ELM
The Eukaryotic Linear Motif resource for
Functional Sites in Proteins
«LIG_SUMO_SIM_par_1« »LIG_TPR»

LIG_SxIP_EBH_1

Accession:
Functional site class:
SxIP motif
Functional site description:
End binding homology (EBH) domains recognize SxIP motifs embedded within basic and Pro/Ser rich sequence regions of microtubule plus-end tracking proteins (+TIPs). The EBH-SxIP interaction is used by numerous +TIPs to target end binding (EB) proteins at growing microtubule ends.
ELM Description:
SxIP motifs within basic and Pro/Ser rich sequence regions bind to EBH domains of EB proteins. Both, the SxIP sequence as well as basic, not strictly conserved, residues in the vicinity of the motif site contribute to the EBH-SxIP binding affinity. Some SxIP motifs are known to be regulated by phosphorylation while acidic residues are strongly disfavoured in the local regions. The current regular expression partially captures this context. There must be either no negative charge within 5 residues or else a basic residue closer to the SxIP than an acidic residue. All SxIP motifs reported by Honnappa,2009 are detected by the pattern. There is one report of a functional SxLP motif in a strongly basic sequence context (Fong,2009). For the moment, the ELM pattern excludes Leu until binding affinities and sequence context of SxLP motifs are better described. Difficult to predict SxIP in entire Proteomes. Possible to predict in proteins known to bind directly to EBs and associated with microtubules.
Pattern: ([KR][^ED]{0,5}[ST].IP[^ED]{5,5})|([^ED]{5,5}[ST].IP[^ED]{0,5}[KR])
Pattern Probability: 0.0002096
Present in taxon: Eukaryota
Interaction Domain:
EB1 (PF03271) EB1-like C-terminal motif (Stochiometry: 1 : 1)
PDB Structure: 3GJO
o See 9 Instances for LIG_SxIP_EBH_1
o Abstract
The end binding homology (EBH) domain (PF03271) is a small, approximately 50-residue protein module highly conserved in organisms from yeast to man. It is exclusively found in end binding (EB) proteins. EB proteins autonomously track growing microtubule plus ends and act as a hub within dynamic microtubule plus-end tracking protein (+TIP) networks. +TIPs constitute a diverse group of evolutionarily conserved microtubule-associated proteins that specifically accumulate at the ends of growing microtubules. They play important roles in essential cellular activities, including chromosome segregation, cell polarization and migration, organelle transport, and intracellular signalling.
The C-terminal EBH domain of EB proteins binds to an array of structurally and functionally unrelated +TIP binding partners, including the adenomatous polyposis coli (APC) tumor suppressor protein, the microtubule-actin crosslinking factor (MACF), the cytoplasmic linker protein (CLIP170), CLIP-associated proteins (CLASPs), the transmembrane protein stromal interaction molecule-1 (STIM1), the dynactin large subunit p150glued, and the mitotic centromere-associated kinesin (MCAK). SxIP motifs embedded within basic and Pro/Ser rich sequence regions of numerous +TIPs specifically bind to highly conserved residues shaping a hydrophobic groove in the EBH domain. Thus EBH domains are SxIP recognition domains. The EBH-SxIP interaction is used to target +TIPs to EBs at growing microtubule ends. Therefore, SxIP motifs act as general microtubule tip localization signals (MtLS).
o 3 selected references:


