ELM IDDescription
CLV_NDR_NDR_1N-Arg dibasic convertase (nardilysine) cleavage site (Xaa-|-Arg-Lys or Arg-|-Arg-Xaa)
CLV_PCSK_PC1ET2_1NEC1/NEC2 cleavage site (Lys-Arg-|-Xaa)
CLV_PCSK_PC7_1Proprotein convertase 7 (PC7, PCSK7) cleavage site (Arg-Xaa-Xaa-Xaa-[Arg/Lys]-Arg-|-Xaa)
CLV_PCSK_SKI1_1Subtilisin/kexin isozyme-1 (SKI1) cleavage site ([RK]-X-[hydrophobic]-[LTKF]-|-X)
CLV_TASPASE1Taspase1 is a threonine aspartase which was first identified as the protease responsible for processing the trithorax (MLL) type of histone methyltransferases.
LIG_14-3-3_1Mode 1 interacting phospho-motif for 14-3-3 proteins with key conservation RxxSxP
LIG_14-3-3_2Longer mode 2 interacting phospho-motif for 14-3-3 proteins with key conservation RxxxS#p.
LIG_14-3-3_3Consensus derived from reported natural interactors which do not match the Mode 1 and Mode 2 ligands.
LIG_AP2alpha_1FxDxF motif responsible for the binding of accessory endocytic proteins to the appendage of the alpha-subunit of adaptor protein complex AP-2
LIG_AP2alpha_2DPF/W motif binds alpha and beta subunits of AP2 adaptor complex.
LIG_APCC_Dbox_1An RxxL-based motif that binds to the Cdh1 and Cdc20 components of APC/C thereby targeting the protein for destruction in a cell cycle dependent manner
LIG_APCC_KENbox_2Motif conserving the exact sequence KEN that binds to the APC/C subunit Cdh1 causing the protein to be targeted for 26S proteasome mediated degradation.
LIG_AP_GAE_1The acidic Phe motif mediates the interaction between a set of accessory proteins and the gamma-ear domain (GAE) of GGAs and AP-1. Proposed roles: in clathrin localization and assembly on TGN/endosome membranes and in traffic between the TGN and endosome.
LIG_BIR_II_1These IBMs are found in pro-apoptotic proteins and function in the abrogation of caspase inhibition by Inhibitor of Apoptosis Proteins (IAPs) in apoptotic cells. The motif binds specifically to type II BIR domains.
LIG_BIR_III_1These IBMs are found in pro-apoptotic proteins and function in the abrogation of caspase inhibition by Inhibitor of Apoptosis Proteins (IAPs) in apoptotic cells. The motif binds specifically to type III BIR domains.
LIG_BIR_III_2These IBMs are found at the N-terminal regions of caspase subunits where they mediate the inhibition of activated caspases by binding to conserved surface grooves on type III BIR domains of Inhibitor of Apoptosis Proteins (IAPs).
LIG_BIR_III_3These IBMs are found in arthropodal pro-apoptotic proteins and function in the abrogation of caspase inhibition by Inhibitor of Apoptosis Proteins (IAPs) in apoptotic cells. The motif binds specifically to type III BIR domains of arthropodal IAPs.
LIG_BIR_III_4These IBMs are found in the N-terminal regions of arthropodal caspase subunits where they mediate the inhibition of activated caspases by binding to conserved surface grooves on type III BIR domains of Inhibitor of Apoptosis Proteins (IAPs)
LIG_BRCT_BRCA1_1Phosphopeptide motif which directly interacts with the BRCT (carboxy-terminal) domain of the Breast Cancer Gene BRCA1 with low affinity
LIG_BRCT_BRCA1_2Phosphopeptide motif which directly interacts with the BRCT (carboxy-terminal) domain of the Breast Cancer Gene BRCA1 with high affinity.
