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Literature summary for 2.7.3.2 extracted from

  • Yang, Y.C.; Fann, M.J.; Chang, W.H.; Tai, L.H.; Jiang, J.H.; Kao, L.S.
    Regulation of sodium-calcium exchanger activity by creatine kinase under energy-compromised conditions (2010), J. Biol. Chem., 285, 28275-28285.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.7.3.2

Protein Variants

Protein Variants Comment Organism
E226Q catalytic site mutants which show no detectable creatine kinase activity demonstrate that enzymatic activity is not required for the regulation of NCX1 activity Homo sapiens
E227L catalytic site mutants which show no detectable creatine kinase activity demonstrate that enzymatic activity is not required for the regulation of NCX1 activity Homo sapiens
E231Q catalytic site mutants which show no detectable creatine kinase activity demonstrate that enzymatic activity is not required for the regulation of NCX1 activity Homo sapiens
E232L catalytic site mutants which show no detectable creatine kinase activity demonstrate that enzymatic activity is not required for the regulation of NCX1 activity Homo sapiens
additional information using chimeric mutants it is shown that C terminus of mitochondrial creatine kinase (sMiCK) and muscle creatine kinase (CKM) is required for the regulation of NCX1 activity Homo sapiens
S123A mutation analysis show that a putative PKC phosphorylation site on sMiCK and CKM is required for the regulation of NCX1 activity: S123A mutant fails to produce a recovery in the decreased NCX1 activity under energy-compromised conditions Homo sapiens
S128A mutation analysis show that a putative PKC phosphorylation site on sMiCK and CKM is required for the regulation of NCX1 activity: S123A mutant fails to produce a recovery in the decreased NCX1 activity under energy-compromised conditions Homo sapiens
T277V autophosphorylation site mutant shows that autophosphorylation is not required for the regulation of NCX1 activity Homo sapiens
T282V autophosphorylation site mutant shows that autophosphorylation is not required for the regulation of NCX1 activity Homo sapiens
T284V autophosphorylation site mutant shows that autophosphorylation is not required for the regulation of NCX1 activity Homo sapiens
T289V autophosphorylation site mutant shows that autophosphorylation is not required for the regulation of NCX1 activity Homo sapiens
T322V autophosphorylation site mutant shows that autophosphorylation is not required for the regulation of NCX1 activity Homo sapiens
T327V autophosphorylation site mutant shows that autophosphorylation is not required for the regulation of NCX1 activity Homo sapiens

Localization

Localization Comment Organism GeneOntology No. Textmining
cytoplasm
-
 Homo sapiens 5737
-
mitochondrion
-
 Homo sapiens 5739
-
plasma membrane under energy-compromised conditions, CKM is recruited to the plasma membrane and co-localizes with NCX1 Homo sapiens 5886
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Homo sapiens using a yeast two-hybrid screening to search for molecules that interact with NCX1 (sodium-calcium exchanger) it is shown that sarcomeric mitochondrial creatine kinase (sMiCK) interacts with NCX1IL. In addition to sMiCK, cytoplasmic muscle-type CK (CKM) is also able to interact with NCX1 in mammalian cells ?
-
 ?

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
heart human heart cDNA library is used Homo sapiens
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information using a yeast two-hybrid screening to search for molecules that interact with NCX1 (sodium-calcium exchanger) it is shown that sarcomeric mitochondrial creatine kinase (sMiCK) interacts with NCX1IL. In addition to sMiCK, cytoplasmic muscle-type CK (CKM) is also able to interact with NCX1 in mammalian cells Homo sapiens ?
-
 ?

Synonyms

Synonyms Comment Organism
CKM
-
 Homo sapiens
mitochondrial creatine kinase
-
 Homo sapiens
muscle-type creatine kinase
-
 Homo sapiens
sMiCK
-
 Homo sapiens

General Information

General Information Comment Organism
physiological function sarcomeric mitochondrial creatine kinase (sMiCK) interacts with NCX1IL (sodium-calcium exchanger). In addition to sMiCK, cytoplasmic muscle-type creatine kinase (CKM) is also able to interact with NCX1 in mammalian cells. Sarcomeric mitochondrial creatine kinase (sMiCK) and cytoplasmic muscle-type CK (CKM) are able to produce a recovery in the decreased NCX1 activity that is lost under energy-compromised conditions Homo sapiens