o 11 GO-Terms:
Biological Process:
Microtubule Cytoskeleton Organization And Biogenesis (also annotated in these classes: LIG_CAP-Gly_1 LIG_CAP-Gly_2 MOD_Plk_1 ELM:old_LIG_14-3-3_2 )
Microtubule-Based Movement (also annotated in these classes: LIG_CAP-Gly_1 LIG_CAP-Gly_2 LIG_Dynein_DLC8_1 )
Establishment And/Or Maintenance Of Microtubule Cytoskeleton Polarity (also annotated in these classes: LIG_CAP-Gly_1 LIG_CAP-Gly_2 )
Microtubule Polymerization Or Depolymerization (also annotated in these classes: LIG_CAP-Gly_1 LIG_CAP-Gly_2 )
Cytoplasmic Microtubule Organization And Biogenesis (also annotated in these classes: LIG_CAP-Gly_2 )
Regulation Of Microtubule-Based Process (also annotated in these classes: LIG_CAP-Gly_1 LIG_CAP-Gly_2 )
Plus-End Directed Microtubule Sliding (also annotated in these classes: LIG_CAP-Gly_1 LIG_CAP-Gly_2 )
Microtubule-Based Process (also annotated in these classes: LIG_CAP-Gly_1 )
Cellular Compartment:
Cytosol (also annotated in these classes: CLV_C14_Caspase3-7 CLV_Separin_Fungi CLV_Separin_Metazoa 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_1 DEG_CRBN_cyclicCter_1 DEG_Kelch_actinfilin_1 DEG_Kelch_Keap1_1 DEG_Kelch_Keap1_2 DEG_Kelch_KLHL12_1 DEG_Kelch_KLHL3_1 DEG_MDM2_SWIB_1 DEG_Nend_Nbox_1 DEG_Nend_UBRbox_1 DEG_Nend_UBRbox_2 DEG_Nend_UBRbox_3 DEG_Nend_UBRbox_4 DEG_ODPH_VHL_1 DEG_SCF_FBW7_1 DEG_SCF_FBW7_2 DEG_SCF_FBXO31_1 DEG_SCF_SKP2-CKS1_1 DEG_SCF_TRCP1_1 DEG_SIAH_1 DOC_AGCK_PIF_1 DOC_AGCK_PIF_2 DOC_AGCK_PIF_3 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_yCln2_LP_2 DOC_GSK3_Axin_1 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_MIT_MIM_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_PUB_PIM_1 DOC_RSK_DDVF_1 DOC_SPAK_OSR1_1 DOC_TBK1_STING_1 DOC_WD40_RPTOR_TOS_1 DOC_WW_Pin1_4 LIG_14-3-3_CanoR_1 LIG_14-3-3_ChREBP_3 LIG_14-3-3_CterR_2 LIG_ActinCP_CPI_1 LIG_ActinCP_TwfCPI_2 LIG_Actin_RPEL_3 LIG_Actin_WH2_1 LIG_Actin_WH2_2 LIG_ANK_PxLPxL_1 LIG_AP2alpha_1 LIG_AP2alpha_2 LIG_APCC_ABBA_1 LIG_APCC_Cbox_1 LIG_APCC_Cbox_2 LIG_AP_GAE_1 LIG_Arc_Nlobe_1 LIG_ARL_BART_1 LIG_BH_BH3_1 LIG_BIR_II_1 LIG_BIR_III_1 LIG_BIR_III_2 LIG_BIR_III_3 LIG_BIR_III_4 LIG_CaM_1-14-15-16_REV_1 LIG_CaM_1-26_7 LIG_CaM_1-5-10-14_3 LIG_CaM_1-8-14_4 LIG_CaM_1-8-9-10_5 LIG_CaM_1-8_REV_2 LIG_CaM_IQ_9 LIG_CaMK_CASK_1 LIG_CaM_NSCaTE_8 LIG_CAP-Gly_1 LIG_CAP-Gly_2 LIG_Clathr_ClatBox_1 LIG_Clathr_ClatBox_2 LIG_CNOT1_NIM_1 LIG_CSK_EPIYA_1 LIG_CtBP_PxDLS_1 LIG_deltaCOP1_diTrp_1 LIG_DLG_GKlike_1 LIG_Dynein_DLC8_1 LIG_EABR_CEP55_1 LIG_EF_ALG2_ABM_1 LIG_EF_ALG2_ABM_2 LIG_EH_1 LIG_eIF4E_1 LIG_eIF4E_2 LIG_EVH1_1 LIG_EVH1_2 LIG_EVH1_3 LIG_FAT_LD_1 LIG_FERM_MyoX_1 LIG_FZD_DVL_PDZ LIG_G3BP_FGDF_1 LIG_GBD_Chelix_1 LIG_GBD_WASP_1 LIG_GSK3_LRP6_1 LIG_GYF LIG_IBAR_NPY_1 LIG_IRF7_LxLS_2 LIG_IRFs_LxIS_1 LIG_KLC1_WD_1 LIG_KLC1_Yacidic_2 LIG_LIR_Apic_2 LIG_LIR_Gen_1 LIG_LIR_LC3C_4 LIG_LIR_Nem_3 LIG_LYPXL_L_2 LIG_LYPXL_S_1 LIG_LYPXL_yS_3 LIG_MYND_3 LIG_OCRL_FandH_1 LIG_PAM2_1 LIG_PAM2_2 LIG_PDZ_Class_1 LIG_PDZ_Class_2 LIG_PDZ_Class_3 LIG_PDZ_Wminus1_1 LIG_Pex14_1 LIG_Pex14_2 LIG_Pex14_3 LIG_Pex14_4 LIG_Pex3_1 LIG_PIP2_ANTH_1 LIG_PIP2_ENTH_1 LIG_PROFILIN_1 LIG_PTAP_UEV_1 LIG_PTB_Apo_2 LIG_PTB_Phospho_1 LIG_SH2_CRK LIG_SH2_GRB2like LIG_SH2_NCK_1 LIG_SH2_PTP2 LIG_SH2_SFK_2 LIG_SH2_SFK_CTail_3 LIG_SH2_STAT3 LIG_SH2_STAT5 LIG_SH2_STAT6 LIG_SH3_1 LIG_SH3_2 LIG_SH3_3 LIG_SH3_4 LIG_SH3_CIN85_PxpxPR_1 LIG_SH3_PxRPPK_7 LIG_SH3_PxxDY_5 LIG_SH3_PxxPPRxxK_8 LIG_SH3_PxxxRxxKP_6 LIG_SPRY_1 LIG_SUFU_1 LIG_TPR LIG_TRAF2like_MATH_loPxQ_2 LIG_TRAF2like_MATH_shPxQ_1 LIG_TRAF3_MATH_PxP_3 LIG_TRAF4_MATH_1 LIG_TRAF6_MATH_1 LIG_TYR_ITAM LIG_TYR_ITIM LIG_TYR_ITSM LIG_UFM1_UFIM_1 LIG_VCP_SHPBox_1 LIG_VCP_VBM_3 LIG_VCP_VIM_2 LIG_Vh1_VBS_1 LIG_WH1 LIG_WRC_WIRS_1 LIG_WW_1 LIG_WW_2 LIG_WW_3 MOD_AAK1BIKe_LxxQxTG_1 MOD_CAAXbox 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_LATS_1 MOD_LOK_YxT_1 MOD_NEK2_1 MOD_NEK2_2 MOD_NMyristoyl MOD_PIKK_1 MOD_PK_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_SPalmitoyl_2 MOD_SPalmitoyl_4 MOD_TYR_CSK MOD_TYR_DYR ELM:old_LIG_14-3-3_1 ELM:old_LIG_14-3-3_2 ELM:old_LIG_14-3-3_3 TRG_AP2beta_CARGO_1 TRG_Cilium_Arf4_1 TRG_Cilium_RVxP_2 TRG_DiLeu_BaEn_1 TRG_DiLeu_BaEn_2 TRG_DiLeu_BaEn_3 TRG_DiLeu_BaEn_4 TRG_DiLeu_BaLyEn_6 TRG_DiLeu_LyEn_5 TRG_ENDOCYTIC_2 TRG_ER_diArg_1 TRG_ER_diLys_1 TRG_ER_FFAT_1 TRG_ER_FFAT_2 TRG_Golgi_diPhe_1 TRG_LysEnd_APsAcLL_1 TRG_LysEnd_APsAcLL_3 TRG_LysEnd_GGAAcLL_1 TRG_LysEnd_GGAAcLL_2 TRG_NES_CRM1_1 TRG_NESrev_CRM1_2 TRG_PTS1 TRG_PTS2 )
Microtubule (also annotated in these classes: LIG_CAP-Gly_1 LIG_CAP-Gly_2 MOD_CDK_SPK_2 MOD_CDK_SPxxK_3 )
Molecular Function:
Microtubule Plus-End Binding (also annotated in these classes: LIG_CAP-Gly_1 LIG_CAP-Gly_2 )


