PTGDS_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: PTGDS_HUMAN
• UniProt AC: P41222
• Protein Name: Prostaglandin-H2 D-isomerase
• Gene Name: PTGDS
• Organism: Homo sapiens (Human).
• Sequence Length: 190
• Subcellular Localization: Rough endoplasmic reticulum . Nucleus membrane . Golgi apparatus . Cytoplasm, perinuclear region . Secreted . Detected on rough endoplasmic reticulum of arachnoid and menigioma cells. Localized to the nuclear envelope, Golgi apparatus, secretory vesi
• Protein Description: 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: MATHHTLWMGLALLGVLGDLQAAPEAQVSVQPNFQQDKFLGRWFSAGLASNSSWLREKKAALSMCKSVVAPATDGGLNLTSTFLRKNQCETRTMLLQPAGSLGSYSYRSPHWGSTYSVSVVETDYDQYALLYSQGSKGPGEDFRMATLYSRTQTPRAELKEKFTAFCKAQGFTEDTIVFLPQTDKCMTEQ

Overview of Protein Modification Sites with Functional and Structural Information

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
29	O-linked_Glycosylation	AAPEAQVSVQPNFQQ HCCCCEEEECCCCCC	11.71	23234360
51	N-linked_Glycosylation	FSAGLASNSSWLREK HHHHHCCCCHHHHHH	34.16	19838169
51	N-linked_Glycosylation	FSAGLASNSSWLREK HHHHHCCCCHHHHHH	34.16	19838169
53	Phosphorylation	AGLASNSSWLREKKA HHHCCCCHHHHHHHH	34.09	24719451
78	N-linked_Glycosylation	PATDGGLNLTSTFLR CCCCCCCCHHHHHHH	44.54	22171320
78	N-linked_Glycosylation	PATDGGLNLTSTFLR CCCCCCCCHHHHHHH	44.54	22171320
93	Phosphorylation	KNQCETRTMLLQPAG HCCCCCCEEEEEECC	21.42	23663014
101	Phosphorylation	MLLQPAGSLGSYSYR EEEEECCCCCCCEEC	31.50	23663014
104	Phosphorylation	QPAGSLGSYSYRSPH EECCCCCCCEECCCC	19.05	23663014
105	Phosphorylation	PAGSLGSYSYRSPHW ECCCCCCCEECCCCC	14.13	23663014
106	Phosphorylation	AGSLGSYSYRSPHWG CCCCCCCEECCCCCC	18.77	24719451
107	Phosphorylation	GSLGSYSYRSPHWGS CCCCCCEECCCCCCC	13.58	23663014
147	Phosphorylation	GEDFRMATLYSRTQT CHHCHHHHHHCCCCC	19.52	24043423
149	Phosphorylation	DFRMATLYSRTQTPR HCHHHHHHCCCCCCC	7.55	18083107
150	Phosphorylation	FRMATLYSRTQTPRA CHHHHHHCCCCCCCH	31.78	24043423
152	Phosphorylation	MATLYSRTQTPRAEL HHHHHCCCCCCCHHH	30.74	24043423
154	Phosphorylation	TLYSRTQTPRAELKE HHHCCCCCCCHHHHH	17.71	24043423
173	Phosphorylation	FCKAQGFTEDTIVFL HHHHCCCCCCEEEEE	39.51	25072903
176	Phosphorylation	AQGFTEDTIVFLPQT HCCCCCCEEEEECCC	16.89	25072903
183	Phosphorylation	TIVFLPQTDKCMTEQ EEEEECCCCCCCCCC	35.17	25072903
188	Phosphorylation	PQTDKCMTEQ----- CCCCCCCCCC-----	40.48	25072903

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of PTGDS_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of PTGDS_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of PTGDS_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
PTGDS_HUMAN	PTGDS	physical	12627223
HRSL4_HUMAN	RARRES3	physical	22960220
HXK2_RAT	Hk2	physical	11068878
HXK3_RAT	Hk3	physical	11068878
PD2R_HUMAN	PTGDR	physical	24493589
HS90A_HUMAN	HSP90AA1	physical	24493589
KR107_HUMAN	KRTAP10-7	physical	25416956
KR103_HUMAN	KRTAP10-3	physical	25416956
ARRB2_HUMAN	ARRB2	physical	21112970
CHIO_HUMAN	CHN2	physical	28514442

Drug and Disease Associations

• Kegg Disease
• There are no disease associations of PTM sites.
• OMIM Disease
• There are no disease associations of PTM sites.
• Kegg Drug
• There are no disease associations of PTM sites.
• DrugBank
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

N-linked Glycosylation

"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.
PubMed: 22171320

"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.
PubMed: 19838169

"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.
PubMed: 19159218

"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.
PubMed: 16335952

"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.
PubMed: 8336134