Type |
Details |
Score |
Publication |
First Author: |
Woodard GE |
Year: |
2005 |
Journal: |
Oncogene |
Title: |
Parafibromin, product of the hyperparathyroidism-jaw tumor syndrome gene HRPT2, regulates cyclin D1/PRAD1 expression. |
Volume: |
24 |
Issue: |
7 |
Pages: |
1272-6 |
|
•
•
•
•
•
|
Publication |
First Author: |
Zhang C |
Year: |
2006 |
Journal: |
Biochem Biophys Res Commun |
Title: |
Parafibromin inhibits cancer cell growth and causes G1 phase arrest. |
Volume: |
350 |
Issue: |
1 |
Pages: |
17-24 |
|
•
•
•
•
•
|
Protein Domain |
Type: |
Domain |
Description: |
This is the N-terminal region of Cdc73 (cell division cycle 73). Cdc73 forms part of the Paf1 post-initiation complex []. As part of the Paf1 complex, Cdc73 associates with RNA-polymerase II and is involved in several transcriptional and posttranscriptional events. In vertebrates, the protein encoded by HRPT2/CCdc73 is known as Parafibromin, and acts as a tumour suppressor [, ]. |
|
•
•
•
•
•
|
Publication |
First Author: |
Chang M |
Year: |
1999 |
Journal: |
Mol Cell Biol |
Title: |
A complex containing RNA polymerase II, Paf1p, Cdc73p, Hpr1p, and Ccr4p plays a role in protein kinase C signaling. |
Volume: |
19 |
Issue: |
2 |
Pages: |
1056-67 |
|
•
•
•
•
•
|
Protein Domain |
Type: |
Domain |
Description: |
CDC73 is an RNA polymerase II accessory factor [], and forms part of the Paf1 complex that has roles in post-initiation events []. More specifically, crystal structure analysis shows the C terminus to be a Ras-like domain that adopts a fold that is highly similar to GTPases of the Ras superfamily. The C-terminal domain contains a large but comparatively flat surface of highly conserved residues, devoid of ligand. Deletion of the Cdc73 C-domain significantly reduces Paf1C occupancy on active genes, which means that the Cdc73 C-domain plays a role in promoting association of Paf1C with chromatin []. The canonical nucleotide binding pocket is altered in CDC73, and there is no nucleotide ligand, but it contributes to histone methylation and Paf1 complex (Paf1C) recruitment to active genes. Thus, together with Rtf1, it combines to couple Paf1C to elongating polymerase []. |
|
•
•
•
•
•
|
Protein Domain |
Type: |
Homologous_superfamily |
Description: |
CDC73 is an RNA polymerase II accessory factor [], and forms part of the Paf1 complex that has roles in post-initiation events []. More specifically, crystal structure analysis shows the C terminus to be a Ras-like domain that adopts a fold that is highly similar to GTPases of the Ras superfamily. The C-terminal domain contains a large but comparatively flat surface of highly conserved residues, devoid of ligand. Deletion of the Cdc73 C-domain significantly reduces Paf1C occupancy on active genes, which means that the Cdc73 C-domain plays a role in promoting association of Paf1C with chromatin []. The canonical nucleotide binding pocket is altered in CDC73, and there is no nucleotide ligand, but it contributes to histone methylation and Paf1 complex (Paf1C) recruitment to active genes. Thus, together with Rtf1, it combines to couple Paf1C to elongating polymerase []. |
|
•
•
•
•
•
|
Publication |
First Author: |
Wade PA |
Year: |
1996 |
Journal: |
Protein Expr Purif |
Title: |
A novel collection of accessory factors associated with yeast RNA polymerase II. |
Volume: |
8 |
Issue: |
1 |
Pages: |
85-90 |
|
•
•
•
•
•
|
Publication |
First Author: |
Shi X |
Year: |
1997 |
Journal: |
Mol Cell Biol |
Title: |
Cdc73p and Paf1p are found in a novel RNA polymerase II-containing complex distinct from the Srbp-containing holoenzyme. |
Volume: |
17 |
Issue: |
3 |
Pages: |
1160-9 |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
531
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Publication |
First Author: |
Han D |
Year: |
2022 |
Journal: |
Sci Adv |
Title: |
A balanced Oct4 interactome is crucial for maintaining pluripotency. |
Volume: |
8 |
Issue: |
7 |
Pages: |
eabe4375 |
|
•
•
•
•
•
|
Publication |
First Author: |
Krogan NJ |
Year: |
2002 |
Journal: |
Mol Cell Biol |
Title: |
RNA polymerase II elongation factors of Saccharomyces cerevisiae: a targeted proteomics approach. |
Volume: |
22 |
Issue: |
20 |
Pages: |
6979-92 |
|
•
•
•
•
•
|
Publication |
First Author: |
Park S |
Year: |
2010 |
Journal: |
Plant Physiol |
Title: |
PLANT HOMOLOGOUS TO PARAFIBROMIN is a component of the PAF1 complex and assists in regulating expression of genes within H3K27ME3-enriched chromatin. |
Volume: |
153 |
Issue: |
2 |
Pages: |
821-31 |
|
•
•
•
•
•
|
Protein Domain |
Type: |
Family |
Description: |
This entry includes Cdc73 from budding yeasts and its animal homologue, parafibromin. They are part of the Paf1 complex involved in histone modifications, transcription elongation and other gene expression processes that include transcript site selection [].In budding yeasts, Paf1 is an RNA polymerase II-associated protein complex containing Paf1, Cdc73, Ctr9, Rtf1 and Leo1. It is required for full expression of a subset of yeast genes, particularly those responsive to signals from the Pkc1/MAP kinase cascade. The complex appears to play an essential role in RNA elongation []. Human parafibromin is a tumour suppressor that may facilitate association of 3' mRNA processing factors with actively-transcribed chromatin. It is a component of the human Paf1 complex (Paf1C), which consists of Paf1, Cdc73, Ctr9, Rtf1, Leo1 and Wdr61 (Ski8). As in yeast, the human Paf1C has a central role in co-transcriptional histone modifications []. The Arabidopsis Cdc73 (also known as PLANT HOMOLOGOUS TO PARAFIBROMIN ,PHP) assists in regulating expression of genes within H3K27ME3-enriched chromatin []and participates in the modification of FLOWERING LOCUS C (FLC) chromatin []. |
|
•
•
•
•
•
|
Publication |
First Author: |
Yoo HS |
Year: |
2014 |
Journal: |
J Immunol |
Title: |
Transcriptional regulator CTR9 inhibits Th17 differentiation via repression of IL-17 expression. |
Volume: |
192 |
Issue: |
4 |
Pages: |
1440-8 |
|
•
•
•
•
•
|
Publication |
First Author: |
Kim J |
Year: |
2010 |
Journal: |
Cell |
Title: |
The human PAF1 complex acts in chromatin transcription elongation both independently and cooperatively with SII/TFIIS. |
Volume: |
140 |
Issue: |
4 |
Pages: |
491-503 |
|
•
•
•
•
•
|