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STRINGSTRING
PRNP PRNP PVRL4 PVRL4 PVR PVR PVRL3 PVRL3 CADM3 CADM3 PVRL1 PVRL1 PARD3 PARD3 MLLT4 MLLT4 PVRL2 PVRL2 CDH1 CDH1 CTNNB1 CTNNB1 CTNNA1 CTNNA1 UBC UBC
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 Size
small protein node
small nodes:
protein of unknown 3D structure
large protein node
large nodes:
some 3D structure is known or predicted
Node Color
colored protein node
colored nodes:
query proteins and first shell of interactors
non-colored protein node
white nodes:
second shell of interactors
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
database edge
from curated databases
experiment edge
experimentally determined
Predicted Interactions
neighborhood edge
gene neighborhood
fusion edge
gene fusions
cooccurrence edge
gene co-occurrence
Others
textmining edge
textmining
coexpression edge
co-expression
homology edge
protein homology
Your Input:
PVRL2poliovirus receptor-related 2 (herpesvirus entry mediator B); Probable cell adhesion protein (538 aa)
CDH1cadherin 1, type 1, E-cadherin (epithelial); Cadherins are calcium-dependent cell adhesion proteins. They preferentially interact with themselves in a homophilic manner in connecting cells; cadherins may thus contribute to the sorting of heterogeneous cell types. CDH1 is involved in mechanisms regulating cell-cell adhesions, mobility and proliferation of epithelial cells. Has a potent invasive suppressor role. It is a ligand for integrin alpha-E/beta-7 (882 aa)
PVRL1poliovirus receptor-related 1 (herpesvirus entry mediator C); Promotes cell-cell contacts by forming homophilic or heterophilic trans-dimers. Heterophilic interactions have been detected between PVRL1/nectin-1 and PVRL3/nectin-3 and between PVRL1/nectin-1 and PVRL4/nectin-4 (517 aa)
CTNNA1catenin (cadherin-associated protein), alpha 1, 102kDa; Associates with the cytoplasmic domain of a variety of cadherins. The association of catenins to cadherins produces a complex which is linked to the actin filament network, and which seems to be of primary importance for cadherins cell-adhesion properties. Can associate with both E- and N-cadherins. Originally believed to be a stable component of E-cadherin/catenin adhesion complexes and to mediate the linkage of cadherins to the actin cytoskeleton at adherens junctions. In contrast, cortical actin was found to be much more dynami [...] (906 aa)
CTNNB1catenin (cadherin-associated protein), beta 1, 88kDa; Key downstream component of the canonical Wnt signaling pathway. In the absence of Wnt, forms a complex with AXIN1, AXIN2, APC, CSNK1A1 and GSK3B that promotes phosphorylation on N-terminal Ser and Thr residues and ubiquitination of CTNNB1 via BTRC and its subsequent degradation by the proteasome. In the presence of Wnt ligand, CTNNB1 is not ubiquitinated and accumulates in the nucleus, where it acts as a coactivator for transcription factors of the TCF/LEF family, leading to activate Wnt responsive genes. Involved in the regulation [...] (781 aa)
UBCubiquitin C (685 aa)
PVRL4poliovirus receptor-related 4; Seems to be involved in cell adhesion through trans- homophilic and -heterophilic interactions, the latter including specifically interactions with PVRL2/nectin-1. Does not act as receptor for alpha-herpesvirus entry into cells (510 aa)
CADM3cell adhesion molecule 3; Involved in the cell-cell adhesion. Has both calcium- independent homophilic cell-cell adhesion activity and calcium- independent heterophilic cell-cell adhesion activity with IGSF4, PVRL1 and PVRL3. Interaction with EPB41L1 may regulate structure or function of cell-cell junctions (By similarity) (432 aa)
PARD3par-3 partitioning defective 3 homolog (C. elegans) (1356 aa)
PRNPprion protein (253 aa)
MLLT4myeloid/lymphoid or mixed-lineage leukemia (trithorax homolog, Drosophila); translocated to, 4 (1651 aa)
PVRpoliovirus receptor; Mediates NK cell adhesion and triggers NK cell effector functions. Binds two different NK cell receptors- CD96 and CD226. These interactions accumulates at the cell-cell contact site, leading to the formation of a mature immunological synapse between NK cell and target cell. This may trigger adhesion and secretion of lytic granules and IFN-gamma and activate cytoxicity of activated NK cells. May also promote NK cell-target cell modular exchange, and PVR transfer to the NK cell. This transfer is more important in some tumor cells expressing a lot of PVR, and may tri [...] (417 aa)
PVRL3poliovirus receptor-related 3; Plays a role in cell-cell adhesion through heterophilic trans-interactions with nectin-like proteins or nectins, such as trans-interaction with PVRL2/nectin-2 at Sertoli-spermatid junctions. Trans-interaction with PVR induces activation of CDC42 and RAC small G proteins through common signaling molecules such as SRC and RAP1. Also involved in the formation of cell-cell junctions, including adherens junctions and synapses. Induces endocytosis-mediated down-regulation of PVR from the cell surface, resulting in reduction of cell movement and proliferation. P [...] (549 aa)
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo, Homo sapiens, human, man
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