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P10646

- TFPI1_HUMAN

UniProt

P10646 - TFPI1_HUMAN

Protein

Tissue factor pathway inhibitor

Gene

TFPI

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 184 (01 Oct 2014)
      Sequence version 1 (01 Jul 1989)
      Previous versions | rss
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    Functioni

    Inhibits factor X (X(a)) directly and, in a Xa-dependent way, inhibits VIIa/tissue factor activity, presumably by forming a quaternary Xa/LACI/VIIa/TF complex. It possesses an antithrombotic action and also the ability to associate with lipoproteins in plasma.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei64 – 652Reactive bond
    Sitei135 – 1362Reactive bond
    Sitei227 – 2282Reactive bond
    Sitei256 – 2561Not glycosylated

    GO - Molecular functioni

    1. endopeptidase inhibitor activity Source: ProtInc
    2. serine-type endopeptidase inhibitor activity Source: UniProtKB-KW

    GO - Biological processi

    1. blood coagulation Source: Reactome
    2. blood coagulation, extrinsic pathway Source: Reactome
    3. negative regulation of endopeptidase activity Source: GOC

    Keywords - Molecular functioni

    Protease inhibitor, Serine protease inhibitor

    Keywords - Biological processi

    Blood coagulation, Hemostasis

    Enzyme and pathway databases

    ReactomeiREACT_1573. Extrinsic Pathway.

    Protein family/group databases

    MEROPSiI02.950.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Tissue factor pathway inhibitor
    Short name:
    TFPI
    Alternative name(s):
    Extrinsic pathway inhibitor
    Short name:
    EPI
    Lipoprotein-associated coagulation inhibitor
    Short name:
    LACI
    Gene namesi
    Name:TFPI
    Synonyms:LACI, TFPI1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:11760. TFPI.

    Subcellular locationi

    Isoform Beta : Microsome membrane 1 Publication; Lipid-anchorGPI-anchor 1 Publication

    GO - Cellular componenti

    1. anchored component of membrane Source: UniProtKB-KW
    2. endoplasmic reticulum Source: UniProtKB-KW
    3. extracellular region Source: Reactome
    4. extracellular space Source: BHF-UCL
    5. organelle membrane Source: UniProtKB-SubCell
    6. plasma membrane Source: Reactome

    Keywords - Cellular componenti

    Endoplasmic reticulum, Membrane, Microsome, Secreted

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi64 – 641K → I: Abolishes inhibition of VII(a)/TF.
    Mutagenesisi135 – 1351R → L: Abolishes inhibition of X(a).
    Mutagenesisi227 – 2271R → L: Abolishes inhibition of VII(a)/TF.

    Organism-specific databases

    PharmGKBiPA36475.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 28283 PublicationsAdd
    BLAST
    Chaini29 – 304276Tissue factor pathway inhibitor1 PublicationPRO_0000016871Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi42 – 421O-linked (GalNAc...); partial1 Publication
    Disulfide bondi54 ↔ 104PROSITE-ProRule annotation
    Disulfide bondi63 ↔ 87PROSITE-ProRule annotation
    Disulfide bondi79 ↔ 100PROSITE-ProRule annotation
    Disulfide bondi125 ↔ 175
    Disulfide bondi134 ↔ 158
    Glycosylationi145 – 1451N-linked (GlcNAc...)3 Publications
    Disulfide bondi150 ↔ 171
    Glycosylationi195 – 1951N-linked (GlcNAc...)2 Publications
    Glycosylationi202 – 2021O-linked (GalNAc...); partial2 Publications
    Glycosylationi203 – 2031O-linked (GalNAc...)2 Publications
    Disulfide bondi217 ↔ 267
    Disulfide bondi226 ↔ 250
    Disulfide bondi242 ↔ 263

    Post-translational modificationi

    O-glycosylated.3 Publications

    Keywords - PTMi

    Disulfide bond, Glycoprotein, GPI-anchor, Lipoprotein

    Proteomic databases

    MaxQBiP10646.
    PaxDbiP10646.
    PeptideAtlasiP10646.
    PRIDEiP10646.

    PTM databases

    PhosphoSiteiP10646.
    UniCarbKBiP10646.

    Miscellaneous databases

    PMAP-CutDBP10646.

    Expressioni

    Tissue specificityi

    Mostly in endothelial cells.

