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Literature summary for 2.7.7.7 extracted from
- Yeast DNA polymerase eta possesses two PIP-like motifs that bind PCNA and Rad6-Rad18 with different specificities (2020), DNA Repair, 95, 102968 .
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Kazachstania naganishii | - |
- |
- |
| Kluyveromyces dobzhanskii | - |
- |
- |
| Kluyveromyces marxianus | W0TAY7 | - |
- |
| Kluyveromyces marxianus DMKU3-1042 | W0TAY7 | - |
- |
| Lachancea fermentati | - |
- |
- |
| Lachancea lanzarotensis | - |
- |
- |
| Naumovozyma castellii | - |
- |
- |
| Naumovozyma dairenensis | - |
- |
- |
| Saccharomyces arboricola | J8LJI8 | - |
- |
| Saccharomyces arboricola H-6 | J8LJI8 | - |
- |
| Saccharomyces cerevisiae | - |
- |
- |
| Saccharomyces kudriavzevii | - |
- |
- |
| Saccharomyces paradoxus | - |
- |
- |
| Saccharomyces pastorianus | - |
- |
- |
| Tetrapisispora blattae | - |
- |
- |
| Tetrapisispora phaffii | - |
- |
- |
| Torulaspora delbrueckii | - |
- |
- |
| Vanderwaltozyma polyspora | - |
- |
- |
| Zygosaccharomyces rouxii | - |
- |
- |
| [Candida] glabrata | - |
- |
- |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| DNA polymerase eta | - |
Saccharomyces pastorianus |
| DNA polymerase eta | - |
Saccharomyces cerevisiae |
| DNA polymerase eta | - |
[Candida] glabrata |
| DNA polymerase eta | - |
Torulaspora delbrueckii |
| DNA polymerase eta | - |
Zygosaccharomyces rouxii |
| DNA polymerase eta | - |
Saccharomyces paradoxus |
| DNA polymerase eta | - |
Saccharomyces kudriavzevii |
| DNA polymerase eta | - |
Vanderwaltozyma polyspora |
| DNA polymerase eta | - |
Saccharomyces arboricola |
| DNA polymerase eta | - |
Kluyveromyces marxianus |
| DNA polymerase eta | - |
Kazachstania naganishii |
| DNA polymerase eta | - |
Kluyveromyces dobzhanskii |
| DNA polymerase eta | - |
Lachancea fermentati |
| DNA polymerase eta | - |
Lachancea lanzarotensis |
| DNA polymerase eta | - |
Naumovozyma castellii |
| DNA polymerase eta | - |
Naumovozyma dairenensis |
| DNA polymerase eta | - |
Tetrapisispora blattae |
| DNA polymerase eta | - |
Tetrapisispora phaffii |
| RAD30 | - |
Saccharomyces pastorianus |
| RAD30 | - |
Saccharomyces cerevisiae |
| RAD30 | - |
[Candida] glabrata |
| RAD30 | - |
Torulaspora delbrueckii |
| RAD30 | - |
Zygosaccharomyces rouxii |
| RAD30 | - |
Saccharomyces paradoxus |
| RAD30 | - |
Saccharomyces kudriavzevii |
| RAD30 | - |
Vanderwaltozyma polyspora |
| RAD30 | - |
Saccharomyces arboricola |
| RAD30 | - |
Kluyveromyces marxianus |
| RAD30 | - |
Kazachstania naganishii |
| RAD30 | - |
Kluyveromyces dobzhanskii |
| RAD30 | - |
Lachancea fermentati |
| RAD30 | - |
Lachancea lanzarotensis |
| RAD30 | - |
Naumovozyma castellii |
| RAD30 | - |
Naumovozyma dairenensis |
| RAD30 | - |
Tetrapisispora blattae |
| RAD30 | - |
Tetrapisispora phaffii |
General Information
| General Information | Comment | Organism |
|---|---|---|
| physiological function | in translesion synthesis (TLS), specialized DNA polymerases, such as polymerase (pol) eta, are recruited to stalled replication forks. The polymerase form a multi-protein complex with PCNA, Rad6-Rad18, and other specialized polymerases. Pol eta interacts with PCNA and Rev1 via a PCNA-interacting protein (PIP) motif in its C-terminal unstructured region. PIP1 likely plays a critical role in the recruiting pol eta to the multi-protein complex. PIP2 likely plays a critical role in maintaining the architecture and the dynamics of this multi-protein complex needed to maximize the efficiency and accuracy of translesion synthesis | Saccharomyces pastorianus |
| physiological function | in translesion synthesis (TLS), specialized DNA polymerases, such as polymerase (pol) eta, are recruited to stalled replication forks. The polymerase form a multi-protein complex with PCNA, Rad6-Rad18, and other specialized polymerases. Pol eta interacts with PCNA and Rev1 via a PCNA-interacting protein (PIP) motif in its C-terminal unstructured region. PIP1 likely plays a critical role in the recruiting pol eta to the multi-protein complex. PIP2 likely plays a critical role in maintaining the architecture and the dynamics of this multi-protein complex needed to maximize the efficiency and accuracy of translesion synthesis | Saccharomyces cerevisiae |
| physiological function | in translesion synthesis (TLS), specialized DNA polymerases, such as polymerase (pol) eta, are recruited to stalled replication forks. The polymerase form a multi-protein complex with PCNA, Rad6-Rad18, and other specialized polymerases. Pol eta interacts with PCNA and Rev1 via a PCNA-interacting protein (PIP) motif in its C-terminal unstructured region. PIP1 likely plays a critical role in the recruiting pol eta to the multi-protein complex. PIP2 likely plays a critical role in maintaining the architecture and the dynamics of this multi-protein complex needed to maximize the efficiency and accuracy of translesion synthesis | [Candida] glabrata |
| physiological function | in translesion synthesis (TLS), specialized DNA polymerases, such as polymerase (pol) eta, are recruited to stalled replication forks. The polymerase form a multi-protein complex with PCNA, Rad6-Rad18, and other specialized polymerases. Pol eta interacts with PCNA and Rev1 via a PCNA-interacting protein (PIP) motif in its C-terminal unstructured region. PIP1 likely plays a critical role in the recruiting pol eta to the multi-protein complex. PIP2 likely plays a critical role in maintaining the architecture and the dynamics of this multi-protein complex needed to maximize the efficiency and accuracy of translesion synthesis | Torulaspora delbrueckii |
| physiological function | in translesion synthesis (TLS), specialized DNA polymerases, such as polymerase (pol) eta, are recruited to stalled replication forks. The polymerase form a multi-protein complex with PCNA, Rad6-Rad18, and other specialized polymerases. Pol eta interacts with PCNA and Rev1 via a PCNA-interacting protein (PIP) motif in its C-terminal unstructured region. PIP1 likely plays a critical role in the recruiting pol eta to the multi-protein complex. PIP2 likely plays a critical role in maintaining the architecture and the dynamics of this multi-protein complex needed to maximize the efficiency and accuracy of translesion synthesis | Zygosaccharomyces rouxii |
| physiological function | in translesion synthesis (TLS), specialized DNA polymerases, such as polymerase (pol) eta, are recruited to stalled replication forks. The polymerase form a multi-protein complex with PCNA, Rad6-Rad18, and other specialized polymerases. Pol eta interacts with PCNA and Rev1 via a PCNA-interacting protein (PIP) motif in its C-terminal unstructured region. PIP1 likely plays a critical role in the recruiting pol eta to the multi-protein complex. PIP2 likely plays a critical role in maintaining the architecture and the dynamics of this multi-protein complex needed to maximize the efficiency and accuracy of translesion synthesis | Saccharomyces paradoxus |
| physiological function | in translesion synthesis (TLS), specialized DNA polymerases, such as polymerase (pol) eta, are recruited to stalled replication forks. The polymerase form a multi-protein complex with PCNA, Rad6-Rad18, and other specialized polymerases. Pol eta interacts with PCNA and Rev1 via a PCNA-interacting protein (PIP) motif in its C-terminal unstructured region. PIP1 likely plays a critical role in the recruiting pol eta to the multi-protein complex. PIP2 likely plays a critical role in maintaining the architecture and the dynamics of this multi-protein complex needed to maximize the efficiency and accuracy of translesion synthesis | Saccharomyces kudriavzevii |
| physiological function | in translesion synthesis (TLS), specialized DNA polymerases, such as polymerase (pol) eta, are recruited to stalled replication forks. The polymerase form a multi-protein complex with PCNA, Rad6-Rad18, and other specialized polymerases. Pol eta interacts with PCNA and Rev1 via a PCNA-interacting protein (PIP) motif in its C-terminal unstructured region. PIP1 likely plays a critical role in the recruiting pol eta to the multi-protein complex. PIP2 likely plays a critical role in maintaining the architecture and the dynamics of this multi-protein complex needed to maximize the efficiency and accuracy of translesion synthesis | Vanderwaltozyma polyspora |
| physiological function | in translesion synthesis (TLS), specialized DNA polymerases, such as polymerase (pol) eta, are recruited to stalled replication forks. The polymerase form a multi-protein complex with PCNA, Rad6-Rad18, and other specialized polymerases. Pol eta interacts with PCNA and Rev1 via a PCNA-interacting protein (PIP) motif in its C-terminal unstructured region. PIP1 likely plays a critical role in the recruiting pol eta to the multi-protein complex. PIP2 likely plays a critical role in maintaining the architecture and the dynamics of this multi-protein complex needed to maximize the efficiency and accuracy of translesion synthesis | Saccharomyces arboricola |
| physiological function | in translesion synthesis (TLS), specialized DNA polymerases, such as polymerase (pol) eta, are recruited to stalled replication forks. The polymerase form a multi-protein complex with PCNA, Rad6-Rad18, and other specialized polymerases. Pol eta interacts with PCNA and Rev1 via a PCNA-interacting protein (PIP) motif in its C-terminal unstructured region. PIP1 likely plays a critical role in the recruiting pol eta to the multi-protein complex. PIP2 likely plays a critical role in maintaining the architecture and the dynamics of this multi-protein complex needed to maximize the efficiency and accuracy of translesion synthesis | Kluyveromyces marxianus |
| physiological function | in translesion synthesis (TLS), specialized DNA polymerases, such as polymerase (pol) eta, are recruited to stalled replication forks. The polymerase form a multi-protein complex with PCNA, Rad6-Rad18, and other specialized polymerases. Pol eta interacts with PCNA and Rev1 via a PCNA-interacting protein (PIP) motif in its C-terminal unstructured region. PIP1 likely plays a critical role in the recruiting pol eta to the multi-protein complex. PIP2 likely plays a critical role in maintaining the architecture and the dynamics of this multi-protein complex needed to maximize the efficiency and accuracy of translesion synthesis | Kazachstania naganishii |
| physiological function | in translesion synthesis (TLS), specialized DNA polymerases, such as polymerase (pol) eta, are recruited to stalled replication forks. The polymerase form a multi-protein complex with PCNA, Rad6-Rad18, and other specialized polymerases. Pol eta interacts with PCNA and Rev1 via a PCNA-interacting protein (PIP) motif in its C-terminal unstructured region. PIP1 likely plays a critical role in the recruiting pol eta to the multi-protein complex. PIP2 likely plays a critical role in maintaining the architecture and the dynamics of this multi-protein complex needed to maximize the efficiency and accuracy of translesion synthesis | Kluyveromyces dobzhanskii |
