Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P05121

- PAI1_HUMAN

UniProt

P05121 - PAI1_HUMAN

Protein

Plasminogen activator inhibitor 1

Gene

SERPINE1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 180 (01 Oct 2014)
      Sequence version 1 (13 Aug 1987)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Serine protease inhibitor. This inhibitor acts as 'bait' for tissue plasminogen activator, urokinase, protein C and matriptase-3/TMPRSS7. Its rapid interaction with PLAT may function as a major control point in the regulation of fibrinolysis.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei369 – 3702Reactive bond

    GO - Molecular functioni

    1. protease binding Source: UniProtKB
    2. protein binding Source: IntAct
    3. serine-type endopeptidase inhibitor activity Source: BHF-UCL

    GO - Biological processi

    1. angiogenesis Source: UniProtKB
    2. blood coagulation Source: Reactome
    3. cellular response to lipopolysaccharide Source: BHF-UCL
    4. chronological cell aging Source: BHF-UCL
    5. defense response to Gram-negative bacterium Source: BHF-UCL
    6. extracellular matrix organization Source: Reactome
    7. fibrinolysis Source: Reactome
    8. gene expression Source: Reactome
    9. negative regulation of blood coagulation Source: BHF-UCL
    10. negative regulation of cell adhesion mediated by integrin Source: BHF-UCL
    11. negative regulation of cell migration Source: BHF-UCL
    12. negative regulation of endopeptidase activity Source: BHF-UCL
    13. negative regulation of endothelial cell apoptotic process Source: BHF-UCL
    14. negative regulation of extrinsic apoptotic signaling pathway via death domain receptors Source: BHF-UCL
    15. negative regulation of fibrinolysis Source: BHF-UCL
    16. negative regulation of plasminogen activation Source: BHF-UCL
    17. negative regulation of smooth muscle cell-matrix adhesion Source: BHF-UCL
    18. negative regulation of smooth muscle cell migration Source: BHF-UCL
    19. negative regulation of vascular wound healing Source: BHF-UCL
    20. negative regulation of wound healing Source: BHF-UCL
    21. platelet activation Source: Reactome
    22. platelet degranulation Source: Reactome
    23. positive regulation of angiogenesis Source: BHF-UCL
    24. positive regulation of blood coagulation Source: BHF-UCL
    25. positive regulation of inflammatory response Source: BHF-UCL
    26. positive regulation of interleukin-8 production Source: BHF-UCL
    27. positive regulation of leukotriene production involved in inflammatory response Source: BHF-UCL
    28. positive regulation of monocyte chemotaxis Source: BHF-UCL
    29. positive regulation of receptor-mediated endocytosis Source: BHF-UCL
    30. positive regulation of transcription from RNA polymerase II promoter Source: Reactome
    31. regulation of cell proliferation Source: Ensembl
    32. regulation of receptor activity Source: BHF-UCL
    33. transcription, DNA-templated Source: Reactome
    34. transcription initiation from RNA polymerase II promoter Source: Reactome
    35. transforming growth factor beta receptor signaling pathway Source: Reactome

    Keywords - Molecular functioni

    Protease inhibitor, Serine protease inhibitor

    Enzyme and pathway databases

    ReactomeiREACT_111118. BMAL1:CLOCK,NPAS2 activates circadian gene expression.
    REACT_120734. SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription.
    REACT_163906. ECM proteoglycans.
    REACT_641. Dissolution of Fibrin Clot.

    Protein family/group databases

    MEROPSiI04.020.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Plasminogen activator inhibitor 1
    Short name:
    PAI
    Short name:
    PAI-1
    Alternative name(s):
    Endothelial plasminogen activator inhibitor
    Serpin E1
    Gene namesi
    Name:SERPINE1
    Synonyms:PAI1, PLANH1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 7

    Organism-specific databases

    HGNCiHGNC:8583. SERPINE1.

