node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
ERH | PVRL4 | ENSP00000451080 | ENSP00000356991 | enhancer of rudimentary homolog (Drosophila); May have a role in the cell cycle | poliovirus 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 | 0.577 |
IGSF11 | PVRL4 | ENSP00000377370 | ENSP00000356991 | immunoglobulin superfamily, member 11; Functions as a cell adhesion molecule through homophilic interaction. Stimulates cell growth | poliovirus 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 | 0.960 |
MLLT4 | PICK1 | ENSP00000375956 | ENSP00000349465 | myeloid/lymphoid or mixed-lineage leukemia (trithorax homolog, Drosophila); translocated to, 4 | protein interacting with PRKCA 1; Probable adapter protein that bind to and organize the subcellular localization of a variety of membrane proteins containing some PDZ recognition sequence. Involved in the clustering of various receptors, possibly by acting at the receptor internalization level. Plays a role in synaptic plasticity by regulating the trafficking and internalization of AMPA receptors. May be regulated upon PRKCA activation. May regulate heteromeric ASIC1/ASIC3 channel | 0.690 |
MLLT4 | PVRL1 | ENSP00000375956 | ENSP00000264025 | myeloid/lymphoid or mixed-lineage leukemia (trithorax homolog, Drosophila); translocated to, 4 | poliovirus 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 | 0.998 |
MLLT4 | PVRL2 | ENSP00000375956 | ENSP00000252483 | myeloid/lymphoid or mixed-lineage leukemia (trithorax homolog, Drosophila); translocated to, 4 | poliovirus receptor-related 2 (herpesvirus entry mediator B); Probable cell adhesion protein | 0.999 |
MLLT4 | PVRL3 | ENSP00000375956 | ENSP00000418070 | myeloid/lymphoid or mixed-lineage leukemia (trithorax homolog, Drosophila); translocated to, 4 | poliovirus 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 [...] | 0.998 |
MLLT4 | PVRL4 | ENSP00000375956 | ENSP00000356991 | myeloid/lymphoid or mixed-lineage leukemia (trithorax homolog, Drosophila); translocated to, 4 | poliovirus 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 | 0.996 |
PARD3 | PVRL1 | ENSP00000363921 | ENSP00000264025 | par-3 partitioning defective 3 homolog (C. elegans) | poliovirus 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 | 0.951 |
PARD3 | PVRL2 | ENSP00000363921 | ENSP00000252483 | par-3 partitioning defective 3 homolog (C. elegans) | poliovirus receptor-related 2 (herpesvirus entry mediator B); Probable cell adhesion protein | 0.814 |
PARD3 | PVRL3 | ENSP00000363921 | ENSP00000418070 | par-3 partitioning defective 3 homolog (C. elegans) | poliovirus 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 [...] | 0.927 |
PARD3 | PVRL4 | ENSP00000363921 | ENSP00000356991 | par-3 partitioning defective 3 homolog (C. elegans) | poliovirus 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 | 0.800 |
PICK1 | MLLT4 | ENSP00000349465 | ENSP00000375956 | protein interacting with PRKCA 1; Probable adapter protein that bind to and organize the subcellular localization of a variety of membrane proteins containing some PDZ recognition sequence. Involved in the clustering of various receptors, possibly by acting at the receptor internalization level. Plays a role in synaptic plasticity by regulating the trafficking and internalization of AMPA receptors. May be regulated upon PRKCA activation. May regulate heteromeric ASIC1/ASIC3 channel | myeloid/lymphoid or mixed-lineage leukemia (trithorax homolog, Drosophila); translocated to, 4 | 0.690 |
PICK1 | PVRL2 | ENSP00000349465 | ENSP00000252483 | protein interacting with PRKCA 1; Probable adapter protein that bind to and organize the subcellular localization of a variety of membrane proteins containing some PDZ recognition sequence. Involved in the clustering of various receptors, possibly by acting at the receptor internalization level. Plays a role in synaptic plasticity by regulating the trafficking and internalization of AMPA receptors. May be regulated upon PRKCA activation. May regulate heteromeric ASIC1/ASIC3 channel | poliovirus receptor-related 2 (herpesvirus entry mediator B); Probable cell adhesion protein | 0.571 |
PICK1 | PVRL4 | ENSP00000349465 | ENSP00000356991 | protein interacting with PRKCA 1; Probable adapter protein that bind to and organize the subcellular localization of a variety of membrane proteins containing some PDZ recognition sequence. Involved in the clustering of various receptors, possibly by acting at the receptor internalization level. Plays a role in synaptic plasticity by regulating the trafficking and internalization of AMPA receptors. May be regulated upon PRKCA activation. May regulate heteromeric ASIC1/ASIC3 channel | poliovirus 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 | 0.579 |
PVRL1 | MLLT4 | ENSP00000264025 | ENSP00000375956 | poliovirus 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 | myeloid/lymphoid or mixed-lineage leukemia (trithorax homolog, Drosophila); translocated to, 4 | 0.998 |
PVRL1 | PARD3 | ENSP00000264025 | ENSP00000363921 | poliovirus 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 | par-3 partitioning defective 3 homolog (C. elegans) | 0.951 |
PVRL1 | PVRL2 | ENSP00000264025 | ENSP00000252483 | poliovirus 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 | poliovirus receptor-related 2 (herpesvirus entry mediator B); Probable cell adhesion protein | 0.918 |
PVRL1 | PVRL3 | ENSP00000264025 | ENSP00000418070 | poliovirus 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 | poliovirus 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 [...] | 0.988 |
PVRL1 | PVRL4 | ENSP00000264025 | ENSP00000356991 | poliovirus 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 | poliovirus 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 | 0.990 |
PVRL1 | TIGIT | ENSP00000264025 | ENSP00000373167 | poliovirus 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 | T cell immunoreceptor with Ig and ITIM domains; Binds with high affinity to the poliovirus receptor (PVR) which causes increased secretion of IL10 and decreased secretion of IL12B and suppresses T-cell activation by promoting the generation of mature immunoregulatory dendritic cells | 0.416 |