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PCMT1 PCMT1 CTSF CTSF CTSW CTSW DPP7 DPP7 FLNB FLNB CTSB CTSB CTSL CTSL CTSK CTSK CTSC CTSC CTSD CTSD JUN JUN CSTB CSTB SEC24A SEC24A PDCD6 PDCD6 CTSS CTSS CTSV CTSV CTSZ CTSZ OLFM4 OLFM4 CST3 CST3 CTSH CTSH PGLYRP1 PGLYRP1 MAT2A MAT2A ALDOC ALDOC NUDC NUDC SARNP SARNP CTSO CTSO
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 Color
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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PGLYRP1Peptidoglycan recognition protein 1; Pattern receptor that binds to murein peptidoglycans (PGN) of Gram-positive bacteria. Has bactericidal activity towards Gram-positive bacteria. May kill Gram-positive bacteria by interfering with peptidoglycan biosynthesis. Binds also to Gram- negative bacteria, and has bacteriostatic activity towards Gram- negative bacteria. Plays a role in innate immunity; Peptidoglycan recognition proteins (196 aa)
CTSZCathepsin Z; Exhibits carboxy-monopeptidase as well as carboxy- dipeptidase activity; Cathepsins (303 aa)
OLFM4Olfactomedin-4; May promote proliferation of pancreatic cancer cells by favoring the transition from the S to G2/M phase. In myeloid leukemic cell lines, inhibits cell growth and induces cell differentiation and apoptosis. May play a role in the inhibition of EIF4EBP1 phosphorylation/deactivation. Facilitates cell adhesion, most probably through interaction with cell surface lectins and cadherin (510 aa)
CTSHPro-cathepsin H; Important for the overall degradation of proteins in lysosomes; Belongs to the peptidase C1 family (335 aa)
ALDOCAldolase, fructose-bisphosphate C (364 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)
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. Involved in the pathogenesis of several diseases such as breast cancer and possibly Alzheimer disease; Cathepsins (412 aa)
PDCD6Programmed cell death protein 6; Calcium sensor that plays a key role in processes such as endoplasmic reticulum (ER)-Golgi vesicular transport, endosomal biogenesis or membrane repair. Acts as an adapter that bridges unrelated proteins or stabilizes weak protein-protein complexes in response to calcium- calcium-binding triggers exposure of apolar surface, promoting interaction with different sets of proteins thanks to 3 different hydrophobic pockets, leading to translocation to membranes. Involved in ER-Golgi transport by promoting the association between PDCD6IP and TSG101, thereby b [...] (191 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)
CSTBCystatin-B; This is an intracellular thiol proteinase inhibitor. Tightly binding reversible inhibitor of cathepsins L, H and B; Belongs to the cystatin family (98 aa)
MAT2AS-adenosylmethionine synthase isoform type-2; Catalyzes the formation of S-adenosylmethionine from methionine and ATP. The reaction comprises two steps that are both catalyzed by the same enzyme- formation of S-adenosylmethionine (AdoMet) and triphosphate, and subsequent hydrolysis of the triphosphate; Belongs to the AdoMet synthase family (395 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)
NUDCNuclear migration protein nudC; Plays a role in neurogenesis and neuronal migration (By similarity). Necessary for correct formation of mitotic spindles and chromosome separation during mitosis. Necessary for cytokinesis and cell proliferation; NudC family (331 aa)
SARNPSAP domain-containing ribonucleoprotein; Binds both single-stranded and double-stranded DNA with higher affinity for the single-stranded form. Specifically binds to scaffold/matrix attachment region DNA. Also binds single- stranded RNA. Enhances RNA unwinding activity of DDX39A. May participate in important transcriptional or translational control of cell growth, metabolism and carcinogenesis. Component of the TREX complex which is thought to couple mRNA transcription, processing and nuclear export, and specifically associates with spliced mRNA and not with unspliced pre-mRNA. TREX is [...] (210 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)
PCMT1Protein-L-isoaspartate(D-aspartate) O-methyltransferase; Catalyzes the methyl esterification of L-isoaspartyl and D-aspartyl residues in peptides and proteins that result from spontaneous decomposition of normal L-aspartyl and L-asparaginyl residues. It plays a role in the repair and/or degradation of damaged proteins. Acts on EIF4EBP2, microtubule-associated protein 2, calreticulin, clathrin light chains a and b, Ubiquitin carboxyl-terminal hydrolase isozyme L1, phosphatidylethanolamine- binding protein 1, stathmin, beta-synuclein and alpha-synuclein; Seven-beta-strand methyltransfera [...] (286 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)
JUNTranscription factor AP-1; Transcription factor that recognizes and binds to the enhancer heptamer motif 5’-TGA[CG]TCA-3’. Promotes activity of NR5A1 when phosphorylated by HIPK3 leading to increased steroidogenic gene expression upon cAMP signaling pathway stimulation. Involved in activated KRAS-mediated transcriptional activation of USP28 in colorectal cancer (CRC) cells. Binds to the USP28 promoter in colorectal cancer (CRC) cells; Basic leucine zipper proteins (331 aa)
DPP7Dipeptidyl peptidase 2; Plays an important role in the degradation of some oligopeptides; DASH family (492 aa)
CST3Cystatin-C; As an inhibitor of cysteine proteinases, this protein is thought to serve an important physiological role as a local regulator of this enzyme activity; Belongs to the cystatin family (146 aa)
SEC24AProtein transport protein Sec24A; Component of the coat protein complex II (COPII) which promotes the formation of transport vesicles from the endoplasmic reticulum (ER). The coat has two main functions, the physical deformation of the endoplasmic reticulum membrane into vesicles and the selection of cargo molecules for their transport to the Golgi complex. Plays a central role in cargo selection within the COPII complex and together with SEC24B may have a different specificity compared to SEC24C and SEC24D. May package preferentially cargos with cytoplasmic DxE or LxxLE motifs and may [...] (1093 aa)
CTSOCathepsin O; Proteolytic enzyme possibly involved in normal cellular protein degradation and turnover; Belongs to the peptidase C1 family (321 aa)
FLNBFilamin-B; Connects cell membrane constituents to the actin cytoskeleton. May promote orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. Anchors various transmembrane proteins to the actin cytoskeleton. Interaction with FLNA may allow neuroblast migration from the ventricular zone into the cortical plate. Various interactions and localizations of isoforms affect myotube morphology and myogenesis. Isoform 6 accelerates muscle differentiation in vitro; Belongs to the filamin family (2633 aa)
CTSVCathepsin L2; Cysteine protease. May have an important role in corneal physiology; Belongs to the peptidase C1 family (334 aa)
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo sapiens, human, man
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