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Cpa3 Cpa3 Ace Ace Cpb1 Cpb1 Gzmg Gzmg Ctsg Ctsg Ctsz Ctsz Cpb2 Cpb2 Cma1 Cma1 Enpep Enpep Atp6ap2 Atp6ap2 Ces1d Ces1d Agt Agt Aopep Aopep Ren1 Ren1 Ace2 Ace2 Ctsd Ctsd Mme Mme
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splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
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query proteins and first shell of interactors
white nodes:
second shell of interactors
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proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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Known Interactions
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experimentally determined
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Cpa3Mast cell carboxypeptidase A. (417 aa)
AceAngiotensin-converting enzyme, soluble form; Converts angiotensin I to angiotensin II by release of the terminal His-Leu, this results in an increase of the vasoconstrictor activity of angiotensin. Also able to inactivate bradykinin, a potent vasodilator. Has also a glycosidase activity which releases GPI- anchored proteins from the membrane by cleaving the mannose linkage in the GPI moiety. This GPIase activity seems to be crucial for the egg- binding ability of the sperm; Belongs to the peptidase M2 family. (1312 aa)
Cpb1Carboxypeptidase B1 (Tissue). (415 aa)
GzmgGranzyme G; This enzyme is probably necessary for target cell lysis in cell-mediated immune responses; Belongs to the peptidase S1 family. Granzyme subfamily. (248 aa)
CtsgCathepsin G; This vimentin-specific protease may regulate the reorganization of vimentin filaments, occurring during cell differentiation, movement and mitosis. (261 aa)
CtszCathepsin Z; Exhibits carboxy-monopeptidase as well as carboxy-dipeptidase activity (By similarity). Capable of producing kinin potentiating peptides (By similarity). (306 aa)
Cpb2Carboxypeptidase B2; Cleaves C-terminal arginine or lysine residues from biologically active peptides such as kinins or anaphylatoxins in the circulation thereby regulating their activities. Down-regulates fibrinolysis by removing C-terminal lysine residues from fibrin that has already been partially degraded by plasmin; Belongs to the peptidase M14 family. (422 aa)
Cma1Chymase; Major secreted protease of mast cells with suspected roles in vasoactive peptide generation, extracellular matrix degradation, and regulation of gland secretion; Belongs to the peptidase S1 family. Granzyme subfamily. (260 aa)
EnpepGlutamyl aminopeptidase; Regulates central hypertension through its calcium-modulated preference to cleave N-terminal acidic residues from peptides such as angiotensin II. (945 aa)
Atp6ap2Renin receptor extracellular fragment; Multifunctional protein which functions as a renin, prorenin cellular receptor and is involved in the assembly of the proton- transporting vacuolar (V)-ATPase protein pump. May mediate renin- dependent cellular responses by activating ERK1 and ERK2. By increasing the catalytic efficiency of renin in AGT/angiotensinogen conversion to angiotensin I, it may also play a role in the renin-angiotensin system (RAS) (By similarity). Probably by controlling the assembly of the V- ATPase pump and thus the acidification of the endo-lysosomal system, plays a [...] (350 aa)
Ces1dCarboxylesterase 1D; Major lipase in white adipose tissue. Involved in the metabolism of xenobiotics and of natural substrates. Hydrolyzes triacylglycerols and monoacylglycerols, with a preference for monoacylglycerols. The susceptibility of the substrate increases with decreasing acyl chain length of the fatty acid moiety. Catalyzes the synthesis of fatty acid ethyl esters. (565 aa)
AgtAngiotensin 1-4; Essential component of the renin-angiotensin system (RAS), a potent regulator of blood pressure, body fluid and electrolyte homeostasis. [Angiotensin-3]: stimulates aldosterone release. Belongs to the serpin family. (482 aa)
AopepAminopeptidase O; Aminopeptidases catalyze the hydrolysis of amino acid residues from the N-terminus of peptide or protein substrates. Able to cleave angiotensin III to generate angiotensin IV, a bioactive peptide of the renin-angiotensin pathway. Not able to cleave angiotensin I and angiotensin II. May play a role in the proteolytic processing of bioactive peptides in tissues such as testis and heart. (823 aa)
Ren1Renin-1; Renin is a highly specific endopeptidase, whose only known function is to generate angiotensin I from angiotensinogen in the plasma, initiating a cascade of reactions that produce an elevation of blood pressure and increased sodium retention by the kidney. (402 aa)
Ace2Processed angiotensin-converting enzyme 2; Carboxypeptidase which converts angiotensin I to angiotensin 1-9, a peptide of unknown function, and angiotensin II to angiotensin 1-7, a vasodilator (By similarity). Also able to hydrolyze apelin-13 and dynorphin-13 with high efficiency (By similarity). By cleavage of angiotensin II, may be an important regulator of heart function. By cleavage of angiotensin II, may also have a protective role in acute lung injury. Plays an important role in amino acid transport by acting as binding partner of amino acid transporter SLC6A19, regulating its tr [...] (805 aa)
CtsdCathepsin D; Acid protease active in intracellular protein breakdown. Plays a role in APP processing following cleavage and activation by ADAM30 which leads to APP degradation; Belongs to the peptidase A1 family. (410 aa)
MmeNeprilysin; Thermolysin-like specificity, but is almost confined on acting on polypeptides of up to 30 amino acids. Biologically important in the destruction of opioid peptides such as Met- and Leu-enkephalins by cleavage of a Gly-Phe bond. Able to cleave angiotensin-1, angiotensin-2 and angiotensin 1-9. Involved in the degradation of atrial natriuretic factor (ANF) (By similarity). Displays UV-inducible elastase activity toward skin preelastic and elastic fibers. (750 aa)
Your Current Organism:
Mus musculus
NCBI taxonomy Id: 10090
Other names: LK3 transgenic mice, M. musculus, Mus sp. 129SV, house mouse, mouse, nude mice, transgenic mice
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