dbPTM

PROC_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PROC_HUMAN
UniProt AC	P04070
Protein Name	Vitamin K-dependent protein C
Gene Name	PROC
Organism	Homo sapiens (Human).
Sequence Length	461
Subcellular Localization	Secreted . Golgi apparatus . Endoplasmic reticulum .
Protein Description	Protein C is a vitamin K-dependent serine protease that regulates blood coagulation by inactivating factors Va and VIIIa in the presence of calcium ions and phospholipids. [PubMed: 25618265 Exerts a protective effect on the endothelial cell barrier function]
Protein Sequence	MWQLTSLLLFVATWGISGTPAPLDSVFSSSERAHQVLRIRKRANSFLEELRHSSLERECIEEICDFEEAKEIFQNVDDTLAFWSKHVDGDQCLVLPLEHPCASLCCGHGTCIDGIGSFSCDCRSGWEGRFCQREVSFLNCSLDNGGCTHYCLEEVGWRRCSCAPGYKLGDDLLQCHPAVKFPCGRPWKRMEKKRSHLKRDTEDQEDQVDPRLIDGKMTRRGDSPWQVVLLDSKKKLACGAVLIHPSWVLTAAHCMDESKKLLVRLGEYDLRRWEKWELDLDIKEVFVHPNYSKSTTDNDIALLHLAQPATLSQTIVPICLPDSGLAERELNQAGQETLVTGWGYHSSREKEAKRNRTFVLNFIKIPVVPHNECSEVMSNMVSENMLCAGILGDRQDACEGDSGGPMVASFHGTWFLVGLVSWGEGCGLLHNYGVYTKVSRYLDWIHGHIRDKEAPQKSWAP

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
5	Phosphorylation	---MWQLTSLLLFVA ---CCHHHHHHHHHH	11.39	24043423
6	Phosphorylation	--MWQLTSLLLFVAT --CCHHHHHHHHHHH	26.13	24043423
13	Phosphorylation	SLLLFVATWGISGTP HHHHHHHHHCCCCCC	20.94	24043423
17	Phosphorylation	FVATWGISGTPAPLD HHHHHCCCCCCCCHH	32.45	24043423
19	O-linked_Glycosylation	ATWGISGTPAPLDSV HHHCCCCCCCCHHHH	14.97	22171320
19	Phosphorylation	ATWGISGTPAPLDSV HHHCCCCCCCCHHHH	14.97	24043423
25	Phosphorylation	GTPAPLDSVFSSSER CCCCCHHHHCCCCHH	32.51	24043423
28	Phosphorylation	APLDSVFSSSERAHQ CCHHHHCCCCHHHHH	30.69	24043423
29	Phosphorylation	PLDSVFSSSERAHQV CHHHHCCCCHHHHHH	25.42	24505115
30	Phosphorylation	LDSVFSSSERAHQVL HHHHCCCCHHHHHHH	29.88	24505115
45	Phosphorylation	RIRKRANSFLEELRH HHHHHHHHHHHHHHC	30.17	27067055
48	Gamma-carboxyglutamic_acid	KRANSFLEELRHSSL HHHHHHHHHHHCCHH	53.64	2991887
48	Gamma-carboxyglutamic_acid	KRANSFLEELRHSSL HHHHHHHHHHHCCHH	53.64	2991887
48	4-carboxyglutamate	KRANSFLEELRHSSL HHHHHHHHHHHCCHH	53.64	-
49	Gamma-carboxyglutamic_acid	RANSFLEELRHSSLE HHHHHHHHHHCCHHH	53.93	2991887
49	4-carboxyglutamate	RANSFLEELRHSSLE HHHHHHHHHHCCHHH	53.93	-
49	Gamma-carboxyglutamic_acid	RANSFLEELRHSSLE HHHHHHHHHHCCHHH	53.93	2991887
56	Gamma-carboxyglutamic_acid	ELRHSSLERECIEEI HHHCCHHHHHHHHHH	48.67	2991887
56	4-carboxyglutamate	ELRHSSLERECIEEI HHHCCHHHHHHHHHH	48.67	-
56	Gamma-carboxyglutamic_acid	ELRHSSLERECIEEI HHHCCHHHHHHHHHH	48.67	2991887
58	4-carboxyglutamate	RHSSLERECIEEICD HCCHHHHHHHHHHCC	30.39	-
58	Gamma-carboxyglutamic_acid	RHSSLERECIEEICD HCCHHHHHHHHHHCC	30.39	2991887
58	Gamma-carboxyglutamic_acid	RHSSLERECIEEICD HCCHHHHHHHHHHCC	30.39	2991887
61	Gamma-carboxyglutamic_acid	SLERECIEEICDFEE HHHHHHHHHHCCHHH	53.63	2991887
61	4-carboxyglutamate	SLERECIEEICDFEE HHHHHHHHHHCCHHH	53.63	-
61	Gamma-carboxyglutamic_acid	SLERECIEEICDFEE HHHHHHHHHHCCHHH	53.63	2991887
62	Gamma-carboxyglutamic_acid	LERECIEEICDFEEA HHHHHHHHHCCHHHH	29.07	2991887
62	Gamma-carboxyglutamic_acid	LERECIEEICDFEEA HHHHHHHHHCCHHHH	29.07	2991887
62	4-carboxyglutamate	LERECIEEICDFEEA HHHHHHHHHCCHHHH	29.07	-
67	Gamma-carboxyglutamic_acid	IEEICDFEEAKEIFQ HHHHCCHHHHHHHHC	43.74	2991887
67	Gamma-carboxyglutamic_acid	IEEICDFEEAKEIFQ HHHHCCHHHHHHHHC	43.74	2991887
67	4-carboxyglutamate	IEEICDFEEAKEIFQ HHHHCCHHHHHHHHC	43.74	-
68	Gamma-carboxyglutamic_acid	EEICDFEEAKEIFQN HHHCCHHHHHHHHCC	66.10	2991887
68	Gamma-carboxyglutamic_acid	EEICDFEEAKEIFQN HHHCCHHHHHHHHCC	66.10	2991887
68	4-carboxyglutamate	EEICDFEEAKEIFQN HHHCCHHHHHHHHCC	66.10	-
71	4-carboxyglutamate	CDFEEAKEIFQNVDD CCHHHHHHHHCCCHH	56.96	-
71	Gamma-carboxyglutamic_acid	CDFEEAKEIFQNVDD CCHHHHHHHHCCCHH	56.96	2991887
71	Gamma-carboxyglutamic_acid	CDFEEAKEIFQNVDD CCHHHHHHHHCCCHH	56.96	2991887
113	Hydroxylation	CGHGTCIDGIGSFSC CCCCEEECCCCCEEC	44.82	2991887
139	N-linked_Glycosylation	QREVSFLNCSLDNGG CEEEEEEEEEECCCC	16.01	2033065
139	N-linked_Glycosylation	QREVSFLNCSLDNGG CEEEEEEEEEECCCC	16.01	2033065
233	Acetylation	QVVLLDSKKKLACGA EEEEECCCCCCCCEE	54.30	7823973
234	Acetylation	VVLLDSKKKLACGAV EEEECCCCCCCCEEE	57.90	7823983
268	Phosphorylation	LLVRLGEYDLRRWEK HHHHHCHHCHHHHHH	20.62	23403867
290	N-linked_Glycosylation	KEVFVHPNYSKSTTD EEEEECCCCCCCCCC	38.54	2991887
290	N-linked_Glycosylation	KEVFVHPNYSKSTTD EEEEECCCCCCCCCC	38.54	2991887
347	Phosphorylation	TGWGYHSSREKEAKR CCCCCCCCHHHHHHH	31.01	8292730
355	N-linked_Glycosylation	REKEAKRNRTFVLNF HHHHHHHCCEEEEEE	46.79	2991887
355	N-linked_Glycosylation	REKEAKRNRTFVLNF HHHHHHHCCEEEEEE	46.79	2991887
371	N-linked_Glycosylation	KIPVVPHNECSEVMS ECCCCCCHHHHHHHH	45.99	2033065
371	N-linked_Glycosylation	KIPVVPHNECSEVMS ECCCCCCHHHHHHHH	45.99	2991887
382	O-linked_Glycosylation	EVMSNMVSENMLCAG HHHHHCCCCCCCCCH	16.69	OGP

