| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| HSP90AA1 | HSP90AB1 | ENSP00000335153 | ENSP00000325875 | heat shock protein 90kDa alpha (cytosolic), class A member 1; Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function | heat shock protein 90kDa alpha (cytosolic), class B member 1; Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function | 0.999 |
| HSP90AA1 | IFIT5 | ENSP00000335153 | ENSP00000360860 | heat shock protein 90kDa alpha (cytosolic), class A member 1; Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function | interferon-induced protein with tetratricopeptide repeats 5; Interferon-induced RNA-binding protein that specifically binds single-stranded RNA bearing a 5’-triphosphate group (PPP- RNA), thereby acting as a sensor of viral single-stranded RNAs. Single-stranded PPP-RNAs, which lack 2’-O-methylation of the 5’ cap and bear a 5’-triphosphate group instead, are specific from viruses, providing a molecular signature to distinguish between self and non-self mRNAs by the host during viral infection. Directly binds PPP-RNA in a non-sequence-specific manner. Also recognizes and binds tRNAs | 0.927 |
| HSP90AA1 | OAS1 | ENSP00000335153 | ENSP00000388001 | heat shock protein 90kDa alpha (cytosolic), class A member 1; Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function | 2’-5’-oligoadenylate synthetase 1, 40/46kDa | 0.904 |
| HSP90AA1 | OASL | ENSP00000335153 | ENSP00000257570 | heat shock protein 90kDa alpha (cytosolic), class A member 1; Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function | 2’-5’-oligoadenylate synthetase-like; Does not have 2’-5’-OAS activity, but can bind double- stranded RNA. Displays antiviral activity against encephalomyocarditis virus (EMCV) and hepatitis C virus (HCV) via an alternative antiviral pathway independent of RNase L | 0.904 |
| HSP90AA1 | TRAP1 | ENSP00000335153 | ENSP00000246957 | heat shock protein 90kDa alpha (cytosolic), class A member 1; Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function | TNF receptor-associated protein 1; Chaperone that expresses an ATPase activity | 0.723 |
| HSP90AB1 | HSP90AA1 | ENSP00000325875 | ENSP00000335153 | heat shock protein 90kDa alpha (cytosolic), class B member 1; Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function | heat shock protein 90kDa alpha (cytosolic), class A member 1; Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function | 0.999 |
| HSP90AB1 | IFIT5 | ENSP00000325875 | ENSP00000360860 | heat shock protein 90kDa alpha (cytosolic), class B member 1; Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function | interferon-induced protein with tetratricopeptide repeats 5; Interferon-induced RNA-binding protein that specifically binds single-stranded RNA bearing a 5’-triphosphate group (PPP- RNA), thereby acting as a sensor of viral single-stranded RNAs. Single-stranded PPP-RNAs, which lack 2’-O-methylation of the 5’ cap and bear a 5’-triphosphate group instead, are specific from viruses, providing a molecular signature to distinguish between self and non-self mRNAs by the host during viral infection. Directly binds PPP-RNA in a non-sequence-specific manner. Also recognizes and binds tRNAs | 0.927 |
| HSP90AB1 | OAS1 | ENSP00000325875 | ENSP00000388001 | heat shock protein 90kDa alpha (cytosolic), class B member 1; Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function | 2’-5’-oligoadenylate synthetase 1, 40/46kDa | 0.904 |
| HSP90AB1 | OASL | ENSP00000325875 | ENSP00000257570 | heat shock protein 90kDa alpha (cytosolic), class B member 1; Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function | 2’-5’-oligoadenylate synthetase-like; Does not have 2’-5’-OAS activity, but can bind double- stranded RNA. Displays antiviral activity against encephalomyocarditis virus (EMCV) and hepatitis C virus (HCV) via an alternative antiviral pathway independent of RNase L | 0.904 |
| HSP90AB1 | TRAP1 | ENSP00000325875 | ENSP00000246957 | heat shock protein 90kDa alpha (cytosolic), class B member 1; Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function | TNF receptor-associated protein 1; Chaperone that expresses an ATPase activity | 0.729 |
