The Eukaryotic Linear Motif resource for
Functional Sites in Proteins
export 28 classes as:
ELM IdentifierDescriptionRegExInstancesInstances in PDB
DOC_AGCK_PIF_1 The DOC_AGCK_PIF_1 motif contains a phosphorylatable serine/threonine residue that allows fine-tuning of the affinity of the motif for the PIF pocket, with the phosphorylated motif showing a higher affinity. F..[FWY][ST][FY] 10 1
DOC_AGCK_PIF_2 In the DOC_AGCK_PIF_2 motif the phosphorylatable serine/threonine residue is replaced by an acidic aspartate or glutamate residue. F..[FWY][DE][FY] 5 0
DOC_AGCK_PIF_3 The DOC_AGCK_PIF_3 variant consists only of the first two core aromatic residues preceding the phosphorylatable or acidic site in the other variants, and the latter of these two aromatic residues is the C-terminal residue of the kinase sequence. F..F$ 5 1
DOC_ANK_TNKS_1 The Tankyrase binding motif interacts with the ankyrin repeat domain region in Tankyrase-1 and Tankyrase-2 to facilitate the PARsylation of the target proteins. .R..[PGAV][DEIP]G. 17 5
DOC_CKS1_1 Phospho-dependent motif that mediates docking of CDK substrates and regulators to cyclin-CDK-bound Cks1. [MPVLIFWYQ].(T)P.. 8 1
DOC_CYCLIN_1 Substrate recognition site that interacts with cyclin and thereby increases phosphorylation by cyclin/cdk complexes. Predicted proteins should have a CDK phosphorylation site. Also used by cyclin/cdk inhibitors. [RK].L.{0,1}[FYLIVMP] 24 6
DOC_GSK3_Axin_1 Docking motif present in Axin protein binds the GSK-3β kinase and aids the phosphorylation of components in the APC destruction complex. V[ED]P[^P][RK]FA[^P]ELI[^P]RLE[^P][VIL] 6 1
DOC_MAPK_DCC_7 A kinase docking motif mediating interaction towards the ERK1/2 and p38 subfamilies of MAP kinases [RK].{2,4}[LIVP]P.[LIV].[LIVMF]|[RK].{2,4}[LIVP].P[LIV].[LIVMF] 11 2
DOC_MAPK_FxFP_2 MAPK interacting molecules (e.g. MAPKKs, substrates, phosphatases) carry docking motif that help to regulate specific interaction in the MAPK cascade. F.[FY]P 15 1
DOC_MAPK_gen_1 MAPK interacting molecules (e.g. MAPKKs, substrates, phosphatases) carry docking motif that help to regulate specific interaction in the MAPK cascade. The classic motif approximates (R/K)xxxx#x# where # is a hydrophobic residue. [KR]{0,2}[KR].{0,2}[KR].{2,4}[ILVM].[ILVF] 15 0
DOC_MAPK_HePTP_8 A kinase docking motif that interacts with the ERK1/2 and p38 subfamilies of MAP kinases. ([LIV][^P][^P][RK]....[LIVMP].[LIV].[LIVMF])|([LIV][^P][^P][RK][RK]G.{4,7}[LIVMP].[LIV].[LIVMF]) 10 3
DOC_MAPK_JIP1_4 A shorter D site specifically recognized by the JNK kinases [RK]P[^P][^P]L.[LIVMF] 29 2
DOC_MAPK_MEF2A_6 A kinase docking motif that mediates interaction towards the ERK1/2 and p38 subfamilies of MAP kinases. [RK].{2,4}[LIVMP].[LIV].[LIVMF] 27 2
DOC_MAPK_NFAT4_5 An extended D site specifically recognized by the JNK kinases [RK][^P][^P][LIM].L.[LIVMF]. 17 1
DOC_MAPK_RevD_3 Reverse (C to N direction) of the classical MAPK docking motif DOC_MAPK_gen_1 with an often extended linker region of the bipartite motif. [LIVMPFA].[LIV].{1,2}[LIVMP].{4,6}[LIV]..[RK][RK] 6 3
DOC_PIKK_1 DOC_PIKK_1 motif is located in the C terminus of Nbs1 and its homologues and interacts with PIKK family members. [DEN][DEN].{2,3}[ILMVA][DEN][DEN]L 4 0
DOC_PP1_MyPhoNE_1 Docking motif that binds to the catalytic subunit of Protein Phosphatase 1 (PP1c) and is generally located N-terminal to an RVxF motif. R[^P][DEQ]Q[VIL]([RK][^P]|[^P][RK])[YW] 9 1
DOC_PP1_RVXF_1 Protein phosphatase 1 catalytic subunit (PP1c) interacting motif binds targeting proteins that dock to the substrate for dephosphorylation. The motif defined is [RK]{0,1}[VI][^P][FW]. ..[RK].{0,1}[VIL][^P][FW]. 19 4
DOC_PP1_SILK_1 Protein phosphatase 1 catalytic subunit (PP1c) interacting motif that often cooperates with and is located N-terminal to the RVXF motif to dock proteins to PP1c. .[GS]IL[KR][^DE] 14 1
DOC_PP2A_B56_1 Docking site required for the regulatory subunit B56 of PP2A for protein dephosphorylation. ([LMFYWIC]..I.E)|(L..[IVLWC].E). 18 1
DOC_PP2B_LxvP_1 Docking motif in calcineurin substrates that binds at the interface of the catalytic CNA and regulatory CNB subunits. L.[LIVAPM]P 8 0
DOC_PP2B_PxIxI_1 Calcineurin substrate docking site, leads to the effective dephosphorylation of serine/threonine phosphorylation sites. .P[^P]I[^P][IV][^P] 10 2
DOC_SPAK_OSR1_1 SPAK/OSR1 kinase binding motif acts as a docking site which aids the interaction with their binding partners including the upstream activators and the phosphorylated substrates. RF[^P][IV]. 13 1
DOC_USP7_MATH_1 The USP7 MATH domain binding motif variant based on the MDM2 and p53 interactions. [PA][^P][^FYWIL]S[^P] 10 6
DOC_USP7_MATH_2 The USP7 MATH domain binding motif variant based on the EBV EBNA1 interaction. P.E[^P].S[^P] 1 1
DOC_USP7_UBL2_3 The USP7 CTD domain binding motif variant based on the ICP0 and DNMT1 interactions K...K 0 0
DOC_WD40_RPTOR_TOS_1 The TOR pathway adaptor protein Raptor links the mTOR kinase to the TOS motif containing substrates 4E-BP1 and S6-beta kinases.
Proteins with TOR motif (e.g. 4E-BP1, S6KB1) participate in the transcription mechanism.
F[EDQS][MILV][ED][MILV]((.{0,1}[ED])|($)) 5 0
DOC_WW_Pin1_4 The Class IV WW domain interaction motif is recognised primarily by the Pin1 phosphorylation-dependent prolyl isomerase. ...([ST])P. 96 1
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DOCHide/Show instances of class type DOC (docking sites)
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Please cite: ELM 2016-data update and new functionality of the eukaryotic linear motif resource. (PMID:26615199)

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