General Information:

Id: 900
Diseases: Glioblastoma
Parkinson disease
Homo sapiens
DBTRG cell, derived from human glioblastoma multiforma tumor
article
Reference: Veeriah S et al.(2010) Somatic mutations of the Parkinsons disease-associated gene PARK2 in glioblastoma and other human malignancies. Nat. Genet. 42: 77-82 [PMID: 19946270]

Interaction Information:

Comment Transfection of WT but not mutant PARK2 into cells from the DBTRG line resulted in a reduction in the rate of cell growth. WT PARK2 decreased tumor growth in vivo, a property that was reduced by the cancer-specific mutations.
Formal Description
Interaction-ID: 5319

gene/protein

PRKN

decreases_activity of

in cancer cells
Comment Transfection of WT but not mutant PARK2 into cells from the DBTRG line resulted in a reduction in the rate of cell growth. WT PARK2 decreased tumor growth in vivo, a property that was reduced by the cancer-specific mutations.
Formal Description
Interaction-ID: 5322

gene/protein mutant

PARK2-p.R42C

NOT decreases_activity of

in cancer cells
Comment Transfection of WT but not mutant PARK2 into cells from the DBTRG line resulted in a reduction in the rate of cell growth. WT PARK2 decreased tumor growth in vivo, a property that was reduced by the cancer-specific mutations.
Formal Description
Interaction-ID: 5326

gene/protein mutant

PARK2-p.N254S

NOT decreases_activity of

in cancer cells
Comment Transfection of WT but not mutant PARK2 into cells from the DBTRG line resulted in a reduction in the rate of cell growth. WT PARK2 decreased tumor growth in vivo, a property that was reduced by the cancer-specific mutations.
Formal Description
Interaction-ID: 5327

gene/protein mutant

PARK2-p.R275Q

NOT decreases_activity of

in cancer cells
Comment Transfection of WT but not mutant PARK2 into cells from the DBTRG line resulted in a reduction in the rate of cell growth. WT PARK2 decreased tumor growth in vivo, a property that was reduced by the cancer-specific mutations.
Formal Description
Interaction-ID: 5328

gene/protein mutant

PARK2-p.E344G

NOT decreases_activity of

in cancer cells
Comment All PARK2 cancer mutations resulted in a decreased ability of PARK2 to interact with cyclin E, a fundamental component of the cell cycle machinery.
Formal Description
Interaction-ID: 5330

gene/protein

PRKN

interacts (colocalizes) with

gene/protein

Cyclin E

in cancer cells
Comment All PARK2 cancer mutations resulted in a decreased ability of PARK2 to interact with cyclin E, a fundamental component of the cell cycle machinery.
Formal Description
Interaction-ID: 5334

gene/protein mutant

PARK2-p.R42C

NOT interacts (colocalizes) with

gene/protein

Cyclin E

in cancer cells
Comment All PARK2 cancer mutations resulted in a decreased ability of PARK2 to interact with cyclin E, a fundamental component of the cell cycle machinery.
Formal Description
Interaction-ID: 5335

gene/protein mutant

PARK2-p.N254S

NOT interacts (colocalizes) with

gene/protein

Cyclin E

in cancer cells
Comment All PARK2 cancer mutations resulted in a decreased ability of PARK2 to interact with cyclin E, a fundamental component of the cell cycle machinery.
Formal Description
Interaction-ID: 5336

gene/protein mutant

PARK2-p.R275Q

NOT interacts (colocalizes) with

gene/protein

Cyclin E

in cancer cells
Comment All PARK2 cancer mutations resulted in a decreased ability of PARK2 to interact with cyclin E, a fundamental component of the cell cycle machinery.
Formal Description
Interaction-ID: 5337

gene/protein mutant

PARK2-p.E344G

NOT interacts (colocalizes) with

gene/protein

Cyclin E

in cancer cells
Comment The cancer-specific mutations compromised the ability of PARK2 to ubiquitinate cyclin E in vitro and degrade it.
Formal Description
Interaction-ID: 5338

gene/protein

PRKN

increases_ubiquitination/sumoylation of

gene/protein

Cyclin E

in cancer cells
Comment The cancer-specific mutations compromised the ability of PARK2 to ubiquitinate cyclin E in vitro and degrade it.
Formal Description
Interaction-ID: 5339

gene/protein mutant

PARK2-p.R42C

NOT increases_ubiquitination/sumoylation of

gene/protein

Cyclin E

in cancer cells
Comment The cancer-specific mutations compromised the ability of PARK2 to ubiquitinate cyclin E in vitro and degrade it.
Formal Description
Interaction-ID: 5340