LIG_BRCT_MDC1_1Phosphopeptide motif which is specifically recognized by the BRCT (Carboxy-terminal) repeats of MDC1
LIG_CAP-Gly_1Short, acidic and aromatic carboxy terminal sequence found in a small group of microtubule-associated-proteins. The EEY/F$ motif is highly conserved and so far limited to a few known proteins, alpha-tubulin, EB proteins and CLIP170.
LIG_Clathr_ClatBox_1Clathrin box motif found on cargo adaptor proteins, it interacts with the beta propeller structure located at the N-terminus of Clathrin heavy chain.
LIG_Clathr_ClatBox_2Clathrin box motif found on cargo adaptor proteins, it mediates binding to the N-terminal beta propeller of clathrin heavy chain. Also called W box, it is found in the central region of Amphiphysins where it coexists with a "classical" clathrin box.
LIG_COP1COP1 binding motif. The ring finger protein COP1 is an E3 ubiquitin ligase that regulates plant light sensitive development and in mammals can target P53 for destruction
LIG_CORNRBOXThe corepressor nuclear receptor box motif confers binding to nuclear receptors.
LIG_CtBPPxDLS motif that interacts with the CtBP protein
LIG_CYCLIN_1Substrate recognition site that interacts with cyclin and thereby increases phosphorylation by cyclin/cdk complexes. Predicted protein should have the MOD_CDK site. Also used by cyclin inhibitors.
LIG_Dynein_DLC8_1The [KR]xTQT motif interacts with the common target-accepting grooves of 8kDa Dynein Light Chain dimer.
LIG_EH_1NPF motif interacting with EH domains, usually during regulation of endocytotic processes
LIG_EH1_1The engrailed homology domain 1 motif is found in homeodomain containing active repressors and other transcription families, and allows for the recruitment of Groucho/TLE corepressors
LIG_EVH1_IA proline-rich motif binding to signal transduction class I EVH1 domains
LIG_EVH1_IIA proline-rich motif binding to signal transduction class II EVH1 domains
LIG_FAT_LD_1The paxillin LD motif is recognized by FAK and other focal adhesion proteins mainly involved in cytoskeletal regulation
LIG_FHA_1Phosphothreonine motif binding a subset of FHA domains that show a preference for a large aliphatic amino acid at the pT+3 position.
LIG_FHA_2Phosphothreonine motif binding a subset of FHA domains that have a preference for an acidic amino acid at the pT+3 position.
LIG_GLEBS_BUB3_1Gle2-binding-sequence motif
LIG_GYFLIG_GYF is a proline-rich sequence specifically recognized by GYF domains
LIG_HCF-1_HBM_1The DHxY Host Cell Factor-1 binding motif (HBM) interacts with the N-terminal kelch propeller domain of the cell cycle regulator HCF-1
LIG_HOMEOBOXThe YPWM motif confers binding to the PBX homeobox domain
LIG_HP1_1Ligand to interface formed by dimerisation of two chromoshadow domains in HP1 proteins.
LIG_IQCalmodulin binding helical peptide motif
LIG_MAD2Mad2 binding motif
LIG_MAPK_1MAPK 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.
LIG_MAPK_2MAPK interacting molecules (e.g. MAPKKs, substrates, phosphatases) carry docking motif that help to regulate specific interaction in the MAPK cascade.
LIG_MDM2Motif found in p53 family members which confers binding to the N-terminal domain of MDM2
LIG_MYNDPxLxP motif, MYND ligand
LIG_NRBOXThe nuclear receptor box motif (LXXLL) confers binding to nuclear receptors
LIG_ODPH_VHL_1Oxygen dependent prolyl hydroxylation motif in the unstructured region of hypoxia-inducible factor protein and bound by the VHL ligand
LIG_PAM2_1Peptide ligand motif that directly interacts with the MLLE/PABC domain found in poly(A) binding proteins and HYD E3 ubiquitin ligases.
LIG_PCNAThe PCNA binding site is found in proteins involved in DNA replication, repair and cell cycle control.