    Gene expression databases

    ArrayExpressiP10646.
    BgeeiP10646.
    CleanExiHS_TFPI.
    GenevestigatoriP10646.

    Organism-specific databases

    HPAiCAB020842.
    HPA005575.

    Interactioni

    Protein-protein interaction databases

    BioGridi112893. 12 interactions.
    STRINGi9606.ENSP00000233156.

    Structurei

    Secondary structure

    1
    304
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi31 – 399
    Helixi52 – 554
    Beta strandi67 – 737
    Turni74 – 774
    Beta strandi78 – 847
    Beta strandi94 – 963
    Helixi97 – 1048
    Beta strandi118 – 1203
    Helixi123 – 1264
    Beta strandi138 – 1447
    Turni145 – 1484
    Beta strandi149 – 1557
    Beta strandi157 – 1593
    Beta strandi165 – 1673
    Helixi168 – 1758
    Beta strandi178 – 1803
    Beta strandi215 – 2195
    Beta strandi224 – 2263
    Beta strandi232 – 2354
    Turni237 – 2393
    Beta strandi241 – 2455
    Beta strandi257 – 2604
    Helixi261 – 2677

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1ADZNMR-A118-182[»]
    1IRHNMR-A210-270[»]
    1TFXX-ray2.60C/D121-178[»]
    4BQDX-ray2.48A/B29-107[»]
    4DTGX-ray1.80K119-178[»]
    ProteinModelPortaliP10646.
    SMRiP10646. Positions 30-107, 120-178, 210-270.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP10646.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini54 – 10451BPTI/Kunitz inhibitor 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini125 – 17551BPTI/Kunitz inhibitor 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini217 – 26751BPTI/Kunitz inhibitor 3PROSITE-ProRule annotationAdd
    BLAST

    Domaini

    This inhibitor contains three inhibitory domains. The first domain interacts with VIIa and TF, the second one with Xa.

    Sequence similaritiesi

    Contains 3 BPTI/Kunitz inhibitor domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, Signal

    Phylogenomic databases

    eggNOGiNOG86404.
    HOGENOMiHOG000231818.
    HOVERGENiHBG056804.
    InParanoidiP10646.
    KOiK03909.
    OMAiFIQRISK.
    OrthoDBiEOG73FQKT.
    PhylomeDBiP10646.
    TreeFamiTF315349.

    Family and domain databases

    Gene3Di4.10.410.10. 3 hits.
    InterProiIPR002223. Prot_inh_Kunz-m.
    IPR008296. Prot_inhib_I2_TFPI.
    IPR020901. Prtase_inh_Kunz-CS.
    [Graphical view]
    PfamiPF00014. Kunitz_BPTI. 3 hits.
    [Graphical view]
    PIRSFiPIRSF001620. TFPI. 1 hit.
    PRINTSiPR00759. BASICPTASE.
    SMARTiSM00131. KU. 3 hits.
    [Graphical view]
    SUPFAMiSSF57362. SSF57362. 3 hits.
    PROSITEiPS00280. BPTI_KUNITZ_1. 3 hits.
    PS50279. BPTI_KUNITZ_2. 3 hits.
    [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

    Isoform Alpha (identifier: P10646-1) [UniParc]FASTAAdd to Basket

    Also known as: TFPIalpha

    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

    MIYTMKKVHA LWASVCLLLN LAPAPLNADS EEDEEHTIIT DTELPPLKLM    50
    HSFCAFKADD GPCKAIMKRF FFNIFTRQCE EFIYGGCEGN QNRFESLEEC 100
    KKMCTRDNAN RIIKTTLQQE KPDFCFLEED PGICRGYITR YFYNNQTKQC 150
    ERFKYGGCLG NMNNFETLEE CKNICEDGPN GFQVDNYGTQ LNAVNNSLTP 200
    QSTKVPSLFE FHGPSWCLTP ADRGLCRANE NRFYYNSVIG KCRPFKYSGC 250
    GGNENNFTSK QECLRACKKG FIQRISKGGL IKTKRKRKKQ RVKIAYEEIF 300
    VKNM 304
    Length:304
    Mass (Da):35,015
    Last modified:July 1, 1989 - v1
    Checksum:i5281E32B758B44FE
    GO
    Isoform Beta (identifier: P10646-2) [UniParc]FASTAAdd to Basket

    Also known as: TFPIbeta

    The sequence of this isoform differs from the canonical sequence as follows:
         210-251: EFHGPSWCLT...CRPFKYSGCG → VTKEGTNDGW...LGLDSISCLC
         252-304: Missing.

