| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| ACTB | CAPZB | ENSPPYP00000019427 | ENSPPYP00000002072 | Actin, cytoplasmic 1, N-terminally processed; Actin is a highly conserved protein that polymerizes to produce filaments that form cross-linked networks in the cytoplasm of cells. Actin exists in both monomeric (G-actin) and polymeric (F-actin) forms, both forms playing key functions, such as cell motility and contraction. In addition to their role in the cytoplasmic cytoskeleton, G- and F-actin also localize in the nucleus, and regulate gene transcription and motility and repair of damaged DNA. | F-actin-capping protein subunit 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 (By similarity). | 0.938 |
| ACTB | DBN1 | ENSPPYP00000019427 | ENSPPYP00000018010 | Actin, cytoplasmic 1, N-terminally processed; Actin is a highly conserved protein that polymerizes to produce filaments that form cross-linked networks in the cytoplasm of cells. Actin exists in both monomeric (G-actin) and polymeric (F-actin) forms, both forms playing key functions, such as cell motility and contraction. In addition to their role in the cytoplasmic cytoskeleton, G- and F-actin also localize in the nucleus, and regulate gene transcription and motility and repair of damaged DNA. | DBN1 isoform 4. | 0.924 |
| ACTB | GSN | ENSPPYP00000019427 | ENSPPYP00000021923 | Actin, cytoplasmic 1, N-terminally processed; Actin is a highly conserved protein that polymerizes to produce filaments that form cross-linked networks in the cytoplasm of cells. Actin exists in both monomeric (G-actin) and polymeric (F-actin) forms, both forms playing key functions, such as cell motility and contraction. In addition to their role in the cytoplasmic cytoskeleton, G- and F-actin also localize in the nucleus, and regulate gene transcription and motility and repair of damaged DNA. | GSN isoform 1. | 0.813 |
| ACTB | HIP1R | ENSPPYP00000019427 | ENSPPYP00000005782 | Actin, cytoplasmic 1, N-terminally processed; Actin is a highly conserved protein that polymerizes to produce filaments that form cross-linked networks in the cytoplasm of cells. Actin exists in both monomeric (G-actin) and polymeric (F-actin) forms, both forms playing key functions, such as cell motility and contraction. In addition to their role in the cytoplasmic cytoskeleton, G- and F-actin also localize in the nucleus, and regulate gene transcription and motility and repair of damaged DNA. | HIP1R isoform 1. | 0.587 |
| CAPG | DBN1 | ENSPPYP00000013640 | ENSPPYP00000018010 | Capping actin protein, gelsolin like. | DBN1 isoform 4. | 0.697 |
| CAPG | TMOD2 | ENSPPYP00000013640 | ENSPPYP00000007342 | Capping actin protein, gelsolin like. | TMOD2 isoform 1. | 0.505 |
| CAPZB | ACTB | ENSPPYP00000002072 | ENSPPYP00000019427 | F-actin-capping protein subunit 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 (By similarity). | Actin, cytoplasmic 1, N-terminally processed; Actin is a highly conserved protein that polymerizes to produce filaments that form cross-linked networks in the cytoplasm of cells. Actin exists in both monomeric (G-actin) and polymeric (F-actin) forms, both forms playing key functions, such as cell motility and contraction. In addition to their role in the cytoplasmic cytoskeleton, G- and F-actin also localize in the nucleus, and regulate gene transcription and motility and repair of damaged DNA. | 0.938 |
| CAPZB | DBN1 | ENSPPYP00000002072 | ENSPPYP00000018010 | F-actin-capping protein subunit 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 (By similarity). | DBN1 isoform 4. | 0.742 |
| DBN1 | ACTB | ENSPPYP00000018010 | ENSPPYP00000019427 | DBN1 isoform 4. | Actin, cytoplasmic 1, N-terminally processed; Actin is a highly conserved protein that polymerizes to produce filaments that form cross-linked networks in the cytoplasm of cells. Actin exists in both monomeric (G-actin) and polymeric (F-actin) forms, both forms playing key functions, such as cell motility and contraction. In addition to their role in the cytoplasmic cytoskeleton, G- and F-actin also localize in the nucleus, and regulate gene transcription and motility and repair of damaged DNA. | 0.924 |
| DBN1 | CAPG | ENSPPYP00000018010 | ENSPPYP00000013640 | DBN1 isoform 4. | Capping actin protein, gelsolin like. | 0.697 |
| DBN1 | CAPZB | ENSPPYP00000018010 | ENSPPYP00000002072 | DBN1 isoform 4. | F-actin-capping protein subunit 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 (By similarity). | 0.742 |
| DBN1 | EPHA1 | ENSPPYP00000018010 | ENSPPYP00000020327 | DBN1 isoform 4. | EPHA1 isoform 1. | 0.723 |
| DBN1 | GSN | ENSPPYP00000018010 | ENSPPYP00000021923 | DBN1 isoform 4. | GSN isoform 1. | 0.926 |
| DBN1 | HIP1R | ENSPPYP00000018010 | ENSPPYP00000005782 | DBN1 isoform 4. | HIP1R isoform 1. | 0.728 |
| DBN1 | HOMER1 | ENSPPYP00000018010 | ENSPPYP00000017426 | DBN1 isoform 4. | Homer scaffold protein 1. | 0.776 |
| DBN1 | HOMER2 | ENSPPYP00000018010 | ENSPPYP00000007642 | DBN1 isoform 4. | HOMER2 isoform 1. | 0.809 |
| DBN1 | TMOD2 | ENSPPYP00000018010 | ENSPPYP00000007342 | DBN1 isoform 4. | TMOD2 isoform 1. | 0.772 |
| DBN1 | ZMYND8 | ENSPPYP00000018010 | ENSPPYP00000012404 | DBN1 isoform 4. | ZMYND8 isoform 16. | 0.766 |
| EPHA1 | DBN1 | ENSPPYP00000020327 | ENSPPYP00000018010 | EPHA1 isoform 1. | DBN1 isoform 4. | 0.723 |
| EPHA1 | HIP1R | ENSPPYP00000020327 | ENSPPYP00000005782 | EPHA1 isoform 1. | HIP1R isoform 1. | 0.576 |
