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.
Node Size
small nodes:
protein of unknown 3D structure
protein of unknown 3D structure
large nodes:
some 3D structure is known or predicted
some 3D structure is known or predicted
Node Color
colored nodes:
query proteins and first shell of interactors
query proteins and first shell of interactors
white nodes:
second shell of interactors
second shell of interactors
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 each other.
Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
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Your Input:
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 | KLK14 | kallikrein-related peptidase 14; Serine-type endopeptidase with a dual trypsin-like and chymotrypsin-like substrate specificity. May activate/inactivate the proteinase-activated receptors F2R, F2RL1 and F2RL3 and other kallikreins including KLK1, KLK3, KLK5 and KLK11. May function in seminal clot liquefaction through direct cleavage of the semenogelin SEMG1 and SEMG2 and activation of KLK3. May function through desmoglein DSG1 cleavage in epidermal desquamation a process by which the most superficial corneocytes are shed from the skin surface. May be involved in several aspects of tumo [...] (267 aa) | ||
 | PDXP | pyridoxal (pyridoxine, vitamin B6) phosphatase; Protein serine phosphatase that dephosphorylates ’Ser-3’ in cofilin and probably also dephosphorylates phospho-serine residues in DSTN. Regulates cofilin-dependent actin cytoskeleton reorganization. Required for normal progress through mitosis and normal cytokinesis. Does not dephosphorylate phospho-threonines in LIMK1. Does not dephosphorylate peptides containing phospho- tyrosine. Pyridoxal phosphate phosphatase. Has some activity towards pyridoxal 5’-phosphate (PLP), pyridoxine 5’-phosphate (PMP) and pyridoxine 5’-phosphate (PNP), with [...] (296 aa) | ||
 | GZMH | granzyme H (cathepsin G-like 2, protein h-CCPX); Cytotoxic chymotrypsin-like serine protease with preference for bulky and aromatic residues at the P1 position and acidic residues at the P3’ and P4’ sites. Probably necessary for target cell lysis in cell-mediated immune responses. Participates in the antiviral response via direct cleavage of several proteins essential for viral replication (246 aa) | ||
 | GZMK | granzyme K (granzyme 3; tryptase II) (264 aa) | ||
 | PRTN3 | proteinase 3 (256 aa) | ||
 | ENSG00000269741 | Kallikrein-9 (250 aa) | ||
 | ELANE | elastase, neutrophil expressed; Modifies the functions of natural killer cells, monocytes and granulocytes. Inhibits C5a-dependent neutrophil enzyme release and chemotaxis (267 aa) | ||
 | KLKB1 | kallikrein B, plasma (Fletcher factor) 1; The enzyme cleaves Lys-Arg and Arg-Ser bonds. It activates, in a reciprocal reaction, factor XII after its binding to a negatively charged surface. It also releases bradykinin from HMW kininogen and may also play a role in the renin-angiotensin system by converting prorenin into renin (638 aa) | ||
 | HABP2 | hyaluronan binding protein 2; Cleaves the alpha-chain at multiple sites and the beta- chain between ’Lys-53’ and ’Lys-54’ but not the gamma-chain of fibrinogen and therefore does not initiate the formation of the fibrin clot and does not cause the fibrinolysis directly. It does not cleave (activate) prothrombin and plasminogen but converts the inactive single chain urinary plasminogen activator (pro- urokinase) to the active two chain form. Activates coagulation factor VII (560 aa) | ||
 | MASP1 | mannan-binding lectin serine peptidase 1 (C4/C2 activating component of Ra-reactive factor) (728 aa) | ||
 | PRSS37 | protease, serine, 37 (235 aa) | ||
 | C2 | complement component 2 (752 aa) | ||
 | PRSS1 | protease, serine, 1 (trypsin 1) (247 aa) | ||
 | KLK2 | kallikrein-related peptidase 2; Glandular kallikreins cleave Met-Lys and Arg-Ser bonds in kininogen to release Lys-bradykinin (261 aa) | ||
 | PRSS50 | protease, serine, 50; May be involved in proteolysis through its threonine endopeptidase activity (385 aa) | ||
 | PRSS57 | protease, serine, 57 (283 aa) | ||
 | C1S | complement component 1, s subcomponent (688 aa) | ||
 | TMPRSS9 | transmembrane protease, serine 9; Serase-1 and serase-2 are serine proteases that hydrolyze the peptides N-t-Boc-Gln-Ala-Arg-AMC and N-t-Boc-Gln- Gly-Arg-AMC. In contrast, N-t-Boc-Ala-Phe-Lys-AMC and N-t-Boc-Ala- Pro-Ala-AMC are not significantly hydrolyzed (1059 aa) | ||
 | PGP | phosphoglycolate phosphatase (321 aa) | ||
 | RIPK4 | receptor-interacting serine-threonine kinase 4; Involved in stratified epithelial development. It is a direct transcriptional target of TP63. Plays a role in NF-kappa-B activation (784 aa) | ||
 | ANGPTL5 | angiopoietin-like 5 (388 aa) | ||
 | CELA2B | chymotrypsin-like elastase family, member 2B; Acts upon elastin (269 aa) | ||
 | LILRB2 | leukocyte immunoglobulin-like receptor, subfamily B (with TM and ITIM domains), member 2; Receptor for class I MHC antigens. Recognizes a broad spectrum of HLA-A, HLA-B, HLA-C and HLA-G alleles. Involved in the down-regulation of the immune response and the development of tolerance. Competes with CD8A for binding to class I MHC antigens. Inhibits FCGR1A-mediated phosphorylation of cellular proteins and mobilization of intracellular calcium ions (598 aa) | ||
 | ACAN | aggrecan; This proteoglycan is a major component of extracellular matrix of cartilagenous tissues. A major function of this protein is to resist compression in cartilage. It binds avidly to hyaluronic acid via an N-terminal globular region (2530 aa) | ||
 | MST1 | macrophage stimulating 1 (hepatocyte growth factor-like) (725 aa) | ||
 | CFB | complement factor B (764 aa) | ||
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo, Homo sapiens, human, man
Other names: H. sapiens, Homo, Homo sapiens, human, man
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