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Literature summary for 2.7.8.27 extracted from

  • Subathra, M.; Qureshi, A.; Luberto, C.
    Sphingomyelin synthases regulate protein trafficking and secretion (2011), PLoS ONE, 6, e23644.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.7.8.27

Inhibitors

Inhibitors Comment Organism Structure
D609
-
 Homo sapiens
D609
-
 Rattus norvegicus

Localization

Localization Comment Organism GeneOntology No. Textmining
Golgi apparatus isoform SMS1 and SMS2 Homo sapiens 5794
-
Golgi apparatus isoform SMS1 and SMS2 Rattus norvegicus 5794
-
plasma membrane isoform SMS2 Homo sapiens 5886
-
plasma membrane isoform SMS2 Rattus norvegicus 5886
-

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-
Rattus norvegicus
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
INS-1 cell
-
 Rattus norvegicus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
phosphatidylcholine + ceramide
-
 Homo sapiens sphingomyelin + 1,2-diacyl-sn-glycerol
-
 ?
phosphatidylcholine + ceramide
-
 Rattus norvegicus sphingomyelin + 1,2-diacyl-sn-glycerol
-
 ?

Synonyms

Synonyms Comment Organism
SMS1 isoform Homo sapiens
SMS1 isoform Rattus norvegicus
SMS2 isoform Homo sapiens
SMS2 isoform Rattus norvegicus

General Information

General Information Comment Organism
malfunction down-regulation of isoform SMS1 and SMS2 reduces the localization of the DAG-binding protein, protein kinase D to the Golgi Homo sapiens
malfunction down-regulation of isoform SMS1 and SMS2 reduces the localization of the DAG-binding protein, protein kinase D to the Golgi. Inhibition of the enzyme significantly reduces insulin secretion in rat INS-1 cells Rattus norvegicus
physiological function isoform SMS1 and SMS2 are capable of regulating trans golgi network-mediated protein trafficking and secretion. Both isoform activities are critical to retain the correct morphology of both cis-Golgi and trans golgi network Homo sapiens
physiological function isoform SMS1 and SMS2 are capable of regulating trans golgi network-mediated protein trafficking and secretion. Both isoform activities are critical to retain the correct morphology of both cis-Golgi and trans-Golgi network Rattus norvegicus