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Q15185

- TEBP_HUMAN

UniProt

Q15185 - TEBP_HUMAN

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Protein
Prostaglandin E synthase 3
Gene
PTGES3, P23, TEBP
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.3 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.

Kineticsi

  1. KM=14 µM for PGH21 Publication

Vmax=190 nmol/min/mg enzyme toward PGH2

Pathwayi

GO - Molecular functioni

  1. prostaglandin-E synthase activity Source: UniProtKB
  2. protein binding Source: IntAct
  3. telomerase activity Source: UniProtKB
  4. unfolded protein binding Source: UniProtKB

GO - Biological processi

  1. RNA-dependent DNA replication Source: GOC
  2. arachidonic acid metabolic process Source: Reactome
  3. chaperone cofactor-dependent protein refolding Source: UniProtKB
  4. cyclooxygenase pathway Source: Reactome
  5. prostaglandin biosynthetic process Source: UniProtKB
  6. signal transduction Source: ProtInc
  7. small molecule metabolic process Source: Reactome
  8. 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_200624. Attenuation phase.
REACT_200744. HSF1 activation.
UniPathwayiUPA00662.

Names & Taxonomyi

Protein namesi
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
Telomerase-binding protein p23
Gene namesi
Name:PTGES3
Synonyms:P23, TEBP
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 12

Organism-specific databases

HGNCiHGNC:16049. PTGES3.

Subcellular locationi

GO - Cellular componenti

  1. chromosome, telomeric region Source: UniProtKB
  2. cytoplasm Source: HPA
  3. cytosol Source: Reactome
  4. extracellular vesicular exosome Source: UniProt
  5. nucleus Source: HPA
  6. 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 3
PRO_0000218952Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei33 – 331N6-acetyllysine1 Publication
Modified residuei113 – 1131Phosphoserine13 Publications
Modified residuei118 – 1181Phosphoserine2 Publications
Modified residuei148 – 1481Phosphoserine3 Publications
Modified residuei151 – 1511Phosphoserine3 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ15185.
PaxDbiQ15185.
PRIDEiQ15185.

PTM databases

PhosphoSiteiQ15185.

Expressioni

Gene expression databases

ArrayExpressiQ15185.
BgeeiQ15185.
CleanExiHS_PTGES3.
GenevestigatoriQ15185.

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.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
AGO2Q9UKV83EBI-1049387,EBI-528269
HSP90AA1P079005EBI-1049387,EBI-296047

Protein-protein interaction databases

BioGridi115952. 61 interactions.
DIPiDIP-279N.
IntActiQ15185. 12 interactions.
MINTiMINT-5000397.
STRINGi9606.ENSP00000262033.

Structurei

Secondary structure

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

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiQ15185.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 9090CS
Add
BLAST

Compositional bias

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

Sequence similaritiesi

Belongs to the p23/wos2 family.
Contains 1 CS domain.

Phylogenomic databases

eggNOGiNOG283591.
HOVERGENiHBG002143.
InParanoidiQ15185.
KOiK15730.
OMAiVNIKTPD.
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. Align

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

MQPASAKWYD RRDYVFIEFC VEDSKDVNVN FEKSKLTFSC LGGSDNFKHL    50
NEIDLFHCID PNDSKHKRTD RSILCCLRKG ESGQSWPRLT KERAKLNWLS 100
VDFNNWKDWE DDSDEDMSNF DRFSEMMNNM GGDEDVDLPE VDGADDDSQD 150
SDDEKMPDLE 160
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.

Show »
Length:139
Mass (Da):16,476
Checksum:i9582520CFE2A0C5A
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei63 – 9533Missing in isoform 2.
VSP_055363Add
BLAST
Alternative sequencei96 – 12530Missing in isoform 3.
VSP_055364Add
BLAST
Alternative sequencei126 – 14621Missing in isoform 4.
VSP_055365Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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]
PIRiA56211.
RefSeqiNP_001269530.1. NM_001282601.1.
NP_001269531.1. NM_001282602.1.
NP_001269532.1. NM_001282603.1.
NP_001269533.1. NM_001282604.1.
NP_001269534.1. NM_001282605.1.
NP_006592.3. NM_006601.6.
UniGeneiHs.50425.

Genome annotation databases

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

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS31836.1. [Q15185-1 ]
PIRi A56211.
RefSeqi NP_001269530.1. NM_001282601.1.
NP_001269531.1. NM_001282602.1.
NP_001269532.1. NM_001282603.1.
NP_001269533.1. NM_001282604.1.
NP_001269534.1. NM_001282605.1.
NP_006592.3. NM_006601.6.
UniGenei Hs.50425.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1EJF X-ray 2.49 A/B 1-125 [» ]
1LG0 model - A 1-110 [» ]
DisProti DP00358.
ProteinModelPortali Q15185.
SMRi Q15185. Positions 1-110.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 115952. 61 interactions.
DIPi DIP-279N.
IntActi Q15185. 12 interactions.
MINTi MINT-5000397.
STRINGi 9606.ENSP00000262033.

PTM databases

PhosphoSitei Q15185.

Proteomic databases

MaxQBi Q15185.
PaxDbi Q15185.
PRIDEi Q15185.

Protocols and materials databases

DNASUi 10728.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000262033 ; ENSP00000262033 ; ENSG00000110958 .
ENST00000414274 ; ENSP00000405299 ; ENSG00000110958 .
ENST00000436399 ; ENSP00000402385 ; ENSG00000110958 .
ENST00000448157 ; ENSP00000414892 ; ENSG00000110958 .
GeneIDi 10728.
KEGGi hsa:10728.
UCSCi uc001slu.4. human. [Q15185-1 ]

Organism-specific databases

CTDi 10728.
GeneCardsi GC12M057057.
HGNCi HGNC:16049. PTGES3.
HPAi CAB034319.
HPA038672.
HPA038673.
MIMi 607061. gene.
neXtProti NX_Q15185.
PharmGKBi PA142671118.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG283591.
HOVERGENi HBG002143.
InParanoidi Q15185.
KOi K15730.
OMAi VNIKTPD.
OrthoDBi EOG77HDGK.
PhylomeDBi Q15185.
TreeFami TF315077.

Enzyme and pathway databases

UniPathwayi UPA00662 .
BioCyci MetaCyc:HS03359-MONOMER.
Reactomei REACT_150149. Synthesis of Prostaglandins (PG) and Thromboxanes (TX).
REACT_200624. Attenuation phase.
REACT_200744. HSF1 activation.

Miscellaneous databases

ChiTaRSi PTGES3. human.
EvolutionaryTracei Q15185.
GeneWikii PTGES3.
GenomeRNAii 10728.
NextBioi 35472063.
PROi Q15185.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q15185.
Bgeei Q15185.
CleanExi HS_PTGES3.
Genevestigatori Q15185.

Family and domain databases

Gene3Di 2.60.40.790. 1 hit.
InterProi IPR007052. CS_dom.
IPR008978. HSP20-like_chaperone.
[Graphical view ]
Pfami PF04969. CS. 1 hit.
[Graphical view ]
SUPFAMi SSF49764. SSF49764. 1 hit.
PROSITEi PS51203. CS. 1 hit.
[Graphical view ]
ProtoNeti Search...

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.
  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. "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: September 3, 2014
This is version 142 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

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