| IFIT5 | HSP90AA1 | ENSP00000360860 | ENSP00000335153 | interferon-induced protein with tetratricopeptide repeats 5; Interferon-induced RNA-binding protein that specifically binds single-stranded RNA bearing a 5’-triphosphate group (PPP- RNA), thereby acting as a sensor of viral single-stranded RNAs. Single-stranded PPP-RNAs, which lack 2’-O-methylation of the 5’ cap and bear a 5’-triphosphate group instead, are specific from viruses, providing a molecular signature to distinguish between self and non-self mRNAs by the host during viral infection. Directly binds PPP-RNA in a non-sequence-specific manner. Also recognizes and binds tRNAs | heat shock protein 90kDa alpha (cytosolic), class A member 1; Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function | 0.927 |
| IFIT5 | HSP90AB1 | ENSP00000360860 | ENSP00000325875 | interferon-induced protein with tetratricopeptide repeats 5; Interferon-induced RNA-binding protein that specifically binds single-stranded RNA bearing a 5’-triphosphate group (PPP- RNA), thereby acting as a sensor of viral single-stranded RNAs. Single-stranded PPP-RNAs, which lack 2’-O-methylation of the 5’ cap and bear a 5’-triphosphate group instead, are specific from viruses, providing a molecular signature to distinguish between self and non-self mRNAs by the host during viral infection. Directly binds PPP-RNA in a non-sequence-specific manner. Also recognizes and binds tRNAs | heat shock protein 90kDa alpha (cytosolic), class B member 1; Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function | 0.927 |
| IFIT5 | MX1 | ENSP00000360860 | ENSP00000381599 | interferon-induced protein with tetratricopeptide repeats 5; Interferon-induced RNA-binding protein that specifically binds single-stranded RNA bearing a 5’-triphosphate group (PPP- RNA), thereby acting as a sensor of viral single-stranded RNAs. Single-stranded PPP-RNAs, which lack 2’-O-methylation of the 5’ cap and bear a 5’-triphosphate group instead, are specific from viruses, providing a molecular signature to distinguish between self and non-self mRNAs by the host during viral infection. Directly binds PPP-RNA in a non-sequence-specific manner. Also recognizes and binds tRNAs | myxovirus (influenza virus) resistance 1, interferon-inducible protein p78 (mouse) | 0.750 |
| IFIT5 | MX2 | ENSP00000360860 | ENSP00000333657 | interferon-induced protein with tetratricopeptide repeats 5; Interferon-induced RNA-binding protein that specifically binds single-stranded RNA bearing a 5’-triphosphate group (PPP- RNA), thereby acting as a sensor of viral single-stranded RNAs. Single-stranded PPP-RNAs, which lack 2’-O-methylation of the 5’ cap and bear a 5’-triphosphate group instead, are specific from viruses, providing a molecular signature to distinguish between self and non-self mRNAs by the host during viral infection. Directly binds PPP-RNA in a non-sequence-specific manner. Also recognizes and binds tRNAs | myxovirus (influenza virus) resistance 2 (mouse); May play a role in regulating nucleocytoplasmic transport and cell-cycle progression | 0.648 |
| IFIT5 | OAS1 | ENSP00000360860 | ENSP00000388001 | interferon-induced protein with tetratricopeptide repeats 5; Interferon-induced RNA-binding protein that specifically binds single-stranded RNA bearing a 5’-triphosphate group (PPP- RNA), thereby acting as a sensor of viral single-stranded RNAs. Single-stranded PPP-RNAs, which lack 2’-O-methylation of the 5’ cap and bear a 5’-triphosphate group instead, are specific from viruses, providing a molecular signature to distinguish between self and non-self mRNAs by the host during viral infection. Directly binds PPP-RNA in a non-sequence-specific manner. Also recognizes and binds tRNAs | 2’-5’-oligoadenylate synthetase 1, 40/46kDa | 0.674 |
