ELM
The Eukaryotic Linear Motif resource for
Functional Sites in Proteins
«LIG_Trf4_IWRxY_1« »LIG_TYR_ITAM»

LIG_TRFH_1

Accession:
Functional site class:
TRFH domain docking motifs
Functional site description:
The TRF1 and TRF2 paralogues are part of a 6 protein complex termed shelterin which protects mammalian telomeres. The TRFs also recruit other proteins to the telomeres. With their TRFH domains, they not only form homodimers but also provide additional protein binding interaction surfaces. Several shelterin-associated proteins have been found to dock to a TRFH surface groove which accepts [FY]xLxP peptide motifs.
ELM Description:
The TRFH binding motifs are found in proteins recruited to the shelterin complex by TRF1 and TRF2. The core motif conservation is [FY]xLxP where TRF1 prefers F and TRF2 prefers Y (Chen,2008). These conserved residues make favourable contacts in a hydrophobic groove, while the peptide backbone also makes several polar contacts. In the solved TRF1-Tin2 complex, a C-terminal extension of the motif in Tin2 has positively charged residues that make favourable contacts. While it may be possible to extend the motif pattern with more data, the peptide in the TRF2-Apollo complex was shorter (and the Apollo sequence lacks equivalent charges anyway). Therefore the generic current motif excludes these interactions. Motifs are confirmed in Tin2, Apollo and PinX1.
Pattern: [FY].L.P
Pattern Probability: 0.0002240
Present in taxon: Eukaryota
Interaction Domain:
TRF (PF08558) Telomere repeat binding factor (TRF) (Stochiometry: 1 : 1)
PDB Structure: 3BUA
o See 3 Instances for LIG_TRFH_1
o Abstract
The ends of human chromosomes are characterised by specific arrays of TTAGGG repeats at the telomeres. A complex formed by six-proteins (called Shelterin), specifically recognises these regions (Palm,2008). This complex allows cells to distinguish telomeres from sites of DNA damage. The components of shelterin were gradually identified over the past 10 years. There are essentially six core shelterin subunits: TRF1, TRF2, TIN2, RAP1, TPP1, and POT1. TRF1, TRF2 and POT1 have DNA-binding domains and directly recognize the human chromosome ends. For the shelterin-associated proteins they are recruited to telomeres through interaction with TRF1 or TRF2. TRF2 is also implicated in the regulation of DNA repair processes.
TRF1 and TRF2 are paralogues with almost the same molecular architecture, yet they interact with different protein sets. They are composed of a C-terminal DNA-binding SANT domain, a dimerisation and protein-interacting TRFH domain (PF08558) and natively disordered linkers. The interaction of the shelterin protein TIN2 with TRF1 TRFH was narrowed down to an FxLxP-based motif which binds in part by anti-parallel beta augmentation (Chen,2008). A similar YxLxP motif in the shelterin accessory factor Apollo (SNM1B) binds equivalently to the TRF2 TFRH. It is thought that the motif binding pockets dictate the specificity for the F and Y residues. TRF1 also interacts with an FxLxP motif in the shelterin associated factor PinX1.
o 2 selected references:


