The Eukaryotic Linear Motif resource for
Functional Sites in Proteins
export 41 classes as:
ELM IdentifierDescriptionRegExInstancesInstances in PDBArticles.ELM
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 articles.ELM
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 articles.ELM
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 articles.ELM
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 articles.ELM
DOC_CDC14_PxL_1 The PxL substrate docking motif enhances the Cdc14 phosphatase–substrate interaction and promotes subsequent dephosphorylation.

[FYLIM]..[YVILA]P.L.. 10 2 articles.ELM
DOC_CKS1_1 Phospho-dependent motif that mediates docking of CDK substrates and regulators to cyclin-CDK-bound Cks1. [MPVLIFWYQ].(T)P.. 8 1 articles.ELM
DOC_CYCLIN_D_Helix_1 The Cyclin D Helical docking motif mediates binding of substrates to a site on Cyclin D different from the hydrophobic pocket and enhances substrate phosphorylation by CyclinD/Cdk4-6 complexes. [FLV][^P][^P][KR]L[^P][^P][LMIV][^P][^P][^P]R 3 0 articles.ELM
DOC_CYCLIN_RevRxL_6 The hydrophobic patch (hp) of Cyclin A2 can bind an RxL-like motif the reverse orientation. [EDST].{0,3}[FL].[ILV][^D][RK][^PD][^EDWNG]((.{0,3}[KRH])|.) 1 1 articles.ELM
DOC_CYCLIN_RxL_1 Both fungal and mammalian S-phase Cyclin/CDK complexes recognize specific RxL docking motifs in their target proteins. (.|([KRH].{0,3}))[^EDWNSG][^D][RK][^D]L.{0,1}[FL].{0,3}[EDST] 31 7 articles.ELM
DOC_CYCLIN_yClb1_LxF_4 The LxF motif found in budding yeasts serves as a docking site for mitotic cyclin-CDK complexes (M-CDK). It is found in both regulators and mitotic phosphorylation target proteins. (P.[KR]L.F)|(.N[KR]L.F)|(.N.L.F[LMIVFY]) 13 0 articles.ELM
DOC_CYCLIN_yClb3_PxF_3 The hydrophobic patch (hp) of the G2 phase cyclin from budding yeast, Clb3, binds a specific PxF docking motif on regulators and target proteins. (PP..P.F)|(P..P.F..[KR]) 4 0 articles.ELM
DOC_CYCLIN_yClb5_NLxxxL_5 Cyclin hydrophobic patch docking motif NLxxxL specific for S-phase cyclins Clb5 and Clb6 in budding yeasts. ([ILVMF]...NL...L)|([KR].{0,2}NL...L) 5 0 articles.ELM
DOC_CYCLIN_yCln2_LP_2 The budding yeast G1/S cyclins Cln1 and 2 bind a specific leucine- and proline-rich (LP) docking motif on G1-specific target proteins. (L[MLIV]PP)|(((L[LMIV]PA)|(L..P))[ILMVAFYW].[MLIVFHPAY]) 18 0 articles.ELM
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 articles.ELM
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 articles.ELM
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 articles.ELM
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 articles.ELM
DOC_MAPK_GRA24_9 A kinase docking motif that mediates interaction towards the ERK1/2 and p38 subfamilies of MAP kinases [LIV][^P][^P][RK][RK]G.{3,6}[LIVP]P.[LIV].[LIVMF]|[LIV][^P][^P][RK][RK]G.{3,6}[LIVP].P[LIV].[LIVMF] 2 1 articles.ELM
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 articles.ELM
DOC_MAPK_JIP1_4 A shorter D site specifically recognized by the JNK kinases [RK]P[^P][^P]L.[LIVMF] 29 2 articles.ELM
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 articles.ELM
DOC_MAPK_NFAT4_5 An extended D site specifically recognized by the JNK kinases [RK][^P][^P][LIM].L.[LIVMF]. 17 1 articles.ELM
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 articles.ELM
DOC_MIT_MIM_1 C-terminal LxxR[FL]xxL based type 1 MIT interacting motif (MIM1) that docks at the MIT domain present in some ESCRT-III proteins. ((F[^P][^P])|([DE].{0,2}))L[^P][^P]R[FL][^P][^P]L[KR]{0,2} 5 5 articles.ELM
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 articles.ELM
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 articles.ELM
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 articles.ELM
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 articles.ELM
DOC_PP2A_B56_1 Docking site required for the regulatory subunit B56 of PP2A for protein dephosphorylation. ([LMFYWIC]..I.E)|(L..[IVLWC].E). 18 2 articles.ELM
DOC_PP2B_LxvP_1 Docking motif in calcineurin substrates that binds at the interface of the catalytic CNA and regulatory CNB subunits. L.VP 50 1 articles.ELM
DOC_PP2B_PxIxIT_1 PxIxIT docking motif in calcineurin substrates that binds the catalytic CNA subunit. P[^P][ILVF][^P][ILVF][TSHDEQNKR] 27 4 articles.ELM
DOC_PP4_FxxP_1 The FxxP-like docking motif recognized by the EVH1 domains of the PPP4R3 regulatory subunits of the PP4 holoenzyme F..P 15 0 articles.ELM
DOC_PP4_MxPP_1 The MxPP-like docking motif recognized by the EVH1 domains of the PPP4R3 regulatory subunits of the PP4 holoenzyme M.PP 2 0 articles.ELM
DOC_PUB_PIM_1 The PIM motif binds to the PUB domain of proteins involved in the regulation of ubiquitination .D[LM]Y. 2 2 articles.ELM
DOC_RSK_DDVF_1 This short, partly acid [DE]-[DE]-V-F motif binds to the surface region of the RSK N-terminal kinase domain [DE][DE]VF 5 1 articles.ELM
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 articles.ELM
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 articles.ELM
DOC_USP7_MATH_2 The USP7 MATH domain binding motif variant based on the EBV EBNA1 interaction. P.E[^P].S[^P] 1 1 articles.ELM
DOC_USP7_UBL2_3 The USP7 CTD domain binding motif variant based on the ICP0 and DNMT1 interactions K...K 7 2 articles.ELM
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 articles.ELM
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 articles.ELM
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Please cite: The Eukaryotic Linear Motif resource: 2022 release. (PMID:34718738)

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