P13726 (TF_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Tissue factor
Short name=TF

Alternative name(s):
Coagulation factor III
Thromboplastin
CD_antigen=CD142

Gene names

Name:

F3

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	295 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.6
Subunit structure	Interacts with HSPE; the interaction, inhibited by heparin, promotes the generation of activated factor X and activates coagulation in the presence of activated factor VII. Ref.15
Subcellular location	Isoform 1: Membrane; Single-pass type I membrane protein Ref.6. Isoform 2: Secreted Ref.6.
Tissue specificity	Lung, placenta and pancreas. Ref.6
Induction	TF expression is highly dependent upon cell type. TF can also be induced by the inflammatory mediators interleukin 1 and TNF-alpha, as well as by endotoxin, to appear on monocytes and vascular endothelial cells as a component of cellular immune response. Ref.14
Sequence similarities	Belongs to the tissue factor family.

Ontologies

Keywords
Biological process	Blood coagulation Hemostasis
Cellular component	Membrane Secreted
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Signal Transmembrane Transmembrane helix
PTM	Disulfide bond Glycoprotein Lipoprotein Palmitate
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	activation of blood coagulation via clotting cascade Inferred by curator PubMed 17469850. Source: BHF-UCL activation of cysteine-type endopeptidase activity involved in apoptotic process Inferred from direct assay PubMed 17898544. Source: BHF-UCL activation of plasma proteins involved in acute inflammatory response Inferred from direct assay PubMed 17469850. Source: BHF-UCL blood coagulation, extrinsic pathway Traceable author statement. Source: Reactome negative regulation of apoptotic process Traceable author statement PubMed 18612547. Source: BHF-UCL positive regulation of angiogenesis Inferred from direct assay PubMed 17898544. Source: BHF-UCL positive regulation of cell migration Traceable author statement PubMed 18612547. Source: BHF-UCL positive regulation of endothelial cell proliferation Inferred from direct assay PubMed 17898544. Source: BHF-UCL positive regulation of platelet-derived growth factor receptor signaling pathway Inferred from direct assay PubMed 17991872. Source: BHF-UCL positive regulation of positive chemotaxis Inferred by curator PubMed 17991872. Source: BHF-UCL positive regulation of protein kinase B signaling cascade Inferred from mutant phenotype PubMed 18612547. Source: BHF-UCL
Cellular_component	extracellular matrix Inferred from direct assay PubMed 2704749. Source: BHF-UCL extracellular space Inferred from direct assay PubMed 19065458. Source: BHF-UCL integral to membrane Traceable author statement Ref.3. Source: ProtInc intrinsic to external side of plasma membrane Inferred by curator PubMed 17469850. Source: BHF-UCL
Molecular_function	cell surface binding Inferred from direct assay PubMed 17898544. Source: BHF-UCL phospholipid binding Inferred from direct assay PubMed 17469850. Source: BHF-UCL
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Note: Additional isoforms may exist.

Isoform 1 (identifier: P13726-1)

Also known as: flTF;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: P13726-2)

Also known as: asHTF;

The sequence of this isoform differs from the canonical sequence as follows:
     199-238: TAKTNTNEFL...TVNRKSTDSP → YSTSLELWYL...WGRAGRRTPH
     239-295: Missing.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 32

32

Chain

33 – 295

263

Tissue factor

PRO_0000033638

Regions

Topological domain

33 – 251

219

Extracellular Potential

Transmembrane

252 – 274

23

Helical; Potential

Topological domain

275 – 295

21

Cytoplasmic Potential

Motif

46 – 48

3

WKS motif

Motif

77 – 79

3

WKS motif

Motif

190 – 192

3

WKS motif

Amino acid modifications

Lipidation

277

1

S-palmitoyl cysteine Ref.13

Glycosylation

156

1

N-linked (GlcNAc...) Potential

Glycosylation

169

1

N-linked (GlcNAc...) Potential

Disulfide bond

81 ↔ 89

Ref.13

Disulfide bond

218 ↔ 241

Ref.13

Natural variations

Alternative sequence

199 – 238

40

TAKTN…STDSP → YSTSLELWYLWSSSLSSSWL YLYTSVERQEWGRAGRRTPH in isoform 2.

VSP_041896

Alternative sequence

239 – 295

57

Missing in isoform 2.

VSP_041897

Natural variant

36

1

T → A. Ref.9
Corresponds to variant rs3917604 [ dbSNP | Ensembl ].

VAR_014298

Natural variant

145

1

I → V. Ref.9
Corresponds to variant rs3917627 [ dbSNP | Ensembl ].

