Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 2.7.11.13 extracted from

  • Wang, Q.J.; Acs, P.; Goodnight, J.; Blumberg, P.M.; Mischak, H.; Mushinski, J.F.
    The catalytic domain of PKC-epsilon, in reciprocal PKC-delta and -epsilon chimeras, is responsible for conferring tumorgenicity to NIH3T3 cells, whereas both regulatory and catalytic domains of PKC-epsilon contribute to in vitro transformation (1998), Oncogene, 16, 53-60.
    View publication on PubMed
Search for more literature for 2.7.11.13

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Mus musculus protein kinase C-epsilon increases growth and cause malignant transformation when overexpressed in NIH3T3 cells the catalytic domain of PKC-epsilon, in reciprocal PKC-delta and PKC-epsilon chimeras, is responsible for conferring tumorgenicity to NIH3T3 cells, whereas both regulatory and catalytic domains of PKC-epsilon contribute to in vitro transformation ?
-
 ?

Organism

Organism UniProt Comment Textmining
Mus musculus P16054
-
-

Source Tissue

Source Tissue Comment Organism Textmining

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information protein kinase C-epsilon increases growth and cause malignant transformation when overexpressed in NIH3T3 cells the catalytic domain of PKC-epsilon, in reciprocal PKC-delta and PKC-epsilon chimeras, is responsible for conferring tumorgenicity to NIH3T3 cells, whereas both regulatory and catalytic domains of PKC-epsilon contribute to in vitro transformation Mus musculus ?
-
 ?

Synonyms

Synonyms Comment Organism
protein kinase C, epsilon type
-
 Mus musculus