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P13726

- TF_HUMAN

UniProt

P13726 - TF_HUMAN

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Protein

Tissue factor

Gene

F3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.1 Publication

GO - Molecular functioni

  1. phospholipid binding Source: BHF-UCL
  2. protease binding Source: BHF-UCL

GO - Biological processi

  1. activation of blood coagulation via clotting cascade Source: BHF-UCL
  2. activation of cysteine-type endopeptidase activity involved in apoptotic process Source: BHF-UCL
  3. activation of plasma proteins involved in acute inflammatory response Source: BHF-UCL
  4. blood coagulation Source: Reactome
  5. blood coagulation, extrinsic pathway Source: Reactome
  6. positive regulation of angiogenesis Source: BHF-UCL
  7. positive regulation of cell migration Source: BHF-UCL
  8. positive regulation of endothelial cell proliferation Source: BHF-UCL
  9. positive regulation of platelet-derived growth factor receptor signaling pathway Source: BHF-UCL
  10. positive regulation of positive chemotaxis Source: BHF-UCL
  11. positive regulation of protein kinase B signaling Source: BHF-UCL
Complete GO annotation...

Keywords - Biological processi

Blood coagulation, Hemostasis

Enzyme and pathway databases

ReactomeiREACT_1573. Extrinsic Pathway.

Names & Taxonomyi

Protein namesi
Recommended name:
Tissue factor
Short name:
TF
Alternative name(s):
Coagulation factor III
Thromboplastin
CD_antigen: CD142
Gene namesi
Name:F3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:3541. F3.

Subcellular locationi

GO - Cellular componenti

  1. cell surface Source: UniProtKB
  2. extracellular matrix Source: BHF-UCL
  3. extracellular space Source: BHF-UCL
  4. extracellular vesicular exosome Source: UniProt
  5. integral component of membrane Source: ProtInc
  6. intrinsic component of external side of plasma membrane Source: BHF-UCL
  7. plasma membrane Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Secreted

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA158.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3232Add
BLAST
Chaini33 – 295263Tissue factorPRO_0000033638Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi81 ↔ 891 Publication
Glycosylationi156 – 1561N-linked (GlcNAc...)Sequence Analysis
Glycosylationi169 – 1691N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi218 ↔ 2411 Publication
Lipidationi277 – 2771S-palmitoyl cysteine1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, Lipoprotein, Palmitate

Proteomic databases

MaxQBiP13726.
PaxDbiP13726.
PRIDEiP13726.

PTM databases

PhosphoSiteiP13726.

Expressioni

Tissue specificityi

Lung, placenta and pancreas.1 Publication

Inductioni

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.1 Publication

Gene expression databases

BgeeiP13726.
CleanExiHS_F3.
ExpressionAtlasiP13726. baseline and differential.
GenevestigatoriP13726.

Organism-specific databases

HPAiCAB009438.
HPA049292.

Interactioni

Subunit structurei

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.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
F7P087096EBI-1040727,EBI-355972

Protein-protein interaction databases

BioGridi108451. 9 interactions.
DIPiDIP-6136N.
IntActiP13726. 1 interaction.
STRINGi9606.ENSP00000334145.

Structurei

Secondary structure

1
295
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi42 – 498
Beta strandi52 – 587
Beta strandi62 – 7211
Beta strandi73 – 753
Beta strandi78 – 858
Beta strandi87 – 904
Helixi92 – 954
Helixi96 – 983
Beta strandi103 – 1119
Helixi113 – 1153
Turni120 – 1223
Beta strandi126 – 1283
Helixi134 – 1374
Beta strandi145 – 1517
Beta strandi154 – 1596
Beta strandi163 – 1686
Beta strandi171 – 1744
Helixi175 – 1795
Helixi180 – 1823
Beta strandi184 – 1907
Beta strandi194 – 1963
Beta strandi198 – 21013
Beta strandi213 – 2153
Beta strandi218 – 2247
Beta strandi229 – 2313
Beta strandi240 – 2434
Beta strandi279 – 2846
Beta strandi289 – 2935

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
4M7LX-ray3.40T37-245[»]
ProteinModelPortaliP13726.
SMRiP13726. Positions 38-242.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP13726.

