(17 nodes) Zn_pept network (Mus musculus)

Nodes:

Network nodes represent proteins

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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colored nodes:
query proteins and first shell of interactors

white nodes:
second shell of interactors

Node Content

empty nodes:
proteins of unknown 3D structure

filled nodes:
a 3D structure is known or predicted

Edges:

Edges represent protein-protein associations

associations are meant to be specific and meaningful, i.e. proteins jointly contribute to a shared function; this does not necessarily mean they are physically binding to each other.

Known Interactions

from curated databases

experimentally determined

Predicted Interactions

gene neighborhood

gene fusions

gene co-occurrence

Others

textmining

co-expression

protein homology

Your Input:
	Aebp1	Adipocyte enhancer-binding protein 1; [Isoform 1]: As a positive regulator of collagen fibrillogenesis, it is probably involved in the organization and remodeling of the extracellular matrix; Belongs to the peptidase M14 family. (1128 aa)
	Cpb1	Carboxypeptidase B1 (Tissue). (415 aa)
	Cpxm1	Probable carboxypeptidase X1; May be involved in cell-cell interactions. No carboxypeptidase activity was found yet. (722 aa)
	Cpa3	Mast cell carboxypeptidase A. (417 aa)
	Cpm	Carboxypeptidase M; Specifically removes C-terminal basic residues (Arg or Lys) from peptides and proteins. It is believed to play important roles in the control of peptide hormone and growth factor activity at the cell surface, and in the membrane-localized degradation of extracellular proteins (By similarity). (443 aa)
	Cpd	Carboxypeptidase D; Belongs to the peptidase M14 family. (1377 aa)
	Cpb2	Carboxypeptidase 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)
	Cpa1	Carboxypeptidase A1; Carboxypeptidase that catalyzes the release of a C-terminal amino acid, but has little or no action with -Asp, -Glu, -Arg, -Lys or -Pro. (419 aa)
	Cpxm2	Inactive carboxypeptidase-like protein X2; May be involved in cell-cell interactions. (764 aa)
	Cpa6	Carboxypeptidase A6; May be involved in the proteolytic inactivation of enkephalins and neurotensin in some brain areas. May convert inactive angiotensin I into the biologically active angiotensin II. Releases a C-terminal amino acid, with preference for large hydrophobic C-terminal amino acids and shows only very weak activity toward small amino acids and histidine. (438 aa)
	Cpz	Carboxypeptidase Z; Cleaves substrates with C-terminal arginine residues. Probably modulates the Wnt signaling pathway, by cleaving some undefined protein. May play a role in cleavage during prohormone processing (By similarity); Belongs to the peptidase M14 family. (654 aa)
	Cpe	Carboxypeptidase E; Sorting receptor that directs prohormones to the regulated secretory pathway. Acts also as a prohormone processing enzyme in neuro/endocrine cells, removing dibasic residues from the C-terminal end of peptide hormone precursors after initial endoprotease cleavage. Belongs to the peptidase M14 family. (476 aa)
	Cpa4	Carboxypeptidase A4; Metalloprotease that could be involved in the histone hyperacetylation pathway. Releases a C-terminal amino acid, with preference for -Phe, -Leu, -Ile, -Met, -Tyr and -Val; Belongs to the peptidase M14 family. (420 aa)
	Cpa5	Carboxypeptidase A5. (436 aa)
	Cpa2	Carboxypeptidase A2. (417 aa)
	Agbl4	Cytosolic carboxypeptidase 6; Metallocarboxypeptidase that mediates deglutamylation of target proteins. Catalyzes the deglutamylation of polyglutamate side chains generated by post-translational polyglutamylation in proteins such as tubulins. Also removes polyglutamates from the carboxy-terminus of target proteins such as MYLK. Mediates deglutamylation of CGAS, regulating the antiviral activity of CGAS. Acts as a long-chain deglutamylase and specifically shortens long polyglutamate chains, while it is not able to remove the branching point glutamate, a process catalyzed by AGBL5/CCP5. (540 aa)
	Cpn1	Carboxypeptidase N catalytic chain; Protects the body from potent vasoactive and inflammatory peptides containing C-terminal Arg or Lys (such as kinins or anaphylatoxins) which are released into the circulation; Belongs to the peptidase M14 family. (457 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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Browse interactions in tabular form:

