Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Pivot Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Target Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Query: EC:2.7.11.22 (
cdc2
)
8,319
document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)
P2P-R
is the alternately spliced product of the
P2P-R
/PACT gene in that
P2P-R
lacks one exon encoding 34 amino acids. The 250 kDa
P2P-R
protein is the predominate product expressed in multiple murine cell lines. It is a highly basic protein that contains multiple domains including an N-terminal RING type zinc finger, a proline rich domain, an RS region, and a C-terminal lysine-rich domain.
P2P-R
binds the p53 and the Rb1 tumor suppressors and is phosphorylated by the
cdc2
and SRPK1a protein kinases.
P2P-R
also interacts with scaffold attachment factor-B (SAF-B), a well characterized MARs (for matrix attachment regions) binding factor, and may interact with nucleolin, another MARs binding factor. In addition,
P2P-R
binds single strand DNA (ssDNA). The expression of
P2P-R
is regulated by differentiation and cell cycle events.
P2P-R
mRNA is markedly repressed during differentiation, whereas immunoreactive
P2P-R
protein levels are >10-fold higher in mitotic than in G(0) cells. The localization of
P2P-R
also is modulated during the cell cycle. During interphase,
P2P-R
is present primarily in nucleoli and nuclear speckles whereas during mitosis,
P2P-R
associates with the periphery of chromosomes. Overexpression of near full length
P2P-R
induces mitotic arrest in prometaphase and mitotic apoptosis, and overexpression of selected
P2P-R
segments also can promote apoptosis. This compendium of data supports the possibility that
P2P-R
may form complexes with the Rb1 and/or p53 tumor suppressors and MARs-related factors, in a cell cycle and cell differentiation-dependent manner, to influence gene transcription/expression and nuclear organization.
...
PMID:Functional potential of P2P-R: a role in the cell cycle and cell differentiation related to its interactions with proteins that bind to matrix associated regions of DNA? 1293 51