| node1 | node2 | node1 annotation | node2 annotation | score |
| A0A182JQE1 | A0A182JWA5 | 60S ribosomal protein L5. | 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. | 0.776 |
| A0A182JQE1 | A0A182JXB0 | 60S ribosomal protein L5. | CHK domain-containing protein. | 0.998 |
| A0A182JQE1 | A0A182JXN9 | 60S ribosomal protein L5. | FACT complex subunit SSRP1; Component of the FACT complex, a general chromatin factor that acts to reorganize nucleosomes. The FACT complex is involved in multiple processes that require DNA as a template such as mRNA elongation, DNA replication and DNA repair. During transcription elongation the FACT complex acts as a histone chaperone that both destabilizes and restores nucleosomal structure. It facilitates the passage of RNA polymerase II and transcription by promoting the dissociation of one histone H2A-H2B dimer from the nucleosome, then subsequently promotes the reestablishment o [...] | 0.939 |
| A0A182JQE1 | A0A182JYA8 | 60S ribosomal protein L5. | Uncharacterized protein. | 0.996 |
| A0A182JQE1 | A0A182K3J5 | 60S ribosomal protein L5. | NOT2_3_5 domain-containing protein. | 0.995 |
| A0A182JQE1 | A0A182K4W1 | 60S ribosomal protein L5. | Uncharacterized protein. | 0.965 |
| A0A182JQE1 | A0A182K5P3 | 60S ribosomal protein L5. | Uncharacterized protein. | 0.996 |
| A0A182JQE1 | A0A182K6R0 | 60S ribosomal protein L5. | Uncharacterized protein. | 0.995 |
| A0A182JQE1 | A0A182KAV3 | 60S ribosomal protein L5. | Endo/exonuclease/phosphatase domain-containing protein. | 0.967 |
| A0A182JQE1 | A0A182KB35 | 60S ribosomal protein L5. | Uncharacterized protein. | 0.997 |
| A0A182JWA5 | A0A182JQE1 | 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. | 60S ribosomal protein L5. | 0.776 |
| A0A182JWA5 | A0A182JXB0 | 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. | CHK domain-containing protein. | 0.920 |
| A0A182JWA5 | A0A182JXN9 | 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. | FACT complex subunit SSRP1; Component of the FACT complex, a general chromatin factor that acts to reorganize nucleosomes. The FACT complex is involved in multiple processes that require DNA as a template such as mRNA elongation, DNA replication and DNA repair. During transcription elongation the FACT complex acts as a histone chaperone that both destabilizes and restores nucleosomal structure. It facilitates the passage of RNA polymerase II and transcription by promoting the dissociation of one histone H2A-H2B dimer from the nucleosome, then subsequently promotes the reestablishment o [...] | 0.849 |
| A0A182JWA5 | A0A182JYA8 | 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. | Uncharacterized protein. | 0.872 |
| A0A182JWA5 | A0A182K3J5 | 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. | NOT2_3_5 domain-containing protein. | 0.904 |
| A0A182JWA5 | A0A182K4W1 | 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. | Uncharacterized protein. | 0.565 |
| A0A182JWA5 | A0A182K5P3 | 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. | Uncharacterized protein. | 0.795 |
| A0A182JWA5 | A0A182KAV3 | 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. | Endo/exonuclease/phosphatase domain-containing protein. | 0.565 |
| A0A182JWA5 | A0A182KB35 | 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. | Uncharacterized protein. | 0.943 |
| A0A182JXB0 | A0A182JQE1 | CHK domain-containing protein. | 60S ribosomal protein L5. | 0.998 |