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular matrix Source: BHF-UCL
    2. extracellular region Source: BHF-UCL
    3. extracellular space Source: BHF-UCL
    4. extracellular vesicular exosome Source: UniProtKB
    5. plasma membrane Source: Reactome
    6. platelet alpha granule lumen Source: Reactome

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Involvement in diseasei

    Plasminogen activator inhibitor-1 deficiency (PAI-1D) [MIM:613329]: A hematologic disorder characterized by increased bleeding after trauma, injury, or surgery. Affected females have menorrhagia. The bleeding defect is due to increased fibrinolysis of fibrin blood clots due to deficiency of plasminogen activator inhibitor-1, which inhibits tissue and urinary activators of plasminogen.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    High concentrations of SERPINE1 seem to contribute to the development of venous but not arterial occlusions.

    Organism-specific databases

    MIMi613329. phenotype.
    Orphaneti465. Congenital plasminogen activator inhibitor type 1 deficiency.
    PharmGKBiPA261.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2323Add
    BLAST
    Chaini24 – 402379Plasminogen activator inhibitor 1PRO_0000032499Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi232 – 2321N-linked (GlcNAc...)
    Glycosylationi288 – 2881N-linked (GlcNAc...)
    Glycosylationi352 – 3521N-linked (GlcNAc...)Sequence Analysis

    Post-translational modificationi

    Inactivated by proteolytic attack of the urokinase-type (u-PA) and the tissue-type (TPA), cleaving the 369-Arg-|-Met-370 bond.

    Keywords - PTMi

    Glycoprotein

    Proteomic databases

    MaxQBiP05121.
    PaxDbiP05121.
    PRIDEiP05121.

    2D gel databases

    OGPiP05121.
    SWISS-2DPAGEP05121.

    PTM databases

    PhosphoSiteiP05121.

    Miscellaneous databases

    PMAP-CutDBP05121.

    Expressioni

    Tissue specificityi

    Found in plasma and platelets and in endothelial, hepatoma and fibrosarcoma cells.

    Gene expression databases

    ArrayExpressiP05121.
    BgeeiP05121.
    CleanExiHS_SERPINE1.
    GenevestigatoriP05121.

    Organism-specific databases

    HPAiHPA050039.

    Interactioni

    Subunit structurei

    Forms protease inhibiting heterodimer with TMPRSS7. Interacts with VTN. Binds LRP1B; binding is followed by internalization and degradation.2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ORM1P027634EBI-953978,EBI-976767

    Protein-protein interaction databases

    BioGridi111091. 14 interactions.
    IntActiP05121. 6 interactions.
    MINTiMINT-202409.
    STRINGi9606.ENSP00000223095.

    Structurei

    Secondary structure

    1
    402
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi27 – 4923
    Beta strandi51 – 533
    Beta strandi55 – 573
    Helixi59 – 7214
    Helixi75 – 8511
    Helixi94 – 10613
    Helixi108 – 1103
    Beta strandi111 – 12313
    Helixi132 – 1409
    Beta strandi145 – 1473
    Helixi149 – 1513
    Helixi152 – 16514
    Turni166 – 1694
    Beta strandi170 – 1723
    Helixi176 – 1794
    Beta strandi186 – 20015
    Helixi204 – 2063
    Beta strandi209 – 2135
    Beta strandi216 – 2183
    Beta strandi219 – 23719
    Turni239 – 2413
    Beta strandi243 – 2519
    Beta strandi254 – 26512
    Helixi271 – 2744
    Helixi279 – 28810
    Beta strandi290 – 29910
    Beta strandi301 – 3088
    Helixi310 – 3156
    Helixi320 – 3223
    Turni324 – 3263
    Turni330 – 3323
    Beta strandi334 – 3363
    Beta strandi340 – 35112
    Beta strandi353 – 36816
    Beta strandi374 – 3763
    Beta strandi380 – 3878
    Turni388 – 3914
    Beta strandi392 – 4009

