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P05121

- PAI1_HUMAN

UniProt

P05121 - PAI1_HUMAN

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Protein
Plasminogen activator inhibitor 1
Gene
SERPINE1, PAI1, PLANH1
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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
Complete GO annotation...

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 migration Source: BHF-UCL
  18. negative regulation of smooth muscle cell-matrix adhesion 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 initiation from RNA polymerase II promoter Source: Reactome
  34. transcription, DNA-templated Source: Reactome
  35. transforming growth factor beta receptor signaling pathway Source: Reactome
Complete GO annotation...

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
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. plasma membrane Source: Reactome
  5. platelet alpha granule lumen Source: Reactome
Complete GO annotation...

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.
Note: The disease is caused by mutations affecting the gene represented in this entry.1 Publication
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 – 2323
Add
BLAST
Chaini24 – 402379Plasminogen activator inhibitor 1
PRO_0000032499Add
BLAST

Amino acid modifications

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

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

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.

Miscellaneous databases

EvolutionaryTraceiP05121.

Family & Domainsi

Sequence similaritiesi

Belongs to the serpin family.

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

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.
VSP_045493Add
BLAST

Sequence conflict

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

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]
ENST00000445463; ENSP00000396766; ENSG00000106366. [P05121-2]
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...

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 ]
ENST00000445463 ; ENSP00000396766 ; ENSG00000106366 . [P05121-2 ]
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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 179 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

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