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini33 – 251219ExtracellularSequence AnalysisAdd
BLAST
Topological domaini275 – 29521CytoplasmicSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei252 – 27423HelicalSequence AnalysisAdd
BLAST

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi46 – 483WKS motif
Motifi77 – 793WKS motif
Motifi190 – 1923WKS motif

Sequence similaritiesi

Belongs to the tissue factor family.Curated

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG43483.
GeneTreeiENSGT00390000012668.
HOGENOMiHOG000043076.
HOVERGENiHBG005051.
InParanoidiP13726.
KOiK03901.
OMAiTECDLTD.
OrthoDBiEOG7C2R28.
PhylomeDBiP13726.
TreeFamiTF352627.

Family and domain databases

Gene3Di2.60.40.10. 2 hits.
InterProiIPR003961. Fibronectin_type3.
IPR013783. Ig-like_fold.
IPR015373. Interferon_alpha/beta_rcpt_bsu.
IPR016354. Tissue_fac/coagulation_fac-3.
IPR001187. Tissue_factor.
[Graphical view]
PfamiPF09294. Interfer-bind. 1 hit.
PF01108. Tissue_fac. 1 hit.
[Graphical view]
PIRSFiPIRSF002498. Tissue_factor_3. 1 hit.
PRINTSiPR00346. TISSUEFACTOR.
SUPFAMiSSF49265. SSF49265. 2 hits.
PROSITEiPS00621. TISSUE_FACTOR. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. Align

Note: Additional isoforms may exist.

Isoform 1 (identifier: P13726) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
METPAWPRVP RPETAVARTL LLGWVFAQVA GASGTTNTVA AYNLTWKSTN
60 70 80 90 100
FKTILEWEPK PVNQVYTVQI STKSGDWKSK CFYTTDTECD LTDEIVKDVK
110 120 130 140 150
QTYLARVFSY PAGNVESTGS AGEPLYENSP EFTPYLETNL GQPTIQSFEQ
160 170 180 190 200
VGTKVNVTVE DERTLVRRNN TFLSLRDVFG KDLIYTLYYW KSSSSGKKTA
210 220 230 240 250
KTNTNEFLID VDKGENYCFS VQAVIPSRTV NRKSTDSPVE CMGQEKGEFR
260 270 280 290
EIFYIIGAVV FVVIILVIIL AISLHKCRKA GVGQSWKENS PLNVS
Length:295
Mass (Da):33,068
Last modified:January 1, 1990 - v1
Checksum:iD3486C713ED8EAD0
GO
Isoform 2 (identifier: P13726-2) [UniParc]FASTAAdd to Basket

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.

Show »
Length:238
Mass (Da):27,145
Checksum:i5021EDB85C12B48C
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti260 – 2601V → A in AAA61151. (PubMed:2823875)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti36 – 361T → A.1 Publication
Corresponds to variant rs3917604 [ dbSNP | Ensembl ].
VAR_014298
Natural varianti145 – 1451I → V.1 Publication
Corresponds to variant rs3917627 [ dbSNP | Ensembl ].
VAR_014299
Natural varianti163 – 1631R → W.
Corresponds to variant rs5901 [ dbSNP | Ensembl ].
VAR_012008
Natural varianti281 – 2811G → E.
Corresponds to variant rs3789683 [ dbSNP | Ensembl ].
VAR_052280

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei199 – 23840TAKTN…STDSP → YSTSLELWYLWSSSLSSSWL YLYTSVERQEWGRAGRRTPH in isoform 2. 1 PublicationVSP_041896Add
BLAST
Alternative sequencei239 – 29557Missing in isoform 2. 1 PublicationVSP_041897Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS53345.1. [P13726-2]
CCDS750.1. [P13726-1]
PIRiA43645. KFHU3.
RefSeqiNP_001171567.1. NM_001178096.1. [P13726-2]
NP_001984.1. NM_001993.4. [P13726-1]
UniGeneiHs.62192.