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1A7CX-ray1.95A24-402[»]
    1B3KX-ray2.99A/B/C/D24-402[»]
    1C5GX-ray2.60A1-402[»]
    1DB2X-ray2.70A/B26-402[»]
    1DVMX-ray2.40A/B/C/D24-402[»]
    1DVNX-ray2.10A24-402[»]
    1LJ5X-ray1.80A24-402[»]
    1OC0X-ray2.28A24-402[»]
    3CVMX-ray2.02A/B21-402[»]
    3EOXX-ray2.61A24-402[»]
    3PB1X-ray2.30I24-402[»]
    3Q02X-ray2.30A/B24-402[»]
    3Q03X-ray2.64A/B24-402[»]
    3R4LX-ray2.70A24-402[»]
    3UT3X-ray2.42A/B/C/D28-402[»]
    4AQHX-ray2.40A/B/C24-402[»]
    4G8OX-ray2.71A/B/C/D28-402[»]
    4G8RX-ray2.19A/B28-402[»]
    4IC0X-ray2.32A/B/C/D24-402[»]
    9PAIX-ray2.70A24-369[»]
    B370-402[»]
    DisProtiDP00320.
    ProteinModelPortaliP05121.
    SMRiP05121. Positions 24-402.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP05121.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the serpin family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG4826.
    HOGENOMiHOG000238519.
    HOVERGENiHBG106493.
    InParanoidiP05121.
    KOiK03982.
    OMAiTNKFNYT.
    OrthoDBiEOG7327PB.
    PhylomeDBiP05121.
    TreeFamiTF352620.

    Family and domain databases

    InterProiIPR023795. Serpin_CS.
    IPR023796. Serpin_dom.
    IPR000215. Serpin_fam.
    [Graphical view]
    PANTHERiPTHR11461. PTHR11461. 1 hit.
    PfamiPF00079. Serpin. 1 hit.
    [Graphical view]
    SMARTiSM00093. SERPIN. 1 hit.
    [Graphical view]
    SUPFAMiSSF56574. SSF56574. 1 hit.
    PROSITEiPS00284. SERPIN. 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

    Isoform 1 (identifier: P05121-1) [UniParc]FASTAAdd to Basket

    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

    MQMSPALTCL VLGLALVFGE GSAVHHPPSY VAHLASDFGV RVFQQVAQAS    50
    KDRNVVFSPY GVASVLAMLQ LTTGGETQQQ IQAAMGFKID DKGMAPALRH 100
    LYKELMGPWN KDEISTTDAI FVQRDLKLVQ GFMPHFFRLF RSTVKQVDFS 150
    EVERARFIIN DWVKTHTKGM ISNLLGKGAV DQLTRLVLVN ALYFNGQWKT 200
    PFPDSSTHRR LFHKSDGSTV SVPMMAQTNK FNYTEFTTPD GHYYDILELP 250
    YHGDTLSMFI AAPYEKEVPL SALTNILSAQ LISHWKGNMT RLPRLLVLPK 300
    FSLETEVDLR KPLENLGMTD MFRQFQADFT SLSDQEPLHV AQALQKVKIE 350
    VNESGTVASS STAVIVSARM APEEIIMDRP FLFVVRHNPT GTVLFMGQVM 400
    EP 402
    Length:402
    Mass (Da):45,060
    Last modified:August 13, 1987 - v1
    Checksum:iA2E181ED28DD6082
    GO
    Isoform 2 (identifier: P05121-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         31-45: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:387
    Mass (Da):43,404
    Checksum:i9BFE4D37D0F81361
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti53 – 531R → A in CAA31208. 1 PublicationCurated
    Sequence conflicti55 – 551V → L in AAA60009. (PubMed:2820474)Curated
    Sequence conflicti75 – 751G → V in CAA31208. 1 PublicationCurated
    Sequence conflicti138 – 1381R → K in CAA31208. 1 PublicationCurated
    Sequence conflicti226 – 2261A → V in BAH12656. (PubMed:14702039)Curated
    Sequence conflicti280 – 2823QLI → HVM in CAA31208. 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti15 – 151A → T.3 Publications
    Corresponds to variant rs6092 [ dbSNP | Ensembl ].
    VAR_007099
    Natural varianti17 – 171V → I.2 Publications
    Corresponds to variant rs6090 [ dbSNP | Ensembl ].
    VAR_011750
    Natural varianti25 – 251H → P.1 Publication
    Corresponds to variant rs2227647 [ dbSNP | Ensembl ].
    VAR_013086
    Natural varianti209 – 2091R → H.1 Publication
    Corresponds to variant rs2227669 [ dbSNP | Ensembl ].
    VAR_013087
    Natural varianti255 – 2551T → N.1 Publication
    Corresponds to variant rs2227685 [ dbSNP | Ensembl ].
    VAR_013088

