Q9R0Q7 (TEBP_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Prostaglandin E synthase 3
EC=5.3.99.3

Alternative name(s):
Cytosolic prostaglandin E2 synthase
Short name=cPGES
Hsp90 co-chaperone
Progesterone receptor complex p23
Sid 3177
Telomerase-binding protein p23

Gene names

Name:	Ptges3
Synonyms:	Sid3177, Tebp

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	160 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Molecular chaperone that localizes to genomic response elements in a hormone-dependent manner and disrupts receptor-mediated transcriptional activation, by promoting disassembly of transcriptional regulatory complexes By similarity.
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.
Pathway	Lipid metabolism; prostaglandin biosynthesis.
Subunit structure	Binds to the progesterone receptor. Interacts with TERT; the interaction, together with HSP90AA1, is required for correct assembly and stabilization of the telomerase holoenzyme complex By similarity.
Subcellular location	Cytoplasm By similarity.
Tissue specificity	Expressed in testis, kidney, bladder and ovary. Ref.1
Sequence similarities	Belongs to the p23/wos2 family. Contains 1 CS domain.

Ontologies

Keywords
Biological process	Fatty acid biosynthesis Fatty acid metabolism Lipid biosynthesis Lipid metabolism Prostaglandin biosynthesis Prostaglandin metabolism
Cellular component	Cytoplasm
Molecular function	Isomerase
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	chaperone cofactor-dependent protein refolding Inferred from electronic annotation. Source: Compara prostaglandin biosynthetic process Inferred from sequence or structural similarity. Source: UniProtKB
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell telomerase holoenzyme complex Inferred from electronic annotation. Source: Compara
Molecular_function	prostaglandin-E synthase activity Inferred from sequence or structural similarity. Source: UniProtKB telomerase activity Inferred from electronic annotation. Source: Compara unfolded protein binding Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 160	160	Prostaglandin E synthase 3		PRO_0000218953
Regions
	Domain	1 – 90	90	CS
	Compositional bias	108 – 160	53	Asp/Glu-rich
Amino acid modifications
	Modified residue	33	1	N6-acetyllysine By similarity
	Modified residue	113	1	Phosphoserine Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13
	Modified residue	118	1	Phosphoserine By similarity
	Modified residue	148	1	Phosphoserine Ref.12
	Modified residue	151	1	Phosphoserine Ref.12
Experimental info
	Sequence conflict	87 – 88	2	PR → LG in AAD39543. Ref.3
	Sequence conflict	108	1	D → N in AAP34198. Ref.1
	Sequence conflict	108	1	D → N in BAB25906. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	Q9R0Q7 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: 7702CB59D7AFD739	FASTA	160	18,721
	10 20 30 40 50 60 MQPASAKWYD RRDYVFIEFC VEDSKDVNVN FEKSKLTFSC LGGSDNFKHL NEIDLFHCID 70 80 90 100 110 120 PNDSKHKRTD RSILCCLRKG ESGQSWPRLT KERAKLNWLS VDFNNWKDWE DDSDEDMSNF 130 140 150 160 DRFSEMMDHM GGDEDVDLPE VDGADDDSQD SDDEKMPDLE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Genomic structure and genitourinary expression of mouse cytosolic prostaglandin E(2) synthase gene." Zhang Y., Schneider A., Rao R., Lu W.J., Fan X., Davis L., Breyer R.M., Breyer M.D., Guan Y. Biochim. Biophys. Acta 1634:15-23(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY. Strain: C57BL/6. Tissue: Kidney.
[2]	"Mouse p23 uniactive progesterone receptor complexes." Seki N., Hattori A., Hayashi A., Kozuma S., Muramatsu M., Saito T. Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	Cheong C., Lee H.-W. Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Brain.
[4]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J and DBA/2. Tissue: Liver and Stomach.
[5]	"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]. Strain: C57BL/6J. Tissue: Mammary gland and Olfactory epithelium.
[6]	Lubec G., Yang J.W., Zigmond M. Submitted (JUL-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 36-48. Tissue: Brain.
[7]	"Phosphoproteomic analysis of the developing mouse brain." Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P. Mol. Cell. Proteomics 3:1093-1101(2004) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113, MASS SPECTROMETRY. Tissue: Embryonic brain.
