node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
ANK3 | KCNQ2 | ENSP00000280772 | ENSP00000352035 | ankyrin 3, node of Ranvier (ankyrin G); In skeletal muscle, required for costamere localization of DMD and betaDAG1 (By similarity). Membrane-cytoskeleton linker. May participate in the maintenance/targeting of ion channels and cell adhesion molecules at the nodes of Ranvier and axonal initial segments | potassium voltage-gated channel, KQT-like subfamily, member 2 | 0.917 |
ANK3 | KCNQ3 | ENSP00000280772 | ENSP00000373648 | ankyrin 3, node of Ranvier (ankyrin G); In skeletal muscle, required for costamere localization of DMD and betaDAG1 (By similarity). Membrane-cytoskeleton linker. May participate in the maintenance/targeting of ion channels and cell adhesion molecules at the nodes of Ranvier and axonal initial segments | potassium voltage-gated channel, KQT-like subfamily, member 3; Probably important in the regulation of neuronal excitability. Associates with KCNQ2 or KCNQ5 to form a potassium channel with essentially identical properties to the channel underlying the native M-current, a slowly activating and deactivating potassium conductance which plays a critical role in determining the subthreshold electrical excitability of neurons as well as the responsiveness to synaptic inputs | 0.585 |
ANK3 | NFASC | ENSP00000280772 | ENSP00000344786 | ankyrin 3, node of Ranvier (ankyrin G); In skeletal muscle, required for costamere localization of DMD and betaDAG1 (By similarity). Membrane-cytoskeleton linker. May participate in the maintenance/targeting of ion channels and cell adhesion molecules at the nodes of Ranvier and axonal initial segments | neurofascin | 0.992 |
ANK3 | NRCAM | ENSP00000280772 | ENSP00000368314 | ankyrin 3, node of Ranvier (ankyrin G); In skeletal muscle, required for costamere localization of DMD and betaDAG1 (By similarity). Membrane-cytoskeleton linker. May participate in the maintenance/targeting of ion channels and cell adhesion molecules at the nodes of Ranvier and axonal initial segments | neuronal cell adhesion molecule; Cell adhesion, ankyrin-binding protein involved in neuron-neuron adhesion. May play a role in the molecular assembly of the nodes of Ranvier (By similarity) | 0.986 |
ANK3 | PTPRN2 | ENSP00000280772 | ENSP00000374069 | ankyrin 3, node of Ranvier (ankyrin G); In skeletal muscle, required for costamere localization of DMD and betaDAG1 (By similarity). Membrane-cytoskeleton linker. May participate in the maintenance/targeting of ion channels and cell adhesion molecules at the nodes of Ranvier and axonal initial segments | protein tyrosine phosphatase, receptor type, N polypeptide 2; Implicated in development of nervous system and pancreatic endocrine cells | 0.477 |
ANK3 | SPTA1 | ENSP00000280772 | ENSP00000357130 | ankyrin 3, node of Ranvier (ankyrin G); In skeletal muscle, required for costamere localization of DMD and betaDAG1 (By similarity). Membrane-cytoskeleton linker. May participate in the maintenance/targeting of ion channels and cell adhesion molecules at the nodes of Ranvier and axonal initial segments | spectrin, alpha, erythrocytic 1 (elliptocytosis 2); Spectrin is the major constituent of the cytoskeletal network underlying the erythrocyte plasma membrane. It associates with band 4.1 and actin to form the cytoskeletal superstructure of the erythrocyte plasma membrane | 0.532 |
ANK3 | SPTBN4 | ENSP00000280772 | ENSP00000263373 | ankyrin 3, node of Ranvier (ankyrin G); In skeletal muscle, required for costamere localization of DMD and betaDAG1 (By similarity). Membrane-cytoskeleton linker. May participate in the maintenance/targeting of ion channels and cell adhesion molecules at the nodes of Ranvier and axonal initial segments | spectrin, beta, non-erythrocytic 4 | 0.832 |
ANK3 | UBC | ENSP00000280772 | ENSP00000344818 | ankyrin 3, node of Ranvier (ankyrin G); In skeletal muscle, required for costamere localization of DMD and betaDAG1 (By similarity). Membrane-cytoskeleton linker. May participate in the maintenance/targeting of ion channels and cell adhesion molecules at the nodes of Ranvier and axonal initial segments | ubiquitin C | 0.674 |
CAPZB | PLS1 | ENSP00000264202 | ENSP00000336831 | capping protein (actin filament) muscle Z-line, beta; F-actin-capping proteins bind in a Ca(2+)-independent manner to the fast growing ends of actin filaments (barbed end) thereby blocking the exchange of subunits at these ends. Unlike other capping proteins (such as gelsolin and severin), these proteins do not sever actin filaments. Plays a role in the regulation of cell morphology and cytoskeletal organization | plastin 1; Actin-bundling protein in the absence of calcium | 0.768 |
CAPZB | SPTA1 | ENSP00000264202 | ENSP00000357130 | capping protein (actin filament) muscle Z-line, beta; F-actin-capping proteins bind in a Ca(2+)-independent manner to the fast growing ends of actin filaments (barbed end) thereby blocking the exchange of subunits at these ends. Unlike other capping proteins (such as gelsolin and severin), these proteins do not sever actin filaments. Plays a role in the regulation of cell morphology and cytoskeletal organization | spectrin, alpha, erythrocytic 1 (elliptocytosis 2); Spectrin is the major constituent of the cytoskeletal network underlying the erythrocyte plasma membrane. It associates with band 4.1 and actin to form the cytoskeletal superstructure of the erythrocyte plasma membrane | 0.502 |
