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Protein

Prostaglandin E synthase 3

Gene

PTGES3

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

Functioni

Cytosolic prostaglandin synthase that catalyzes the oxidoreduction of prostaglandin endoperoxide H2 (PGH2) to prostaglandin E2 (PGE2) (PubMed:10922363). 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 (PubMed:11274138, PubMed:12077419). Facilitates HIF alpha proteins hydroxylation via interaction with EGLN1/PHD2, leading to recruit EGLN1/PHD2 to the HSP90 pathway (PubMed:24711448).4 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.1 Publication

Kineticsi

  1. KM=14 µM for PGH21 Publication
  1. Vmax=190 nmol/min/mg enzyme toward PGH21 Publication

Pathway: prostaglandin biosynthesis

This protein is involved in the pathway prostaglandin biosynthesis, which is part of Lipid metabolism.1 Publication
View all proteins of this organism that are known to be involved in the pathway prostaglandin biosynthesis and in Lipid metabolism.

GO - Molecular functioni

  • prostaglandin-E synthase activity Source: UniProtKB
  • telomerase activity Source: UniProtKB
  • unfolded protein binding Source: UniProtKB

GO - Biological processi

  • arachidonic acid metabolic process Source: Reactome
  • cellular response to heat Source: Reactome
  • chaperone cofactor-dependent protein refolding Source: UniProtKB
  • cyclooxygenase pathway Source: Reactome
  • prostaglandin biosynthetic process Source: UniProtKB
  • regulation of cellular response to heat Source: Reactome
  • RNA-dependent DNA replication Source: GOC
  • signal transduction Source: ProtInc
  • small molecule metabolic process Source: Reactome
  • telomere maintenance Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Chaperone, Isomerase

Keywords - Biological processi

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

Enzyme and pathway databases

BioCyciMetaCyc:HS03359-MONOMER.
ReactomeiREACT_150149. Synthesis of Prostaglandins (PG) and Thromboxanes (TX).
REACT_264071. HSF1 activation.
REACT_264075. Attenuation phase.
UniPathwayiUPA00662.

Names & Taxonomyi

Protein namesi
Recommended name:
Prostaglandin E synthase 3 (EC:5.3.99.31 Publication)
Alternative name(s):
Cytosolic prostaglandin E2 synthase
Short name:
cPGES
Hsp90 co-chaperone
Progesterone receptor complex p23
Telomerase-binding protein p23
Gene namesi
Name:PTGES3
Synonyms:P23, TEBP
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 12

Organism-specific databases

HGNCiHGNC:16049. PTGES3.

Subcellular locationi

GO - Cellular componenti

  • chromosome, telomeric region Source: UniProtKB
  • cytoplasm Source: HPA
  • cytosol Source: Reactome
  • extracellular exosome Source: UniProtKB
  • nucleoplasm Source: HPA
  • nucleus Source: UniProtKB
  • telomerase holoenzyme complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA142671118.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 160160Prostaglandin E synthase 3PRO_0000218952Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei33 – 331N6-acetyllysine1 Publication
Modified residuei85 – 851Phosphoserine1 Publication
Modified residuei113 – 1131Phosphoserine14 Publications
Modified residuei118 – 1181Phosphoserine2 Publications
Modified residuei148 – 1481Phosphoserine4 Publications
Modified residuei151 – 1511Phosphoserine4 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ15185.
PaxDbiQ15185.
PRIDEiQ15185.

PTM databases

PhosphoSiteiQ15185.

Expressioni

Gene expression databases

BgeeiQ15185.
CleanExiHS_PTGES3.
ExpressionAtlasiQ15185. baseline and differential.
GenevisibleiQ15185. HS.

Organism-specific databases

HPAiCAB034319.
HPA038672.
HPA038673.

Interactioni

Subunit structurei

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. Interacts (via PXLE motif) with EGLN1/PHD2, recruiting EGLN1/PHD2 to the HSP90 pathway to facilitate HIF alpha proteins hydroxylation.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
AGO2Q9UKV83EBI-1049387,EBI-528269
HSP90AA1P079006EBI-1049387,EBI-296047
IRS4O146542EBI-1049387,EBI-356594

Protein-protein interaction databases

BioGridi115952. 67 interactions.
DIPiDIP-279N.
IntActiQ15185. 39 interactions.
MINTiMINT-5000397.
STRINGi9606.ENSP00000262033.