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei31 – 4515Missing in isoform 2. 1 PublicationVSP_045493Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X04429 mRNA. Translation: CAA28025.1.
    M14083 mRNA. Translation: AAA60008.1.
    X04729 mRNA. Translation: CAA28438.1.
    X04731 mRNA. Translation: CAA28442.1.
    M16006 mRNA. Translation: AAA60003.1.
    M22321
    , M22314, M22315, M22316, M22317, M22318, M22319, M22320 Genomic DNA. Translation: AAA60009.1.
    X13323 Genomic DNA. No translation available.
    X13338 Genomic DNA. Translation: CAA31722.1.
    X13339 Genomic DNA. Translation: CAB51639.1.
    X13340 Genomic DNA. Translation: CAB51737.1.
    X13341 Genomic DNA. Translation: CAB51606.1.
    X13342 Genomic DNA. Translation: CAB51607.1.
    X13343 Genomic DNA. Translation: CAB51738.1.
    X13344 Genomic DNA. Translation: CAB51739.1.
    X13345 Genomic DNA. Translation: CAA31729.1.
    J03764 Genomic DNA. Translation: AAA60007.1.
    X12701 mRNA. Translation: CAA31208.1.
    AF386492 Genomic DNA. Translation: AAK60338.1.
    AK297728 mRNA. Translation: BAH12656.1.
    AC004876 Genomic DNA. Translation: AAD45828.1.
    BC010860 mRNA. Translation: AAH10860.1.
    X04744 mRNA. Translation: CAA28444.1.
    CCDSiCCDS5711.1. [P05121-1]
    PIRiA28107. ITHUP1.
    RefSeqiNP_000593.1. NM_000602.4. [P05121-1]
    UniGeneiHs.414795.
    Hs.713079.
    Hs.741440.

    Genome annotation databases

    EnsembliENST00000223095; ENSP00000223095; ENSG00000106366. [P05121-1]
    GeneIDi5054.
    KEGGihsa:5054.
    UCSCiuc003uxt.4. human. [P05121-1]

