SERPINE1

Gene Information

Official Symbol: SERPINE1
Official Name: serpin family E member 1
Aliases and Previous Symbols: N/A
Entrez ID: 5054
UniProt: P05121
Interactions: BioGRID
PubMed articles: Open PubMed
OMIM: Open OMIM

Function Summary

Entrez Summary: This gene encodes a member of the serine proteinase inhibitor (serpin) superfamily. This member is the principal inhibitor of tissue plasminogen activator (tPA) and urokinase (uPA), and hence is an inhibitor of fibrinolysis. Defects in this gene are the cause of plasminogen activator inhibitor-1 deficiency (PAI-1 deficiency), and high concentrations of the gene product are associated with thrombophilia. Alternatively spliced transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Sep 2009].
UniProt Summary: Serine protease inhibitor. Inhibits TMPRSS7 (PubMed:15853774). Is a primary inhibitor of tissue-type plasminogen activator (PLAT) and urokinase-type plasminogen activator (PLAU). As PLAT inhibitor, it is required for fibrinolysis down-regulation and is responsible for the controlled degradation of blood clots (PubMed:8481516, PubMed:9207454, PubMed:17912461). As PLAU inhibitor, it is involved in the regulation of cell adhesion and spreading (PubMed:9175705). Acts as a regulator of cell migration, independently of its role as protease inhibitor (PubMed:15001579, PubMed:9168821). It is required for stimulation of keratinocyte migration during cutaneous injury repair (PubMed:18386027). It is involved in cellular and replicative senescence (PubMed:16862142). Plays a role in alveolar type 2 cells senescence in the lung (By similarity). Is involved in the regulation of cementogenic differentiation of periodontal ligament stem cells, and regulates odontoblast differentiation and dentin formation during odontogenesis (PubMed:25808697, PubMed:27046084). {ECO:0000250|UniProtKB:P22777, ECO:0000269|PubMed:15001579, ECO:0000269|PubMed:15853774, ECO:0000269|PubMed:16862142, ECO:0000269|PubMed:17912461, ECO:0000269|PubMed:18386027, ECO:0000269|PubMed:25808697, ECO:0000269|PubMed:27046084, ECO:0000269|PubMed:8481516, ECO:0000269|PubMed:9168821, ECO:0000269|PubMed:9175705, ECO:0000269|PubMed:9207454}.

Pfam Domains GO Terms

CRISPR Data

Compound Hit Most Correlated Genes in Chemogenomics Tissues where Essential in the Avana Dataset (DepMap 20Q1)

Global Fraction of Cell Lines Where Essential: 0/739

Tissue	Fraction Of Cell Lines Where Essential
1290807.0	0/1
909776.0	0/1
bile duct	0/28
blood	0/28
bone	0/26
breast	0/33
central nervous system	0/56
cervix	0/4
colorectal	0/17
esophagus	0/13
fibroblast	0/1
gastric	0/16
kidney	0/21
liver	0/20
lung	0/75
lymphocyte	0/16
ovary	0/26
pancreas	0/24
peripheral nervous system	0/16
plasma cell	0/15
prostate	0/1
skin	0/24
soft tissue	0/9
thyroid	0/2
upper aerodigestive	0/22
urinary tract	0/29
uterus	0/5

Essentiality in NALM6

Essentiality Rank: 9759
Expression level (log2 read counts): 0.3

Expression Distribution

positive regulation of odontoblast differentiation
positive regulation of leukotriene production involved in inflammatory response
negative regulation of vascular wound healing
regulation of leukotriene production involved in inflammatory response
negative regulation of smooth muscle cell-matrix adhesion
chronological cell aging
positive regulation of neuroepithelial cell differentiation
regulation of odontoblast differentiation
regulation of smooth muscle cell-matrix adhesion
regulation of vascular wound healing
negative regulation of plasminogen activation
dentinogenesis
negative regulation of fibrinolysis
negative regulation of cell adhesion mediated by integrin
replicative senescence
regulation of fibrinolysis
regulation of plasminogen activation
positive regulation of monocyte chemotaxis
fibrinolysis
negative regulation of smooth muscle cell migration
positive regulation of mononuclear cell migration
regulation of monocyte chemotaxis
positive regulation of hemostasis
positive regulation of blood coagulation
positive regulation of coagulation
negative regulation of endothelial cell apoptotic process
negative regulation of protein maturation
negative regulation of protein processing
negative regulation of extrinsic apoptotic signaling pathway via death domain receptors
negative regulation of cell-matrix adhesion
negative regulation of epithelial cell apoptotic process
regulation of mononuclear cell migration
regulation of cell adhesion mediated by integrin
positive regulation of interleukin-8 production
regulation of endothelial cell apoptotic process
negative regulation of blood coagulation
negative regulation of hemostasis
negative regulation of coagulation
positive regulation of receptor-mediated endocytosis
positive regulation of wound healing