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P13726 (TF_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 165. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Tissue factor

Short name=TF
Alternative name(s):
Coagulation factor III
Thromboplastin
CD_antigen=CD142
Gene names
Name:F3
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length295 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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 processBlood coagulation
Hemostasis
   Cellular componentMembrane
Secreted
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainSignal
Transmembrane
Transmembrane helix
   PTMDisulfide bond
Glycoprotein
Lipoprotein
Palmitate
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processactivation 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

Traceable author statement. Source: Reactome

blood coagulation, extrinsic pathway

Traceable author statement. Source: Reactome

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

Inferred from mutant phenotype PubMed 18612547. Source: BHF-UCL

   Cellular_componentcell surface

Inferred from direct assay PubMed 17898544. Source: BHF-UCL

extracellular matrix

Inferred from direct assay PubMed 2704749. Source: BHF-UCL

extracellular space

Inferred from direct assay PubMed 19065458. Source: BHF-UCL

integral component of membrane

Traceable author statement Ref.3. Source: ProtInc

intrinsic component of external side of plasma membrane

Inferred by curator PubMed 17469850. Source: BHF-UCL

plasma membrane

Traceable author statement. Source: Reactome

   Molecular_functionphospholipid binding

Inferred from direct assay PubMed 17469850. Source: BHF-UCL

protease binding

Inferred from physical interaction PubMed 3455766. Source: BHF-UCL

protein binding

Inferred from physical interaction Ref.15. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

F7P087095EBI-1040727,EBI-355972

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3232
Chain33 – 295263Tissue factor
PRO_0000033638

Regions

Topological domain33 – 251219Extracellular Potential
Transmembrane252 – 27423Helical; Potential
Topological domain275 – 29521Cytoplasmic Potential
Motif46 – 483WKS motif
Motif77 – 793WKS motif
Motif190 – 1923WKS motif

Amino acid modifications

Lipidation2771S-palmitoyl cysteine Ref.13
Glycosylation1561N-linked (GlcNAc...) Potential
Glycosylation1691N-linked (GlcNAc...) Potential
Disulfide bond81 ↔ 89 Ref.13
Disulfide bond218 ↔ 241 Ref.13

Natural variations

Alternative sequence199 – 23840TAKTN…STDSP → YSTSLELWYLWSSSLSSSWL YLYTSVERQEWGRAGRRTPH in isoform 2.
VSP_041896
Alternative sequence239 – 29557Missing in isoform 2.
VSP_041897
Natural variant361T → A. Ref.9
Corresponds to variant rs3917604 [ dbSNP | Ensembl ].
VAR_014298
Natural variant1451I → V. Ref.9
Corresponds to variant rs3917627 [ dbSNP | Ensembl ].
VAR_014299
Natural variant1631R → W.
Corresponds to variant rs5901 [ dbSNP | Ensembl ].
VAR_012008
Natural variant2811G → E.
Corresponds to variant rs3789683 [ dbSNP | Ensembl ].
VAR_052280

Experimental info

Sequence conflict2601V → A in AAA61151. Ref.1

Secondary structure

..................................................... 295
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (flTF) [UniParc].

Last modified January 1, 1990. Version 1.
Checksum: D3486C713ED8EAD0

FASTA29533,068
        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 

« Hide

Isoform 2 (asHTF) [UniParc].

Checksum: 5021EDB85C12B48C
Show »