| IFIT5 | OASL | ENSP00000360860 | ENSP00000257570 | interferon-induced protein with tetratricopeptide repeats 5; Interferon-induced RNA-binding protein that specifically binds single-stranded RNA bearing a 5’-triphosphate group (PPP- RNA), thereby acting as a sensor of viral single-stranded RNAs. Single-stranded PPP-RNAs, which lack 2’-O-methylation of the 5’ cap and bear a 5’-triphosphate group instead, are specific from viruses, providing a molecular signature to distinguish between self and non-self mRNAs by the host during viral infection. Directly binds PPP-RNA in a non-sequence-specific manner. Also recognizes and binds tRNAs | 2’-5’-oligoadenylate synthetase-like; Does not have 2’-5’-OAS activity, but can bind double- stranded RNA. Displays antiviral activity against encephalomyocarditis virus (EMCV) and hepatitis C virus (HCV) via an alternative antiviral pathway independent of RNase L | 0.710 |
| IFIT5 | SETD2 | ENSP00000360860 | ENSP00000386759 | interferon-induced protein with tetratricopeptide repeats 5; Interferon-induced RNA-binding protein that specifically binds single-stranded RNA bearing a 5’-triphosphate group (PPP- RNA), thereby acting as a sensor of viral single-stranded RNAs. Single-stranded PPP-RNAs, which lack 2’-O-methylation of the 5’ cap and bear a 5’-triphosphate group instead, are specific from viruses, providing a molecular signature to distinguish between self and non-self mRNAs by the host during viral infection. Directly binds PPP-RNA in a non-sequence-specific manner. Also recognizes and binds tRNAs | SET domain containing 2 | 0.647 |
| IFIT5 | TRAP1 | ENSP00000360860 | ENSP00000246957 | interferon-induced protein with tetratricopeptide repeats 5; Interferon-induced RNA-binding protein that specifically binds single-stranded RNA bearing a 5’-triphosphate group (PPP- RNA), thereby acting as a sensor of viral single-stranded RNAs. Single-stranded PPP-RNAs, which lack 2’-O-methylation of the 5’ cap and bear a 5’-triphosphate group instead, are specific from viruses, providing a molecular signature to distinguish between self and non-self mRNAs by the host during viral infection. Directly binds PPP-RNA in a non-sequence-specific manner. Also recognizes and binds tRNAs | TNF receptor-associated protein 1; Chaperone that expresses an ATPase activity | 0.733 |
| IFIT5 | USP18 | ENSP00000360860 | ENSP00000215794 | interferon-induced protein with tetratricopeptide repeats 5; Interferon-induced RNA-binding protein that specifically binds single-stranded RNA bearing a 5’-triphosphate group (PPP- RNA), thereby acting as a sensor of viral single-stranded RNAs. Single-stranded PPP-RNAs, which lack 2’-O-methylation of the 5’ cap and bear a 5’-triphosphate group instead, are specific from viruses, providing a molecular signature to distinguish between self and non-self mRNAs by the host during viral infection. Directly binds PPP-RNA in a non-sequence-specific manner. Also recognizes and binds tRNAs | ubiquitin specific peptidase 18; Can efficiently cleave only ISG15 fusions including native ISG15 conjugates linked via isopeptide bonds. Necessary to maintain a critical cellular balance of ISG15-conjugated proteins in both healthy and stressed organisms | 0.642 |
| IFIT5 | USP33 | ENSP00000360860 | ENSP00000350009 | interferon-induced protein with tetratricopeptide repeats 5; Interferon-induced RNA-binding protein that specifically binds single-stranded RNA bearing a 5’-triphosphate group (PPP- RNA), thereby acting as a sensor of viral single-stranded RNAs. Single-stranded PPP-RNAs, which lack 2’-O-methylation of the 5’ cap and bear a 5’-triphosphate group instead, are specific from viruses, providing a molecular signature to distinguish between self and non-self mRNAs by the host during viral infection. Directly binds PPP-RNA in a non-sequence-specific manner. Also recognizes and binds tRNAs | ubiquitin specific peptidase 33; Deubiquitinating enzyme involved in various processes such as centrosome duplication, cellular migration and beta-2 adrenergic receptor/ADRB2 recycling. Involved in regulation of centrosome duplication by mediating deubiquitination of CCP110 in S and G2/M phase, leading to stabilize CCP110 during the period which centrioles duplicate and elongate. Involved in cell migration via its interaction with intracellular domain of ROBO1, leading to regulate the Slit signaling. Plays a role in commissural axon guidance cross the ventral midline of the neural tube [...] | 0.740 |
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