VAR_014299

Natural variant

163

1

R → W.
Corresponds to variant rs5901 [ dbSNP | Ensembl ].

VAR_012008

Natural variant

281

1

G → E.
Corresponds to variant rs3789683 [ dbSNP | Ensembl ].

VAR_052280

Experimental info

Sequence conflict

260

1

V → A in AAA61151. Ref.1

Secondary structure

1

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295

Helix Strand Turn

Details...

Beta strand

42 – 49

8

Beta strand

52 – 58

7

Beta strand

62 – 72

11

Beta strand

73 – 75

3

Beta strand

78 – 85

8

Beta strand

87 – 90

4

Helix

92 – 95

4

Helix

96 – 98

3

Beta strand

103 – 111

9

Helix

113 – 115

3

Turn

120 – 122

3

Beta strand

126 – 128

3

Helix

134 – 137

4

Beta strand

145 – 151

7

Beta strand

154 – 159

6

Beta strand

163 – 168

6

Beta strand

171 – 174

4

Helix

175 – 179

5

Helix

180 – 182

3

Beta strand

184 – 190

7

Beta strand

194 – 196

3

Beta strand

198 – 210

13

Beta strand

213 – 215

3

Beta strand

218 – 224

7

Beta strand

229 – 231

3

Beta strand

240 – 243

4

Beta strand

279 – 284

6

Beta strand

289 – 293

5

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (flTF) [UniParc]. Last modified January 1, 1990. Version 1. Checksum: D3486C713ED8EAD0	FASTA	295	33,068
	10 20 30 40 50 60 METPAWPRVP RPETAVARTL LLGWVFAQVA GASGTTNTVA AYNLTWKSTN FKTILEWEPK 70 80 90 100 110 120 PVNQVYTVQI STKSGDWKSK CFYTTDTECD LTDEIVKDVK QTYLARVFSY PAGNVESTGS 130 140 150 160 170 180 AGEPLYENSP EFTPYLETNL GQPTIQSFEQ VGTKVNVTVE DERTLVRRNN TFLSLRDVFG 190 200 210 220 230 240 KDLIYTLYYW KSSSSGKKTA KTNTNEFLID VDKGENYCFS VQAVIPSRTV NRKSTDSPVE 250 260 270 280 290 CMGQEKGEFR EIFYIIGAVV FVVIILVIIL AISLHKCRKA GVGQSWKENS PLNVS
	Isoform 2 (asHTF) [UniParc]. Checksum: 5021EDB85C12B48C	FASTA	238	27,145
	10 20 30 40 50 60 METPAWPRVP RPETAVARTL LLGWVFAQVA GASGTTNTVA AYNLTWKSTN FKTILEWEPK 70 80 90 100 110 120 PVNQVYTVQI STKSGDWKSK CFYTTDTECD LTDEIVKDVK QTYLARVFSY PAGNVESTGS 130 140 150 160 170 180 AGEPLYENSP EFTPYLETNL GQPTIQSFEQ VGTKVNVTVE DERTLVRRNN TFLSLRDVFG 190 200 210 220 230 KDLIYTLYYW KSSSSGKKYS TSLELWYLWS SSLSSSWLYL YTSVERQEWG RAGRRTPH