gene/protein mutant

PARK2-p.N254S

NOT increases_ubiquitination/sumoylation of

gene/protein

Cyclin E

in cancer cells
Comment The cancer-specific mutations compromised the ability of PARK2 to ubiquitinate cyclin E in vitro and degrade it.
Formal Description
Interaction-ID: 5341

gene/protein mutant

PARK2-p.R275Q

NOT increases_ubiquitination/sumoylation of

gene/protein

Cyclin E

in cancer cells
Comment The cancer-specific mutations compromised the ability of PARK2 to ubiquitinate cyclin E in vitro and degrade it.
Formal Description
Interaction-ID: 5342

gene/protein mutant

PARK2-p.E344G

NOT increases_ubiquitination/sumoylation of

gene/protein

Cyclin E

in cancer cells
Comment The cancer-specific mutations compromised the ability of PARK2 to ubiquitinate cyclin E in vitro and degrade it.
Formal Description
Interaction-ID: 5343

gene/protein

PRKN

decreases_quantity of

gene/protein

Cyclin E

in cancer cells; via ubiquitin-mediated proteasomal degradation
Comment The cancer-specific mutations compromised the ability of PARK2 to ubiquitinate cyclin E in vitro and degrade it.
Formal Description
Interaction-ID: 5344

gene/protein mutant

PARK2-p.R42C

NOT decreases_quantity of

gene/protein

Cyclin E

in cancer cells; via ubiquitin-mediated proteasomal degradation
Comment The cancer-specific mutations compromised the ability of PARK2 to ubiquitinate cyclin E in vitro and degrade it.
Formal Description
Interaction-ID: 5345

gene/protein mutant

PARK2-p.N254S

NOT decreases_quantity of

gene/protein

Cyclin E

in cancer cells; via ubiquitin-mediated proteasomal degradation
Comment The cancer-specific mutations compromised the ability of PARK2 to ubiquitinate cyclin E in vitro and degrade it.
Formal Description
Interaction-ID: 5346

gene/protein mutant

PARK2-p.R275Q

NOT decreases_quantity of

gene/protein

Cyclin E

in cancer cells; via ubiquitin-mediated proteasomal degradation
Comment The cancer-specific mutations compromised the ability of PARK2 to ubiquitinate cyclin E in vitro and degrade it.
Formal Description
Interaction-ID: 5347

gene/protein mutant

PARK2-p.E344G

NOT decreases_quantity of

gene/protein

Cyclin E

in cancer cells; via ubiquitin-mediated proteasomal degradation
Comment PARK2 mutations did not alter its ability to regulate phosphorylation of c-Jun.
Formal Description
Interaction-ID: 5350

gene/protein

PRKN

affects_phosphorylation of

gene/protein

JUN

in cancer cells
Drugbank entries Show/Hide entries for JUN
Comment PARK2 mutations did not alter its ability to regulate phosphorylation of c-Jun.
Formal Description
Interaction-ID: 5352

gene/protein mutant

PARK2-p.R42C

affects_phosphorylation of

gene/protein

JUN

in cancer cells
Drugbank entries Show/Hide entries for JUN
Comment PARK2 mutations did not alter its ability to regulate phosphorylation of c-Jun.
Formal Description
Interaction-ID: 5353

gene/protein mutant

PARK2-p.N254S

affects_phosphorylation of

gene/protein

JUN

in cancer cells
Drugbank entries Show/Hide entries for JUN
Comment PARK2 mutations did not alter its ability to regulate phosphorylation of c-Jun.
Formal Description
Interaction-ID: 5355

gene/protein mutant

PARK2-p.R275Q

affects_phosphorylation of

gene/protein

JUN

in cancer cells
Drugbank entries Show/Hide entries for JUN
Comment PARK2 mutations did not alter its ability to regulate phosphorylation of c-Jun.
Formal Description
Interaction-ID: 5356

gene/protein mutant

PARK2-p.E344G

affects_phosphorylation of

gene/protein

JUN

in cancer cells
Drugbank entries Show/Hide entries for JUN
Comment PARK2 inactivation can lead to impaired mitosis.
Formal Description
Interaction-ID: 5358

gene/protein

PRKN

affects_activity of

in cancer cells
Comment The cancer-specific mutations compromised ability of PARK2 to ubiquitinate cyclin E in vitro and degrade it. Therefore cyclin E levels increase and cells began to cycle again.
Formal Description
Interaction-ID: 16457

gene/protein

PRKN

decreases_activity of

process

cell cycle

by increasing ubiquitination of cyclin E resulting in increased degradation of cyclin E
Comment The cancer-specific mutations compromised ability of PARK2 to ubiquitinate cyclin E in vitro and degrade it.
Formal Description
Interaction-ID: 16461

gene/protein

PRKN

affects_activity of

disease

Glioblastoma