FA7_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: FA7_HUMAN
• UniProt AC: P08709
• Protein Name: Coagulation factor VII
• Gene Name: F7
• Organism: Homo sapiens (Human).
• Sequence Length: 466
• Subcellular Localization: Secreted.
• Protein Description: Initiates the extrinsic pathway of blood coagulation. Serine protease that circulates in the blood in a zymogen form. Factor VII is converted to factor VIIa by factor Xa, factor XIIa, factor IXa, or thrombin by minor proteolysis. In the presence of tissue factor and calcium ions, factor VIIa then converts factor X to factor Xa by limited proteolysis. Factor VIIa will also convert factor IX to factor IXa in the presence of tissue factor and calcium..
• Protein Sequence: MVSQALRLLCLLLGLQGCLAAGGVAKASGGETRDMPWKPGPHRVFVTQEEAHGVLHRRRRANAFLEELRPGSLERECKEEQCSFEEAREIFKDAERTKLFWISYSDGDQCASSPCQNGGSCKDQLQSYICFCLPAFEGRNCETHKDDQLICVNENGGCEQYCSDHTGTKRSCRCHEGYSLLADGVSCTPTVEYPCGKIPILEKRNASKPQGRIVGGKVCPKGECPWQVLLLVNGAQLCGGTLINTIWVVSAAHCFDKIKNWRNLIAVLGEHDLSEHDGDEQSRRVAQVIIPSTYVPGTTNHDIALLRLHQPVVLTDHVVPLCLPERTFSERTLAFVRFSLVSGWGQLLDRGATALELMVLNVPRLMTQDCLQQSRKVGDSPNITEYMFCAGYSDGSKDSCKGDSGGPHATHYRGTWYLTGIVSWGQGCATVGHFGVYTRVSQYIEWLQKLMRSEPRPGVLLRAPFP

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
66	Gamma-carboxyglutamic_acid	RRANAFLEELRPGSL HHHHHHHHHHCCCCH	48.83	3264725
66	Gamma-carboxyglutamic_acid	RRANAFLEELRPGSL HHHHHHHHHHCCCCH	48.83	3264725
66	4-carboxyglutamate	RRANAFLEELRPGSL HHHHHHHHHHCCCCH	48.83	-
67	4-carboxyglutamate	RANAFLEELRPGSLE HHHHHHHHHCCCCHH	52.83	-
67	Gamma-carboxyglutamic_acid	RANAFLEELRPGSLE HHHHHHHHHCCCCHH	52.83	3264725
67	Gamma-carboxyglutamic_acid	RANAFLEELRPGSLE HHHHHHHHHCCCCHH	52.83	3264725
72	Phosphorylation	LEELRPGSLERECKE HHHHCCCCHHHHHHH	29.73	26091039
74	4-carboxyglutamate	ELRPGSLERECKEEQ HHCCCCHHHHHHHHC	48.40	-
74	Gamma-carboxyglutamic_acid	ELRPGSLERECKEEQ HHCCCCHHHHHHHHC	48.40	3264725
74	Gamma-carboxyglutamic_acid	ELRPGSLERECKEEQ HHCCCCHHHHHHHHC	48.40	3264725
76	Gamma-carboxyglutamic_acid	RPGSLERECKEEQCS CCCCHHHHHHHHCCC	40.33	3264725
76	Gamma-carboxyglutamic_acid	RPGSLERECKEEQCS CCCCHHHHHHHHCCC	40.33	3264725
76	4-carboxyglutamate	RPGSLERECKEEQCS CCCCHHHHHHHHCCC	40.33	-
79	Gamma-carboxyglutamic_acid	SLERECKEEQCSFEE CHHHHHHHHCCCHHH	66.03	3264725
79	4-carboxyglutamate	SLERECKEEQCSFEE CHHHHHHHHCCCHHH	66.03	-
79	Gamma-carboxyglutamic_acid	SLERECKEEQCSFEE CHHHHHHHHCCCHHH	66.03	3264725
80	Gamma-carboxyglutamic_acid	LERECKEEQCSFEEA HHHHHHHHCCCHHHH	42.24	3264725
80	Gamma-carboxyglutamic_acid	LERECKEEQCSFEEA HHHHHHHHCCCHHHH	42.24	3264725
80	4-carboxyglutamate	LERECKEEQCSFEEA HHHHHHHHCCCHHHH	42.24	-
85	Gamma-carboxyglutamic_acid	KEEQCSFEEAREIFK HHHCCCHHHHHHHHH	34.16	3264725
85	4-carboxyglutamate	KEEQCSFEEAREIFK HHHCCCHHHHHHHHH	34.16	-
85	Gamma-carboxyglutamic_acid	KEEQCSFEEAREIFK HHHCCCHHHHHHHHH	34.16	3264725
86	4-carboxyglutamate	EEQCSFEEAREIFKD HHCCCHHHHHHHHHH	51.52	-
86	Gamma-carboxyglutamic_acid	EEQCSFEEAREIFKD HHCCCHHHHHHHHHH	51.52	3264725
86	Gamma-carboxyglutamic_acid	EEQCSFEEAREIFKD HHCCCHHHHHHHHHH	51.52	3264725
89	4-carboxyglutamate	CSFEEAREIFKDAER CCHHHHHHHHHHHCC	60.88	-
89	Gamma-carboxyglutamic_acid	CSFEEAREIFKDAER CCHHHHHHHHHHHCC	60.88	3264725
89	Gamma-carboxyglutamic_acid	CSFEEAREIFKDAER CCHHHHHHHHHHHCC	60.88	3264725
95	Gamma-carboxyglutamic_acid	REIFKDAERTKLFWI HHHHHHHCCCEEEEE	71.64	3264725
95	Gamma-carboxyglutamic_acid	REIFKDAERTKLFWI HHHHHHHCCCEEEEE	71.64	3264725
95	4-carboxyglutamate	REIFKDAERTKLFWI HHHHHHHCCCEEEEE	71.64	-
112	O-linked_Glycosylation	SDGDQCASSPCQNGG CCCCCCCCCCCCCCC	42.30	2511201
120	O-linked_Glycosylation	SPCQNGGSCKDQLQS CCCCCCCCHHHHHHH	21.28	9023546
123	Hydroxylation	QNGGSCKDQLQSYIC CCCCCHHHHHHHHHH	59.77	3264725
186	Phosphorylation	SLLADGVSCTPTVEY CEECCCEECCCCEEC	20.15	-
205	N-linked_Glycosylation	IPILEKRNASKPQGR CCEEHHCCCCCCCCE	60.68	3264725
205	N-linked_Glycosylation	IPILEKRNASKPQGR CCEEHHCCCCCCCCE	60.68	19167329
298	Sulfoxidation	PSTYVPGTTNHDIAL CCCCCCCCCCHHEEE	20.53	10079116
306	Sulfoxidation	TNHDIALLRLHQPVV CCHHEEEEEECCCEE	3.96	10079116
382	N-linked_Glycosylation	RKVGDSPNITEYMFC HHHCCCCCCEEEEEE	58.74	3264725
382	N-linked_Glycosylation	RKVGDSPNITEYMFC HHHCCCCCCEEEEEE	58.74	19167329
443	Phosphorylation	VYTRVSQYIEWLQKL HHHHHHHHHHHHHHH	8.03	24719451
453	Phosphorylation	WLQKLMRSEPRPGVL HHHHHHCCCCCCCCE	37.68	22210691