o 9 Instances for LIG_SxIP_EBH_1
(click table headers for sorting; Notes column: =Number of Switches, =Number of Interactions)
Acc., Gene-, NameStartEndSubsequenceLogic#Ev.OrganismNotes
Q6PGN9 PSRC1
PSRC1_HUMAN 		276 289 SSSQLPIPSAIPRPASRMPL TP 1 Homo sapiens (Human)
Q91V27 Mlph
MELPH_MOUSE 		493 506 PSGKPRRKSGIPIFLPRVTE TP 1 Mus musculus (House mouse)
Q9C0H9 SRCIN1
SRCN1_HUMAN 		1032 1046 SEKPSASRTSIPVLTSFGAR TP 1 Homo sapiens (Human)
Q99661 KIF2C
KIF2C_HUMAN 		93 104 QKQKRRSVNSKIPAPKESLR TP 4 Homo sapiens (Human)
1
Q13586 STIM1
STIM1_HUMAN 		637 651 ALQASRNTRIPHLAGKKAVA TP 4 Homo sapiens (Human)
O75122 CLASP2
CLAP2_HUMAN 		515 525 LSVARSSRIPRPSVSQGCSR TP 4 Homo sapiens (Human)
1
O75122 CLASP2
CLAP2_HUMAN 		492 502 ASAQKRSKIPRSQGCSREAS TP 4 Homo sapiens (Human)
Q03001 DST
DYST_HUMAN 		7545 7558 SRPSTAKPSKIPTPQRKSPA TP 6 Homo sapiens (Human)
P25054 APC
APC_HUMAN 		2801 2811 STSARPSQIPTPVNNNTKKR TP 6 Homo sapiens (Human)
1
Please cite: ELM-the Eukaryotic Linear Motif resource-2024 update. (PMID:37962385)

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