Genome annotation databases

EnsembliENST00000334047; ENSP00000334145; ENSG00000117525. [P13726-1]
ENST00000370207; ENSP00000359226; ENSG00000117525. [P13726-2]
GeneIDi2152.
KEGGihsa:2152.
UCSCiuc001dqr.3. human. [P13726-1]
uc001dqs.3. human. [P13726-2]

Polymorphism databases

DMDMi135666.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

SeattleSNPs
SHMPD

The Singapore human mutation and polymorphism database

Wikipedia

Tissue factor entry

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS53345.1. [P13726-2 ]
CCDS750.1. [P13726-1 ]
PIRi A43645. KFHU3.
RefSeqi NP_001171567.1. NM_001178096.1. [P13726-2 ]
NP_001984.1. NM_001993.4. [P13726-1 ]
UniGenei Hs.62192.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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 [» ]
4IBL X-ray 1.80 T 33-251 [» ]
4M7L X-ray 3.40 T 37-245 [» ]
ProteinModelPortali P13726.
SMRi P13726. Positions 38-242.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 108451. 9 interactions.
DIPi DIP-6136N.
IntActi P13726. 1 interaction.
STRINGi 9606.ENSP00000334145.

Chemistry

BindingDBi P13726.
ChEMBLi CHEMBL2095194.
DrugBanki DB00036. Coagulation factor VIIa.

PTM databases

PhosphoSitei P13726.

Polymorphism databases

DMDMi 135666.

Proteomic databases

MaxQBi P13726.
PaxDbi P13726.
PRIDEi P13726.

Protocols and materials databases

DNASUi 2152.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000334047 ; ENSP00000334145 ; ENSG00000117525 . [P13726-1 ]
ENST00000370207 ; ENSP00000359226 ; ENSG00000117525 . [P13726-2 ]
GeneIDi 2152.
KEGGi hsa:2152.
UCSCi uc001dqr.3. human. [P13726-1 ]
uc001dqs.3. human. [P13726-2 ]

Organism-specific databases

CTDi 2152.
GeneCardsi GC01M094994.
HGNCi HGNC:3541. F3.
HPAi CAB009438.
HPA049292.
MIMi 134390. gene.
neXtProti NX_P13726.
PharmGKBi PA158.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG43483.
GeneTreei ENSGT00390000012668.
HOGENOMi HOG000043076.
HOVERGENi HBG005051.
InParanoidi P13726.
KOi K03901.
OMAi TECDLTD.
OrthoDBi EOG7C2R28.
PhylomeDBi P13726.
TreeFami TF352627.

Enzyme and pathway databases

Reactomei REACT_1573. Extrinsic Pathway.

Miscellaneous databases

ChiTaRSi F3. human.
EvolutionaryTracei P13726.
GeneWikii Tissue_factor.
GenomeRNAii 2152.
NextBioi 8697.
PROi P13726.
SOURCEi Search...

Gene expression databases

Bgeei P13726.
CleanExi HS_F3.
ExpressionAtlasi P13726. baseline and differential.
Genevestigatori P13726.

Family and domain databases

Gene3Di 2.60.40.10. 2 hits.
InterProi IPR003961. Fibronectin_type3.
IPR013783. Ig-like_fold.
IPR015373. Interferon_alpha/beta_rcpt_bsu.
IPR016354. Tissue_fac/coagulation_fac-3.
IPR001187. Tissue_factor.
[Graphical view ]
Pfami PF09294. Interfer-bind. 1 hit.
PF01108. Tissue_fac. 1 hit.
[Graphical view ]
PIRSFi PIRSF002498. Tissue_factor_3. 1 hit.
PRINTSi PR00346. TISSUEFACTOR.
SUPFAMi SSF49265. SSF49265. 2 hits.
PROSITEi PS00621. TISSUE_FACTOR. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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. 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.

Entry informationi

Entry nameiTF_HUMAN
AccessioniPrimary (citable) accession number: P13726
Secondary accession number(s): D3DT47, Q6FHG2, Q86WH4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 1, 1990
Last modified: October 29, 2014
This is version 168 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human cell differentiation molecules
    CD nomenclature of surface proteins of human leucocytes and list of entries
  2. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  3. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3