Q9H7Z7 (PGES2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Prostaglandin E synthase 2
EC=5.3.99.3

Alternative name(s):
Microsomal prostaglandin E synthase 2
Short name=mPGES-2

Cleaved into the following chain:

1. Prostaglandin E synthase 2 truncated form

Gene names

Name:	PTGES2
Synonyms:	C9orf15, PGES2

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	377 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Isomerase that catalyzes the conversion of unstable intermediate of prostaglandin E2 H2 (PGH2) into the more stable prostaglandin E2 (PGE2) form. May also have transactivation activity toward IFN-gamma (IFNG), possibly via an interaction with CEBPB; however, the relevance of transcription activation activity remains unclear.
Catalytic activity	(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.
Cofactor	Dihydrolipoic acid. Ref.6
Pathway	Lipid metabolism; prostaglandin biosynthesis.
Subunit structure	Homodimer. May interact with CEBPB By similarity. Interacts with EXOSC10. Ref.8
Subcellular location	Golgi apparatus membrane; Single-pass membrane protein Ref.7. Prostaglandin E synthase 2 truncated form: Cytoplasm › perinuclear region. Note: Synthetized 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. Ref.7
Tissue specificity	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. Ref.5
Sequence similarities	Belongs to the GST superfamily. Contains 1 glutaredoxin domain. Contains 1 GST C-terminal domain.
Sequence caution	The sequence CAI13822.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Biological process	Fatty acid biosynthesis Fatty acid metabolism Lipid biosynthesis Lipid metabolism Prostaglandin biosynthesis Prostaglandin metabolism
Cellular component	Cytoplasm Golgi apparatus Membrane
Coding sequence diversity	Polymorphism
Domain	Transmembrane Transmembrane helix
Molecular function	Isomerase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cell redox homeostasis Inferred from electronic annotation. Source: InterPro positive regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: Compara prostaglandin biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway secretion Inferred from electronic annotation. Source: Compara
Cellular_component	Golgi membrane Inferred from electronic annotation. Source: UniProtKB-SubCell cytosol Inferred from electronic annotation. Source: Compara integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW mitochondrion Inferred from direct assay. Source: LIFEdb nucleus Inferred from electronic annotation. Source: Compara perinuclear region of cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	DNA binding Inferred from electronic annotation. Source: Compara electron carrier activity Inferred from electronic annotation. Source: InterPro prostaglandin-E synthase activity Inferred from electronic annotation. Source: EC protein disulfide oxidoreductase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 377	377	Prostaglandin E synthase 2		PRO_0000013127
	Chain	88 – 377	290	Prostaglandin E synthase 2 truncated form By similarity		PRO_0000013128
Regions
	Topological domain	1 – 57	57	Lumenal Potential
	Transmembrane	58 – 74	17	Helical; Potential
	Topological domain	75 – 377	303	Cytoplasmic Potential
	Domain	90 – 193	104	Glutaredoxin
	Domain	263 – 377	115	GST C-terminal
	Region	164 – 165	2	Glutathione binding By similarity
Sites
	Binding site	148	1	Glutathione; via amide nitrogen and carbonyl oxygen By similarity
	Site	87 – 88	2	Cleavage By similarity
Natural variations
	Natural variant	298	1	R → H. Corresponds to variant rs13283456 [ dbSNP | Ensembl ].		VAR_049494
Experimental info
	Mutagenesis	110	1	C → S: Loss of function. Ref.6
	Mutagenesis	113	1	C → S: Does not strongly affect enzyme activity. Ref.6
	Sequence conflict	319	1	G → S in BAD97240. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q9H7Z7 [UniParc]. Last modified March 1, 2001. Version 1. Checksum: 82F2DF867BB8337C	FASTA	377	41,943
	10 20 30 40 50 60 MDPAARVVRA LWPGGCALAW RLGGRPQPLL PTQSRAGFAG AAGGPSPVAA ARKGSPRLLG 70 80 90 100 110 120 AAALALGGAL GLYHTARWHL RAQDLHAERS AAQLSLSSRL QLTLYQYKTC PFCSKVRAFL 130 140 150 160 170 180 DFHALPYQVV EVNPVRRAEI KFSSYRKVPI LVAQEGESSQ QLNDSSVIIS ALKTYLVSGQ 190 200 210 220 230 240 PLEEIITYYP AMKAVNEQGK EVTEFGNKYW LMLNEKEAQQ VYGGKEARTE EMKWRQWADD 250 260 270 280 290 300 WLVHLISPNV YRTPTEALAS FDYIVREGKF GAVEGAVAKY MGAAAMYLIS KRLKSRHRLQ 310 320 330 340 350 360 DNVREDLYEA ADKWVAAVGK DRPFMGGQKP NLADLAVYGV LRVMEGLDAF DDLMQHTHIQ 370 PWYLRVERAI TEASPAH