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

Oops, there are no upstream regulatory protein records of FA7_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
205	N	Glycosylation	N-glycosylation at Asn-205 occurs cotranslationally and is mediated by STT3A-containing complexes, while glycosylation at Asn-382 is post-translational and is mediated STT3B-containing complexes before folding.	3264725
382	N	Glycosylation	N-glycosylation at Asn-205 occurs cotranslationally and is mediated by STT3A-containing complexes, while glycosylation at Asn-382 is post-translational and is mediated STT3B-containing complexes before folding.	3264725

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of FA7_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
TF_HUMAN	F3	physical	9925787
ZN363_HUMAN	RCHY1	physical	21988832
C1QRF_HUMAN	C1QL1	physical	28514442
NMU_HUMAN	NMU	physical	28514442
CREL2_HUMAN	CRELD2	physical	28514442

Drug and Disease Associations

• Kegg Disease
• There are no disease associations of PTM sites.
• OMIM Disease
• 227500: Factor VII deficiency (FA7D)
• 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

Gamma-carboxyglutamic acid

"Characterization of a cDNA coding for human factor VII.";
Hagen F.S., Gray C.L., O'Hara P.J., Grant F.J., Saari G.C.,Woodbury R.G., Hart C.E., Insley M.Y., Kisiel W., Kurachi K.,Davie E.W.;
Proc. Natl. Acad. Sci. U.S.A. 83:2412-2416(1986).
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A AND B).
PubMed: 3486420

N-linked Glycosylation

"Amino acid sequence and posttranslational modifications of humanfactor VIIa from plasma and transfected baby hamster kidney cells.";
Thim L., Bjoern S., Christensen M., Nicolaisen E.M., Lund-Hansen T.,Pedersen A.H., Hedner U.;
Biochemistry 27:7785-7793(1988).
Cited for: PROTEIN SEQUENCE OF 61-466, AND POST-TRANSLATIONAL MODIFICATIONS.
PubMed: 3264725

O-linked Glycosylation

"Human plasma and recombinant factor VII. Characterization of O-glycosylations at serine residues 52 and 60 and effects of site-directed mutagenesis of serine 52 to alanine.";
Bjoern S., Foster D.C., Thim L., Wiberg F.C., Christensen M.,Komiyama Y., Pedersen A.H., Kisiel W.;
J. Biol. Chem. 266:11051-11057(1991).
Cited for: GLYCOSYLATION AT SER-112 AND SER-120.
PubMed: 1904059