o 6 GO-Terms:
Biological Process:
Telomere Maintenance (also annotated in these classes: LIG_RPA_C_Plants LIG_RPA_C_Vert )
Regulation Of Telomerase Activity (also annotated in class: )
Cellular Compartment:
Chromosome, Telomeric Region (also annotated in these classes: DOC_ANK_TNKS_1 )
Telomere (also annotated in class: )
Nucleus (also annotated in these classes: CLV_C14_Caspase3-7 CLV_Separin_Fungi CLV_Separin_Metazoa CLV_TASPASE1 DEG_APCC_DBOX_1 DEG_APCC_KENBOX_2 DEG_APCC_TPR_1 DEG_Cend_DCAF12_1 DEG_Cend_FEM1AC_1 DEG_Cend_FEM1B_2 DEG_Cend_KLHDC2_1 DEG_Cend_TRIM7_1 DEG_COP1 DEG_COP1_1 DEG_CRL4_CDT2_1 DEG_CRL4_CDT2_2 DEG_Kelch_Keap1_1 DEG_Kelch_Keap1_2 DEG_MDM2_SWIB_1 DEG_ODPH_VHL_1 DEG_SCF_COI1_1 DEG_SCF_FBW7_1 DEG_SCF_FBW7_2 DEG_SCF_FBXO31_1 DEG_SCF_SKP2-CKS1_1 DEG_SCF_TIR1_1 DEG_SCF_TRCP1_1 DEG_SIAH_1 DEG_SPOP_SBC_1 DOC_ANK_TNKS_1 DOC_CDC14_PxL_1 DOC_CKS1_1 DOC_CYCLIN_D_Helix_1 DOC_CYCLIN_RevRxL_6 DOC_CYCLIN_RxL_1 DOC_CYCLIN_yClb1_LxF_4 DOC_CYCLIN_yClb3_PxF_3 DOC_CYCLIN_yClb5_NLxxxL_5 DOC_CYCLIN_yCln2_LP_2 DOC_MAPK_DCC_7 DOC_MAPK_FxFP_2 DOC_MAPK_gen_1 DOC_MAPK_GRA24_9 DOC_MAPK_HePTP_8 DOC_MAPK_JIP1_4 DOC_MAPK_MEF2A_6 DOC_MAPK_NFAT4_5 DOC_MAPK_RevD_3 DOC_PIKK_1 DOC_PP1_MyPhoNE_1 DOC_PP1_RVXF_1 DOC_PP1_SILK_1 DOC_PP2A_B56_1 DOC_PP2A_KARD_1 DOC_PP2B_LxvP_1 DOC_PP2B_PxIxIT_1 DOC_PP4_FxxP_1 DOC_PP4_MxPP_1 DOC_USP7_MATH_1 DOC_USP7_MATH_2 DOC_USP7_UBL2_3 DOC_WW_Pin1_4 LIG_14-3-3_CanoR_1 LIG_14-3-3_ChREBP_3 LIG_14-3-3_CterR_2 LIG_ANK_PxLPxL_1 LIG_APCC_ABBA_1 LIG_APCC_Cbox_1 LIG_APCC_Cbox_2 LIG_ARL_BART_1 LIG_ARS2_EDGEI_1 LIG_BRCT_BRCA1_1 LIG_BRCT_BRCA1_2 LIG_BRCT_MDC1_1 LIG_CaM_1-14-15-16_REV_1 LIG_CaMK_CASK_1 LIG_CORNRBOX LIG_CSL_BTD_1 LIG_CtBP_PxDLS_1 LIG_CtBP_RRT_2 LIG_DCNL_PONY_1 LIG_EF_ALG2_ABM_1 LIG_EF_ALG2_ABM_2 LIG_EH1_1 LIG_FHA_1 LIG_FHA_2 LIG_GLEBS_BUB3_1 LIG_HCF-1_HBM_1 LIG_HOMEOBOX LIG_HP1_1 LIG_IRF7_LxLS_2 LIG_IRFs_LxIS_1 LIG_KEPE_1 LIG_KEPE_2 LIG_KEPE_3 LIG_LEDGF_IBM_1 LIG_LSD1_SNAG_1 LIG_MAD2 LIG_Menin_MBM1_1 LIG_MLH1_MIPbox_1 LIG_MSH2_SHIPbox_1 LIG_MTR4_AIM_1 LIG_Mtr4_Air2_1 LIG_Mtr4_Trf4_1 LIG_Mtr4_Trf4_2 LIG_MYND_1 LIG_MYND_2 LIG_MYND_3 LIG_NBox_RRM_1 LIG_NRBOX LIG_Nrd1CID_NIM_1 LIG_PALB2_WD40_1 LIG_PCNA_APIM_2 LIG_PCNA_PIPBox_1 LIG_PCNA_TLS_4 LIG_PCNA_yPIPBox_3 LIG_PTAP_UEV_1 LIG_RBL1_LxSxE_2 LIG_RB_LxCxE_1 LIG_RB_pABgroove_1 LIG_REV1ctd_RIR_1 LIG_RPA_C_Plants LIG_RPA_C_Vert LIG_RRM_PRI_1 LIG_Rrp6Rrp47_Mtr4_1 LIG_Sin3_1 