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Human tissue factor: cDNA sequence and chromosome localization of the gene." Scarpati E.M., Wen D., Broze G.J. Jr., Miletich J.P., Flandermeyer R.R., Siegel N.R., Sadler J.E. Biochemistry 26:5234-5238(1987) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]	"Molecular cloning of the cDNA for tissue factor, the cellular receptor for the initiation of the coagulation protease cascade." Morrissey J.H., Fakhrai H., Edgington T.S. Cell 50:129-135(1987) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[3]	"Isolation of cDNA clones coding for human tissue factor: primary structure of the protein and cDNA." Spicer E.K., Horton R., Bloem L., Bach R., Williams K.R., Guha A., Kraus J., Lin T.C., Nemerson Y., Konigsberg W.H. Proc. Natl. Acad. Sci. U.S.A. 84:5148-5152(1987) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[4]	"Cloning and expression of human tissue factor cDNA." Fisher K.L., Gorman C.M., Vehar G.A., O'Brien D.P., Lawn R.M. Thromb. Res. 48:89-99(1987) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[5]	"Complete sequence of the human tissue factor gene, a highly regulated cellular receptor that initiates the coagulation protease cascade." Mackman N., Morrissey J.H., Fowler B., Edgington T.S. Biochemistry 28:1755-1762(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[6]	"Alternatively spliced human tissue factor: a circulating, soluble, thrombogenic protein." Bogdanov V.Y., Balasubramanian V., Hathcock J., Vele O., Lieb M., Nemerson Y. Nat. Med. 9:458-462(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[7]	"Cloning of human full-length CDSs in BD Creator(TM) system donor vector." Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A. Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[8]	"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)." Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B. Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[9]	SeattleSNPs variation discovery resource Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ALA-36 AND VAL-145.
[10]	"The DNA sequence and biological annotation of human chromosome 1." Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R. Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[11]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[12]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Prostate.
[13]	"Human tissue factor contains thioester-linked palmitate and stearate on the cytoplasmic half-cystine." Bach R., Konigsberg W.H., Nemerson Y. Biochemistry 27:4227-4231(1988) [PubMed] [Europe PMC] [Abstract] Cited for: DISULFIDE BONDS, PALMITOYLATION AT CYS-277.
[14]	"Cdc2-like kinases and DNA topoisomerase I regulate alternative splicing of tissue factor in human endothelial cells." Eisenreich A., Bogdanov V.Y., Zakrzewicz A., Pries A., Antoniak S., Poller W., Schultheiss H.P., Rauch U. Circ. Res. 104:589-599(2009) [PubMed] [Europe PMC] [Abstract] Cited for: ALTERNATIVE SPLICING, INDUCTION.
[15]	"Heparanase enhances the generation of activated factor X in the presence of tissue factor and activated factor VII." Nadir Y., Brenner B., Fux L., Shafat I., Attias J., Vlodavsky I. Haematologica 95:1927-1934(2010) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH HPSE.
[16]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[17]	"Structure of the extracellular domain of human tissue factor: location of the factor VIIa binding site." Muller Y.A., Ultsch M.H., Kelley R.F., de Vos A.M. Biochemistry 33:10864-10870(1994) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 33-243.
[18]	"The crystal structure of the extracellular domain of human tissue factor refined to 1.7-A resolution." Muller Y.A., Ultsch M.H., de Vos A.M. J. Mol. Biol. 256:144-159(1996) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 33-243.
[19]	"The crystal structure of the complex of blood coagulation factor VIIa with soluble tissue factor." Banner D.W., D'Arcy A., Chene C., Winkler F.K., Guha A., Konigsberg W.H., Nemreson Y., Kirchhofer D. Nature 380:41-46(1996) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 33-251 IN COMPLEX WITH FVIIA.
[20]	"Structure of extracellular tissue factor complexed with factor VIIa inhibited with a BPTI mutant." Zhang E., St Charles R., Tulinsky A. J. Mol. Biol. 285:2089-2104(1999) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 37-242 IN COMPLEX WITH FVIIA.
+	Additional computationally mapped references.

Web resources

SeattleSNPs

SHMPD

The Singapore human mutation and polymorphism database

Wikipedia

Tissue factor entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M16553 mRNA. Translation: AAA61151.1.
J02931 mRNA. Translation: AAA61150.1.
M27436 mRNA. Translation: AAA36734.1.
J02846 Genomic DNA. Translation: AAA61152.1.
BT019808 mRNA. Translation: AAV38611.1.
CR541792 mRNA. Translation: CAG46591.1.
AF487337 mRNA. Translation: AAO61150.1.
AF540377 Genomic DNA. Translation: AAN01236.1.
AC093117 Genomic DNA. No translation available.
CH471097 Genomic DNA. Translation: EAW73044.1.
CH471097 Genomic DNA. Translation: EAW73045.1.
BC011029 mRNA. Translation: AAH11029.1.

IPI

IPI00010338.

PIR

KFHU3. A43645.

RefSeq

NP_001171567.1. NM_001178096.1.
NP_001984.1. NM_001993.4.

