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Group by :Switch typeMotif classProteinEnzymePathway         Show inferred   Group Index    Colouring Info              Filtered: PFAM:PF00498 (8 hits) x
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          Curated          inferred


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Casein kinase II subunit alphaCyclin-dependent kinase 1Glycogen synthase kinase-3 beta
Probable serine/threonine-protein kinase pknG (Mycobacterium)Serine/threonine-protein kinase pknB (Mycobacterium)


MotifProteinStartEndSwitch TypeSwitch SubtypeSwitch descriptionInformationEvidence

Casein kinase II subunit alpha - CSNK2A1 -  Homo sapiens
LIG_FHA_2 XRCC1_HUMAN521527BinaryPhysicochemical compatibilityPhosphorylation of T523 in the FHA-binding motif of DNA repair protein XRCC1 (XRCC1) by Casein kinase II subunit alpha (CSNK2A1) induces binding to the Aprataxin (APTX) protein.
details
Curated

Cyclin-dependent kinase 1 - CDK1 -  Homo sapiens
LIG_FHA_2 MK67I_HUMAN238244SpecificityAltered binding specificityPhosphorylation of T238 of MKI67 FHA domain-interacting nucleolar phosphoprotein (MKI67IP) by Cyclin-dependent kinase 1 (CDK1) primes for phosphorylation of T234 by Glycogen synthase kinase-3 beta (GSK3B), which primes for phosphorylation of S230 by GSK3B. Triple-phosphorylated hNIFK (MKI67IP) binds strongly to Antigen KI-67 (MKI67).
details
Curated

Glycogen synthase kinase-3 beta - GSK3B -  Homo sapiens
LIG_FHA_2 MK67I_HUMAN238244SpecificityAltered binding specificityPhosphorylation of T238 of MKI67 FHA domain-interacting nucleolar phosphoprotein (MKI67IP) by Cyclin-dependent kinase 1 (CDK1) primes for phosphorylation of T234 by Glycogen synthase kinase-3 beta (GSK3B), which primes for phosphorylation of S230 by GSK3B. Triple-phosphorylated hNIFK (MKI67IP) binds strongly to Antigen KI-67 (MKI67).
details
Curated
LIG_FHA_2 MK67I_HUMAN238244SpecificityAltered binding specificityPhosphorylation of T238 of MKI67 FHA domain-interacting nucleolar phosphoprotein (MKI67IP) by Cyclin-dependent kinase 1 (CDK1) primes for phosphorylation of T234 by Glycogen synthase kinase-3 beta (GSK3B), which primes for phosphorylation of S230 by GSK3B. Triple-phosphorylated hNIFK (MKI67IP) binds strongly to Antigen KI-67 (MKI67).
details
Curated
LIG_FHA_2 MK67I_HUMAN238244CumulativeRheostaticPhosphorylation of T238 in MKI67 FHA domain-interacting nucleolar phosphoprotein (MKI67IP) by Cyclin-dependent kinase 1 (CDK1) primes for phosphorylation of T234 by Glycogen synthase kinase-3 beta (GSK3B), which primes for phosphorylation of S230 by Glycogen synthase kinase-3 beta (GSK3B). Triple-phosphorylated hNIFK (MKI67 FHA domain-interacting nucleolar phosphoprotein (MKI67IP)) binds strongly to Antigen KI-67 (MKI67). See also switch details
details
Curated
LIG_FHA_2 MK67I_HUMAN238244CumulativeRheostaticPhosphorylation of T238 in MKI67 FHA domain-interacting nucleolar phosphoprotein (MKI67IP) by Cyclin-dependent kinase 1 (CDK1) primes for phosphorylation of T234 by Glycogen synthase kinase-3 beta (GSK3B), which primes for phosphorylation of S230 by Glycogen synthase kinase-3 beta (GSK3B). Triple-phosphorylated hNIFK (MKI67 FHA domain-interacting nucleolar phosphoprotein (MKI67IP)) binds strongly to Antigen KI-67 (MKI67). See also switch details
details
Curated

Probable serine/threonine-protein kinase pknG - PKNG -  Mycobacterium tuberculosis
LIG_FHA_1 Y1827_MYCTU1925BinaryPhysicochemical compatibilityPhosphorylation of T21 in the FHA-binding motif of Uncharacterized protein Rv1827/MT1875 (Rv1827) by Probable serine/threonine-protein kinase pknG (pknG) results in auto-inhibition due to an intramolecular interaction with the FHA domain. As a result, phosphorylation-independent interactions of the FHA domain with metabolic enzymes, which regulate the catalytic activity of these enzymes, are blocked (See also switch details).
details
Curated

Serine/threonine-protein kinase pknB - PKNB -  Mycobacterium tuberculosis
LIG_FHA_1 Y1827_MYCTU2026BinaryPhysicochemical compatibilityPhosphorylation of T22 in the FHA-binding motif of Uncharacterized protein Rv1827/MT1875 (Rv1827) by Serine/threonine-protein kinase pknB (pknB) results in auto-inhibition due to an intramolecular interaction with the FHA domain. As a result, phosphorylation-independent interactions of the FHA domain with metabolic enzymes, which regulate the catalytic activity of these enzymes, are blocked (See also switch details).
details
Curated
           
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