LIG_Sin3_2 LIG_Sin3_3 LIG_SUFU_1 LIG_SUMO_SIM_anti_2 LIG_SUMO_SIM_par_1 LIG_TPR LIG_Trf4_IWRxY_1 LIG_UBA3_1 LIG_ULM_U2AF65_1 LIG_VCP_SHPBox_1 LIG_VCP_VBM_3 LIG_VCP_VIM_2 LIG_WD40_WDR5_VDV_1 LIG_WD40_WDR5_VDV_2 LIG_WD40_WDR5_WIN_1 LIG_WD40_WDR5_WIN_2 LIG_WD40_WDR5_WIN_3 LIG_WRPW_1 LIG_WRPW_2 LIG_WW_2 MOD_AAK1BIKe_LxxQxTG_1 MOD_CDC14_SPxK_1 MOD_CDK_SPK_2 MOD_CDK_SPxK_1 MOD_CDK_SPxxK_3 MOD_CK1_1 MOD_CK2_1 MOD_DYRK1A_RPxSP_1 MOD_GSK3_1 MOD_NEK2_1 MOD_NEK2_2 MOD_PIKK_1 MOD_PKA_1 MOD_PKA_2 MOD_PKB_1 MOD_PLK MOD_Plk_1 MOD_Plk_2-3 MOD_Plk_4 MOD_PRMT_GGRGG_1 MOD_ProDKin_1 MOD_SUMO_for_1 MOD_SUMO_rev_2 ELM:old_LIG_14-3-3_1 ELM:old_LIG_14-3-3_2 ELM:old_LIG_14-3-3_3 TRG_NES_CRM1_1 TRG_NESrev_CRM1_2 TRG_NLS_Bipartite_1 TRG_NLS_MonoCore_2 TRG_NLS_MonoExtC_3 TRG_NLS_MonoExtN_4 )
Molecular Function:
Protein Domain Specific Binding (also annotated in these classes: DEG_APCC_DBOX_1 DEG_APCC_KENBOX_2 DEG_Cend_DCAF12_1 DEG_Cend_FEM1AC_1 DEG_Cend_FEM1B_2 DEG_Cend_KLHDC2_1 DEG_Cend_TRIM7_1 DEG_Kelch_actinfilin_1 DEG_Kelch_Keap1_1 DEG_Kelch_Keap1_2 DEG_Kelch_KLHL3_1 DOC_MIT_MIM_1 LIG_14-3-3_CanoR_1 LIG_14-3-3_CterR_2 LIG_AP_GAE_1 LIG_ARS2_EDGEI_1 LIG_BRCT_BRCA1_1 LIG_BRCT_BRCA1_2 LIG_BRCT_MDC1_1 LIG_CAP-Gly_1 LIG_CSK_EPIYA_1 LIG_CSL_BTD_1 LIG_deltaCOP1_diTrp_1 LIG_EH_1 LIG_EVH1_1 LIG_EVH1_2 LIG_EVH1_3 LIG_FHA_1 LIG_FHA_2 LIG_G3BP_FGDF_1 LIG_MSH2_SHIPbox_1 LIG_MTR4_AIM_1 LIG_PAM2_1 LIG_PAM2_2 LIG_PDZ_Class_1 LIG_PDZ_Class_2 LIG_PDZ_Class_3 LIG_PDZ_Wminus1_1 LIG_PTB_Apo_2 LIG_PTB_Phospho_1 LIG_RRM_PRI_1 LIG_SH3_1 LIG_SH3_2 LIG_SH3_3 LIG_SH3_4 LIG_SH3_PxRPPK_7 LIG_SH3_PxxDY_5 LIG_SH3_PxxPPRxxK_8 LIG_SH3_PxxxRxxKP_6 LIG_Trf4_IWRxY_1 LIG_ULM_U2AF65_1 LIG_WH1 ELM:old_LIG_14-3-3_1 ELM:old_LIG_14-3-3_2 ELM:old_LIG_14-3-3_3 )


o 3 Instances for LIG_TRFH_1
(click table headers for sorting; Notes column: =Number of Switches, =Number of Interactions)
Acc., Gene-, NameStartEndSubsequenceLogic#Ev.OrganismNotes
Q9H816 DCLRE1B
DCR1B_HUMAN 		504 508 FRGLALKYLLTPVNFFQAGY TP 4 Homo sapiens (Human)
Q96BK5 PINX1
PINX1_HUMAN 		289 293 QPPEGRDFTLKPKKRRGKKK TP 2 Homo sapiens (Human)
Q9BSI4 TINF2
TINF2_HUMAN 		258 262 EPLAGRHFNLAPLGRRRVQS TP 4 Homo sapiens (Human)
Please cite: ELM-the Eukaryotic Linear Motif resource-2024 update. (PMID:37962385)

ELM data can be downloaded & distributed for non-commercial use according to the ELM Software License Agreement

AltStyle によって変換されたページ (->オリジナル) /