    Polymorphism databases

    DMDMi129576.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    Wikipedia

    Plasminogen activator inhibitor-1 entry

    SeattleSNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X04429 mRNA. Translation: CAA28025.1 .
    M14083 mRNA. Translation: AAA60008.1 .
    X04729 mRNA. Translation: CAA28438.1 .
    X04731 mRNA. Translation: CAA28442.1 .
    M16006 mRNA. Translation: AAA60003.1 .
    M22321
    , M22314 , M22315 , M22316 , M22317 , M22318 , M22319 , M22320 Genomic DNA. Translation: AAA60009.1 .
    X13323 Genomic DNA. No translation available.
    X13338 Genomic DNA. Translation: CAA31722.1 .
    X13339 Genomic DNA. Translation: CAB51639.1 .
    X13340 Genomic DNA. Translation: CAB51737.1 .
    X13341 Genomic DNA. Translation: CAB51606.1 .
    X13342 Genomic DNA. Translation: CAB51607.1 .
    X13343 Genomic DNA. Translation: CAB51738.1 .
    X13344 Genomic DNA. Translation: CAB51739.1 .
    X13345 Genomic DNA. Translation: CAA31729.1 .
    J03764 Genomic DNA. Translation: AAA60007.1 .
    X12701 mRNA. Translation: CAA31208.1 .
    AF386492 Genomic DNA. Translation: AAK60338.1 .
    AK297728 mRNA. Translation: BAH12656.1 .
    AC004876 Genomic DNA. Translation: AAD45828.1 .
    BC010860 mRNA. Translation: AAH10860.1 .
    X04744 mRNA. Translation: CAA28444.1 .
    CCDSi CCDS5711.1. [P05121-1 ]
    PIRi A28107. ITHUP1.
    RefSeqi NP_000593.1. NM_000602.4. [P05121-1 ]
    UniGenei Hs.414795.
    Hs.713079.
    Hs.741440.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1A7C X-ray 1.95 A 24-402 [» ]
    1B3K X-ray 2.99 A/B/C/D 24-402 [» ]
    1C5G X-ray 2.60 A 1-402 [» ]
    1DB2 X-ray 2.70 A/B 26-402 [» ]
    1DVM X-ray 2.40 A/B/C/D 24-402 [» ]
    1DVN X-ray 2.10 A 24-402 [» ]
    1LJ5 X-ray 1.80 A 24-402 [» ]
    1OC0 X-ray 2.28 A 24-402 [» ]
    3CVM X-ray 2.02 A/B 21-402 [» ]
    3EOX X-ray 2.61 A 24-402 [» ]
    3PB1 X-ray 2.30 I 24-402 [» ]
    3Q02 X-ray 2.30 A/B 24-402 [» ]
    3Q03 X-ray 2.64 A/B 24-402 [» ]
    3R4L X-ray 2.70 A 24-402 [» ]
    3UT3 X-ray 2.42 A/B/C/D 28-402 [» ]
    4AQH X-ray 2.40 A/B/C 24-402 [» ]
    4G8O X-ray 2.71 A/B/C/D 28-402 [» ]
    4G8R X-ray 2.19 A/B 28-402 [» ]
    4IC0 X-ray 2.32 A/B/C/D 24-402 [» ]
    9PAI X-ray 2.70 A 24-369 [» ]
    B 370-402 [» ]
    DisProti DP00320.
    ProteinModelPortali P05121.
    SMRi P05121. Positions 24-402.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111091. 14 interactions.
    IntActi P05121. 6 interactions.
    MINTi MINT-202409.
    STRINGi 9606.ENSP00000223095.

    Chemistry

    BindingDBi P05121.
    ChEMBLi CHEMBL3475.
    DrugBanki DB01076. Atorvastatin.
    DB01093. Dimethyl sulfoxide.
    DB00055. Drotrecogin alfa.
    DB00641. Simvastatin.
    DB00031. Tenecteplase.
    DB00197. Troglitazone.
    DB00013. Urokinase.

    Protein family/group databases

    MEROPSi I04.020.

    PTM databases

    PhosphoSitei P05121.

    Polymorphism databases

    DMDMi 129576.

    2D gel databases

    OGPi P05121.
    SWISS-2DPAGE P05121.

    Proteomic databases

    MaxQBi P05121.
    PaxDbi P05121.
    PRIDEi P05121.

    Protocols and materials databases

    DNASUi 5054.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000223095 ; ENSP00000223095 ; ENSG00000106366 . [P05121-1 ]
    GeneIDi 5054.
    KEGGi hsa:5054.
    UCSCi uc003uxt.4. human. [P05121-1 ]

    Organism-specific databases

    CTDi 5054.
    GeneCardsi GC07P100770.
    HGNCi HGNC:8583. SERPINE1.
    HPAi HPA050039.
    MIMi 173360. gene.
    613329. phenotype.
    neXtProti NX_P05121.
    Orphaneti 465. Congenital plasminogen activator inhibitor type 1 deficiency.
    PharmGKBi PA261.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG4826.
    HOGENOMi HOG000238519.
    HOVERGENi HBG106493.
    InParanoidi P05121.
    KOi K03982.
    OMAi TNKFNYT.
    OrthoDBi EOG7327PB.
    PhylomeDBi P05121.
    TreeFami TF352620.