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

Modified Location	Modified Residue	Modification	Type of Upstream Proteins	Gene Name of Upstream Proteins	UniProt AC of Upstream Proteins	Sources
347	S	Phosphorylation	Kinase	FAM20C	Q8IXL6	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
371	N	Glycosylation	2991887
Partial (70%) N-glycosylation of Asn-371 with an atypical N-X-C site produces a higher molecular weight form referred to as alpha.
371	N	Glycosylation	2991887
The lower molecular weight form, not N-glycosylated at Asn-371, is beta.

Disease-associated PTM Sites based on SAP

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

Modified Location	Modification	Variant Position (Distance <= 10)	Residue Change	SAP	Related Disease	Reference
Oops, there are no SNP-PTM records of PROC_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
EPCR_HUMAN	PROCR	physical	10681521
IPSP_HUMAN	SERPINA5	physical	11123896
EPHA6_HUMAN	EPHA6	physical	28514442
QCR6_HUMAN	UQCRH	physical	28514442
DEFM_HUMAN	PDF	physical	28514442
PROS_HUMAN	PROS1	physical	28514442
WNT5A_HUMAN	WNT5A	physical	28514442

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
176860	Thrombophilia due to protein C deficiency, autosomal dominant (THPH3)
612304	Thrombophilia due to protein C deficiency, autosomal recessive (THPH4)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of PROC_HUMAN

Related Literatures of Post-Translational Modification

Gamma-carboxyglutamic acid
Reference	PubMed
"The nucleotide sequence of the gene for human protein C."; Foster D.C., Yoshitake S., Davie E.W.; Proc. Natl. Acad. Sci. U.S.A. 82:4673-4677(1985). Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].	2991887 [Abstract]
N-linked Glycosylation
Reference	PubMed
"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-290, AND MASSSPECTROMETRY.	16335952 [Abstract]
"Beta protein C is not glycosylated at asparagine 329. The rate oftranslation may influence the frequency of usage at asparagine-X-cysteine sites."; Miletich J.P., Broze G.J. Jr.; J. Biol. Chem. 265:11397-11404(1990). Cited for: GLYCOSYLATION AT ASN-371.	1694179 [Abstract]
O-linked Glycosylation
Reference	PubMed
"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 THR-19, STRUCTURE OF CARBOHYDRATES, AND MASSSPECTROMETRY.	22171320 [Abstract]

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