[8]	"Phosphoproteome analysis of mouse liver using immobilized metal affinity purification and linear ion trap mass spectrometry." Jin W.-H., Dai J., Zhou H., Xia Q.-C., Zou H.-F., Zeng R. Rapid Commun. Mass Spectrom. 18:2169-2176(2004) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT SER-113.
[9]	"Protein phosphorylation and expression profiling by Yin-yang multidimensional liquid chromatography (Yin-yang MDLC) mass spectrometry." Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R. J. Proteome Res. 6:250-262(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113, MASS SPECTROMETRY. Tissue: Liver.
[10]	"Qualitative and quantitative analyses of protein phosphorylation in naive and stimulated mouse synaptosomal preparations." Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F., Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B., Panse C., Schlapbach R., Mansuy I.M. Mol. Cell. Proteomics 6:283-293(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113, MASS SPECTROMETRY. Tissue: Brain cortex.
[11]	"Specific phosphopeptide enrichment with immobilized titanium ion affinity chromatography adsorbent for phosphoproteome analysis." Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H. J. Proteome Res. 7:3957-3967(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113, MASS SPECTROMETRY. Tissue: Liver.
[12]	"Solid tumor proteome and phosphoproteome analysis by high resolution mass spectrometry." Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J., Faessler R., Mann M. J. Proteome Res. 7:5314-5326(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113; SER-148 AND SER-151, MASS SPECTROMETRY. Tissue: Melanoma.
[13]	"The phagosomal proteome in interferon-gamma-activated macrophages." Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P. Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113, MASS SPECTROMETRY. Tissue: Macrophage.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AY281130 mRNA. Translation: AAP34198.1. AB024935 mRNA. Translation: BAA84684.1. AF153479 mRNA. Translation: AAD39543.1. AK008805 mRNA. Translation: BAB25906.1. AK075932 mRNA. Translation: BAC36062.1. AK075987 mRNA. Translation: BAC36099.1. AK077538 mRNA. Translation: BAC36854.1. AK168073 mRNA. Translation: BAE40047.1. AK168210 mRNA. Translation: BAE40169.1. AK168721 mRNA. Translation: BAE40563.1. BC003708 mRNA. Translation: AAH03708.1. BC085264 mRNA. Translation: AAH85264.1.
IPI	IPI00127989.
RefSeq	NP_062740.1. NM_019766.4. XP_003945448.1. XM_003945399.1. XP_003946238.1. XM_003946189.1.
UniGene	Mm.305816.
3D structure databases
ProteinModelPortal	Q9R0Q7.
SMR	Q9R0Q7. Positions 1-110.
ModBase	Search...
Protein-protein interaction databases
MINT	MINT-3289867.
STRING	10090.ENSMUSP00000050292.
PTM databases
PhosphoSite	Q9R0Q7.
Proteomic databases
PaxDb	Q9R0Q7.
PRIDE	Q9R0Q7.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000052798; ENSMUSP00000050292; ENSMUSG00000071072.
GeneID	100043508. 100048119. 56351.
KEGG	mmu:100043508. mmu:100048119. mmu:56351.
UCSC	uc007hld.1. mouse.
Organism-specific databases
CTD	10728.
MGI	MGI:1929282. Ptges3.
Phylogenomic databases
eggNOG	NOG283591.
GeneTree	ENSGT00510000046493.
HOGENOM	HOG000177563.
HOVERGEN	HBG002143.
InParanoid	Q9R0Q7.
KO	K15730.
OMA	FCVADSK.
OrthoDB	EOG48WC3C.
Enzyme and pathway databases
UniPathway	UPA00662.
Gene expression databases
ArrayExpress	Q9R0Q7.
Bgee	Q9R0Q7.
CleanEx	MM_PTGES3.
Genevestigator	Q9R0Q7.
GermOnline	ENSMUSG00000040078. Mus musculus.
Family and domain databases
InterPro	IPR007052. CS-like_domain. IPR017447. CS_domain. IPR008978. HSP20-like_chaperone. [Graphical view]
Pfam	PF04969. CS. 1 hit. [Graphical view]
SUPFAM	SSF49764. HSP20_chap. 1 hit.
PROSITE	PS51203. CS. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	PTGES3. mouse.
NextBio	312354.
SOURCE	Search...

Entry information

Entry name

TEBP_MOUSE

Accession

Primary (citable) accession number: Q9R0Q7
Secondary accession number(s): Q542V4, Q9D7V0, Q9WV83

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	May 1, 2000
Last modified:	May 29, 2013
This is version 119 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program