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  • 11.0 [archived version]
STRINGSTRING
LCN1 LCN1 ZG16B ZG16B ELN ELN HTN3 HTN3 LTF LTF CRYAB CRYAB CLU CLU LYZ LYZ BCAS2 BCAS2 A2M A2M NOS2 NOS2 HSPA5 HSPA5 NFKBIB NFKBIB HSPA6 HSPA6 IKBKB IKBKB HSPA4 HSPA4 HSPA12B HSPA12B SMAD6 SMAD6 HSPH1 HSPH1 HSPA13 HSPA13 HSPA12A HSPA12A CLUL1 CLUL1 HSPA9 HSPA9 ANKRD45 ANKRD45 HSPA4L HSPA4L SLC9C2 SLC9C2
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
Your Input:
LTFLactotransferrin; Lactoferroxins A, B and C have opioid antagonist activity. Lactoferroxin A shows preference for mu-receptors, while lactoferroxin B and C have somewhat higher degrees of preference for kappa-receptors than for mu-receptors; Transferrins (710 aa)
HSPA12BHeat shock protein family A member 12B; Belongs to the heat shock protein 70 family (686 aa)
LYZLysozyme C; Lysozymes have primarily a bacteriolytic function; those in tissues and body fluids are associated with the monocyte- macrophage system and enhance the activity of immunoagents; Lysozymes, c-type (148 aa)
LCN1Lipocalin-1; Could play a role in taste reception. Could be necessary for the concentration and delivery of sapid molecules in the gustatory system. Can bind various ligands, with chemical structures ranging from lipids and retinoids to the macrocyclic antibiotic rifampicin and even to microbial siderophores. Exhibits an extremely wide ligand pocket; Belongs to the calycin superfamily. Lipocalin family (176 aa)
HSPA13Heat shock 70 kDa protein 13; Has peptide-independent ATPase activity; Heat shock 70kDa proteins (471 aa)
SMAD6Mothers against decapentaplegic homolog 6; Acts as a mediator of TGF-beta and BMP antiflammatory activity. Suppresses IL1R-TLR signaling through its direct interaction with PEL1, preventing NF-kappa-B activation, nuclear transport and NF-kappa-B-mediated expression of proinflammatory genes. May block the BMP-SMAD1 signaling pathway by competing with SMAD4 for receptor-activated SMAD1-binding. Binds to regulatory elements in target promoter regions (496 aa)
HSPA4LHeat shock 70 kDa protein 4L; Possesses chaperone activity in vitro where it inhibits aggregation of citrate synthase; Belongs to the heat shock protein 70 family (839 aa)
HSPA9Stress-70 protein, mitochondrial; Chaperone protein which plays an important role in mitochondrial iron-sulfur cluster (ISC) biogenesis. Interacts with and stabilizes ISC cluster assembly proteins FXN, NFU1, NFS1 and ISCU. Regulates erythropoiesis via stabilization of ISC assembly. May play a role in the control of cell proliferation and cellular aging (By similarity); Belongs to the heat shock protein 70 family (679 aa)
HSPA4Heat shock protein family A member 4; Belongs to the heat shock protein 70 family (840 aa)
HSPA6Heat shock 70 kDa protein 6; Molecular chaperone implicated in a wide variety of cellular processes, including protection of the proteome from stress, folding and transport of newly synthesized polypeptides, activation of proteolysis of misfolded proteins and the formation and dissociation of protein complexes. Plays a pivotal role in the protein quality control system, ensuring the correct folding of proteins, the re-folding of misfolded proteins and controlling the targeting of proteins for subsequent degradation. This is achieved through cycles of ATP binding, ATP hydrolysis and ADP [...] (643 aa)
NFKBIBNF-kappa-B inhibitor beta; Inhibits NF-kappa-B by complexing with and trapping it in the cytoplasm. However, the unphosphorylated form resynthesized after cell stimulation is able to bind NF-kappa-B allowing its transport to the nucleus and protecting it to further NFKBIA- dependent inactivation. Association with inhibitor kappa B- interacting NKIRAS1 and NKIRAS2 prevent its phosphorylation rendering it more resistant to degradation, explaining its slower degradation; Ankyrin repeat domain containing (356 aa)
CLUClusterin; Isoform 1 functions as extracellular chaperone that prevents aggregation of nonnative proteins. Prevents stress- induced aggregation of blood plasma proteins. Inhibits formation of amyloid fibrils by APP, APOC2, B2M, CALCA, CSN3, SNCA and aggregation-prone LYZ variants (in vitro). Does not require ATP. Maintains partially unfolded proteins in a state appropriate for subsequent refolding by other chaperones, such as HSPA8/HSC70. Does not refold proteins by itself. Binding to cell surface receptors triggers internalization of the chaperone-client complex and subsequent lysosom [...] (449 aa)