LIG_PDZ_Class_1The C-terminal class 1 PDZ-binding motif is classically represented by a pattern like (ST)X(VIL)*
LIG_PDZ_Class_2The C-terminal class 2 PDZ-binding motif is classically represented by a pattern such as (VYF)X(VIL)*
LIG_PDZ_Class_3The C-terminal class 3 PDZ-binding motif is classically represented by a pattern such as (DE)X(VIL)*
LIG_PP1Protein 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].
LIG_PP2B_1Calcineurin substrate docking site, leads to the effective dephosphorylation of serine/threonine phosphorylation sites.
LIG_PTAP_UEV_1PTAP motif binds the N-terminal UEV domain of Tsg10
LIG_PTB_Apo_2These phosphorylation-independent motifs bind to Dab-like PTB domains. Unlike the phosphorylation-dependent PTB motif, binding is not driven by contacts at the 0 or FY position, but instead is dependent upon the large number of hydrophobic and hydrogen bo
LIG_PTB_Phospho_1This phosphorylation-dependent motif binds to Shc-like and IRS-like PTB domains. The pTyr is positioned within a highly basic-charged anchoring pocket. A hydrophobic residue -5 (compared to pY) increases the affinity of the interaction
LIG_RAPTOR_TOS_1The 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. The proteins are activated or deactivated
LIG_Rb_LxCxE_1Interacts with the Retinoblastoma protein
LIG_Rb_pABgroove_1The LxxLFD motif binds in a deep groove between pocket A and pocket B of the Retinoblastoma protein
LIG_RGDThe RGD motif can be found in many proteins of the extracellular matrix and it is recognized by different members of the integrin family. The structure of the tenth type III module of fibronectin has shown that the RGD motif lies on an exposed flexible loop
LIG_RRM_PRI_1The PTB RRM2 Interacting (PRI) motif is found in some splicing regulators, possibly only in the chordate lineage. As part of splicing complex regulation, it interacts with the 2nd RNA binding domain (RRM) of PTB, the polypyrimidine tract binding protein.
LIG_SCF_FBW7_1The TPxxS phospho-dependent degron binds the FBW7 F box proteins of the SCF (Skp1_Cullin-Fbox) complex.
LIG_SCF_FBW7_2The TPxxE phospho-dependent degron binds the FBW7 F box proteins of the SCF (Skp1_Cullin-Fbox) complex.
LIG_SCF-TrCP1_1The DSGxxS phospho-dependent degron binds the F box protein of the SCF-betaTrCP1 complex. The degron is found in various proteins that function in regulation of cell state.
LIG_SH2_GRB2GRB2-like Src Homology 2 (SH2) domains binding motif.
LIG_SH2_PTP2SH-PTP2 and phospholipase C-gamma Src Homology 2 (SH2) domains binding motif.
LIG_SH2_SRCSrc-family Src Homology 2 (SH2) domains binding motif
LIG_SH2_STAT3YXXQ motif found in the cytoplasmic region of cytokine receptors that bind STAT3 SH2 domain.
LIG_SH2_STAT5STAT5 Src Homology 2 (SH2) domain binding motif.
LIG_SH2_STAT6STAT6 Src Homology 2 (SH2) domain binding motif.
LIG_SH3_1This is the motif recognized by class I SH3 domains
LIG_SH3_2This is the motif recognized by class II SH3 domains
LIG_SH3_4This is the motif recognized by those SH3 domains with a non-canonical class II recognition specificity
LIG_SH3_5PXXDY motif recognized by some SH3 domains
LIG_SIAH_1The PxAxVxP peptide binds to the substrate-binding domain (SBD) of the Siah family members
LIG_Sin3_1Motif interacts with PAH2 domain in the Sin3 scaffold protein
LIG_Sin3_2 Motif interacts with PAH2 domain in the Sin3 scaffold protein. (sp-1 like)
LIG_Sin3_3Motif interacts with PAH2 domain in the Sin3 scaffold protein. (not mad or sp-1 like)
LIG_SPAK-OSR1_1SPAK/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.
