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Literature summary for 3.4.22.B75 extracted from

  • Gonzalez-Prieto, R.; Cuijpers, S.A.; Kumar, R.; Hendriks, I.A.; Vertegaal, A.C.
    c-Myc is targeted to the proteasome for degradation in a SUMOylation-dependent manner, regulated by PIAS1, SENP7 and RNF4 (2015), Cell Cycle, 14, 1859-1872.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.4.22.B75

Protein Variants

Protein Variants Comment Organism
additional information lentivirus mediated SENP7 enzyme knockdown Homo sapiens

Localization

Localization Comment Organism GeneOntology No. Textmining
nucleus
-
 Homo sapiens 5634
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
SUMOylated c-Myc + H2O Homo sapiens
-
 deSUMOylated c-Myc + SUMO
-
 ?

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
breast cancer cell
-
 Homo sapiens
-
colonic cancer cell
-
 Homo sapiens
-
lung cancer cell
-
 Homo sapiens
-
osteosarcoma cell
-
 Homo sapiens
-
U2-OS cell
-
 Homo sapiens
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information SENP7 is a SUMO protease with a preference for deconjugating SUMO2 and SUMO3, particularly in a polymeric form. Precursor SUMO1, SUMO2 and SUMO3 and SUMO1 polymers are poorly processed by SENP7 Homo sapiens ?
-
 ?
SUMOylated c-Myc + H2O
-
 Homo sapiens deSUMOylated c-Myc + SUMO
-
 ?

Synonyms

Synonyms Comment Organism
SENP7
-
 Homo sapiens

General Information

General Information Comment Organism
malfunction increased SUMOylation of c-Myc occurs upon knockdown of the SUMO protease SENP7 Homo sapiens
metabolism oncogene c-Myc-driven tumours are strongly dependent on the SUMO pathway. c-Myc is a target protein for SUMOylation, and SUMOylated c-Myc is subsequently ubiquitylated and degraded by the proteasome.. SUMO protease SENP7 is involved in c-Myc SUMOylation and regulation. Multiple SUMO monomers conjugated to c-Myc could be sufficient to direct SUMOylated c-Myc to the ubiquitin-proteasome pathway. PIAS1 and SENP7 regulate reversible SUMOylation of c-Myc Homo sapiens
additional information the catalytic domain of SENP7 consists of two separate parts interrupted by a stretch of amino acids. This feature is thought to contribute to its specificity for SUMO chains Homo sapiens
physiological function PIAS1 and SENP7 regulate reversible SUMOylation of c-Myc, SENP7 is responsible for removing SUMOs from c-Myc. Closely spaced SUMOs on c-Myc might be important for the regulation of SUMOylated c-Myc by SENP7 providing an alternative binding site for RNF4, a known regulator of SUMO polymers Homo sapiens