    Note: GPI-anchored.

    Show »
    Length:251
    Mass (Da):28,653
    Checksum:i9B3F276A52B4F0B9
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti292 – 2921V → M.1 Publication
    Corresponds to variant rs5940 [ dbSNP | Ensembl ].
    VAR_012004

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei210 – 25142EFHGP…YSGCG → VTKEGTNDGWKNAAHIYQVF LNAFCIHASMFFLGLDSISC LC in isoform Beta. 2 PublicationsVSP_003030Add
    BLAST
    Alternative sequencei252 – 30453Missing in isoform Beta. 2 PublicationsVSP_003031Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J03225 mRNA. Translation: AAA52022.1.
    M58650
    , M58644, M58645, M58646, M58647, M58648, M58649 Genomic DNA. Translation: AAA59480.1.
    M59499
    , M59493, M59494, M59495, M59496, M59497, M59498 Genomic DNA. Translation: AAA59526.1.
    AF021834 mRNA. Translation: AAD01700.1.
    AY263365 Genomic DNA. Translation: AAO89075.1.
    AC007319 Genomic DNA. Translation: AAY14807.1.
    CH471058 Genomic DNA. Translation: EAX10921.1.
    CH471058 Genomic DNA. Translation: EAX10922.1.
    BC015514 mRNA. Translation: AAH15514.1.
    CCDSiCCDS2294.1. [P10646-1]
    CCDS33349.1. [P10646-2]
    PIRiA23712. TIHUGK.
    RefSeqiNP_001027452.1. NM_001032281.2. [P10646-2]
    NP_006278.1. NM_006287.4. [P10646-1]
    XP_005246875.1. XM_005246818.1. [P10646-1]
    XP_005246876.1. XM_005246819.1. [P10646-1]
    XP_005246877.1. XM_005246820.1. [P10646-2]
    XP_006712783.1. XM_006712720.1. [P10646-1]
    UniGeneiHs.516578.

    Genome annotation databases

    EnsembliENST00000233156; ENSP00000233156; ENSG00000003436. [P10646-1]
    ENST00000339091; ENSP00000342306; ENSG00000003436. [P10646-2]
    ENST00000392365; ENSP00000376172; ENSG00000003436. [P10646-1]
    ENST00000409676; ENSP00000386344; ENSG00000003436. [P10646-2]
    GeneIDi7035.
    KEGGihsa:7035.
    UCSCiuc002upy.3. human. [P10646-1]
    uc002uqa.2. human. [P10646-2]

    Polymorphism databases

    DMDMi125932.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    Wikipedia

    TFPI entry

    SeattleSNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J03225 mRNA. Translation: AAA52022.1 .
    M58650
    , M58644 , M58645 , M58646 , M58647 , M58648 , M58649 Genomic DNA. Translation: AAA59480.1 .
    M59499
    , M59493 , M59494 , M59495 , M59496 , M59497 , M59498 Genomic DNA. Translation: AAA59526.1 .
    AF021834 mRNA. Translation: AAD01700.1 .
    AY263365 Genomic DNA. Translation: AAO89075.1 .
    AC007319 Genomic DNA. Translation: AAY14807.1 .
    CH471058 Genomic DNA. Translation: EAX10921.1 .
    CH471058 Genomic DNA. Translation: EAX10922.1 .
    BC015514 mRNA. Translation: AAH15514.1 .
    CCDSi CCDS2294.1. [P10646-1 ]
    CCDS33349.1. [P10646-2 ]
    PIRi A23712. TIHUGK.
    RefSeqi NP_001027452.1. NM_001032281.2. [P10646-2 ]
    NP_006278.1. NM_006287.4. [P10646-1 ]
    XP_005246875.1. XM_005246818.1. [P10646-1 ]
    XP_005246876.1. XM_005246819.1. [P10646-1 ]
    XP_005246877.1. XM_005246820.1. [P10646-2 ]
    XP_006712783.1. XM_006712720.1. [P10646-1 ]
    UniGenei Hs.516578.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1ADZ NMR - A 118-182 [» ]
    1IRH NMR - A 210-270 [» ]
    1TFX X-ray 2.60 C/D 121-178 [» ]
    4BQD X-ray 2.48 A/B 29-107 [» ]
    4DTG X-ray 1.80 K 119-178 [» ]
    ProteinModelPortali P10646.
    SMRi P10646. Positions 30-107, 120-178, 210-270.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112893. 12 interactions.
    STRINGi 9606.ENSP00000233156.

