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. 2015 Nov 28;44(Database issue):D294–D300. doi: 10.1093/nar/gkv1291

Table 2. 49 novel1 ELM classes that have been added since the last ELM publication (21), together with the number of associated instances (middle column) and a short description.

ELM class identifier Instances ELM class description
DEG_Kelch_KLHL3_1 4 An acidic degron motif present in wnk kinases necessary to interact with kelch domain of KLHL2 and KLHL3 proteins for efficient ubiquitination degradation.
DEG_Kelch_Keap1_1 13 Motif that binds to the Kelch domain of KEAP1 with high affinity. This high affinity motif is required for the
DEG_Kelch_Keap1_2 1 efficient recruitment of target proteins to the Cul3-based E3 ligase.
DEG_Kelch_actinfilin_1 1 A hydrophobic degron motif present in some kainate receptors necessary to interact with kelch domain of actinfilin protein for efficient ubiquitination and degradation.
DEG_Nend_Nbox_1 0 N-terminal motif that initiates protein degradation by binding to the N-box of N-recognins. This N-degron variant comprises a bulky hydrophobic residue as destabilizing residue.
DEG_Nend_UBRbox_1 0 N-terminal motifs that initiate protein degradation by binding to the UBR-box of N-recognins. Four different
DEG_Nend_UBRbox_2 0 N-degron variants comprise different N-terminal residues. Type I destabilizing residues can either occur as primary
DEG_Nend_UBRbox_3 0 destabilizing residues, which are positively charged amino acids directly recognized by N-recognins, or as
DEG_Nend_UBRbox_4 8 secondary and tertiary destabilizing amino acids, which can be conjugated to a primary destabilizing residue.
DEG_SPOP_SBC_1 8 The S/T rich motif known as the SPOP-binding consensus (SBC) of the MATH-BTB protein, SPOP, is present in substrates that undergo SPOP/Cul3-dependant ubiquitination.
DOC_CKS1_1 8 Phospho-dependent motif that mediates docking of CDK substrates and regulators to cyclin-CDK-bound Cks1.
DOC_GSK3_Axin_1 6 Docking motif present in Axin protein binds the GSK-3β kinase and aids the phosphorylation of components in the APC destruction complex.
DOC_PP1_MyPhoNE_1 9 Docking motif that binds to the catalytic subunit of Protein Phosphatase 1 (PP1c).
DOC_PP1_SILK_1 14 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.
DOC_PP2A_KARD_1 1 Protein Phosphatase 2A (PP2A)-binding motif found in BubR1 for docking to the regulatory subunit B56 of PP2A.
DOC_PP2B_LxvP_1 8 Docking motif in calcineurin substrates that binds at the interface of the catalytic CNA and regulatory CNB subunits.
DOC_USP7_UBL2_3 0 The USP7 CTD domain binding motif variant based on the ICP0 and DNMT1 interactions.
LIG_Axin_LRP6_1 0 Motif in LRP6, which in its phosphorylated form binds Axin in a pseudo-substrate manner.
LIG_CID_NIM_1 1 The NIM motif in Trf4 interacts with the CTD-interacting domain (CID) of Nrd1.
LIG_CNOT1_NIM_1 10 The CNOT1-interacting motif (NIM) found in Nanos proteins mediates recruitment of the CCR4-NOT deadenylase complex.
LIG_CaMK_CASK_1 6 Motif mediating binding to the calmodulin-dependent protein kinase (CaMK) domain of the membrane protein CASK/Lin2.
LIG_DCNL_PONY_1 2 DCNL PONY domain binding motif variant based on the UBE2M and UBE2F interactions.
LIG_EF_ALG2_ABM_1 9 This isoform-specific ALG-2-binding motif binds to the EF hand domains of the proapoptotic Ca2 +-binding
LIG_EF_ALG2_ABM_2 3 ALG-2 protein in a calcium-dependent manner.
LIG_FZD_DVL_PDZ 0 A short internal motif near the C-terminus of Frizzleds, which interacts with the PDZ domain of DVL in Wnt pathway.
LIG_GBD_WASP_1 4 A hydrophobic motif of double function – it acts as an autoinhibitory element of the GTPase- binding domain (GDB), as well as mediating the protein's interactions with the Arp2/3 complex.
LIG_GSK3_LRP6_1 8 Motif present five times on membrane receptor LRP6, responsible for GSK3 binding and inhibition when phosphorylated.
LIG_LIR_Apic_2 1 Apicomplexa-specific variant of the canonical LIR motif that binds to Atg8 protein family members.
LIG_LIR_Gen_1 21 Canonical LIR motif that binds to Atg8 protein family members to mediate processes involved in autophagy.
LIG_LIR_LC3C_4 1 Non-canonical variant of the LIR motif that binds to Atg8 protein family members to mediate processes involved in autophagy.
LIG_LIR_Nem_3 1 Nematode-specific variant of the canonical LIR motif that binds to Atg8 protein family members.
LIG_LRP6_Inhibitor_1 0 Short motif present in extracellular of some Wnt antagonists recognized by the N-terminal β-propeller domain of LRP5/6 and thus inhibits the Wnt pathway.
LIG_Mtr4_Air2_1 3 This motif on Air2 interacts with the DExH core of Mtr4, forming a part of the nucleus-located TRAMP complex.
LIG_Mtr4_Trf4_1 4 This motif on Trf4 interacts with the DExH core of Mtr4, forming a part of the nucleus-located TRAMP complex.
LIG_Mtr4_Trf4_2 3 This motif on PAPD5 interacts with the DExH core of SKIV2L2, forming a part of the nucleus-located TRAMP complex.
LIG_Pex14_3 1 Motif in Pex5 interacting with the N-terminal domain (NTD) of Pex14
LIG_Pex14_4 0 Fungal motif in Pex5 interacting with the N-terminal domain of Pex14
LIG_RPA_C_Fungi 1 Fungi version of the RPA interacting motif.
LIG_RPA_C_Insects 0 Insect version of the RPA interacting motif.
LIG_RPA_C_Plants 0 Plant version of the RPA interacting motif, which is located on DNA replication and repair proteins UNG2, XPA, TIPIN, SMARCAL1 and RAD14 and interacts with Replication Protein A (RPA), a DNA binding protein.
LIG_RPA_C_Vert 4 The RPA interacting motif is located on DNA replication and repair proteins UNG2, XPA, TIPIN, SMARCAL1 and RAD14 and interacts with Replication Protein A (RPA), a DNA binding protein.
LIG_SUFU_1 5 A hydrophobic motif in GLI transcription factors required for binding to SUFU protein, which inhibits their activity and hence negatively regulates hedgehog signalling.
LIG_UBA3_1 2 UBA3 adenylation domain binding motif variant based on the UBE2M and UBE2F interactions.
LIG_WD40_WDR5_VDV_1 3 This WDR5-binding motif binds to a cleft between blades 5 and 6 of the WD40 repeat domain of WDR5, opposite
LIG_WD40_WDR5_VDV_2 2 of the Win motif-binding site, to mediate assembly of histone modification complexes.
LIG_WD40_WDR5_WIN_1 7 Known as the Win (WDR5 interaction) motif, this peptide contains an invariant arginine residue that inserts into the
LIG_WD40_WDR5_WIN_2 4 central tunnel of the WD40 repeat domain of WDR5 to mediate assembly of histone modification complexes.
LIG_WD40_WDR5_WIN_3 3 Surrounding this arginine are small residues that fit tightly at the entrance of the arginine-binding pocket.
MOD_SUMO_rev_2 20 Inverted version of SUMOylation motif recognized for modification by SUMO-1

1 as of November 2015.