dbPTM

TF_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	TF_HUMAN
UniProt AC	P13726
Protein Name	Tissue factor
Gene Name	F3
Organism	Homo sapiens (Human).
Sequence Length	295
Subcellular Localization	Isoform 1: Membrane Single-pass type I membrane protein . Isoform 2: Secreted .
Protein Description	Initiates blood coagulation by forming a complex with circulating factor VII or VIIa. The [TF:VIIa] complex activates factors IX or X by specific limited protolysis. TF plays a role in normal hemostasis by initiating the cell-surface assembly and propagation of the coagulation protease cascade..
Protein Sequence	METPAWPRVPRPETAVARTLLLGWVFAQVAGASGTTNTVAAYNLTWKSTNFKTILEWEPKPVNQVYTVQISTKSGDWKSKCFYTTDTECDLTDEIVKDVKQTYLARVFSYPAGNVESTGSAGEPLYENSPEFTPYLETNLGQPTIQSFEQVGTKVNVTVEDERTLVRRNNTFLSLRDVFGKDLIYTLYYWKSSSSGKKTAKTNTNEFLIDVDKGENYCFSVQAVIPSRTVNRKSTDSPVECMGQEKGEFREIFYIIGAVVFVVIILVIILAISLHKCRKAGVGQSWKENSPLNVS

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
60	Ubiquitination	TILEWEPKPVNQVYT EEEEEECCCCCEEEE	50.51	23503661
73	Ubiquitination	YTVQISTKSGDWKSK EEEEEEECCCCCCCC	45.72	23503661
78	Ubiquitination	STKSGDWKSKCFYTT EECCCCCCCCEEEEC	44.79	23503661
97	Ubiquitination	DLTDEIVKDVKQTYL CCCHHHHHHHHHHHH	63.57	22817900
100	Ubiquitination	DEIVKDVKQTYLARV HHHHHHHHHHHHHHE	47.24	21906983
120	Phosphorylation	GNVESTGSAGEPLYE CCCCCCCCCCCCCCC	32.94	-
156	N-linked_Glycosylation	EQVGTKVNVTVEDER HHCCCEEEEEECCHH	25.87	19349973
156	N-linked_Glycosylation	EQVGTKVNVTVEDER HHCCCEEEEEECCHH	25.87	19349973
169	N-linked_Glycosylation	ERTLVRRNNTFLSLR HHHHECCCCEEEEHH	41.13	UniProtKB CARBOHYD
171	Phosphorylation	TLVRRNNTFLSLRDV HHECCCCEEEEHHHH	29.51	19845377
174	Phosphorylation	RRNNTFLSLRDVFGK CCCCEEEEHHHHHCC	19.71	19845377
188	Phosphorylation	KDLIYTLYYWKSSSS CHHEEEEEEEECCCC	10.24	19845377
241	Glutathionylation	STDSPVECMGQEKGE CCCCCCCCCCCCCCC	3.65	22833525
277	S-palmitoylation	LAISLHKCRKAGVGQ HHHHHHHHHHCCCCC	3.62	3166978
285	Phosphorylation	RKAGVGQSWKENSPL HHCCCCCCCCCCCCC	33.90	18297283
287	Ubiquitination	AGVGQSWKENSPLNV CCCCCCCCCCCCCCC	52.87	23000965
287	Methylation	AGVGQSWKENSPLNV CCCCCCCCCCCCCCC	52.87	-
290	Phosphorylation	GQSWKENSPLNVS-- CCCCCCCCCCCCC--	31.68	25159151
295	Phosphorylation	ENSPLNVS------- CCCCCCCC-------	33.17	15630487

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
285	S	Phosphorylation	Kinase	PRKCA	P17252	GPS
285	S	Phosphorylation	Kinase	MAPK14	Q16539	GPS
285	S	Phosphorylation	Kinase	PKC-FAMILY	-	GPS
285	S	Phosphorylation	Kinase	PKC_GROUP	-	PhosphoELM
290	S	Phosphorylation	Kinase	PRKCA	P17252	GPS
290	S	Phosphorylation	Kinase	MAPK14	Q16539	GPS
290	S	Phosphorylation	Kinase	PKC-FAMILY	-	GPS
290	S	Phosphorylation	Kinase	PKC_GROUP	-	PhosphoELM

Functions of PTM Sites

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

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
FA7_HUMAN	F7	physical	12787023
DAD1_HUMAN	DAD1	physical	26186194
TM9S4_HUMAN	TM9SF4	physical	26186194
RAB13_HUMAN	RAB13	physical	26186194
STX12_HUMAN	STX12	physical	26186194
TM9S4_HUMAN	TM9SF4	physical	28514442
DAD1_HUMAN	DAD1	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.

Regulatory Network of TF_HUMAN

Related Literatures of Post-Translational Modification

Palmitoylation
Reference	PubMed
"Human tissue factor contains thioester-linked palmitate and stearateon the cytoplasmic half-cystine."; Bach R., Konigsberg W.H., Nemerson Y.; Biochemistry 27:4227-4231(1988). Cited for: DISULFIDE BONDS, AND PALMITOYLATION AT CYS-277.	3166978 [Abstract]