    Chemistry

    DrugBanki DB00036. Coagulation factor VIIa.

    Protein family/group databases

    MEROPSi I02.950.

    PTM databases

    PhosphoSitei P10646.
    UniCarbKBi P10646.

    Polymorphism databases

    DMDMi 125932.

    Proteomic databases

    MaxQBi P10646.
    PaxDbi P10646.
    PeptideAtlasi P10646.
    PRIDEi P10646.

    Protocols and materials databases

    DNASUi 7035.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000233156 ; ENSP00000233156 ; ENSG00000003436 . [P10646-1 ]
    ENST00000339091 ; ENSP00000342306 ; ENSG00000003436 . [P10646-2 ]
    ENST00000392365 ; ENSP00000376172 ; ENSG00000003436 . [P10646-1 ]
    ENST00000409676 ; ENSP00000386344 ; ENSG00000003436 . [P10646-2 ]
    GeneIDi 7035.
    KEGGi hsa:7035.
    UCSCi uc002upy.3. human. [P10646-1 ]
    uc002uqa.2. human. [P10646-2 ]

    Organism-specific databases

    CTDi 7035.
    GeneCardsi GC02M188328.
    HGNCi HGNC:11760. TFPI.
    HPAi CAB020842.
    HPA005575.
    MIMi 152310. gene.
    neXtProti NX_P10646.
    PharmGKBi PA36475.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG86404.
    HOGENOMi HOG000231818.
    HOVERGENi HBG056804.
    InParanoidi P10646.
    KOi K03909.
    OMAi FIQRISK.
    OrthoDBi EOG73FQKT.
    PhylomeDBi P10646.
    TreeFami TF315349.

    Enzyme and pathway databases

    Reactomei REACT_1573. Extrinsic Pathway.

    Miscellaneous databases

    ChiTaRSi TFPI. human.
    EvolutionaryTracei P10646.
    GeneWikii Tissue_factor_pathway_inhibitor.
    GenomeRNAii 7035.
    NextBioi 27483.
    PMAP-CutDB P10646.
    PROi P10646.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P10646.
    Bgeei P10646.
    CleanExi HS_TFPI.
    Genevestigatori P10646.