Structurei

Secondary structure

1
160
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi6 – 105Combined sources
Beta strandi12 – 198Combined sources
Beta strandi24 – 329Combined sources
Beta strandi35 – 428Combined sources
Turni43 – 464Combined sources
Beta strandi47 – 5711Combined sources
Beta strandi59 – 6810Combined sources
Beta strandi73 – 819Combined sources
Beta strandi87 – 926Combined sources
Beta strandi99 – 1013Combined sources
Turni103 – 1053Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1EJFX-ray2.49A/B1-125[»]
1LG0model-A1-110[»]
DisProtiDP00358.
ProteinModelPortaliQ15185.
SMRiQ15185. Positions 1-110.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ15185.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 9090CSPROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi157 – 1604PXLE motif1 Publication

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi108 – 16053Asp/Glu-richAdd
BLAST

Domaini

The PXLE motif mediates interaction with EGLN1/PHD2.1 Publication

Sequence similaritiesi

Belongs to the p23/wos2 family.Curated
Contains 1 CS domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG283591.
GeneTreeiENSGT00510000046493.
HOGENOMiHOG000177563.
HOVERGENiHBG002143.
InParanoidiQ15185.
KOiK15730.
OMAiSDEEMGN.
OrthoDBiEOG77HDGK.
PhylomeDBiQ15185.
TreeFamiTF315077.

Family and domain databases

Gene3Di2.60.40.790. 1 hit.
InterProiIPR007052. CS_dom.
IPR008978. HSP20-like_chaperone.
[Graphical view]
PfamiPF04969. CS. 1 hit.
[Graphical view]
SUPFAMiSSF49764. SSF49764. 1 hit.
PROSITEiPS51203. CS. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q15185-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MQPASAKWYD RRDYVFIEFC VEDSKDVNVN FEKSKLTFSC LGGSDNFKHL
60 70 80 90 100
NEIDLFHCID PNDSKHKRTD RSILCCLRKG ESGQSWPRLT KERAKLNWLS
110 120 130 140 150
VDFNNWKDWE DDSDEDMSNF DRFSEMMNNM GGDEDVDLPE VDGADDDSQD
160
SDDEKMPDLE
Length:160
Mass (Da):18,697
Last modified:November 1, 1996 - v1
Checksum:i23538BB9D7AFD73F
GO
Isoform 2 (identifier: Q15185-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     63-95: Missing.

Note: No experimental confirmation available.
Show »
Length:127
Mass (Da):14,844
Checksum:i6C189780960CB97D
GO
Isoform 3 (identifier: Q15185-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     96-125: Missing.

Note: No experimental confirmation available.
Show »
Length:130
Mass (Da):14,959
Checksum:iDAA51580AD82CA72
GO
Isoform 4 (identifier: Q15185-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     126-146: Missing.

Note: No experimental confirmation available. Contains a phosphoserine at position 130.1 Publication
Show »
Length:139
Mass (Da):16,476
Checksum:i9582520CFE2A0C5A
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei63 – 9533Missing in isoform 2. 1 PublicationVSP_055363Add
BLAST
Alternative sequencei96 – 12530Missing in isoform 3. 1 PublicationVSP_055364Add
BLAST
Alternative sequencei126 – 14621Missing in isoform 4. 1 PublicationVSP_055365Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L24804 mRNA. Translation: AAA18537.1.
AK291945 mRNA. Translation: BAF84634.1.
AK295208 mRNA. Translation: BAG58204.1.
AK298147 mRNA. Translation: BAG60423.1.
AK298160 mRNA. Translation: BAG60433.1.
AC117378 Genomic DNA. No translation available.
CH471054 Genomic DNA. Translation: EAW96953.1.
CH471054 Genomic DNA. Translation: EAW96958.1.
BC003005 mRNA. Translation: AAH03005.1.
BC021167 mRNA. Translation: AAH21167.1.
CCDSiCCDS31836.1. [Q15185-1]
CCDS61158.1. [Q15185-2]
CCDS61159.1. [Q15185-3]
CCDS61160.1. [Q15185-4]
PIRiA56211.
RefSeqiNP_001269530.1. NM_001282601.1. [Q15185-4]
NP_001269531.1. NM_001282602.1. [Q15185-3]
NP_001269532.1. NM_001282603.1. [Q15185-2]
NP_001269533.1. NM_001282604.1.
NP_001269534.1. NM_001282605.1.
NP_006592.3. NM_006601.6. [Q15185-1]
UniGeneiHs.50425.