UniGene

Hs.62192.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1AHW	X-ray	3.00	C/F	33-251	[»]
1BOY	X-ray	2.20	A	33-251	[»]
1DAN	X-ray	2.00	T	37-116	[»]
			U	122-242	[»]
1FAK	X-ray	2.10	T	37-242	[»]
1J9C	X-ray	2.90	T	33-242	[»]
1JPS	X-ray	1.85	T	33-251	[»]
1NL8	model	-	T	33-242	[»]
1O5D	X-ray	2.05	T	34-251	[»]
1TFH	X-ray	2.40	A/B	33-251	[»]
1UJ3	X-ray	2.10	C	38-242	[»]
1W0Y	X-ray	2.50	T	33-242	[»]
1W2K	X-ray	3.00	T	33-242	[»]
1WQV	X-ray	2.50	T	33-250	[»]
1WSS	X-ray	2.60	T	33-250	[»]
1WTG	X-ray	2.20	T	33-250	[»]
1WUN	X-ray	2.40	T	33-250	[»]
1WV7	X-ray	2.70	T	33-250	[»]
1Z6J	X-ray	2.00	T	33-243	[»]
2A2Q	X-ray	1.80	T	38-242	[»]
2AEI	X-ray	2.52	T	33-243	[»]
2AER	X-ray	1.87	T	38-242	[»]
2B7D	X-ray	2.24	T	34-251	[»]
2B8O	X-ray	2.80	T	38-242	[»]
2C4F	X-ray	1.72	T	38-112	[»]
			U	123-242	[»]
2CEF	NMR	-	A	277-295	[»]
2CEH	NMR	-	A	277-295	[»]
2CEZ	NMR	-	A	277-295	[»]
2CFJ	NMR	-	A	277-295	[»]
2EC9	X-ray	2.00	T	38-112	[»]
			U	123-242	[»]
2F9B	X-ray	2.54	T	34-251	[»]
2FIR	X-ray	2.00	T	38-242	[»]
2FLB	X-ray	1.95	T	34-251	[»]
2FLR	X-ray	2.35	T	34-251	[»]
2HFT	X-ray	1.69	A	33-243	[»]
2PUQ	X-ray	2.05	T	38-241	[»]
2ZP0	X-ray	2.70	T	33-250	[»]
2ZWL	X-ray	2.20	T	33-250	[»]
2ZZU	X-ray	2.50	T	33-250	[»]
3ELA	X-ray	2.20	T	33-241	[»]
3TH2	X-ray	1.72	T	38-242	[»]
3TH3	X-ray	2.70	T	38-242	[»]
3TH4	X-ray	1.80	T	38-242	[»]

ProteinModelPortal

P13726.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-6136N.

IntAct

P13726. 1 interaction.

STRING

9606.ENSP00000334145.

PTM databases

PhosphoSite

P13726.

Polymorphism databases

DMDM

135666.

Proteomic databases

PaxDb

P13726.

PRIDE

P13726.

Protocols and materials databases

DNASU

2152.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000334047; ENSP00000334145; ENSG00000117525.
ENST00000370207; ENSP00000359226; ENSG00000117525.

GeneID

2152.

KEGG

hsa:2152.

UCSC

uc001dqr.3. human.

Organism-specific databases

CTD

2152.

GeneCards

GC01M094994.

HGNC

HGNC:3541. F3.

HPA

CAB009438.

MIM

134390. gene.

neXtProt

NX_P13726.

PharmGKB

PA158.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG43483.

HOGENOM

HOG000043076.

HOVERGEN

HBG005051.

InParanoid

P13726.

KO

K03901.

OMA

TECDLTD.

OrthoDB

EOG4D7Z6C.

PhylomeDB

P13726.

Enzyme and pathway databases

Reactome

REACT_604. Hemostasis.

Gene expression databases

ArrayExpress

P13726.

Bgee

P13726.

CleanEx

HS_F3.

Genevestigator

P13726.

GermOnline

ENSG00000117525. Homo sapiens.

Family and domain databases

Gene3D

2.60.40.10. 2 hits.

InterPro

IPR003961. Fibronectin_type3.
IPR013783. Ig-like_fold.
IPR015373. Interferon_alpha/beta_rcpt_bsu.
IPR016354. Tissue_fac/coagulation_fac-3.
IPR001187. Tissue_factor.
[Graphical view]

Pfam

PF09294. Interfer-bind. 1 hit.
[Graphical view]

PIRSF

PIRSF002498. Tissue_factor_3. 1 hit.

PRINTS

PR00346. TISSUEFACTOR.

SUPFAM

SSF49265. FN_III-like. 2 hits.

PROSITE

PS00621. TISSUE_FACTOR. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

P13726.

ChEMBL

CHEMBL4081.

ChiTaRS

F3. human.

DrugBank

DB00036. Coagulation factor VIIa.

EvolutionaryTrace

P13726.

GenomeRNAi

2152.

NextBio

8697.

SOURCE

Search...

Entry information

Entry name

TF_HUMAN

Accession

Primary (citable) accession number: P13726
Secondary accession number(s): D3DT47, Q6FHG2, Q86WH4

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1990
Last sequence update:	January 1, 1990
Last modified:	May 1, 2013
This is version 152 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.