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: COFACTOR, MUTAGENESIS OF CYS-110 AND CYS-113.
[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]	"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].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	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.
IPI	IPI00303568.
RefSeq	NP_001243264.1. NM_001256335.1. NP_079348.1. NM_025072.6. NP_945176.1. NM_198938.2.
UniGene	Hs.495219.
3D structure databases
ProteinModelPortal	Q9H7Z7.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9H7Z7. 6 interactions.
STRING	9606.ENSP00000345341.
PTM databases
PhosphoSite	Q9H7Z7.
Polymorphism databases
DMDM	73921741.
Proteomic databases
PaxDb	Q9H7Z7.
PRIDE	Q9H7Z7.
Protocols and materials databases
DNASU	80142.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000338961; ENSP00000345341; ENSG00000148334. ENST00000449878; ENSP00000411378; ENSG00000148334.
GeneID	80142.
KEGG	hsa:80142.
UCSC	uc004bti.3. human.
Organism-specific databases
CTD	80142.
GeneCards	GC09M130882.
HGNC	HGNC:17822. PTGES2.
HPA	HPA020631.
MIM	608152. gene.
neXtProt	NX_Q9H7Z7.
PharmGKB	PA33949.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG316980.
HOGENOM	HOG000231901.
HOVERGEN	HBG069136.
InParanoid	Q9H7Z7.
KO	K05309.
OMA	AMYFISK.
OrthoDB	EOG4R7VB3.
Enzyme and pathway databases
BRENDA	5.3.99.3. 2681.
Pathway_Interaction_DB	ifngpathway. IFN-gamma pathway.
UniPathway	UPA00662.
Gene expression databases
ArrayExpress	Q9H7Z7.
Bgee	Q9H7Z7.
CleanEx	HS_PTGES2.
Genevestigator	Q9H7Z7.
GermOnline	ENSG00000148334. Homo sapiens.
Family and domain databases
Gene3D	1.20.1050.10. 2 hits. 3.40.30.10. 1 hit.
InterPro	IPR002109. Glutaredoxin. IPR010987. Glutathione-S-Trfase_C-like. IPR017933. Glutathione_S_Trfase/Cl_chnl_C. IPR004046. GST_C. IPR012336. Thioredoxin-like_fold. [Graphical view]
Pfam	PF00043. GST_C. 1 hit. [Graphical view]
SUPFAM	SSF47616. GST_C_like. 1 hit. SSF52833. Thiordxn-like_fd. 1 hit.
PROSITE	PS00195. GLUTAREDOXIN_1. 1 hit. PS51354. GLUTAREDOXIN_2. 1 hit. PS50405. GST_CTER. 1 hit. [Graphical view]
ProtoNet	Search...
Other
BindingDB	Q9H7Z7.
ChEMBL	CHEMBL4411.
ChiTaRS	PTGES2. human.
GenomeRNAi	80142.
NextBio	70401.
SOURCE	Search...

Entry information

Entry name

PGES2_HUMAN

Accession

Primary (citable) accession number: Q9H7Z7
Secondary accession number(s): Q53EW9 , Q5SYV6, Q96GI0, Q96GL2

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 30, 2005
Last sequence update:	March 1, 2001
Last modified:	May 1, 2013
This is version 113 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.