    Enzyme and pathway databases

    Reactomei REACT_111118. BMAL1:CLOCK,NPAS2 activates circadian gene expression.
    REACT_120734. SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription.
    REACT_163906. ECM proteoglycans.
    REACT_641. Dissolution of Fibrin Clot.

    Miscellaneous databases

    ChiTaRSi SERPINE1. human.
    EvolutionaryTracei P05121.
    GeneWikii Plasminogen_activator_inhibitor-1.
    GenomeRNAii 5054.
    NextBioi 19480.
    PMAP-CutDB P05121.
    PROi P05121.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P05121.
    Bgeei P05121.
    CleanExi HS_SERPINE1.
    Genevestigatori P05121.

    Family and domain databases

    InterProi IPR023795. Serpin_CS.
    IPR023796. Serpin_dom.
    IPR000215. Serpin_fam.
    [Graphical view ]
    PANTHERi PTHR11461. PTHR11461. 1 hit.
    Pfami PF00079. Serpin. 1 hit.
    [Graphical view ]
    SMARTi SM00093. SERPIN. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56574. SSF56574. 1 hit.
    PROSITEi PS00284. SERPIN. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Endothelial plasminogen activator inhibitor (PAI): a new member of the Serpin gene family."
      Pannekoek H., Veerman H., Lambers H., Diergaarde P., Verweij C.L., van Zonneveld A.-J., van Mourik J.A.
      EMBO J. 5:2539-2544(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. "Structure of the human plasminogen activator inhibitor 1 gene: nonrandom distribution of introns."
      Loskutoff D.J., Linders M., Keijer J., Veerman H., van Heerikhuizen H., Pannekoek H.
      Biochemistry 26:3763-3768(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "cDNA cloning of human plasminogen activator-inhibitor from endothelial cells."
      Ginsburg D., Zeheb R., Yang A.Y., Rafferty U.M., Andreasen P.A., Nielsen L., Dano K., Lebo R.V., Gelehrter T.D.
      J. Clin. Invest. 78:1673-1680(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    4. "Structure and expression of the human gene encoding plasminogen activator inhibitor, PAI-1."
      Follo M., Ginsburg D.
      Gene 84:447-453(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    5. "The organization of the human-plasminogen-activator-inhibitor-1 gene. Implications on the evolution of the serine-protease inhibitor family."
      Strandberg L., Lawrence D., Ny T.
      Eur. J. Biochem. 176:609-616(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    6. "Human plasminogen activator inhibitor-1 gene. Promoter and structural gene nucleotide sequences."
      Bosma P.J., van den Berg E.A., Kooistra T., Siemieniak D.R., Slightom J.L.
      J. Biol. Chem. 263:9129-9141(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    7. Pannekoek H.
      Submitted (FEB-1992) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    8. SeattleSNPs variation discovery resource
      Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS THR-15; ILE-17; PRO-25; HIS-209 AND ASN-255.
    9. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    10. "The DNA sequence of human chromosome 7."
      Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L.
      , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
      Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    11. "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: Lung.
    12. "Cloning and sequence of a cDNA coding for the human beta-migrating endothelial-cell-type plasminogen activator inhibitor."
      Ny T., Sawdey M., Lawrence D., Millan J.L., Loskutoff D.J.
      Proc. Natl. Acad. Sci. U.S.A. 83:6776-6780(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 20-402 (ISOFORM 1).
    13. "Plasminogen activator inhibitor type-1: reactive center and amino-terminal heterogeneity determined by protein and cDNA sequencing."
      Andreasen P.A., Riccio A., Welinder K.G., Douglas R., Sartorio R., Nielsen L.S., Oppenheimer C., Blasi F., Danoe K.