    Family and domain databases

    Gene3Di 4.10.410.10. 3 hits.
    InterProi IPR002223. Prot_inh_Kunz-m.
    IPR008296. Prot_inhib_I2_TFPI.
    IPR020901. Prtase_inh_Kunz-CS.
    [Graphical view ]
    Pfami PF00014. Kunitz_BPTI. 3 hits.
    [Graphical view ]
    PIRSFi PIRSF001620. TFPI. 1 hit.
    PRINTSi PR00759. BASICPTASE.
    SMARTi SM00131. KU. 3 hits.
    [Graphical view ]
    SUPFAMi SSF57362. SSF57362. 3 hits.
    PROSITEi PS00280. BPTI_KUNITZ_1. 3 hits.
    PS50279. BPTI_KUNITZ_2. 3 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and characterization of a cDNA coding for the lipoprotein-associated coagulation inhibitor shows that it consists of three tandem Kunitz-type inhibitory domains."
      Wun T.-C., Kretzmer K.K., Girard T.J., Miletich J.P., Broze G.J. Jr.
      J. Biol. Chem. 263:6001-6004(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA).
    2. "Identification of the 1.4 kb and 4.0 kb messages for the lipoprotein associated coagulation inhibitor and expression of the encoded protein."
      Girard T.J., Warren L.A., Novotny W.F., Bejcek B.E., Miletich J.P., Broze G.J. Jr.
      Thromb. Res. 55:37-50(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA).
    3. "Intron-exon organization of the human gene coding for the lipoprotein-associated coagulation inhibitor: the factor Xa dependent inhibitor of the extrinsic pathway of coagulation."
      van der Logt C.P.E., Reitsma P.H., Bertina R.M.
      Biochemistry 30:1571-1577(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM ALPHA).
    4. "Structure of the human lipoprotein-associated coagulation inhibitor gene. Intro/exon gene organization and localization of the gene to chromosome 2."
      Girard T.J., Eddy R., Wesselschmidt R.L., Macphail L.A., Likert K.M., Byers M.G., Shows T.B., Broze G.J. Jr.
      J. Biol. Chem. 266:5036-5041(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM ALPHA).
    5. Chang J.-Y., Monroe D.M., Roberts H.R.
      Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM BETA).
    6. SeattleSNPs variation discovery resource
      Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    7. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
      Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
      , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
      Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    9. "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 BETA).
      Tissue: Pancreas.
    10. "Biochemical characterization of plasma-derived tissue factor pathway inhibitor: post-translational modification of free, full-length form with particular reference to the sugar chain."
      Mori Y., Hamuro T., Nakashima T., Hamamoto T., Natsuka S., Hase S., Iwanaga S.
      J. Thromb. Haemost. 7:111-120(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 29-304, IDENTIFICATION BY MASS SPECTROMETRY, GLYCOSYLATION AT THR-42; ASN-145; ASN-195; SER-202 AND THR-203.
    11. "Purification and characterization of the lipoprotein-associated coagulation inhibitor from human plasma."
      Novotny W.F., Girard T.J., Miletich J.P., Broze G.J. Jr.
      J. Biol. Chem. 264:18832-18837(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 29-50.
    12. "Signal peptide prediction based on analysis of experimentally verified cleavage sites."
      Zhang Z., Henzel W.J.
      Protein Sci. 13:2819-2824(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 29-43.
    13. "Functional significance of the Kunitz-type inhibitory domains of lipoprotein-associated coagulation inhibitor."
      Girard T.J., Warren L.A., Novotny W.F., Likert K.M., Brown S.G., Miletich J.P., Broze G.J. Jr.
      Nature 338:518-520(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: INHIBITORY SITES.
    14. "Amino acid sequence and carbohydrate structure of a recombinant human tissue factor pathway inhibitor expressed in Chinese hamster ovary cells: one N- and two O-linked carbohydrate chains are located between Kunitz domains 2 and 3 and one N-linked carbohydrate chain is in Kunitz domain 2."
      Nakahara Y., Miyata T., Hamuro T., Funatsu A., Miyagi M., Tsunasawa S., Kato H.
      Biochemistry 35:6450-6459(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION AT ASN-145; ASN-195; SER-202 AND THR-203.
    15. "Regulation of coagulation by a multivalent Kunitz-type inhibitor."
      Broze G.J. Jr., Girard T.J., Novotny W.F.
      Biochemistry 29:7539-7546(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW.
    16. "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry."
      Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.
      J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-145.
      Tissue: Plasma.
    17. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    18. "TFPIbeta is the GPI-anchored TFPI isoform on human endothelial cells and placental microsomes."
      Girard T.J., Tuley E., Broze G.J. Jr.
      Blood 119:1256-1262(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION (ISOFORM BETA), GPI-ANCHOR.
    19. "The three-dimensional structure of recombinant leech-derived tryptase inhibitor in complex with trypsin. Implications for the structure of human mast cell tryptase and its inhibition."
      Stubbs M.T., Morenweiser R., Stuerzebecher J., Bauer M., Bode W., Huber R., Piechottka G.P., Matschiner G., Sommerhoff C.P., Fritz H., Auerswald E.A.
      J. Biol. Chem. 272:19931-19937(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 121-178 IN COMPLEX WITH TRYPSIN.
    20. "The second Kunitz domain of human tissue factor pathway inhibitor: cloning, structure determination and interaction with factor Xa."
      Burgering M.J.M., Orbons L.P.M., van der Doelen A., Mulders J., Theunissen H.J.M., Grootenhuis P.D.J., Bode W., Huber R., Stubbs M.T.
      J. Mol. Biol. 269:395-407(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 121-182.
    21. "Structural mechanism for heparin-binding of the third Kunitz domain of human tissue factor pathway inhibitor."
      Mine S., Yamazaki T., Miyata T., Hara S., Kato H.
      Biochemistry 41:78-85(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 210-270.
    22. Cited for: VARIANT MET-292.

    Entry informationi

    Entry nameiTFPI1_HUMAN
    AccessioniPrimary (citable) accession number: P10646
    Secondary accession number(s): O95103, Q53TS4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1989
    Last sequence update: July 1, 1989
    Last modified: October 1, 2014
    This is version 184 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, Direct protein sequencing, Reference proteome

    Documents

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

    External Data

    Dasty 3