Genome annotation databases

EnsembliENST00000262033; ENSP00000262033; ENSG00000110958. [Q15185-1]
ENST00000414274; ENSP00000405299; ENSG00000110958. [Q15185-3]
ENST00000436399; ENSP00000402385; ENSG00000110958. [Q15185-2]
ENST00000448157; ENSP00000414892; ENSG00000110958. [Q15185-4]
GeneIDi10728.
KEGGihsa:10728.
UCSCiuc001slu.4. human. [Q15185-1]
uc001slv.4. human.
uc010sqs.2. human.
uc010sqt.2. human.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L24804 mRNA. Translation: AAA18537.1.
AK291945 mRNA. Translation: BAF84634.1.
AK295208 mRNA. Translation: BAG58204.1.
AK298147 mRNA. Translation: BAG60423.1.
AK298160 mRNA. Translation: BAG60433.1.
AC117378 Genomic DNA. No translation available.
CH471054 Genomic DNA. Translation: EAW96953.1.
CH471054 Genomic DNA. Translation: EAW96958.1.
BC003005 mRNA. Translation: AAH03005.1.
BC021167 mRNA. Translation: AAH21167.1.
CCDSiCCDS31836.1. [Q15185-1]
CCDS61158.1. [Q15185-2]
CCDS61159.1. [Q15185-3]
CCDS61160.1. [Q15185-4]
PIRiA56211.
RefSeqiNP_001269530.1. NM_001282601.1. [Q15185-4]
NP_001269531.1. NM_001282602.1. [Q15185-3]
NP_001269532.1. NM_001282603.1. [Q15185-2]
NP_001269533.1. NM_001282604.1.
NP_001269534.1. NM_001282605.1.
NP_006592.3. NM_006601.6. [Q15185-1]
UniGeneiHs.50425.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1EJFX-ray2.49A/B1-125[»]
1LG0model-A1-110[»]
DisProtiDP00358.
ProteinModelPortaliQ15185.
SMRiQ15185. Positions 1-110.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115952. 67 interactions.
DIPiDIP-279N.
IntActiQ15185. 39 interactions.
MINTiMINT-5000397.
STRINGi9606.ENSP00000262033.

PTM databases

PhosphoSiteiQ15185.

Proteomic databases

MaxQBiQ15185.
PaxDbiQ15185.
PRIDEiQ15185.

Protocols and materials databases

DNASUi10728.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000262033; ENSP00000262033; ENSG00000110958. [Q15185-1]
ENST00000414274; ENSP00000405299; ENSG00000110958. [Q15185-3]
ENST00000436399; ENSP00000402385; ENSG00000110958. [Q15185-2]
ENST00000448157; ENSP00000414892; ENSG00000110958. [Q15185-4]
GeneIDi10728.
KEGGihsa:10728.
UCSCiuc001slu.4. human. [Q15185-1]
uc001slv.4. human.
uc010sqs.2. human.
uc010sqt.2. human.

Organism-specific databases

CTDi10728.
GeneCardsiGC12M057057.
HGNCiHGNC:16049. PTGES3.
HPAiCAB034319.
HPA038672.
HPA038673.
MIMi607061. gene.
neXtProtiNX_Q15185.
PharmGKBiPA142671118.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG283591.
GeneTreeiENSGT00510000046493.
HOGENOMiHOG000177563.
HOVERGENiHBG002143.
InParanoidiQ15185.
KOiK15730.
OMAiSDEEMGN.
OrthoDBiEOG77HDGK.
PhylomeDBiQ15185.
TreeFamiTF315077.

Enzyme and pathway databases

UniPathwayiUPA00662.
BioCyciMetaCyc:HS03359-MONOMER.
ReactomeiREACT_150149. Synthesis of Prostaglandins (PG) and Thromboxanes (TX).
REACT_264071. HSF1 activation.
REACT_264075. Attenuation phase.

