Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Prostaglandin-H2 D-isomerase  

UniProtKB / Swiss-Prot ID :  PTGDS_HUMAN

Gene Name (Synonyms) : 
PTGDS, PDS  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Rough endoplasmic reticulum. Nucleus membrane. Golgi apparatus. Cytoplasm, perinuclear region. Secreted. Note=Detected on rough endoplasmic reticulum of arachnoid and menigioma cells. Localized to the nuclear envelope, Golgi apparatus, secretory vesicles 

Protein Function :  Catalyzes the conversion of PGH2 to PGD2, a prostaglandin involved in smooth muscle contraction/relaxation and a potent inhibitor of platelet aggregation. Involved in a variety of CNS functions, such as sedation, NREM sleep and PGE2-induced allodynia, and may have an anti-apoptotic role in oligodendrocytes. Binds small non-substrate lipophilic molecules, including biliverdin, bilirubin, retinal, retinoic acid and thyroid hormone, and may act as a scavenger for harmful hydrophopic molecules and as a secretory retinoid and thyroid hormone transporter. Possibly involved in development and maintenance of the blood-brain, blood-retina, blood-aqueous humor and blood-testis barrier. It is likely to play important roles in both maturation and maintenance of the central nervous system and male reproductive system. 

Protein Sequence MATHHTLWMGLALLGVLGDLQAAPEAQVSVQPNFQQDKFLGRWFSAGLASNSSWLREKKAALSMCKSVVA...
Predicted Secondary Structure CCCCHHHHHHHHHHHHHCCCCCCCCCCCCCCCCCCHHHHCCEEEEEEEEECCHHHHCCCCCCEEEEEEEE...
Protein Variant
LocationDescription
56R -> Q (in dbSNP:rs11552179). VAR_004273
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
Protein Variant
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
51N-linked (Glc...)GLASNSSWL
EEEECCHHH
34.16HPRD
Link
51N-linked (GlcNAc...) (complex).GLASNSSWL
EEEECCHHH
34.16UniProtKB
Link
78N-linked (Glc...)DGGLNLTST
CCCEEEEEE
44.54HPRD
Link
78N-linked (GlcNAc...) (complex).DGGLNLTST
CCCEEEEEE
44.54UniProtKB
Link
149PhosphotyrosineMATLYSRTQ
EEEEEECCC
7.55Phosphositeplus
Link
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
ATX1_HUMANphysical interactionMINT-2862294MINT16713569
ATX1_HUMANphysical interactionMINT-2862313MINT16713569
PE2R1_HUMANin vivoHPRD:08904HPRD8253813
SHBG_HUMANyeast 2-hybridHPRD:08904HPRD15862967
ATX1_HUMANyeast 2-hybridHPRD:08904HPRD16713569
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Disease Reference
Kegg disease
There are no disease associations of PTM sites.
Drug Reference
There are no disease associations of PTM sites.
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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Purification and chemical characterization of beta-trace protein fromhuman cerebrospinal fluid: its identification as prostaglandin Dsynthase.";
Hoffmann A., Conradt H.S., Gross G., Nimtz M., Lottspeich F.,Wurster U.;
J. Neurochem. 61:451-456(1993).
Cited for: PROTEIN SEQUENCE OF 23-190, AND GLYCOSYLATION AT ASN-51 AND ASN-78.
"Human plasma N-glycoproteome analysis by immunoaffinity subtraction,hydrazide chemistry, and mass spectrometry.";
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,Moore R.J., Smith R.D.;
J. Proteome Res. 4:2070-2080(2005).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-78, AND MASS SPECTROMETRY.
"Glycoproteomics analysis of human liver tissue by combination ofmultiple enzyme digestion and hydrazide chemistry.";
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
J. Proteome Res. 8:651-661(2009).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-51, AND MASS SPECTROMETRY.
"Enrichment of glycopeptides for glycan structure and attachment siteidentification.";
Nilsson J., Rueetschi U., Halim A., Hesse C., Carlsohn E.,Brinkmalm G., Larson G.;
Nat. Methods 6:809-811(2009).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-51 AND ASN-78, STRUCTUREOF CARBOHYDRATES, AND MASS SPECTROMETRY.
"Human urinary glycoproteomics; attachment site specific analysis ofN-and O-linked glycosylations by CID and ECD.";
Halim A., Nilsson J., Ruetschi U., Hesse C., Larson G.;
Mol. Cell. Proteomics 0:0-0(2011).
Cited for: GLYCOSYLATION AT ASN-78, STRUCTURE OF CARBOHYDRATES, AND MASSSPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures