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Literature summary extracted from

  • Ripley, B.M.; Reusch, D.T.; Washington, M.T.
    Yeast DNA polymerase eta possesses two PIP-like motifs that bind PCNA and Rad6-Rad18 with different specificities (2020), DNA Repair, 95, 102968.
    View publication on PubMed

Organism

EC Number Organism UniProt Comment Textmining
2.7.7.7 Henningerozyma blattae
-
-
-
2.7.7.7 Huiozyma naganishii
-
-
-
2.7.7.7 Kluyveromyces dobzhanskii
-
-
-
2.7.7.7 Kluyveromyces marxianus W0TAY7
-
-
2.7.7.7 Kluyveromyces marxianus DMKU3-1042 W0TAY7
-
-
2.7.7.7 Lachancea fermentati
-
-
-
2.7.7.7 Lachancea lanzarotensis
-
-
-
2.7.7.7 Nakaseomyces glabratus
-
-
-
2.7.7.7 Naumovozyma castellii
-
-
-
2.7.7.7 Naumovozyma dairenensis
-
-
-
2.7.7.7 Saccharomyces arboricola J8LJI8
-
-
2.7.7.7 Saccharomyces arboricola H-6 J8LJI8
-
-
2.7.7.7 Saccharomyces cerevisiae
-
-
-
2.7.7.7 Saccharomyces kudriavzevii
-
-
-
2.7.7.7 Saccharomyces paradoxus
-
-
-
2.7.7.7 Saccharomyces pastorianus
-
-
-
2.7.7.7 Tetrapisispora phaffii
-
-
-
2.7.7.7 Torulaspora delbrueckii
-
-
-
2.7.7.7 Vanderwaltozyma polyspora
-
-
-
2.7.7.7 Zygosaccharomyces rouxii
-
-
-

Synonyms

EC Number Synonyms Comment Organism
2.7.7.7 DNA polymerase eta
-
 Saccharomyces cerevisiae
2.7.7.7 DNA polymerase eta
-
 Saccharomyces arboricola
2.7.7.7 DNA polymerase eta
-
 Saccharomyces kudriavzevii
2.7.7.7 DNA polymerase eta
-
 Saccharomyces paradoxus
2.7.7.7 DNA polymerase eta
-
 Saccharomyces pastorianus
2.7.7.7 DNA polymerase eta
-
 Nakaseomyces glabratus
2.7.7.7 DNA polymerase eta
-
 Huiozyma naganishii
2.7.7.7 DNA polymerase eta
-
 Kluyveromyces dobzhanskii
2.7.7.7 DNA polymerase eta
-
 Kluyveromyces marxianus
2.7.7.7 DNA polymerase eta
-
 Lachancea fermentati
2.7.7.7 DNA polymerase eta
-
 Lachancea lanzarotensis
2.7.7.7 DNA polymerase eta
-
 Naumovozyma castellii
2.7.7.7 DNA polymerase eta
-
 Naumovozyma dairenensis
2.7.7.7 DNA polymerase eta
-
 Henningerozyma blattae
2.7.7.7 DNA polymerase eta
-
 Tetrapisispora phaffii
2.7.7.7 DNA polymerase eta
-
 Torulaspora delbrueckii
2.7.7.7 DNA polymerase eta
-
 Vanderwaltozyma polyspora
2.7.7.7 DNA polymerase eta
-
 Zygosaccharomyces rouxii
2.7.7.7 RAD30
-
 Saccharomyces cerevisiae
2.7.7.7 RAD30
-
 Saccharomyces arboricola
2.7.7.7 RAD30
-
 Saccharomyces kudriavzevii
2.7.7.7 RAD30
-
 Saccharomyces paradoxus
2.7.7.7 RAD30
-
 Saccharomyces pastorianus
2.7.7.7 RAD30
-
 Nakaseomyces glabratus
2.7.7.7 RAD30
-
 Huiozyma naganishii
2.7.7.7 RAD30
-
 Kluyveromyces dobzhanskii
2.7.7.7 RAD30
-
 Kluyveromyces marxianus
2.7.7.7 RAD30
-
 Lachancea fermentati
2.7.7.7 RAD30
-
 Lachancea lanzarotensis
2.7.7.7 RAD30
-
 Naumovozyma castellii
2.7.7.7 RAD30
-
 Naumovozyma dairenensis
2.7.7.7 RAD30
-
 Henningerozyma blattae
2.7.7.7 RAD30
-
 Tetrapisispora phaffii
2.7.7.7 RAD30
-
 Torulaspora delbrueckii
2.7.7.7 RAD30
-
 Vanderwaltozyma polyspora
2.7.7.7 RAD30
-
 Zygosaccharomyces rouxii

General Information

EC Number General Information Comment Organism
2.7.7.7 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
2.7.7.7 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
2.7.7.7 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
2.7.7.7 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
2.7.7.7 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
2.7.7.7 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 Nakaseomyces glabratus
2.7.7.7 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 Huiozyma naganishii
2.7.7.7 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
2.7.7.7 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
2.7.7.7 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
2.7.7.7 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
2.7.7.7 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
2.7.7.7 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
2.7.7.7 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 Henningerozyma blattae
2.7.7.7 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
2.7.7.7 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
2.7.7.7 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
2.7.7.7 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