dbPTM

PROS_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PROS_HUMAN
UniProt AC	P07225
Protein Name	Vitamin K-dependent protein S
Gene Name	PROS1
Organism	Homo sapiens (Human).
Sequence Length	676
Subcellular Localization	Secreted.
Protein Description	Anticoagulant plasma protein; it is a cofactor to activated protein C in the degradation of coagulation factors Va and VIIIa. It helps to prevent coagulation and stimulating fibrinolysis..
Protein Sequence	MRVLGGRCGALLACLLLVLPVSEANFLSKQQASQVLVRKRRANSLLEETKQGNLERECIEELCNKEEAREVFENDPETDYFYPKYLVCLRSFQTGLFTAARQSTNAYPDLRSCVNAIPDQCSPLPCNEDGYMSCKDGKASFTCTCKPGWQGEKCEFDINECKDPSNINGGCSQICDNTPGSYHCSCKNGFVMLSNKKDCKDVDECSLKPSICGTAVCKNIPGDFECECPEGYRYNLKSKSCEDIDECSENMCAQLCVNYPGGYTCYCDGKKGFKLAQDQKSCEVVSVCLPLNLDTKYELLYLAEQFAGVVLYLKFRLPEISRFSAEFDFRTYDSEGVILYAESIDHSAWLLIALRGGKIEVQLKNEHTSKITTGGDVINNGLWNMVSVEELEHSISIKIAKEAVMDINKPGPLFKPENGLLETKVYFAGFPRKVESELIKPINPRLDGCIRSWNLMKQGASGIKEIIQEKQNKHCLVTVEKGSYYPGSGIAQFHIDYNNVSSAEGWHVNVTLNIRPSTGTGVMLALVSGNNTVPFAVSLVDSTSEKSQDILLSVENTVIYRIQALSLCSDQQSHLEFRVNRNNLELSTPLKIETISHEDLQRQLAVLDKAMKAKVATYLGGLPDVPFSATPVNAFYNGCMEVNINGVQLDLDEAISKHNDIRAHSCPSVWKKTKNS