CAPZB | SPTAN1 | ENSP00000264202 | ENSP00000361824 | capping protein (actin filament) muscle Z-line, beta; F-actin-capping proteins bind in a Ca(2+)-independent manner to the fast growing ends of actin filaments (barbed end) thereby blocking the exchange of subunits at these ends. Unlike other capping proteins (such as gelsolin and severin), these proteins do not sever actin filaments. Plays a role in the regulation of cell morphology and cytoskeletal organization | spectrin, alpha, non-erythrocytic 1 | 0.502 |
CAPZB | SPTB | ENSP00000264202 | ENSP00000374372 | capping protein (actin filament) muscle Z-line, beta; F-actin-capping proteins bind in a Ca(2+)-independent manner to the fast growing ends of actin filaments (barbed end) thereby blocking the exchange of subunits at these ends. Unlike other capping proteins (such as gelsolin and severin), these proteins do not sever actin filaments. Plays a role in the regulation of cell morphology and cytoskeletal organization | spectrin, beta, erythrocytic; Spectrin is the major constituent of the cytoskeletal network underlying the erythrocyte plasma membrane. It associates with band 4.1 and actin to form the cytoskeletal superstructure of the erythrocyte plasma membrane | 0.474 |
CAPZB | SPTBN1 | ENSP00000264202 | ENSP00000349259 | capping protein (actin filament) muscle Z-line, beta; F-actin-capping proteins bind in a Ca(2+)-independent manner to the fast growing ends of actin filaments (barbed end) thereby blocking the exchange of subunits at these ends. Unlike other capping proteins (such as gelsolin and severin), these proteins do not sever actin filaments. Plays a role in the regulation of cell morphology and cytoskeletal organization | spectrin, beta, non-erythrocytic 1; Fodrin, which seems to be involved in secretion, interacts with calmodulin in a calcium-dependent manner and is thus candidate for the calcium-dependent movement of the cytoskeleton at the membrane | 0.485 |
CAPZB | SPTBN2 | ENSP00000264202 | ENSP00000311489 | capping protein (actin filament) muscle Z-line, beta; F-actin-capping proteins bind in a Ca(2+)-independent manner to the fast growing ends of actin filaments (barbed end) thereby blocking the exchange of subunits at these ends. Unlike other capping proteins (such as gelsolin and severin), these proteins do not sever actin filaments. Plays a role in the regulation of cell morphology and cytoskeletal organization | spectrin, beta, non-erythrocytic 2; Probably plays an important role in neuronal membrane skeleton | 0.475 |
CAPZB | SPTBN4 | ENSP00000264202 | ENSP00000263373 | capping protein (actin filament) muscle Z-line, beta; F-actin-capping proteins bind in a Ca(2+)-independent manner to the fast growing ends of actin filaments (barbed end) thereby blocking the exchange of subunits at these ends. Unlike other capping proteins (such as gelsolin and severin), these proteins do not sever actin filaments. Plays a role in the regulation of cell morphology and cytoskeletal organization | spectrin, beta, non-erythrocytic 4 | 0.474 |
CAPZB | SPTBN5 | ENSP00000264202 | ENSP00000317790 | capping protein (actin filament) muscle Z-line, beta; F-actin-capping proteins bind in a Ca(2+)-independent manner to the fast growing ends of actin filaments (barbed end) thereby blocking the exchange of subunits at these ends. Unlike other capping proteins (such as gelsolin and severin), these proteins do not sever actin filaments. Plays a role in the regulation of cell morphology and cytoskeletal organization | spectrin, beta, non-erythrocytic 5 | 0.474 |
CAPZB | UBC | ENSP00000264202 | ENSP00000344818 | capping protein (actin filament) muscle Z-line, beta; F-actin-capping proteins bind in a Ca(2+)-independent manner to the fast growing ends of actin filaments (barbed end) thereby blocking the exchange of subunits at these ends. Unlike other capping proteins (such as gelsolin and severin), these proteins do not sever actin filaments. Plays a role in the regulation of cell morphology and cytoskeletal organization | ubiquitin C | 0.897 |
DISC1 | SPTBN4 | ENSP00000355593 | ENSP00000263373 | disrupted in schizophrenia 1 | spectrin, beta, non-erythrocytic 4 | 0.880 |
FYN | HRAS | ENSP00000346671 | ENSP00000309845 | FYN oncogene related to SRC, FGR, YES; Non-receptor tyrosine-protein kinase that plays a role in many biological processes including regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. Inactive FYN is phosphorylated on its C-terminal tail within the catalytic domain. Following activation by PKA, the protein subsequently associates with PTK2/FAK1, allowing PTK2/FAK1 phosphorylation, activation and targeting to focal adhesions. Involved in the regulation of cell adhesion and motilit [...] | v-Ha-ras Harvey rat sarcoma viral oncogene homolog; Ras proteins bind GDP/GTP and possess intrinsic GTPase activity | 0.986 |
FYN | KRAS | ENSP00000346671 | ENSP00000256078 | FYN oncogene related to SRC, FGR, YES; Non-receptor tyrosine-protein kinase that plays a role in many biological processes including regulation of cell growth and survival, cell adhesion, integrin-mediated signaling, cytoskeletal remodeling, cell motility, immune response and axon guidance. Inactive FYN is phosphorylated on its C-terminal tail within the catalytic domain. Following activation by PKA, the protein subsequently associates with PTK2/FAK1, allowing PTK2/FAK1 phosphorylation, activation and targeting to focal adhesions. Involved in the regulation of cell adhesion and motilit [...] | v-Ki-ras2 Kirsten rat sarcoma viral oncogene homolog; Ras proteins bind GDP/GTP and possess intrinsic GTPase activity | 0.963 |