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.