Miscellaneous databases

ChiTaRSiPTGES3. human.
EvolutionaryTraceiQ15185.
GeneWikiiPTGES3.
GenomeRNAii10728.
NextBioi35472063.
PROiQ15185.
SOURCEiSearch...

Gene expression databases

BgeeiQ15185.
CleanExiHS_PTGES3.
ExpressionAtlasiQ15185. baseline and differential.
GenevisibleiQ15185. HS.

Family and domain databases

Gene3Di2.60.40.790. 1 hit.
InterProiIPR007052. CS_dom.
IPR008978. HSP20-like_chaperone.
[Graphical view]
PfamiPF04969. CS. 1 hit.
[Graphical view]
SUPFAMiSSF49764. SSF49764. 1 hit.
PROSITEiPS51203. CS. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Characterization of a novel 23-kilodalton protein of unactive progesterone receptor complexes."
    Johnson J.L., Beito T.G., Krco C.J., Toft D.O.
    Mol. Cell. Biol. 14:1956-1963(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Testis.
  2. "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] (ISOFORMS 1; 2; 3 AND 4).
    Tissue: Caudate nucleus.
  3. "The finished DNA sequence of human chromosome 12."
    Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
    , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
    Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  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] (ISOFORM 1).
    Tissue: Lung and Urinary bladder.
  6. Bienvenut W.V., Waridel P., Quadroni M.
    Submitted (MAR-2009) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 13-65; 72-88 AND 96-122, PHOSPHORYLATION AT SER-113, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Embryonic kidney.
  7. "Stable association of hsp90 and p23, but Not hsp70, with active human telomerase."
    Forsythe H.L., Jarvis J.L., Turner J.W., Elmore L.W., Holt S.E.
    J. Biol. Chem. 276:15571-15574(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TERT, FUNCTION AS A CO-CHAPERONE IN TELOMERASE HOLOENZYME ASSEMBLY.
  8. "Disassembly of transcriptional regulatory complexes by molecular chaperones."
    Freeman B.C., Yamamoto K.R.
    Science 296:2232-2235(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS A CHAPERONE.
  9. "Molecular identification of cytosolic prostaglandin E2 synthase that is functionally coupled with cyclooxygenase-1 in immediate prostaglandin E2 biosynthesis."
    Tanioka T., Nakatani Y., Semmyo N., Murakami M., Kudo I.
    J. Biol. Chem. 275:32775-32782(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS A PROSTAGLANDIN SYNTHASE, BIOPHYSICOCHEMICAL PROPERTIES, CATALYTIC ACTIVITY, PATHWAY.
  10. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113; SER-118; SER-148 AND SER-151, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Pituitary.
  12. "Toward a global characterization of the phosphoproteome in prostate cancer cells: identification of phosphoproteins in the LNCaP cell line."
    Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S.
    Electrophoresis 28:2027-2034(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Prostate cancer.
  13. "Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment."
    Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.
    J. Proteome Res. 7:5167-5176(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: T-cell.
  14. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Platelet.
  15. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113; SER-148 AND SER-151, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  16. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113; SER-148 AND SER-151, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  17. "Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography."
    Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J.
    Proteomics 8:1346-1361(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  18. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  19. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  20. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  21. "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-33, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  22. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113 AND SER-118, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  23. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  24. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  25. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  26. "Defective Tibetan PHD2 binding to p23 links high altitude adaption to altered oxygen sensing."
    Song D., Li L.S., Arsenault P.R., Tan Q., Bigham A.W., Heaton-Johnson K.J., Master S.R., Lee F.S.
    J. Biol. Chem. 289:14656-14665(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH EGLN1.
  27. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-85; SER-113; SER-148 AND SER-151, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-130 (ISOFORM 4), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  28. "Crystal structure and activity of human p23, a heat shock protein 90 co-chaperone."
    Weaver A.J., Sullivan W.P., Felts S.J., Owen B.A.L., Toft D.O.
    J. Biol. Chem. 275:23045-23052(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.49 ANGSTROMS) OF 1-125.

Entry informationi

Entry nameiTEBP_HUMAN
AccessioniPrimary (citable) accession number: Q15185
Secondary accession number(s): A8K7D0
, B4DHP2, B4DP11, B4DP21, Q8WU70
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: November 1, 1996
Last modified: June 24, 2015
This is version 152 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

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  5. 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.