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STRINGSTRING
CTSE CTSE KLK7 KLK7 PRSS55 PRSS55 CELA1 CELA1 ARL17B ARL17B TTLL4 TTLL4 PCSK2 PCSK2 VPS39 VPS39 PRSS57 PRSS57 TGFBRAP1 TGFBRAP1 FBXL13 FBXL13 AGTPBP1 AGTPBP1 TMOD1 TMOD1 PHLPP1 PHLPP1 PRSS36 PRSS36 ARL17A ARL17A FOXK1 FOXK1 PNKP PNKP TMPRSS9 TMPRSS9
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
Your Input:
TMOD1Tropomodulin-1; Blocks the elongation and depolymerization of the actin filaments at the pointed end. The Tmod/TM complex contributes to the formation of the short actin protofilament, which in turn defines the geometry of the membrane skeleton. May play an important role in regulating the organization of actin filaments by preferentially binding to a specific tropomyosin isoform at its N-terminus; Tropomodulins (359 aa)
PCSK2Neuroendocrine convertase 2; Involved in the processing of hormone and other protein precursors at sites comprised of pairs of basic amino acid residues. Responsible for the release of glucagon from proglucagon in pancreatic A cells; Belongs to the peptidase S8 family. Furin subfamily (638 aa)
PHLPP1PH domain leucine-rich repeat-containing protein phosphatase 1; Protein phosphatase involved in regulation of Akt and PKC signaling. Mediates dephosphorylation in the C-terminal domain hydrophobic motif of members of the AGC Ser/Thr protein kinase family; specifically acts on ’Ser-473’ of AKT2 and AKT3, ’Ser-660’ of PRKCB and ’Ser-657’ of PRKCA. Isoform 2 seems to have a major role in regulating Akt signaling in hippocampal neurons (By similarity). Akt regulates the balance between cell survival and apoptosis through a cascade that primarily alters the function of transcription factors [...] (1717 aa)
PRSS36Polyserase-2; Serine protease. Hydrolyzes the peptides N-t-Boc-Gln- Ala-Arg-AMC and N-t-Boc-Gln-Gly-Arg-AMC and, to a lesser extent, N-t-Boc-Ala-Phe-Lys-AMC and N-t-Boc-Val-Leu-Lys-AMC. Has a preference for substrates with an Arg instead of a Lys residue in position P1; Belongs to the peptidase S1 family (855 aa)
CELA1Chymotrypsin-like elastase family member 1; Acts upon elastin (258 aa)
FBXL13F-box/LRR-repeat protein 13; Substrate-recognition component of the SCF (SKP1-CUL1-F- box protein)-type E3 ubiquitin ligase complex; Cilia and flagella associated (735 aa)
PNKPBifunctional polynucleotide phosphatase/kinase; Plays a key role in the repair of DNA damage, functioning as part of both the non-homologous end-joining (NHEJ) and base excision repair (BER) pathways. Through its two catalytic activities, PNK ensures that DNA termini are compatible with extension and ligation by either removing 3’-phosphates from, or by phosphorylating 5’-hydroxyl groups on, the ribose sugar of the DNA backbone; HAD Asp-based non-protein phosphatases (521 aa)
FOXK1Forkhead box protein K1; Transcriptional regulator that binds to the upstream enhancer region (CCAC box) of myoglobin gene (By similarity). Important regulatory factor of the myogenic progenitor cell population (By similarity). Involved in the cell cycle process, promotes proliferation by repressing Foxo4 transcriptional activity and the cyclin-dependent kinase inhibitor, p21CIP, in the myogenic progenitor cells (By similarity). Represses myogenic differentiation by inhibiting MEFC acitivity (By similarity). Has a role in remodeling processes of adult muscles that occur in response to [...] (733 aa)
TMPRSS9Transmembrane 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; Belongs to the peptidase S1 family (1059 aa)
PRSS55Serine protease 55; Probable serine protease (352 aa)
VPS39Vam6/Vps39-like protein; Regulator of TGF-beta/activin signaling, inhibiting SMAD3- and activating SMAD2-dependent transcription. Acts by interfering with SMAD3/SMAD4 complex formation, this would lead to inhibition of SMAD3-dependent transcription and relieve SMAD3 inhibition of SMAD2-dependent promoters, thus increasing SMAD2- dependent transcription. Does not affect TGF-beta-induced SMAD2 or SMAD3 phosphorylation, nor SMAD2/SMAD4 complex formation; Belongs to the VAM6/VPS39 family (886 aa)
ARL17AADP ribosylation factor like GTPase 17A; GTP-binding protein that functions as an allosteric activator of the cholera toxin catalytic subunit, an ADP- ribosyltransferase. Involved in protein trafficking; may modulate vesicle budding and uncoating within the Golgi apparatus (By similarity); ARF GTPase family (177 aa)
AGTPBP1Cytosolic carboxypeptidase 1; 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 gene-encoded polyglutamates from the carboxy-terminus of target proteins such as MYLK. 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; Armadillo-like helical domain containing (1278 aa)
CTSECathepsin E; May have a role in immune function. Probably involved in the processing of antigenic peptides during MHC class II-mediated antigen presentation. May play a role in activation-induced lymphocyte depletion in the thymus, and in neuronal degeneration and glial cell activation in the brain; Cathepsins (396 aa)
KLK7Kallikrein-7; May catalyze the degradation of intercellular cohesive structures in the cornified layer of the skin in the continuous shedding of cells from the skin surface. Specific for amino acid residues with aromatic side chains in the P1 position. Cleaves insulin A chain at ’14-Tyr-|-Gln-15’ and insulin B chain at ’6- Leu-|-Cys-7’, ’16-Tyr-|-Leu-17’, ’25-Phe-|-Tyr-26’ and ’26-Tyr-|- Thr-27’. Could play a role in the activation of precursors to inflammatory cytokines; Kallikreins (253 aa)
TTLL4Tubulin polyglutamylase TTLL4; Glutamylase which preferentially modifies beta-tubulin and non-tubulin proteins, such as NAP1L1, NAP1L4 and CGAS/MB21D1. Involved in the side-chain initiation step of the polyglutamylation reaction rather than in the elongation step. Involved in formation of short side-chains. Mediates initiation of polyglutamylation of nucleosome assembly proteins NAP1L1 and NAP1L4. Also acts as a monoglutamylase- generates monoglutamylation of CGAS/MB21D1, leading to impair the nucleotidyltransferase activity of CGAS/MB21D1; Tubulin tyrosine ligase family (1199 aa)
TGFBRAP1Transforming growth factor-beta receptor-associated protein 1; Plays a role in the TGF-beta/activin signaling pathway. It associates with inactive heteromeric TGF-beta and activin receptor complexes, mainly through the type II receptor, and is released upon activation of signaling. May recruit SMAD4 to the vicinity of the receptor complex and facilitate its interaction with receptor-regulated Smads, such as SMAD2 (860 aa)
ARL17BADP-ribosylation factor-like protein 17; GTP-binding protein that functions as an allosteric activator of the cholera toxin catalytic subunit, an ADP- ribosyltransferase. Involved in protein trafficking; may modulate vesicle budding and uncoating within the Golgi apparatus (By similarity); ARF GTPase family (177 aa)
PRSS57Serine protease 57; Serine protease that cleaves preferentially after Arg residues. Can also cleave after citrulline (deimidated arginine) and methylarginine residues; Belongs to the peptidase S1 family (283 aa)
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo sapiens, human, man
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