      FEBS Lett. 209:213-218(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-47 AND 364-402 (ISOFORM 1).
    14. "cDNA cloning and expression in E. coli of a plasminogen activator inhibitor (PAI) related to a PAI produced by Hep G2 hepatoma cell."
      Wun T.C., Kretzmer K.K.
      FEBS Lett. 210:11-16(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 17-402 (ISOFORM 1), PARTIAL PROTEIN SEQUENCE.
      Tissue: Placenta.
    15. "Identification of a PAI-1 binding site in vitronectin."
      Sigurdardottir O., Wiman B.
      Biochim. Biophys. Acta 1208:104-110(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH VTN.
    16. "Human plasminogen activator inhibitor-1 (PAI-1) deficiency: characterization of a large kindred with a null mutation in the PAI-1 gene."
      Fay W.P., Parker A.C., Condrey L.R., Shapiro A.D.
      Blood 90:204-208(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: INVOLVEMENT IN PAI-1D.
    17. "The putative tumor suppressor LRP1B, a novel member of the low density lipoprotein (LDL) receptor family, exhibits both overlapping and distinct properties with the LDL receptor-related protein."
      Liu C.-X., Li Y., Obermoeller-McCormick L.M., Schwartz A.L., Bu G.
      J. Biol. Chem. 276:28889-28896(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH LRP1B.
    18. "Matriptase-3 is a novel phylogenetically preserved membrane-anchored serine protease with broad serpin reactivity."
      Szabo R., Netzel-Arnett S., Hobson J.P., Antalis T.M., Bugge T.H.
      Biochem. J. 390:231-242(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN MEMBRANE-ANCHORED SERINE PROTEASE TMPRSS7 INHIBITION, HETERODIMER WITH TMPRSS7.
    19. Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
    20. "Mechanisms contributing to the conformational and functional flexibility of plasminogen activator inhibitor-1."
      Aertgeerts K., de Bondt H.L., de Ranter C.J., Declerck P.J.
      Nat. Struct. Biol. 2:891-897(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
    21. "Interfering with the inhibitory mechanism of serpins: crystal structure of a complex formed between cleaved plasminogen activator inhibitor type 1 and a reactive-centre loop peptide."
      Xue Y., Bjoerquist P., Inghardt T., Linschoten M., Musil D., Sjoelin L., Deinum J.
      Structure 6:627-636(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS).
    22. "The active conformation of plasminogen activator inhibitor 1, a target for drugs to control fibrinolysis and cell adhesion."
      Sharp A.M., Stein P.E., Pannu N.S., Carrell R.W., Berkenpas M.B., Ginsburg D., Lawrence D.A., Read R.J.
      Structure 7:111-118(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.99 ANGSTROMS).
    23. "Plasminogen activator inhibitor 1. Structure of the native serpin, comparison to its other conformers and implications for serpin inactivation."
      Nar H., Bauer M., Stassen J.M., Lang D., Gils A., Declerck P.J.
      J. Mol. Biol. 297:683-695(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
    24. "Mutational analysis of the genes encoding urokinase-type plasminogen activator (uPA) and its inhibitor PAI-1 in advanced ovarian cancer."
      Turkmen B., Schmitt M., Schmalfeldt B., Trommler P., Hell W., Creutzburg S., Graeff H., Magdolen V.
      Electrophoresis 18:686-689(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT THR-15.
    25. Cited for: VARIANTS THR-15 AND ILE-17.

    Entry informationi

    Entry nameiPAI1_HUMAN
    AccessioniPrimary (citable) accession number: P05121
    Secondary accession number(s): B7Z4S0, F8WD53
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 13, 1987
    Last sequence update: August 13, 1987
    Last modified: October 1, 2014
    This is version 180 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 7
      Human chromosome 7: 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