| physiological function | in translesion synthesis (TLS), specialized DNA polymerases, such as polymerase (pol) eta, are recruited to stalled replication forks. The polymerase form a multi-protein complex with PCNA, Rad6-Rad18, and other specialized polymerases. Pol eta interacts with PCNA and Rev1 via a PCNA-interacting protein (PIP) motif in its C-terminal unstructured region. PIP1 likely plays a critical role in the recruiting pol eta to the multi-protein complex. PIP2 likely plays a critical role in maintaining the architecture and the dynamics of this multi-protein complex needed to maximize the efficiency and accuracy of translesion synthesis | Lachancea fermentati |
| physiological function | in translesion synthesis (TLS), specialized DNA polymerases, such as polymerase (pol) eta, are recruited to stalled replication forks. The polymerase form a multi-protein complex with PCNA, Rad6-Rad18, and other specialized polymerases. Pol eta interacts with PCNA and Rev1 via a PCNA-interacting protein (PIP) motif in its C-terminal unstructured region. PIP1 likely plays a critical role in the recruiting pol eta to the multi-protein complex. PIP2 likely plays a critical role in maintaining the architecture and the dynamics of this multi-protein complex needed to maximize the efficiency and accuracy of translesion synthesis | Lachancea lanzarotensis |
| physiological function | in translesion synthesis (TLS), specialized DNA polymerases, such as polymerase (pol) eta, are recruited to stalled replication forks. The polymerase form a multi-protein complex with PCNA, Rad6-Rad18, and other specialized polymerases. Pol eta interacts with PCNA and Rev1 via a PCNA-interacting protein (PIP) motif in its C-terminal unstructured region. PIP1 likely plays a critical role in the recruiting pol eta to the multi-protein complex. PIP2 likely plays a critical role in maintaining the architecture and the dynamics of this multi-protein complex needed to maximize the efficiency and accuracy of translesion synthesis | Naumovozyma castellii |
| physiological function | in translesion synthesis (TLS), specialized DNA polymerases, such as polymerase (pol) eta, are recruited to stalled replication forks. The polymerase form a multi-protein complex with PCNA, Rad6-Rad18, and other specialized polymerases. Pol eta interacts with PCNA and Rev1 via a PCNA-interacting protein (PIP) motif in its C-terminal unstructured region. PIP1 likely plays a critical role in the recruiting pol eta to the multi-protein complex. PIP2 likely plays a critical role in maintaining the architecture and the dynamics of this multi-protein complex needed to maximize the efficiency and accuracy of translesion synthesis | Naumovozyma dairenensis |
| physiological function | in translesion synthesis (TLS), specialized DNA polymerases, such as polymerase (pol) eta, are recruited to stalled replication forks. The polymerase form a multi-protein complex with PCNA, Rad6-Rad18, and other specialized polymerases. Pol eta interacts with PCNA and Rev1 via a PCNA-interacting protein (PIP) motif in its C-terminal unstructured region. PIP1 likely plays a critical role in the recruiting pol eta to the multi-protein complex. PIP2 likely plays a critical role in maintaining the architecture and the dynamics of this multi-protein complex needed to maximize the efficiency and accuracy of translesion synthesis | Tetrapisispora blattae |
| physiological function | in translesion synthesis (TLS), specialized DNA polymerases, such as polymerase (pol) eta, are recruited to stalled replication forks. The polymerase form a multi-protein complex with PCNA, Rad6-Rad18, and other specialized polymerases. Pol eta interacts with PCNA and Rev1 via a PCNA-interacting protein (PIP) motif in its C-terminal unstructured region. PIP1 likely plays a critical role in the recruiting pol eta to the multi-protein complex. PIP2 likely plays a critical role in maintaining the architecture and the dynamics of this multi-protein complex needed to maximize the efficiency and accuracy of translesion synthesis | Tetrapisispora phaffii |
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