LIG_SxIP_EBH_1SxIP motifs bind to EBH domains.
LIG_TNKBMThe poly(ADP-ribose) polymerases Tankyrase-1 (TNK1_HUMAN) and Tankyrase-2 (TNK2_HUMAN) and bind proteins through an ankyrin-repeat domain (SM0248). The recognised motif (tankyrase-binding motif) is RxxPDG
LIG_TPRLigands of the TPR (tetratricopeptide repeat motif) domains are EEVD motifs, C-terminal sequences highly conserved in all eukaryotic members of the Hsp70 and Hsp90 families.
LIG_TRAF2_1Major TRAF2-binding consensus motif. Members of the tumor necrosis factor receptor (TNFR) superfamily initiate intracellular signaling by recruiting the C-domain of the TNFR-associated factors (TRAFs) through their cytoplasmic tails.
LIG_TRAF2_2Minor TRAF2-binding consensus motif. Members of the tumor necrosis factor receptor (TNFR) superfamily initiate intracellular signaling by recruiting the C-domain of the TNFR-associated factors (TRAFs) through their cytoplasmic tails.
LIG_TRAF6TRAF6 binding site. Members of the tumor necrosis factor receptor (TNFR) superfamily initiate intracellular signaling by recruiting the C-domain of the TNFR-associated factors (TRAFs) through their cytoplasmatic tails.
LIG_TRFH_1TRF1 and TRF2 both bind to another shelterin protein: TIN2. The TRF1-TIN2 interaction was mediated by a short motif in the N-Ter of TIN2. TIN2 connects TRF1 to TRF2; this link contributes to the stabilization of TRF2 on telomeres. TRF2 probably binds al
LIG_ULM_U2AF65_1Pattern encompassing the ULMs in SF1 and SAP155 which bind to the UHM of U2AF65
LIG_USP7_1The USP7 NTD domain binding motif variant based on the MDM2 and P53 interactions.
LIG_USP7_2The USP7 NTD domain binding motif variant based on the EBV EBNA1 interaction
LIG_WRPW_1The WRPW motif mediates recruitment of transcriptional co-repressors of the Groucho/transducin-like enhancer-of-split (TLE) family. LIG_WRPW_1 is based on the C-terminus located motifs found in the Hairy and Runt family proteins
LIG_WRPW_2The WRPW motif mediates recruitment of transcriptional co-repressors of the Groucho/transducin-like enhancer-of-split (TLE) family. LIG_WRPW_2 is not restricted to the C-terminus (in contrast to LIG_WRPW_1).
LIG_WW_1PPXY is the motif recognized by WW domains of Group I
LIG_WW_2PPLP is the motif recognized by WW domains of Group II
LIG_WW_3WW domain of group III binding motif
LIG_WW_4Class IV WW domains interaction motif; phosphorylation-dependent interaction.
MOD_CAAXboxGeneric CAAX box prenylation motif
MOD_CK1_1CK1 phosphorylation site
MOD_CK2_1CK2 phosphorylation site
MOD_Cter_AmidationPeptide C-terminal amidationd>
MOD_GSK3_1GSK3 phosphorylation recognition site
MOD_N-GLC_1Generic motif for N-glycosylation. Shakin-Eshleman et al. showed that Trp, Asp, and Glu are uncommon before the Ser/Thr position. Efficient glycosylation usually occurs when ~60 residues or more separate the glycosylation acceptor site from the C-terminus
MOD_NMyristoylGeneric motif for N-Myristoylation site.
MOD_OFUCOSYSite for attachment of a fucose residue to serin
MOD_PIKK_1(ST)Q motif which is phosphorylated by PIKK family members
MOD_PKA_1Main preference for PKA-type AGC kinase phosphorylation.