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
47	Gamma-carboxyglutamic_acid	RRANSLLEETKQGNL HHHHHHHHHHHCCCH	69.76	2820795
47	4-carboxyglutamate	RRANSLLEETKQGNL HHHHHHHHHHHCCCH	69.76	-
47	Gamma-carboxyglutamic_acid	RRANSLLEETKQGNL HHHHHHHHHHHCCCH	69.76	2820795
48	4-carboxyglutamate	RANSLLEETKQGNLE HHHHHHHHHHCCCHH	62.36	-
48	Gamma-carboxyglutamic_acid	RANSLLEETKQGNLE HHHHHHHHHHCCCHH	62.36	2820795
48	Gamma-carboxyglutamic_acid	RANSLLEETKQGNLE HHHHHHHHHHCCCHH	62.36	2820795
55	Gamma-carboxyglutamic_acid	ETKQGNLERECIEEL HHHCCCHHHHHHHHH	50.89	2820795
55	Gamma-carboxyglutamic_acid	ETKQGNLERECIEEL HHHCCCHHHHHHHHH	50.89	2820795
55	4-carboxyglutamate	ETKQGNLERECIEEL HHHCCCHHHHHHHHH	50.89	-
57	Gamma-carboxyglutamic_acid	KQGNLERECIEELCN HCCCHHHHHHHHHCC	30.39	2820795
57	4-carboxyglutamate	KQGNLERECIEELCN HCCCHHHHHHHHHCC	30.39	-
57	Gamma-carboxyglutamic_acid	KQGNLERECIEELCN HCCCHHHHHHHHHCC	30.39	2820795
60	4-carboxyglutamate	NLERECIEELCNKEE CHHHHHHHHHCCHHH	57.48	-
60	Gamma-carboxyglutamic_acid	NLERECIEELCNKEE CHHHHHHHHHCCHHH	57.48	2820795
60	Gamma-carboxyglutamic_acid	NLERECIEELCNKEE CHHHHHHHHHCCHHH	57.48	2820795
61	4-carboxyglutamate	LERECIEELCNKEEA HHHHHHHHHCCHHHH	38.42	-
61	Gamma-carboxyglutamic_acid	LERECIEELCNKEEA HHHHHHHHHCCHHHH	38.42	2820795
61	Gamma-carboxyglutamic_acid	LERECIEELCNKEEA HHHHHHHHHCCHHHH	38.42	2820795
66	4-carboxyglutamate	IEELCNKEEAREVFE HHHHCCHHHHHHHHC	42.78	-
66	Gamma-carboxyglutamic_acid	IEELCNKEEAREVFE HHHHCCHHHHHHHHC	42.78	2820795
66	Gamma-carboxyglutamic_acid	IEELCNKEEAREVFE HHHHCCHHHHHHHHC	42.78	2820795
67	Gamma-carboxyglutamic_acid	EELCNKEEAREVFEN HHHCCHHHHHHHHCC	55.42	2820795
67	Gamma-carboxyglutamic_acid	EELCNKEEAREVFEN HHHCCHHHHHHHHCC	55.42	2820795
67	4-carboxyglutamate	EELCNKEEAREVFEN HHHCCHHHHHHHHCC	55.42	-
70	Gamma-carboxyglutamic_acid	CNKEEAREVFENDPE CCHHHHHHHHCCCCC	59.62	2820795
70	4-carboxyglutamate	CNKEEAREVFENDPE CCHHHHHHHHCCCCC	59.62	-
70	Gamma-carboxyglutamic_acid	CNKEEAREVFENDPE CCHHHHHHHHCCCCC	59.62	2820795
73	Gamma-carboxyglutamic_acid	EEAREVFENDPETDY HHHHHHHCCCCCCCC	66.94	2820795
73	Gamma-carboxyglutamic_acid	EEAREVFENDPETDY HHHHHHHCCCCCCCC	66.94	2820795
73	4-carboxyglutamate	EEAREVFENDPETDY HHHHHHHCCCCCCCC	66.94	-
77	Gamma-carboxyglutamic_acid	EVFENDPETDYFYPK HHHCCCCCCCCCCHH	58.12	2820795
77	4-carboxyglutamate	EVFENDPETDYFYPK HHHCCCCCCCCCCHH	58.12	-
77	Gamma-carboxyglutamic_acid	EVFENDPETDYFYPK HHHCCCCCCCCCCHH	58.12	2820795
78	Phosphorylation	VFENDPETDYFYPKY HHCCCCCCCCCCHHH	41.19	-
91	Phosphorylation	KYLVCLRSFQTGLFT HHHHHHHHHHCCHHH	14.57	22210691
98	O-linked_Glycosylation	SFQTGLFTAARQSTN HHHCCHHHHHHHCCC	25.17	OGP
104	Phosphorylation	FTAARQSTNAYPDLR HHHHHHCCCCCCCHH	18.61	-
104	O-linked_Glycosylation	FTAARQSTNAYPDLR HHHHHHCCCCCCCHH	18.61	OGP
110	Phosphorylation	STNAYPDLRSCVNAI CCCCCCCHHHHHHCC	3.62	-
122	Phosphorylation	NAIPDQCSPLPCNED HCCCCCCCCCCCCCC	24.68	-
122	O-linked_Glycosylation	NAIPDQCSPLPCNED HCCCCCCCCCCCCCC	24.68	OGP
136	Hydroxylation	DGYMSCKDGKASFTC CCCEECCCCCEEEEE	69.06	-
259	Phosphorylation	CAQLCVNYPGGYTCY HHHHHHCCCCCEEEE	5.26	-
266	Phosphorylation	YPGGYTCYCDGKKGF CCCCEEEEECCCCCE	5.93	-
297	Phosphorylation	PLNLDTKYELLYLAE ECCCCCHHHHHHHHH	17.57	27461979
301	Phosphorylation	DTKYELLYLAEQFAG CCHHHHHHHHHHHHH	19.25	27461979
312	Phosphorylation	QFAGVVLYLKFRLPE HHHHHHHEEEECCCC	9.02	27461979
331	Phosphorylation	SAEFDFRTYDSEGVI EEEEECCEECCCCEE	31.51	25072903
332	Phosphorylation	AEFDFRTYDSEGVIL EEEECCEECCCCEEE	17.14	25072903
334	Phosphorylation	FDFRTYDSEGVILYA EECCEECCCCEEEEE	26.32	25072903
340	Phosphorylation	DSEGVILYAESIDHS CCCCEEEEEEECCCH	9.37	25072903
343	Phosphorylation	GVILYAESIDHSAWL CEEEEEEECCCHHHH	25.74	25072903
347	Phosphorylation	YAESIDHSAWLLIAL EEEECCCHHHHHHHH	19.86	25072903
394	Phosphorylation	SVEELEHSISIKIAK CHHHHCCCEEEEEHH	14.51	24719451
396	Phosphorylation	EELEHSISIKIAKEA HHHCCCEEEEEHHHH	22.35	24719451
423	Phosphorylation	PENGLLETKVYFAGF CCCCCEEEEEEECCC	26.27	29083192
499	N-linked_Glycosylation	QFHIDYNNVSSAEGW EEEEECCCCCCCCCE	28.90	UniProtKB CARBOHYD
509	N-linked_Glycosylation	SAEGWHVNVTLNIRP CCCCEEEEEEEEEEC	14.25	UniProtKB CARBOHYD
530	N-linked_Glycosylation	MLALVSGNNTVPFAV EEEEEECCCCCCEEE	33.23	16335952
531	N-linked_Glycosylation	LALVSGNNTVPFAVS EEEEECCCCCCEEEE	46.08	2940598
562	N-linked_Glycosylation	ENTVIYRIQALSLCS ECCCHHHHHHHHHCC	1.25	16335952
594	Phosphorylation	STPLKIETISHEDLQ CCCEEEEECCHHHHH	31.11	28270605
596	Phosphorylation	PLKIETISHEDLQRQ CEEEEECCHHHHHHH	28.39	28270605

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

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of PROS_HUMAN !!

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 PROS_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
FA5_HUMAN	F5	physical	10593904
RSSA_HUMAN	RPSA	physical	21988832
TBK1_HUMAN	TBK1	physical	21988832
C4BPB_HUMAN	C4BPB	physical	9628846

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
612336	Thrombophilia due to protein S deficiency, autosomal dominant (THPH5)
614514	Thrombophilia due to protein S deficiency, autosomal recessive (THPH6)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of PROS_HUMAN

Related Literatures of Post-Translational Modification

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-530, AND MASSSPECTROMETRY.	16335952 [Abstract]