ELM - instance MOD_CDC14_SPxK_1 in sequence Q08981 at position 3

ELM
The Eukaryotic Linear Motif resource for
Functional Sites in Proteins
MOD_CDC14_SPxK_1

o Instance

Accession Acc. Gene-, NameStartEndSubsequenceLogic PDB OrganismLength
ELMI004320 Q08981 ACM1
ACM1_YEAST
3 6 MISPSKKRTILSSKNINQKP TP --- Saccharomyces cerevisiae S288c 209

o Instance evidence

Evidence classPSI-MIMethodBioSourcePubMedLogicReliabilityNotes
experimental MI:0434 phosphatase assay in vitro Miller,2015 support certain InteractionDetection
experimental MI:0074 mutation analysis in vivo/in vitro Li,2015 support certain FeatureDetection
experimental MI:0434 phosphatase assay in vitro Li,2015 support certain InteractionDetection
experimental MI:0019 coimmunoprecipitation in vivo/in vitro Bremmer,2012 support certain InteractionDetection
experimental MI:0074 mutation analysis in vivo/in vitro Bremmer,2012 support certain FeatureDetection
experimental MI:0943 detection by mass spectrometry in vivo/in vitro Bremmer,2012 support certain InteractionDetection
experimental MI:0434 phosphatase assay in vitro Bremmer,2012 support certain InteractionDetection

o Interactions

Uniprot Id Domain family Domain Start Domain End Affinity Min/Max (µMol) Notes
(Q9UNH5) CC14A_HUMAN PF00782 (DSPc)
Dual specificity phosphatase, catalytic domain
207 328 [mitab] [xml]
(O60729) CC14B_HUMAN PF00782 (DSPc)
Dual specificity phosphatase, catalytic domain
240 366 [mitab] [xml]
(Q00684) CDC14_YEAST PF00782 (DSPc)
Dual specificity phosphatase, catalytic domain
198 335 [mitab] [xml]
(I1RAL2) I1RAL2_GIBZE PF00782 (DSPc)
Dual specificity phosphatase, catalytic domain
265 393 [mitab] [xml]
Please cite: ELM-the Eukaryotic Linear Motif resource-2024 update. (PMID:37962385)

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