MOD_PKA_2Secondary preference for PKA-type AGC kinase phosphorylation.
MOD_PKB_1PKB Phosphorylation site
MOD_PLKSite phosphorylated by the Polo-like-kinase
MOD_ProDKin_1Proline-Directed Kinase (e.g. MAPK) phosphorylation site in higher eukaryotes.
MOD_SUMOMotif recognised for modification by SUMO-1
MOD_TYR_ITAMITAM (immunoreceptor tyrosine-based activatory motif). ITAM consists of partially conserved short sequence of amino acid found in the cytoplasmatic tail of antigen and Fc receptors.
MOD_TYR_ITIMITIM (immunoreceptor tyrosine-based inhibitory motif). Phosphorylation of the ITIM motif, found in the cytoplasmic tail of some inhibitory receptors (KIRs) that bind MHC Class I, leads to the recruitment and activation of a protein tyrosine phosphatase
MOD_TYR_ITSMITSM (immunoreceptor tyrosine-based switch motif). This motif is present in the cytoplasmic region of the CD150 subfamily within the CD2 family and it enables these receptors to bind to and to be regulated by SH2 adaptor molecules, as SH2DIA.
MOD_WntLipidPalmitoylation site in WNT signalling proteins that is required for correct processing in the endoplasmic reticulum
TRG_AP2beta_CARGO_1AP-2 beta appendage platform subdomain (top surface) binding motif used in targeting cargo for internalisation.
TRG_ENDOCYTIC_2Tyrosine-based sorting signal responsible for the interaction with mu subunit of AP (Adaptor Protein) complex
TRG_ER_diLys_1ER retention and retrieving signal found at the C-terminus of type I ER membrane proteins (cytoplasmic in this topology). Di-Lysine signal is reponsible for COP-I mediated retrieval from post ER compartments.
TRG_ER_FFAT_1VAP-A/Scs2 MSP-domain binding FFAT (diphenylalanine [FF] in an Acidic Tract) motif
TRG_ER_KDEL_1Golgi-to-ER retrieving signal found at the C-terminus of many ER soluble proteins. It interacts with the KDEL receptor which in turns interacts with components of the coatomer (COP I).
TRG_LysEnd_APsAcLL_1Sorting and internalisation signal found in the cytoplasmic juxta-membrane region of type I transmembrane proteins. Targets them from the Trans Golgi Network to the lysosomal-endosomal-melanosomal compartments. Interacts with adaptor protein (AP) complexes
TRG_LysEnd_APsAcLL_3Sorting signal found in the cytoplasmic juxta-membrane region of type I transmembrane lysosomal, endosomal and melanosomal proteins. Based on experimental evidence and alignments, this very specific ELM represents the best combination for AP3 binding.
TRG_LysEnd_GGAAcLL_1Sorting signal directing type I transmembrane proteins from the Trans Golgi Network (TGN) to the lysosomal-endosomal compartment. It is found near the C-terminus and interacts with the VHS domain of GGAs adaptor proteins.
TRG_NES_CRM1_1Some proteins re-exported from the nucleus contain a Leucine-rich nuclear export signal (NES) binding to the CRM1 exportin protein.
TRG_NLS_Bipartite_1Bipartite variant of the classical basically charged NLS
TRG_NLS_MonoCore_2Monopartite variant of the classical basically charged NLS. Strong core version.
TRG_NLS_MonoExtC_3Monopartite variant of the classical basically charged NLS. C-extended version.
TRG_NLS_MonoExtN_4Monopartite variant of the classical basically charged NLS. N-extended version.
TRG_PEXSpecific ELM present in Pex5p and binding to Pex13p and Pex14p. Part of the peroxisomal matrix protein import system
TRG_PTS1Generic PTS1 ELM for all eukaryote
TRG_PTS2Generic PTS2 pattern for all eukaryotes (except lineages which have lost it)