A2M report

I. Expression across cell types

II. Expression across tissues

III. Associated gene sets

GO_0007584Biological processresponse to nutrient
GO_0001869Biological processnegative regulation of complement activation, lectin pathway
GO_0006953Biological processacute-phase response
GO_0001553Biological processluteinization
GO_0010037Biological processresponse to carbon dioxide
GO_1990402Biological processembryonic liver development
GO_0051384Biological processresponse to glucocorticoid
GO_0034695Biological processresponse to prostaglandin E
GO_0048863Biological processstem cell differentiation
GO_0002438Biological processacute inflammatory response to antigenic stimulus
GO_0005615Cellular componentextracellular space
GO_0005576Cellular componentextracellular region
GO_0070062Cellular componentextracellular exosome
GO_0062023Cellular componentcollagen-containing extracellular matrix
GO_0072562Cellular componentblood microparticle
GO_0031093Cellular componentplatelet alpha granule lumen
GO_0019899Molecular functionenzyme binding
GO_0043120Molecular functiontumor necrosis factor binding
GO_0019966Molecular functioninterleukin-1 binding
GO_0004866Molecular functionendopeptidase inhibitor activity
GO_0004867Molecular functionserine-type endopeptidase inhibitor activity
GO_0042802Molecular functionidentical protein binding
GO_0005102Molecular functionsignaling receptor binding
GO_0048403Molecular functionbrain-derived neurotrophic factor binding
GO_0002020Molecular functionprotease binding
GO_0048306Molecular functioncalcium-dependent protein binding
GO_0019838Molecular functiongrowth factor binding
GO_0048406Molecular functionnerve growth factor binding
GO_0019959Molecular functioninterleukin-8 binding
GO_0005515Molecular functionprotein binding

IV. Literature review

[source]
Gene nameA2M
Protein nameAlternative protein A2M
Alpha-2-macroglobulin (Alpha-2-M) (C3 and PZP-like alpha-2-macroglobulin domain-containing protein 5)
Alpha-2-macroglobulin
SynonymsCPAMD5
FWP007
DescriptionFUNCTION: Is able to inhibit all four classes of proteinases by a unique 'trapping' mechanism. This protein has a peptide stretch, called the 'bait region' which contains specific cleavage sites for different proteinases. When a proteinase cleaves the bait region, a conformational change is induced in the protein which traps the proteinase. The entrapped enzyme remains active against low molecular weight substrates (activity against high molecular weight substrates is greatly reduced). Following cleavage in the bait region, a thioester bond is hydrolyzed and mediates the covalent binding of the protein to the proteinase.

AccessionsL0R6B6
F5H1E8
ENST00000404455.2
H0YFH1
ENST00000546069.1
P01023
ENST00000318602.12
F8W7L3
ENST00000539638.5
Q9BQ22