FASTA23827,145

References

« Hide '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. expand/collapse author list , 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. expand/collapse author list , 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.
CCDSCCDS53345.1. [P13726-2]
CCDS750.1. [P13726-1]
PIRKFHU3. A43645.
RefSeqNP_001171567.1. NM_001178096.1. [P13726-2]
NP_001984.1. NM_001993.4. [P13726-1]
UniGeneHs.62192.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1AHWX-ray3.00C/F33-251[»]
1BOYX-ray2.20A33-251[»]
1DANX-ray2.00T37-116[»]
U122-242[»]
1FAKX-ray2.10T37-242[»]
1J9CX-ray2.90T33-242[»]
1JPSX-ray1.85T33-251[»]
1NL8model-T33-242[»]
1O5DX-ray2.05T34-251[»]
1TFHX-ray2.40A/B33-251[»]
1UJ3X-ray2.10C38-242[»]
1W0YX-ray2.50T33-242[»]
1W2KX-ray3.00T33-242[»]
1WQVX-ray2.50T33-250[»]
1WSSX-ray2.60T33-250[»]
1WTGX-ray2.20T33-250[»]
1WUNX-ray2.40T33-250[»]
1WV7X-ray2.70T33-250[»]
1Z6JX-ray2.00T33-243[»]
2A2QX-ray1.80T38-242[»]
2AEIX-ray2.52T33-243[»]
2AERX-ray1.87T38-242[»]
2B7DX-ray2.24T34-251[»]
2B8OX-ray2.80T38-242[»]
2C4FX-ray1.72T38-112[»]
U123-242[»]
2CEFNMR-A277-295[»]
2CEHNMR-A277-295[»]
2CEZNMR-A277-295[»]
2CFJNMR-A277-295[»]
2EC9X-ray2.00T38-112[»]
U123-242[»]
2F9BX-ray2.54T34-251[»]
2FIRX-ray2.00T38-242[»]
2FLBX-ray1.95T34-251[»]
2FLRX-ray2.35T34-251[»]
2HFTX-ray1.69A33-243[»]
2PUQX-ray2.05T38-241[»]
2ZP0X-ray2.70T33-250[»]
2ZWLX-ray2.20T33-250[»]
2ZZUX-ray2.50T33-250[»]
3ELAX-ray2.20T33-241[»]
3TH2X-ray1.72T38-242[»]
3TH3X-ray2.70T38-242[»]
3TH4X-ray1.80T38-242[»]
4IBLX-ray1.80T33-251[»]
ProteinModelPortalP13726.
SMRP13726. Positions 38-242.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108451. 5 interactions.
DIPDIP-6136N.
IntActP13726. 1 interaction.
STRING9606.ENSP00000334145.

Chemistry

BindingDBP13726.
ChEMBLCHEMBL2095194.
DrugBankDB00036. Coagulation factor VIIa.

PTM databases

PhosphoSiteP13726.

Polymorphism databases

DMDM135666.

Proteomic databases

MaxQBP13726.
PaxDbP13726.
PRIDEP13726.

Protocols and materials databases

DNASU2152.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000334047; ENSP00000334145; ENSG00000117525. [P13726-1]
ENST00000370207; ENSP00000359226; ENSG00000117525. [P13726-2]
GeneID2152.
KEGGhsa:2152.
UCSCuc001dqr.3. human. [P13726-1]
uc001dqs.3. human. [P13726-2]

Organism-specific databases

CTD2152.
GeneCardsGC01M094994.
HGNCHGNC:3541. F3.
HPACAB009438.
HPA049292.
MIM134390. gene.
neXtProtNX_P13726.
PharmGKBPA158.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG43483.
HOGENOMHOG000043076.
HOVERGENHBG005051.
InParanoidP13726.
KOK03901.
OMATECDLTD.
OrthoDBEOG7C2R28.
PhylomeDBP13726.
TreeFamTF352627.

Enzyme and pathway databases

ReactomeREACT_604. Hemostasis.

Gene expression databases

ArrayExpressP13726.
BgeeP13726.
CleanExHS_F3.
GenevestigatorP13726.

Family and domain databases

Gene3D2.60.40.10. 2 hits.
InterProIPR003961. Fibronectin_type3.
IPR013783. Ig-like_fold.
IPR015373. Interferon_alpha/beta_rcpt_bsu.
IPR016354. Tissue_fac/coagulation_fac-3.
IPR001187. Tissue_factor.
[Graphical view]
PfamPF09294. Interfer-bind. 1 hit.
PF01108. Tissue_fac. 1 hit.
[Graphical view]
PIRSFPIRSF002498. Tissue_factor_3. 1 hit.
PRINTSPR00346. TISSUEFACTOR.
SUPFAMSSF49265. SSF49265. 2 hits.
PROSITEPS00621. TISSUE_FACTOR. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSF3. human.
EvolutionaryTraceP13726.
GeneWikiTissue_factor.
GenomeRNAi2152.
NextBio8697.
PROP13726.
SOURCESearch...

Entry information

Entry nameTF_HUMAN
AccessionPrimary (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: July 9, 2014
This is version 165 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM

Human cell differentiation molecules

CD nomenclature of surface proteins of human leucocytes and list of entries