactioni

Subunit structurei

Homodimer. May interact with CEBPB (By similarity). Interacts with EXOSC10.By similarity1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
C1orf189Q5VU693EBI-681645,EBI-10247920

Protein-protein interaction databases

BioGridi123135. 12 interactions.
IntActiQ9H7Z7. 7 interactions.
STRINGi9606.ENSP00000345341.

Structurei

3D structure databases

ProteinModelPortaliQ9H7Z7.
SMRiQ9H7Z7. Positions 100-373.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini90 – 193104GlutaredoxinPROSITE-ProRule annotationAdd
BLAST
Domaini263 – 377115GST C-terminalAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni164 – 1652Glutathione bindingBy similarity

Sequence similaritiesi

Belongs to the GST superfamily.Curated
Contains 1 glutaredoxin domain.PROSITE-ProRule annotation
Contains 1 GST C-terminal domain.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG316980.
GeneTreeiENSGT00390000000224.
HOGENOMiHOG000231901.
HOVERGENiHBG069136.
InParanoidiQ9H7Z7.
KOiK05309.
OMAiSTYRKVP.
OrthoDBiEOG7060R5.
PhylomeDBiQ9H7Z7.
TreeFamiTF314304.

Family and domain databases

Gene3Di1.20.1050.10. 2 hits.
3.40.30.10. 1 hit.
InterProiIPR002109. Glutaredoxin.
IPR010987. Glutathione-S-Trfase_C-like.
IPR004045. Glutathione_S-Trfase_N.
IPR004046. GST_C.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamiPF14497. GST_C_3. 1 hit.
PF13417. GST_N_3. 1 hit.
[Graphical view]
SUPFAMiSSF47616. SSF47616. 1 hit.
SSF52833. SSF52833. 1 hit.
PROSITEiPS00195. GLUTAREDOXIN_1. 1 hit.
PS51354. GLUTAREDOXIN_2. 1 hit.
PS50405. GST_CTER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q9H7Z7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDPAARVVRA LWPGGCALAW RLGGRPQPLL PTQSRAGFAG AAGGPSPVAA
60 70 80 90 100
ARKGSPRLLG AAALALGGAL GLYHTARWHL RAQDLHAERS AAQLSLSSRL
110 120 130 140 150
QLTLYQYKTC PFCSKVRAFL DFHALPYQVV EVNPVRRAEI KFSSYRKVPI
160 170 180 190 200
LVAQEGESSQ QLNDSSVIIS ALKTYLVSGQ PLEEIITYYP AMKAVNEQGK
210 220 230 240 250
EVTEFGNKYW LMLNEKEAQQ VYGGKEARTE EMKWRQWADD WLVHLISPNV
260 270 280 290 300
YRTPTEALAS FDYIVREGKF GAVEGAVAKY MGAAAMYLIS KRLKSRHRLQ
310 320 330 340 350
DNVREDLYEA ADKWVAAVGK DRPFMGGQKP NLADLAVYGV LRVMEGLDAF
360 370
DDLMQHTHIQ PWYLRVERAI TEASPAH
Length:377
Mass (Da):41,943
Last modified:March 1, 2001 - v1
Checksum:i82F2DF867BB8337C
GO

Sequence cautioni

The sequence CAI13822.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti319 – 3191G → S in BAD97240 (Ref. 2) Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti298 – 2981R → H.
Corresponds to variant rs13283456 [ dbSNP | Ensembl ].
VAR_049494

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK024100 mRNA. Translation: BAB14826.1.
AK223520 mRNA. Translation: BAD97240.1.
AL590708 Genomic DNA. Translation: CAI13821.1.
AL590708 Genomic DNA. Translation: CAI13822.1. Sequence problems.
BC009397 mRNA. Translation: AAH09397.2.
BC009456 mRNA. Translation: AAH09456.1.
BC011613 mRNA. Translation: AAH11613.1.
CCDSiCCDS6891.1.
RefSeqiNP_001243264.1. NM_001256335.1.
NP_079348.1. NM_025072.6.
NP_945176.1. NM_198938.2.
UniGeneiHs.495219.

Genome annotation databases

EnsembliENST00000338961; ENSP00000345341; ENSG00000148334.
GeneIDi80142.
KEGGihsa:80142.
UCSCiuc004bti.4. human.

Polymorphism and mutation databases

BioMutaiPTGES2.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK024100 mRNA. Translation: BAB14826.1.
AK223520 mRNA. Translation: BAD97240.1.
AL590708 Genomic DNA. Translation: CAI13821.1.
AL590708 Genomic DNA. Translation: CAI13822.1. Sequence problems.
BC009397 mRNA. Translation: AAH09397.2.
BC009456 mRNA. Translation: AAH09456.1.
BC011613 mRNA. Translation: AAH11613.1.
CCDSiCCDS6891.1.
RefSeqiNP_001243264.1. NM_001256335.1.
NP_079348.1. NM_025072.6.
NP_945176.1. NM_198938.2.
UniGeneiHs.495219.

3D structure databases

ProteinModelPortaliQ9H7Z7.
SMRiQ9H7Z7. Positions 100-373.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi123135. 12 interactions.
IntActiQ9H7Z7. 7 interactions.
STRINGi9606.ENSP00000345341.

Chemistry

BindingDBiQ9H7Z7.
ChEMBLiCHEMBL4411.

