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  • 11.0 [archived version]
STRINGSTRING
VAT1L VAT1L F10 F10 F2 F2 F11 F11 PROC PROC RBBP5 RBBP5 SERPIND1 SERPIND1 KMT2A KMT2A ASH2L ASH2L PRSS21 PRSS21 CTSW CTSW WDR37 WDR37 CTSK CTSK CTSG CTSG CTSV CTSV ELANE ELANE CTSC CTSC CTSL CTSL GRN GRN CTSB CTSB CTSZ CTSZ CTSO CTSO CTSH CTSH CTSS CTSS CTSF CTSF IRF2 IRF2
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:
some 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 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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PRSS21Testisin; Could regulate proteolytic events associated with testicular germ cell maturation; Serine proteases (314 aa)
GRNGranulins; Granulins have possible cytokine-like activity. They may play a role in inflammation, wound repair, and tissue remodeling (593 aa)
SERPIND1Heparin cofactor 2; Thrombin inhibitor activated by the glycosaminoglycans, heparin or dermatan sulfate. In the presence of the latter, HC-II becomes the predominant thrombin inhibitor in place of antithrombin III (AT-III). Also inhibits chymotrypsin, but in a glycosaminoglycan-independent manner; Belongs to the serpin family (499 aa)
CTSGCathepsin G; Serine protease with trypsin- and chymotrypsin-like specificity. Cleaves complement C3. Has antibacterial activity against the Gram-negative bacterium P.aeruginosa, antibacterial activity is inhibited by LPS from P.aeruginosa, Z-Gly-Leu-Phe- CH2Cl and phenylmethylsulfonyl fluoride; Belongs to the peptidase S1 family (255 aa)
CTSZCathepsin Z; Exhibits carboxy-monopeptidase as well as carboxy- dipeptidase activity; Cathepsins (303 aa)
CTSHPro-cathepsin H; Important for the overall degradation of proteins in lysosomes; Belongs to the peptidase C1 family (335 aa)
CTSCDipeptidyl peptidase 1; Thiol protease. Has dipeptidylpeptidase activity. Active against a broad range of dipeptide substrates composed of both polar and hydrophobic amino acids. Proline cannot occupy the P1 position and arginine cannot occupy the P2 position of the substrate. Can act as both an exopeptidase and endopeptidase. Activates serine proteases such as elastase, cathepsin G and granzymes A and B. Can also activate neuraminidase and factor XIII (463 aa)
PROCVitamin K-dependent protein C; Protein C is a vitamin K-dependent serine protease that regulates blood coagulation by inactivating factors Va and VIIIa in the presence of calcium ions and phospholipids. Exerts a protective effect on the endothelial cell barrier function; Belongs to the peptidase S1 family (461 aa)
RBBP5Retinoblastoma-binding protein 5; In embryonic stem (ES) cells, plays a crucial role in the differentiation potential, particularly along the neural lineage, regulating gene induction and H3 ’Lys-4’ methylation at key developmental loci, including that mediated by retinoic acid (By similarity). As part of the MLL1/MLL complex, involved in mono-, di- and trimethylation at ’Lys-4’ of histone H3. Histone H3 ’Lys-4’ methylation represents a specific tag for epigenetic transcriptional activation; WD repeat domain containing (538 aa)
CTSKCathepsin K; Closely involved in osteoclastic bone resorption and may participate partially in the disorder of bone remodeling. Displays potent endoprotease activity against fibrinogen at acid pH. May play an important role in extracellular matrix degradation; Cathepsins (329 aa)
VAT1LSynaptic vesicle membrane protein VAT-1 homolog-like; Vesicle amine transport 1 like; Belongs to the zinc-containing alcohol dehydrogenase family. Quinone oxidoreductase subfamily (419 aa)
F2Prothrombin; Thrombin, which cleaves bonds after Arg and Lys, converts fibrinogen to fibrin and activates factors V, VII, VIII, XIII, and, in complex with thrombomodulin, protein C. Functions in blood homeostasis, inflammation and wound healing; Belongs to the peptidase S1 family (622 aa)
CTSFCathepsin F; Thiol protease which is believed to participate in intracellular degradation and turnover of proteins. Has also been implicated in tumor invasion and metastasis; Cathepsins (484 aa)
CTSWCathepsin W; May have a specific function in the mechanism or regulation of T-cell cytolytic activity; Cathepsins (376 aa)
ASH2LSet1/Ash2 histone methyltransferase complex subunit ASH2; Component of the Set1/Ash2 histone methyltransferase (HMT) complex, a complex that specifically methylates ’Lys-4’ of histone H3, but not if the neighboring ’Lys-9’ residue is already methylated. As part of the MLL1/MLL complex it is involved in methylation and dimethylation at ’Lys-4’ of histone H3. May function as a transcriptional regulator. May play a role in hematopoiesis; PHD finger proteins (628 aa)
CTSLCathepsin L1; Important for the overall degradation of proteins in lysosomes; Cathepsins (333 aa)
CTSBCathepsin B; Thiol protease which is believed to participate in intracellular degradation and turnover of proteins. Has also been implicated in tumor invasion and metastasis; Cathepsins (339 aa)
WDR37WD repeat-containing protein 37; WD repeat domain containing (494 aa)
CTSSCathepsin S; Thiol protease. Key protease responsible for the removal of the invariant chain from MHC class II molecules. The bond- specificity of this proteinase is in part similar to the specificities of cathepsin L and cathepsin N; Cathepsins (331 aa)
F10Coagulation factor X; Factor Xa is a vitamin K-dependent glycoprotein that converts prothrombin to thrombin in the presence of factor Va, calcium and phospholipid during blood clotting; Gla domain containing (488 aa)
IRF2Interferon regulatory factor 2; Specifically binds to the upstream regulatory region of type I IFN and IFN-inducible MHC class I genes (the interferon consensus sequence (ICS)) and represses those genes. Also acts as an activator for several genes including H4 and IL7. Constitutively binds to the ISRE promoter to activate IL7. Involved in cell cycle regulation through binding the site II (HiNF-M) promoter region of H4 and activating transcription during cell growth. Antagonizes IRF1 transcriptional activation (349 aa)
F11Coagulation factor XI; Factor XI triggers the middle phase of the intrinsic pathway of blood coagulation by activating factor IX (625 aa)
CTSOCathepsin O; Proteolytic enzyme possibly involved in normal cellular protein degradation and turnover; Belongs to the peptidase C1 family (321 aa)
KMT2AHistone-lysine N-methyltransferase 2A; Histone methyltransferase that plays an essential role in early development and hematopoiesis. Catalytic subunit of the MLL1/MLL complex, a multiprotein complex that mediates both methylation of ’Lys-4’ of histone H3 (H3K4me) complex and acetylation of ’Lys-16’ of histone H4 (H4K16ac). In the MLL1/MLL complex, it specifically mediates H3K4me, a specific tag for epigenetic transcriptional activation. Has weak methyltransferase activity by itself, and requires other component of the MLL1/MLL complex to obtain full methyltransferase activity. Has no [...] (3972 aa)
CTSVCathepsin L2; Cysteine protease. May have an important role in corneal physiology; Belongs to the peptidase C1 family (334 aa)
ELANENeutrophil elastase; Modifies the functions of natural killer cells, monocytes and granulocytes. Inhibits C5a-dependent neutrophil enzyme release and chemotaxis (267 aa)
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo sapiens, human, man
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