HSPH1Heat shock protein 105 kDa; Acts as a nucleotide-exchange factor (NEF) for chaperone proteins HSPA1A and HSPA1B, promoting the release of ADP from HSPA1A/B thereby triggering client/substrate protein release. Prevents the aggregation of denatured proteins in cells under severe stress, on which the ATP levels decrease markedly. Inhibits HSPA8/HSC70 ATPase and chaperone activities (By similarity); Heat shock 70kDa proteins (858 aa)
A2MAlpha-2-macroglobulin; Is able to inhibit all four classes of proteinases by a unique ’trapping’ mechanism. This protein has a peptide stretch, called the ’bait region’ which contains specific cleavage sites for different proteinases. When a proteinase cleaves the bait region, a conformational change is induced in the protein which traps the proteinase. The entrapped enzyme remains active against low molecular weight substrates (activity against high molecular weight substrates is greatly reduced). Following cleavage in the bait region, a thioester bond is hydrolyzed and mediates the c [...] (1474 aa)
HSPA578 kDa glucose-regulated protein; Plays a role in facilitating the assembly of multimeric protein complexes inside the endoplasmic reticulum. Involved in the correct folding of proteins and degradation of misfolded proteins via its interaction with DNAJC10, probably to facilitate the release of DNAJC10 from its substrate (By similarity); Belongs to the heat shock protein 70 family (654 aa)
NOS2Nitric oxide synthase, inducible; Produces nitric oxide (NO) which is a messenger molecule with diverse functions throughout the body. In macrophages, NO mediates tumoricidal and bactericidal actions. Also has nitrosylase activity and mediates cysteine S-nitrosylation of cytoplasmic target proteins such PTGS2/COX2 (By similarity). As component of the iNOS-S100A8/9 transnitrosylase complex involved in the selective inflammatory stimulus-dependent S-nitrosylation of GAPDH on ’Cys-247’ implicated in regulation of the GAIT complex activity and probably multiple targets including ANXA5, EZR [...] (1153 aa)
ANKRD45Ankyrin repeat domain-containing protein 45; Ankyrin repeat domain containing (266 aa)
ELNElastin; Major structural protein of tissues such as aorta and nuchal ligament, which must expand rapidly and recover completely. Molecular determinant of the late arterial morphogenesis, stabilizing arterial structure by regulating proliferation and organization of vascular smooth muscle (By similarity) (786 aa)
SLC9C2Sodium/hydrogen exchanger 11; Involved in pH regulation; Solute carriers (1124 aa)
HSPA12AHeat shock protein family A member 12A (675 aa)
BCAS2Pre-mRNA-splicing factor SPF27; Component of the PRP19-CDC5L complex that forms an integral part of the spliceosome and is required for activating pre-mRNA splicing. May have a scaffolding role in the spliceosome assembly as it contacts all other components of the core complex. The PRP19-CDC5L complex may also play a role in the response to DNA damage (DDR) (225 aa)
ZG16BZymogen granule protein 16B; Belongs to the jacalin lectin family (208 aa)
IKBKBInhibitor of nuclear factor kappa-B kinase subunit beta; Serine kinase that plays an essential role in the NF- kappa-B signaling pathway which is activated by multiple stimuli such as inflammatory cytokines, bacterial or viral products, DNA damages or other cellular stresses. Acts as part of the canonical IKK complex in the conventional pathway of NF-kappa-B activation and phosphorylates inhibitors of NF-kappa-B on 2 critical serine residues. These modifications allow polyubiquitination of the inhibitors and subsequent degradation by the proteasome. In turn, free NF-kappa-B is transloc [...] (756 aa)
HTN3Histatin-3; Histatins are salivary proteins that are considered to be major precursors of the protective proteinaceous structure on tooth surfaces (enamel pellicle). In addition, histatins exhibit antibacterial and antifungal activities. His3-(20-43)-peptide (histatin-5) is especially effective against C.albicans and C.neoformans, and inhibits Lys-gingipain and Arg-gingipain (rgpB) from P.gingivalis. In addition, His3-(20-43)-peptide is a potent inhibitor of metalloproteinases MMP2 and MMP9 (51 aa)
CRYABAlpha-crystallin B chain; May contribute to the transparency and refractive index of the lens. Has chaperone-like activity, preventing aggregation of various proteins under a wide range of stress conditions; Small heat shock proteins (175 aa)
CLUL1Clusterin-like protein 1; Clusterin like 1 (518 aa)
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo sapiens, human, man
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