PTM databases

PhosphoSiteiQ9H7Z7.

Polymorphism and mutation databases

BioMutaiPTGES2.
DMDMi73921741.

Proteomic databases

MaxQBiQ9H7Z7.
PaxDbiQ9H7Z7.
PRIDEiQ9H7Z7.

Protocols and materials databases

DNASUi80142.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000338961; ENSP00000345341; ENSG00000148334.
GeneIDi80142.
KEGGihsa:80142.
UCSCiuc004bti.4. human.

Organism-specific databases

CTDi80142.
GeneCardsiGC09M130882.
HGNCiHGNC:17822. PTGES2.
HPAiHPA020631.
MIMi608152. gene.
neXtProtiNX_Q9H7Z7.
PharmGKBiPA33949.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG316980.
GeneTreeiENSGT00390000000224.
HOGENOMiHOG000231901.
HOVERGENiHBG069136.
InParanoidiQ9H7Z7.
KOiK05309.
OMAiSTYRKVP.
OrthoDBiEOG7060R5.
PhylomeDBiQ9H7Z7.
TreeFamiTF314304.

Enzyme and pathway databases

UniPathwayiUPA00662.
BioCyciMetaCyc:HS07514-MONOMER.
BRENDAi5.3.99.3. 2681.

Miscellaneous databases

ChiTaRSiPTGES2. human.
GeneWikiiPTGES2.
GenomeRNAii80142.
NextBioi70401.
PROiQ9H7Z7.
SOURCEiSearch...

Gene expression databases

BgeeiQ9H7Z7.
CleanExiHS_PTGES2.
ExpressionAtlasiQ9H7Z7. baseline and differential.
GenevestigatoriQ9H7Z7.

Family and domain databases

Gene3Di1.20.1050.10. 2 hits.
3.40.30.10. 1 hit.
InterProiIPR002109. Glutaredoxin.
IPR010987. Glutathione-S-Trfase_C-like.
IPR004045. Glutathione_S-Trfase_N.
IPR004046. GST_C.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamiPF14497. GST_C_3. 1 hit.
PF13417. GST_N_3. 1 hit.
[Graphical view]
SUPFAMiSSF47616. SSF47616. 1 hit.
SSF52833. SSF52833. 1 hit.
PROSITEiPS00195. GLUTAREDOXIN_1. 1 hit.
PS51354. GLUTAREDOXIN_2. 1 hit.
PS50405. GST_CTER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Embryo.
  2. Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
    Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  3. "DNA sequence and analysis of human chromosome 9."
    Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
    , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
    Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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].
    Tissue: Brain and Lung.
  5. "Identification and characterization of a novel type of membrane-associated prostaglandin E synthase."
    Tanikawa N., Ohmiya Y., Ohkubo H., Hashimoto K., Kangawa K., Kojima M., Ito S., Watanabe K.
    Biochem. Biophys. Res. Commun. 291:884-889(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  6. "Essential 110Cys in active site of membrane-associated prostaglandin E synthase-2."
    Watanabe K., Ohkubo H., Niwa H., Tanikawa N., Koda N., Ito S., Ohmiya Y.
    Biochem. Biophys. Res. Commun. 306:577-581(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: CATALYTIC ACTIVITY, MUTAGENESIS OF CYS-110 AND CYS-113, ENZYME REGULATION.
  7. "Cellular prostaglandin E2 production by membrane-bound prostaglandin E synthase-2 via both cyclooxygenases-1 and -2."
    Murakami M., Nakashima K., Kamei D., Masuda S., Ishikawa Y., Ishii T., Ohmiya Y., Watanabe K., Kudo I.
    J. Biol. Chem. 278:37937-37947(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: CLEAVAGE, SUBCELLULAR LOCATION.
  8. "A protein interaction framework for human mRNA degradation."
    Lehner B., Sanderson C.M.
    Genome Res. 14:1315-1323(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH EXOSC10.
  9. "Studies on membrane-associated prostaglandin E synthase-2 with reference to production of 12L-hydroxy-5,8,10-heptadecatrienoic acid (HHT)."
    Watanabe K., Ito S., Yamamoto S.
    Biochem. Biophys. Res. Commun. 367:782-786(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, CAUTION.
  10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "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.

Entry informationi

Entry nameiPGES2_HUMAN
AccessioniPrimary (citable) accession number: Q9H7Z7
Secondary accession number(s): Q53EW9
, Q5SYV6, Q96GI0, Q96GL2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 30, 2005
Last sequence update: March 1, 2001
Last modified: April 29, 2015
This is version 130 of the entry and version 1 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

Caution

Heme and GST are not required for prostaglandin synthase activity, but the protein copurifies with heme and GST when DTT is omitted during the purification procedure. The GSH-heme complex-bound enzyme (mPGES-2h) has been proposed to act as a lyase and catalyze the degradation of prostaglandin E2 H2 (PGH2) to 12(S)-hydroxy-5(Z),8(E),10(E)-heptadecatrienoic acid (HHT) and malondialdehyde (MDA), but this activity may well be spurious. According to PubMed:18198127, boiling the enzyme leads to loss of prostaglandin synthase activity, but does not eliminate the lyase activity. Besides, free heme can catalyze the formation of 12L-hydroxy-5,8,10-heptadecatrienoic acid (HHT).Curated1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 9
    Human chromosome 9: 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  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.