| Predicate | Object |
|---|---|
| rdf:type | |
| http://www.biopax.org/relea... |
cpath:CPATH-LOCAL-430686,
cpath:CPATH-LOCAL-430686,
cpath:CPATH-LOCAL-430687,
cpath:CPATH-LOCAL-430687,
cpath:CPATH-LOCAL-430688,
cpath:CPATH-LOCAL-430688,
cpath:CPATH-LOCAL-430689,
cpath:CPATH-LOCAL-430689,
cpath:CPATH-LOCAL-430690,
cpath:CPATH-LOCAL-430690,
cpath:CPATH-LOCAL-430691,
cpath:CPATH-LOCAL-430691,
cpath:CPATH-LOCAL-430692,
cpath:CPATH-LOCAL-430692,
cpath:CPATH-LOCAL-430693,
cpath:CPATH-LOCAL-430693,
cpath:CPATH-LOCAL-430694,
cpath:CPATH-LOCAL-430694,
cpath:CPATH-LOCAL-430695,
cpath:CPATH-LOCAL-430695,
cpath:CPATH-LOCAL-437260,
cpath:CPATH-LOCAL-437260
|
| http://www.biopax.org/relea... |
Tumor suppressor p53-binding protein 1,
Tumor suppressor p53-binding protein 1
|
| http://www.biopax.org/relea... |
TP53B_HUMAN,
TP53B_HUMAN
|
| http://www.biopax.org/relea... | |
| http://www.biopax.org/relea... |
53BP1,
53BP1,
p53-binding protein 1,
p53-binding protein 1,
p53BP1,
p53BP1
|
| http://www.biopax.org/relea... |
FUNCTION: May have a role in checkpoint signaling during mitosis (By similarity). Enhances TP53-mediated transcriptional activation. Plays a role in the response to DNA damage. SUBUNIT: Interacts with IFI202A (By similarity). Binds to the central domain of p53/TP53. May form homooligomers. Interacts with DCLRE1C. Interacts with histone H2AFX and this requires phosphorylation of H2AFX on 'Ser-139'. Interacts with histone H4 that has been dimethylated at 'Lys-20'. Has low affinity for histone H4 containing monomethylated 'Lys-20'. Does not bind histone H4 containing unmethylated or trimethylated 'Lys-20'. Has low affinity for histone H3 that has been dimethylated on 'Lys- 79'. Has very low affinity for histone H3 that has been monomethylated on 'Lys-79' (in vitro). Does not bind unmethylated histone H3. Interacts with MUM1/EXPAND1. SUBCELLULAR LOCATION: Nucleus. Chromosome, centromere, kinetochore. Note=Associated with kinetochores. Both nuclear and cytoplasmic in some cells. Recruited to sites of DNA damage, such as double stand breaks. Methylation of histone H4 at 'Lys-20' is required for efficient localization to double strand breaks. ALTERNATIVE PRODUCTS: Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q12888-1; Sequence=Displayed; Name=2; IsoId=Q12888-2; Sequence=VSP_018390; PTM: Asymmetrically dimethylated on Arg residues by PRMT1. Methylation is required for DNA binding. PTM: Phosphorylated at basal level in the absence of DNA damage. Hyper-phosphorylated in an ATM-dependent manner in response to DNA damage induced by ionizing radiation. Hyper-phosphorylated in an ATR-dependent manner in response to DNA damage induced by UV irradiation. SIMILARITY: Contains 2 BRCT domains. SEQUENCE CAUTION: Sequence=BAE06107.1; Type=Erroneous initiation; WEB RESOURCE: Name=NIEHS-SNPs; URL="http://egp.gs.washington.edu/data/tp53bp1/"; COPYRIGHT: Protein annotation is derived from the UniProt Consortium (http://www.uniprot.org/). Distributed under the Creative Commons Attribution-NoDerivs License.,
FUNCTION: May have a role in checkpoint signaling during mitosis (By similarity). Enhances TP53-mediated transcriptional activation. Plays a role in the response to DNA damage. SUBUNIT: Interacts with IFI202A (By similarity). Binds to the central domain of p53/TP53. May form homooligomers. Interacts with DCLRE1C. Interacts with histone H2AFX and this requires phosphorylation of H2AFX on 'Ser-139'. Interacts with histone H4 that has been dimethylated at 'Lys-20'. Has low affinity for histone H4 containing monomethylated 'Lys-20'. Does not bind histone H4 containing unmethylated or trimethylated 'Lys-20'. Has low affinity for histone H3 that has been dimethylated on 'Lys- 79'. Has very low affinity for histone H3 that has been monomethylated on 'Lys-79' (in vitro). Does not bind unmethylated histone H3. Interacts with MUM1/EXPAND1. SUBCELLULAR LOCATION: Nucleus. Chromosome, centromere, kinetochore. Note=Associated with kinetochores. Both nuclear and cytoplasmic in some cells. Recruited to sites of DNA damage, such as double stand breaks. Methylation of histone H4 at 'Lys-20' is required for efficient localization to double strand breaks. ALTERNATIVE PRODUCTS: Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q12888-1; Sequence=Displayed; Name=2; IsoId=Q12888-2; Sequence=VSP_018390; PTM: Asymmetrically dimethylated on Arg residues by PRMT1. Methylation is required for DNA binding. PTM: Phosphorylated at basal level in the absence of DNA damage. Hyper-phosphorylated in an ATM-dependent manner in response to DNA damage induced by ionizing radiation. Hyper-phosphorylated in an ATR-dependent manner in response to DNA damage induced by UV irradiation. SIMILARITY: Contains 2 BRCT domains. SEQUENCE CAUTION: Sequence=BAE06107.1; Type=Erroneous initiation; WEB RESOURCE: Name=NIEHS-SNPs; URL="http://egp.gs.washington.edu/data/tp53bp1/"; COPYRIGHT: Protein annotation is derived from the UniProt Consortium (http://www.uniprot.org/). Distributed under the Creative Commons Attribution-NoDerivs License.
|
| skos:exactMatch | |
| skos:closeMatch |