EPCR_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: EPCR_HUMAN
• UniProt AC: Q9UNN8
• Protein Name: Endothelial protein C receptor
• Gene Name: PROCR
• Organism: Homo sapiens (Human).
• Sequence Length: 238
• Subcellular Localization: Membrane; Single-pass type I membrane protein.
• Protein Description: Binds activated protein C. Enhances protein C activation by the thrombin-thrombomodulin complex; plays a role in the protein C pathway controlling blood coagulation..
• Protein Sequence: MLTTLLPILLLSGWAFCSQDASDGLQRLHMLQISYFRDPYHVWYQGNASLGGHLTHVLEGPDTNTTIIQLQPLQEPESWARTQSGLQSYLLQFHGLVRLVHQERTLAFPLTIRCFLGCELPPEGSRAHVFFEVAVNGSSFVSFRPERALWQADTQVTSGVVTFTLQQLNAYNRTRYELREFLEDTCVQYVQKHISAENTKGSQTSRSYTSLVLGVLVGSFIIAGVAVGIFLCTGGRRC

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
3	Phosphorylation	-----MLTTLLPILL -----CCCCHHHHHH	17.69	24043423
4	Phosphorylation	----MLTTLLPILLL ----CCCCHHHHHHH	23.49	24043423
12	Phosphorylation	LLPILLLSGWAFCSQ HHHHHHHHHHHHCCC	32.05	24043423
18	Phosphorylation	LSGWAFCSQDASDGL HHHHHHCCCCCCHHH	25.33	24043423
22	Phosphorylation	AFCSQDASDGLQRLH HHCCCCCCHHHHHHH	40.27	24043423
34	Phosphorylation	RLHMLQISYFRDPYH HHHEEEEEECCCCCE	12.78	24043423
35	Phosphorylation	LHMLQISYFRDPYHV HHEEEEEECCCCCEE	12.31	24043423
47	N-linked_Glycosylation	YHVWYQGNASLGGHL CEEEEECCCCCCCEE	15.72	11099506
47	N-linked_Glycosylation	YHVWYQGNASLGGHL CEEEEECCCCCCCEE	15.72	11099506
64	N-linked_Glycosylation	VLEGPDTNTTIIQLQ EEECCCCCCEEEEEE	42.47	11099506
64	N-linked_Glycosylation	VLEGPDTNTTIIQLQ EEECCCCCCEEEEEE	42.47	11099506
136	N-linked_Glycosylation	VFFEVAVNGSSFVSF EEEEEEECCCCEEEE	34.59	11099506
136	N-linked_Glycosylation	VFFEVAVNGSSFVSF EEEEEEECCCCEEEE	34.59	11099506
172	N-linked_Glycosylation	LQQLNAYNRTRYELR HHHHHCCCCHHHHHH	36.11	11099506
172	N-linked_Glycosylation	LQQLNAYNRTRYELR HHHHHCCCCHHHHHH	36.11	11099506
195	Phosphorylation	QYVQKHISAENTKGS HHHHHHHCCCCCCCC	29.29	29759185
204	Phosphorylation	ENTKGSQTSRSYTSL CCCCCCCCCHHHHHH	28.01	-
205	Phosphorylation	NTKGSQTSRSYTSLV CCCCCCCCHHHHHHH	16.16	24719451
219	Phosphorylation	VLGVLVGSFIIAGVA HHHHHHHHHHHHHHH	13.04	24719451

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

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

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of EPCR_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 EPCR_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
VATH_HUMAN	ATP6V1H	physical	22939629
PAR1_HUMAN	F2R	physical	20826780
CAV1_HUMAN	CAV1	physical	20826780

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

"The crystal structure of the endothelial protein C receptor and abound phospholipid.";
Oganesyan V., Oganesyan N., Terzyan S., Qu D., Dauter Z., Esmon N.L.,Esmon C.T.;
J. Biol. Chem. 277:24851-24854(2002).
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 18-210, GLYCOSYLATION ATASN-47; ASN-136 AND ASN-172, AND DISULFIDE BOND.
PubMed: 12034704