STRINGSTRING
Vtn Vtn Hsp90ab1 Hsp90ab1 Ins2 Ins2 Acan Acan Cilp Cilp Prg4 Prg4 Col11a1 Col11a1 Spp1 Spp1 Aspnl1 Aspnl1 Ogn-2 Ogn-2 Comp Comp Thbs1 Thbs1 Matn3 Matn3 Col2a1 Col2a1 Ppia Ppia Clu Clu Bgn Bgn Col12a1 Col12a1 Hspa5 Hspa5 Aspn Aspn Ogn Ogn Col9a1 Col9a1 Lum Lum Dcn Dcn Col1a1 Col1a1 Chad Chad Fmod Fmod Prelp Prelp Col6a2 Col6a2 Col6a1 Col6a1
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:
a 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 to 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:
VtnVitronectin. (490 aa)
Hsp90ab1Heat shock protein HSP 90-beta; Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co- chaperones that modulate its substrate recognition, ATPase cycle and chaperone function. Engages with a range of client protein classes via its interact [...] (724 aa)
Ins2Insulin-2 A chain; Insulin decreases blood glucose concentration. It increases cell permeability to monosaccharides, amino acids and fatty acids. It accelerates glycolysis, the pentose phosphate cycle, and glycogen synthesis in liver. (110 aa)
AcanAggrecan core protein; 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. May play a regulatory role in the matrix assembly of the cartilage. (2162 aa)
CilpCartilage intermediate layer protein. (1183 aa)
Prg4Proteoglycan 4. (1060 aa)
Col11a1Collagen alpha-1(XI) chain; May play an important role in fibrillogenesis by controlling lateral growth of collagen II fibrils. (1804 aa)
Spp1Osteopontin; Binds tightly to hydroxyapatite. Appears to form an integral part of the mineralized matrix. Probably important to cell-matrix interaction; Belongs to the osteopontin family. (317 aa)
Aspnl1Asporin. (375 aa)
Ogn-2Osteoglycin. (298 aa)
CompCartilage oligomeric matrix protein; May play a role in the structural integrity of cartilage via its interaction with other extracellular matrix proteins such as the collagens and fibronectin. Can mediate the interaction of chondrocytes with the cartilage extracellular matrix through interaction with cell surface integrin receptors. Could play a role in the pathogenesis of osteoarthritis. Potent suppressor of apoptosis in both primary chondrocytes and transformed cells. Suppresses apoptosis by blocking the activation of caspase-3 and by inducing the IAP family of survival proteins (BI [...] (755 aa)
Thbs1Thrombospondin 1. (1152 aa)
Matn3Matrilin 3. (463 aa)
Col2a1Collagen alpha-1(II) chain; Type II collagen is specific for cartilaginous tissues. It is essential for the normal embryonic development of the skeleton, for linear growth and for the ability of cartilage to resist compressive forces. (1419 aa)
PpiaPeptidyl-prolyl cis-trans isomerase; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family. (167 aa)
CluClusterin alpha chain; Functions as extracellular chaperone that prevents aggregation of non native 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 lysos [...] (447 aa)
BgnBiglycan; May be involved in collagen fiber assembly. (369 aa)
Col12a1Collagen alpha-1(XII) chain; Type XII collagen interacts with type I collagen-containing fibrils, the COL1 domain could be associated with the surface of the fibrils, and the COL2 and NC3 domains may be localized in the perifibrillar matrix. (3143 aa)
Hspa5Endoplasmic reticulum chaperone BiP; Endoplasmic reticulum chaperone that plays a key role in protein folding and quality control in the endoplasmic reticulum lumen (By similarity). Involved in the correct folding of proteins and degradation of misfolded proteins via its interaction with DNAJC10/ERdj5, probably to facilitate the release of DNAJC10/ERdj5 from its substrate (By similarity). Acts as a key repressor of the ERN1/IRE1-mediated unfolded protein response (UPR). In the unstressed endoplasmic reticulum, recruited by DNAJB9/ERdj4 to the luminal region of ERN1/IRE1, leading to dis [...] (654 aa)
AspnAsporin. (375 aa)
OgnOsteoglycin (Predicted). (298 aa)
Col9a1Collagen alpha-1(IX) chain; Structural component of hyaline cartilage and vitreous of the eye; Belongs to the fibril-associated collagens with interrupted helices (FACIT) family. (934 aa)
LumLumican; Belongs to the small leucine-rich proteoglycan (SLRP) family. SLRP class II subfamily. (338 aa)
DcnDecorin; May affect the rate of fibrils formation (By similarity). May be implicated in the dilatation of the rat cervix. (354 aa)
Col1a1Collagen alpha-1(I) chain; Type I collagen is a member of group I collagen (fibrillar forming collagen); Belongs to the fibrillar collagen family. (1453 aa)
ChadChondroadherin; Promotes attachment of chondrocytes, fibroblasts, and osteoblasts. This binding is mediated (at least for chondrocytes and fibroblasts) by the integrin alpha(2)beta(1). May play an important role in the regulation of chondrocyte growth and proliferation (By similarity); Belongs to the small leucine-rich proteoglycan (SLRP) family. SLRP class IV subfamily. (401 aa)
FmodFibromodulin; Affects the rate of fibrils formation. May have a primary role in collagen fibrillogenesis (By similarity); Belongs to the small leucine-rich proteoglycan (SLRP) family. SLRP class II subfamily. (376 aa)
PrelpProlargin; May anchor basement membranes to the underlying connective tissue; Belongs to the small leucine-rich proteoglycan (SLRP) family. SLRP class II subfamily. (377 aa)
Col6a2Procollagen, type VI, alpha 2, isoform CRA_a. (1027 aa)
Col6a1Collagen type VI alpha 1 chain. (1025 aa)
Your Current Organism:
Rattus norvegicus
NCBI taxonomy Id: 10116
Other names: Buffalo rat, Norway rat, R. norvegicus, Rattus PC12 clone IS, Rattus sp. strain Wistar, Sprague-Dawley rat, Wistar rats, brown rat, laboratory rat, rat, rats, zitter rats
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