Version 5.4
Homo sapiens Protein: SERPINE1
Summary
InnateDB Protein IDBP-32961.6
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol SERPINE1
Protein Name serpin peptidase inhibitor, clade E (nexin, plasminogen activator inhibitor type 1), member 1
Synonyms PAI; PAI-1; PAI1; PLANH1;
Species Homo sapiens
Ensembl Protein ENSP00000223095
InnateDB Gene IDBG-32959 (SERPINE1)
Protein Structure
UniProt Annotation
Function 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. {ECO:0000269PubMed:15853774}.
Subcellular Localization Secreted.
Disease Associations 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. {ECO:0000269PubMed:9207454}. Note=The disease is caused by mutations affecting the gene represented in this entry.Note=High concentrations of SERPINE1 seem to contribute to the development of venous but not arterial occlusions.
Tissue Specificity Found in plasma and platelets and in endothelial, hepatoma and fibrosarcoma cells.
Comments
Interactions
Number of Interactions This gene and/or its encoded proteins are associated with 29 experimentally validated interaction(s) in this database.
They are also associated with 1 interaction(s) predicted by orthology.
Experimentally validated
Total 29 [view]
Protein-Protein 16 [view]
Protein-DNA 13 [view]
Protein-RNA 0
DNA-DNA 0
RNA-RNA 0
DNA-RNA 0
Predicted by orthology
Total 1 [view]
Gene Ontology

Molecular Function
Accession GO Term
GO:0002020 protease binding
GO:0004867 serine-type endopeptidase inhibitor activity
GO:0005102 receptor binding
GO:0005515 protein binding
Biological Process
GO:0001300 chronological cell aging
GO:0001525 angiogenesis
GO:0002576 platelet degranulation
GO:0006351 transcription, DNA-templated
GO:0006367 transcription initiation from RNA polymerase II promoter
GO:0007179 transforming growth factor beta receptor signaling pathway
GO:0007596 blood coagulation
GO:0010467 gene expression
GO:0010469 regulation of receptor activity
GO:0010757 negative regulation of plasminogen activation
GO:0010951 negative regulation of endopeptidase activity
GO:0014912 negative regulation of smooth muscle cell migration
GO:0030168 platelet activation
GO:0030194 positive regulation of blood coagulation
GO:0030195 negative regulation of blood coagulation
GO:0030198 extracellular matrix organization
GO:0030336 negative regulation of cell migration
GO:0032757 positive regulation of interleukin-8 production
GO:0033629 negative regulation of cell adhesion mediated by integrin
GO:0035491 positive regulation of leukotriene production involved in inflammatory response
GO:0042127 regulation of cell proliferation
GO:0042730 fibrinolysis
GO:0045087 innate immune response (InnateDB)
GO:0045765 regulation of angiogenesis
GO:0045766 positive regulation of angiogenesis
GO:0045944 positive regulation of transcription from RNA polymerase II promoter
GO:0048260 positive regulation of receptor-mediated endocytosis
GO:0050729 positive regulation of inflammatory response
GO:0050829 defense response to Gram-negative bacterium
GO:0051918 negative regulation of fibrinolysis
GO:0061044 negative regulation of vascular wound healing
GO:0061045 negative regulation of wound healing
GO:0071222 cellular response to lipopolysaccharide
GO:0090026 positive regulation of monocyte chemotaxis
GO:1902042 negative regulation of extrinsic apoptotic signaling pathway via death domain receptors
GO:2000098 negative regulation of smooth muscle cell-matrix adhesion
GO:2000352 negative regulation of endothelial cell apoptotic process
Cellular Component
GO:0005576 extracellular region
GO:0005615 extracellular space
GO:0005886 plasma membrane
GO:0031012 extracellular matrix
GO:0031093 platelet alpha granule lumen
Protein Structure and Domains
PDB ID
InterPro IPR023796 Serpin domain
PFAM PF00079
PRINTS
PIRSF
SMART SM00093
TIGRFAMs
Post-translational Modifications
Modification
Cross-References
SwissProt P05121
PhosphoSite PhosphoSite-P05121
TrEMBL B7ZAB0
UniProt Splice Variant
Entrez Gene 5054
UniGene Hs.741440
RefSeq NP_000593
HUGO HGNC:8583
OMIM 173360
CCDS CCDS5711
HPRD 01418
IMGT
EMBL AC004876 AF386492 AK293248 AK297728 AK316225 BC010860 CH471197 J03764 M14083 M16006 M22314 M22315 M22316 M22317 M22318 M22319 M22320 M22321 X04429 X04729 X04731 X04744 X12701 X13323 X13338 X13339 X13340 X13341 X13342 X13343 X13344 X13345
GenPept AAA60003 AAA60007 AAA60008 AAA60009 AAD45828 AAH10860 AAK60338 BAH11475 BAH12656 BAH14596 CAA28025 CAA28438 CAA28442 CAA28444 CAA31208 CAA31722 CAA31729 CAB51606 CAB51607 CAB51639 CAB51737 CAB51738 CAB51739 EAW50196 EAW50197

If you use InnateDB for your research, please cite the following publication:

Breuer et al., InnateDB: systems biology of innate immunity and beyond - recent updates and continuing curation. Nucl. Acids Res. (2013) 41 (D1) 

InnateDB is being developed jointly by the Brinkman Laboratory (Simon Fraser University, British Columbia, Canada), the Hancock Laboratory (University of British Columbia, Vancouver, British Columbia) and the Lynn EMBL Australia Group (South Australian Health & Medical Research Institute and Flinders University, Adelaide, Australia).

Funding is currently provided by Allergen and EMBL Australia. Previous funding has been provided by Genome Canada, the Foundation for the National Institutes of Health through the Grand Challenges in Global Health initiative and by Teagasc. InnateDB curated interactions are licensed under the Design Science License. All other data is licensed under the terms of the originating database. Contact: innatedb-mail@sfu.ca