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P13726

- TF_HUMAN

UniProt

P13726 - TF_HUMAN

Protein

Tissue factor

Gene

F3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
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    • History
      Entry version 167 (01 Oct 2014)
      Sequence version 1 (01 Jan 1990)
      Previous versions | rss
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    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
    3. protein binding Source: UniProtKB

    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

    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: BHF-UCL
    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

    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

    ArrayExpressiP13726.
    BgeeiP13726.
    CleanExiHS_F3.
    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. 5 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[»]
    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.
    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: P13726-1) [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

    METPAWPRVP RPETAVARTL LLGWVFAQVA GASGTTNTVA AYNLTWKSTN    50
    FKTILEWEPK PVNQVYTVQI STKSGDWKSK CFYTTDTECD LTDEIVKDVK 100
    QTYLARVFSY PAGNVESTGS AGEPLYENSP EFTPYLETNL GQPTIQSFEQ 150
    VGTKVNVTVE DERTLVRRNN TFLSLRDVFG KDLIYTLYYW KSSSSGKKTA 200
    KTNTNEFLID VDKGENYCFS VQAVIPSRTV NRKSTDSPVE CMGQEKGEFR 250
    EIFYIIGAVV FVVIILVIIL AISLHKCRKA GVGQSWKENS PLNVS 295
    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 [» ]
    ProteinModelPortali P13726.
    SMRi P13726. Positions 38-242.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108451. 5 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.
    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

    ArrayExpressi P13726.
    Bgeei P13726.
    CleanExi HS_F3.
    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

    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 1, 2014
    This is version 167 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