node1	node2	node1 accession	node2 accession	node1 annotation	node2 annotation	score
Cpa1	Cpa2	ENSMUSP00000031806	ENSMUSP00000093771	Carboxypeptidase A1; Carboxypeptidase that catalyzes the release of a C-terminal amino acid, but has little or no action with -Asp, -Glu, -Arg, -Lys or -Pro.	Carboxypeptidase A2.	0.966
Cpa1	Cpa3	ENSMUSP00000031806	ENSMUSP00000001921	Carboxypeptidase A1; Carboxypeptidase that catalyzes the release of a C-terminal amino acid, but has little or no action with -Asp, -Glu, -Arg, -Lys or -Pro.	Mast cell carboxypeptidase A.	0.917
Cpa1	Cpb1	ENSMUSP00000031806	ENSMUSP00000011607	Carboxypeptidase A1; Carboxypeptidase that catalyzes the release of a C-terminal amino acid, but has little or no action with -Asp, -Glu, -Arg, -Lys or -Pro.	Carboxypeptidase B1 (Tissue).	0.999
Cpa2	Cpa1	ENSMUSP00000093771	ENSMUSP00000031806	Carboxypeptidase A2.	Carboxypeptidase A1; Carboxypeptidase that catalyzes the release of a C-terminal amino acid, but has little or no action with -Asp, -Glu, -Arg, -Lys or -Pro.	0.966
Cpa2	Cpa3	ENSMUSP00000093771	ENSMUSP00000001921	Carboxypeptidase A2.	Mast cell carboxypeptidase A.	0.917
Cpa2	Cpb1	ENSMUSP00000093771	ENSMUSP00000011607	Carboxypeptidase A2.	Carboxypeptidase B1 (Tissue).	0.654
Cpa3	Cpa1	ENSMUSP00000001921	ENSMUSP00000031806	Mast cell carboxypeptidase A.	Carboxypeptidase A1; Carboxypeptidase that catalyzes the release of a C-terminal amino acid, but has little or no action with -Asp, -Glu, -Arg, -Lys or -Pro.	0.917
Cpa3	Cpa2	ENSMUSP00000001921	ENSMUSP00000093771	Mast cell carboxypeptidase A.	Carboxypeptidase A2.	0.917
Cpa6	Cpe	ENSMUSP00000035435	ENSMUSP00000048555	Carboxypeptidase A6; May be involved in the proteolytic inactivation of enkephalins and neurotensin in some brain areas. May convert inactive angiotensin I into the biologically active angiotensin II. Releases a C-terminal amino acid, with preference for large hydrophobic C-terminal amino acids and shows only very weak activity toward small amino acids and histidine.	Carboxypeptidase E; Sorting receptor that directs prohormones to the regulated secretory pathway. Acts also as a prohormone processing enzyme in neuro/endocrine cells, removing dibasic residues from the C-terminal end of peptide hormone precursors after initial endoprotease cleavage. Belongs to the peptidase M14 family.	0.413
Cpb1	Cpa1	ENSMUSP00000011607	ENSMUSP00000031806	Carboxypeptidase B1 (Tissue).	Carboxypeptidase A1; Carboxypeptidase that catalyzes the release of a C-terminal amino acid, but has little or no action with -Asp, -Glu, -Arg, -Lys or -Pro.	0.999
Cpb1	Cpa2	ENSMUSP00000011607	ENSMUSP00000093771	Carboxypeptidase B1 (Tissue).	Carboxypeptidase A2.	0.654
Cpb1	Cpb2	ENSMUSP00000011607	ENSMUSP00000022576	Carboxypeptidase B1 (Tissue).	Carboxypeptidase 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.	0.916
Cpb1	Cpe	ENSMUSP00000011607	ENSMUSP00000048555	Carboxypeptidase B1 (Tissue).	Carboxypeptidase E; Sorting receptor that directs prohormones to the regulated secretory pathway. Acts also as a prohormone processing enzyme in neuro/endocrine cells, removing dibasic residues from the C-terminal end of peptide hormone precursors after initial endoprotease cleavage. Belongs to the peptidase M14 family.	0.731
Cpb1	Cpn1	ENSMUSP00000011607	ENSMUSP00000026210	Carboxypeptidase B1 (Tissue).	Carboxypeptidase N catalytic chain; Protects the body from potent vasoactive and inflammatory peptides containing C-terminal Arg or Lys (such as kinins or anaphylatoxins) which are released into the circulation; Belongs to the peptidase M14 family.	0.507
Cpb2	Cpb1	ENSMUSP00000022576	ENSMUSP00000011607	Carboxypeptidase 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.	Carboxypeptidase B1 (Tissue).	0.916
Cpb2	Cpe	ENSMUSP00000022576	ENSMUSP00000048555	Carboxypeptidase 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.	Carboxypeptidase E; Sorting receptor that directs prohormones to the regulated secretory pathway. Acts also as a prohormone processing enzyme in neuro/endocrine cells, removing dibasic residues from the C-terminal end of peptide hormone precursors after initial endoprotease cleavage. Belongs to the peptidase M14 family.	0.617
Cpb2	Cpm	ENSMUSP00000022576	ENSMUSP00000020399	Carboxypeptidase 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.	Carboxypeptidase M; Specifically removes C-terminal basic residues (Arg or Lys) from peptides and proteins. It is believed to play important roles in the control of peptide hormone and growth factor activity at the cell surface, and in the membrane-localized degradation of extracellular proteins (By similarity).	0.517
Cpb2	Cpn1	ENSMUSP00000022576	ENSMUSP00000026210	Carboxypeptidase 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.	Carboxypeptidase N catalytic chain; Protects the body from potent vasoactive and inflammatory peptides containing C-terminal Arg or Lys (such as kinins or anaphylatoxins) which are released into the circulation; Belongs to the peptidase M14 family.	0.755
Cpe	Cpa6	ENSMUSP00000048555	ENSMUSP00000035435	Carboxypeptidase E; Sorting receptor that directs prohormones to the regulated secretory pathway. Acts also as a prohormone processing enzyme in neuro/endocrine cells, removing dibasic residues from the C-terminal end of peptide hormone precursors after initial endoprotease cleavage. Belongs to the peptidase M14 family.	Carboxypeptidase A6; May be involved in the proteolytic inactivation of enkephalins and neurotensin in some brain areas. May convert inactive angiotensin I into the biologically active angiotensin II. Releases a C-terminal amino acid, with preference for large hydrophobic C-terminal amino acids and shows only very weak activity toward small amino acids and histidine.	0.413
Cpe	Cpb1	ENSMUSP00000048555	ENSMUSP00000011607	Carboxypeptidase E; Sorting receptor that directs prohormones to the regulated secretory pathway. Acts also as a prohormone processing enzyme in neuro/endocrine cells, removing dibasic residues from the C-terminal end of peptide hormone precursors after initial endoprotease cleavage. Belongs to the peptidase M14 family.	Carboxypeptidase B1 (Tissue).	0.731