The Eukaryote Linear Motif resource for Functional Sites in Proteins

o Summary for sequence 'EPN1_HUMAN'.

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DEG_SCF_FBW7_1DOC_CKS1_1CLV_PCSK_PC1ET2_1MOD_PKA_2MOD_CDK_SPxK_1CLV_PCSK_KEX2_1MOD_PKA_1MOD_CDK_SPxxK_3LIG_Clathr_ClatBox_1LIG_CSL_BTD_1LIG_TRAF2_1MOD_NEK2_1MOD_NEK2_2LIG_WW_1TRG_ENDOCYTIC_2Secondary StructureLIG_TRAF6LIG_LIR_Apic_2LIG_AP2alpha_2MOD_PLKLIG_SH2_STAT5LIG_SH2_STAT3LIG_FHA_2LIG_CaM_IQ_9LIG_FHA_1LIG_RGDLIG_TYR_ITIMSubmit to SmartSubmit to PfamCLV_PCSK_SKI1_1LIG_LIR_Gen_1DOC_MAPK_MEF2A_6LIG_MYND_1LIG_NRBOXCLV_NRD_NRD_1LIG_SUMO_SIM_anti_2LIG_SH2_PTP2LIG_SH3_1LIG_Pex14_2LIG_Pex14_1LIG_SH3_2CLV_PCSK_FUR_1DOC_MAPK_gen_1MOD_PIKK_1LIG_EH_1LIG_SUMO_SIM_par_1Submit to GlobPlotDEG_APCC_KENBOX_2LIG_BIR_II_1MOD_N-GLC_1PhosphoELMTRG_AP2beta_CARGO_1LIG_eIF4E_1LIG_UBA3_1LIG_LIR_Nem_3TRG_ER_diArg_1TRG_LysEnd_APsAcLL_1DOC_CYCLIN_1LIG_PDZ_Class_2LIG_BRCT_BRCA1_1DOC_USP7_UBL2_3ConscoredConscoredCLV_PCSK_PC1ET2_1<b>[62,64]</b><br /><b>KRL</b><br /><b><br /><b>BestStruct: d1h0aa_</b><br /><b>AccessScore: 0.237</b><br /><b>SecStrScore: 0.55</b><br /><b>TotalScore: 0.787</b><br /><b>TotalScoreP-value: </b></b><br />ConscoredMOD_PKA_2<b>[90,96]</b><br /><b>ERVSQQC</b><br /><b><br /><b>BestStruct: d1h0aa_</b><br /><b>AccessScore: 0.287</b><br /><b>SecStrScore: 0.55</b><br /><b>TotalScore: 0.837</b><br /><b>TotalScoreP-value: </b></b><br />ConscoredConscoredConscoredCLV_PCSK_KEX2_1<b>[7,9]</b><br /><b>RRQ</b><br /><b><br /><b>BestStruct: d1h0aa_</b><br /><b>AccessScore: 0.487</b><br /><b>SecStrScore: 0.55</b><br /><b>TotalScore: 1.037</b><br /><b>TotalScoreP-value: </b></b><br />CLV_PCSK_KEX2_1<b>[62,64]</b><br /><b>KRL</b><br /><b><br /><b>BestStruct: d1h0aa_</b><br /><b>AccessScore: 0.237</b><br /><b>SecStrScore: 0.55</b><br /><b>TotalScore: 0.787</b><br /><b>TotalScoreP-value: </b></b><br />ConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredMOD_NEK2_1<b>[1,6]</b><br /><b>MSTSSL</b><br /><b><br /><b>BestStruct: d1h0aa_</b><br /><b>AccessScore: 0.53</b><br /><b>SecStrScore: 0.708</b><br /><b>TotalScore: 1.238</b><br /><b>TotalScoreP-value: </b></b><br />MOD_NEK2_1<b>[84,89]</b><br /><b>LIKTGS</b><br /><b><br /><b>BestStruct: d1h0aa_</b><br /><b>AccessScore: 0.115</b><br /><b>SecStrScore: 0.867</b><br /><b>TotalScore: 0.982</b><br /><b>TotalScoreP-value: </b></b><br />MOD_NEK2_1<b>[154,159]</b><br /><b>LAQTAT</b><br /><b><br /><b>BestStruct: d1h0aa_</b><br /><b>AccessScore: 0.783</b><br /><b>SecStrScore: 1.025</b><br /><b>TotalScore: 1.808</b><br /><b>TotalScoreP-value: </b></b><br />ConscoredConscoredMOD_NEK2_2<b>[102,107]</b><br /><b>AVQTLK</b><br /><b><br /><b>BestStruct: d1h0aa_</b><br /><b>AccessScore: 0.297</b><br /><b>SecStrScore: 0.81</b><br /><b>TotalScore: 1.107</b><br /><b>TotalScoreP-value: </b></b><br />ConscoredTRG_ENDOCYTIC_2<b>[48,51]</b><br /><b>YNVV</b><br /><b><br /><b>BestStruct: d1h0aa_</b><br /><b>AccessScore: 0.595</b><br /><b>SecStrScore: 1.025</b><br /><b>TotalScore: 1.62</b><br /><b>TotalScoreP-value: </b></b><br />TRG_ENDOCYTIC_2<b>[75,78]</b><br /><b>YKAM</b><br /><b><br /><b>BestStruct: d1h0aa_</b><br /><b>AccessScore: 0.085</b><br /><b>SecStrScore: 0.55</b><br /><b>TotalScore: 0.635</b><br /><b>TotalScoreP-value: </b></b><br />loop: <b>[1,1]</b><br /><b>M</b><br /><b>BestStruct: none</b><br />helix: <b>[2,15]</b><br /><b>STSSLRRQMKNIVH</b><br /><b>BestStruct: none</b><br />loop: <b>[16,18]</b><br /><b>NYS</b><br /><b>BestStruct: none</b><br />helix: <b>[19,27]</b><br /><b>EAEIKVREA</b><br /><b>BestStruct: none</b><br />loop: <b>[28,36]</b><br /><b>TSNDPWGPS</b><br /><b>BestStruct: none</b><br />helix: <b>[37,46]</b><br /><b>SSLMSEIADL</b><br /><b>BestStruct: none</b><br />loop: <b>[47,49]</b><br /><b>TYN</b><br /><b>BestStruct: none</b><br />helix: <b>[50,64]</b><br /><b>VVAFSEIMSMIWKRL</b><br /><b>BestStruct: none</b><br />loop: <b>[65,67]</b><br /><b>NDH</b><br /><b>BestStruct: none</b><br />3/10 helix: <b>[68,70]</b><br /><b>GKN</b><br /><b>BestStruct: none</b><br />helix: <b>[71,87]</b><br /><b>WRHVYKAMTLMEYLIKT</b><br /><b>BestStruct: none</b><br />loop: <b>[88,89]</b><br /><b>GS</b><br /><b>BestStruct: none</b><br />helix: <b>[90,98]</b><br /><b>ERVSQQCKE</b><br /><b>BestStruct: none</b><br />loop: <b>[99,99]</b><br /><b>N</b><br /><b>BestStruct: none</b><br />helix: <b>[100,105]</b><br /><b>MYAVQT</b><br /><b>BestStruct: none</b><br />3/10 helix: <b>[106,108]</b><br /><b>LKD</b><br /><b>BestStruct: none</b><br />loop: <b>[109,120]</b><br /><b>FQYVDRDGKDQG</b><br /><b>BestStruct: none</b><br />helix: <b>[121,134]</b><br /><b>VNVREKAKQLVALL</b><br /><b>BestStruct: none</b><br />loop: <b>[135,136]</b><br /><b>RD</b><br /><b>BestStruct: none</b><br />helix: <b>[137,156]</b><br /><b>EDRLREERAHALKTKEKLAQ
</b><br /><b>BestStruct: none</b><br />loop: <b>[157,158]</b><br /><b>TA</b><br /><b>BestStruct: none</b><br />ConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredLIG_AP2alpha_2<b>[31,33]</b><br /><b>DPW</b><br /><b><br /><b>BestStruct: d1h0aa_</b><br /><b>AccessScore: 0.42</b><br /><b>SecStrScore: 1.5</b><br /><b>TotalScore: 1.92</b><br /><b>TotalScoreP-value: </b></b><br />ConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredConscoredLIG_SH2_STAT5<b>[83,86]</b><br /><b>YLIK</b><br /><b><br /><b>BestStruct: d1h0aa_</b><br /><b>AccessScore: 0.128</b><br /><b>SecStrScore: 0.55</b><br /><b>TotalScore: 0.678</b><br /><b>TotalScoreP-value: </b></b><br />LIG_SH2_STAT5<b>[111,114]</b><br /><b>YVDR</b><br /><b><br /><b>BestStruct: d1h0aa_</b><br /><b>AccessScore: 0.513</b><br /><b>SecStrScore: 1.5</b><br /><b>TotalScore: 2.013</b><br /><b>TotalScoreP-value: </b></b><br />ConscoredLIG_SH2_STAT3<b>[101,104]</b><br /><b>YAVQ</b><br /><b><br /><b>BestStruct: d1h0aa_</b><br /><b>AccessScore: 0.39</b><br /><b>SecStrScore: 0.55</b><br /><b>TotalScore: 0.94</b><br /><b>TotalScoreP-value: </b></b><br />LIG_FHA_2<b>[26,32]</b><br /><b>EATSNDP</b><br /><b><br /><b>BestStruct: d1h0aa_</b><br /><b>AccessScore: 0.209</b><br /><b>SecStrScore: 1.229</b><br /><b>TotalScore: 1.437</b><br /><b>TotalScoreP-value: </b></b><br />LIG_FHA_2<b>[77,83]</b><br /><b>AMTLMEY</b><br /><b><br /><b>BestStruct: d1h0aa_</b><br /><b>AccessScore: 0.091</b><br /><b>SecStrScore: 0.55</b><br /><b>TotalScore: 0.641</b><br /><b>TotalScoreP-value: </b></b><br />LIG_FHA_2<b>[85,91]</b><br /><b>IKTGSER</b><br /><b><br /><b>BestStruct: d1h0aa_</b><br /><b>AccessScore: 0.259</b><br /><b>SecStrScore: 0.821</b><br /><b>TotalScore: 1.08</b><br /><b>TotalScoreP-value: </b></b><br />LIG_FHA_2<b>[103,109]</b><br /><b>VQTLKDF</b><br /><b><br /><b>BestStruct: d1h0aa_</b><br /><b>AccessScore: 0.311</b><br /><b>SecStrScore: 1.02</b><br /><b>TotalScore: 1.331</b><br /><b>TotalScoreP-value: </b></b><br />ConscoredLIG_CaM_IQ_9<b>[106,121]</b><br /><b>LKDFQYVDRDGKDQGV</b><br /><b><br /><b>BestStruct: d1h0aa_</b><br /><b>AccessScore: 0.464</b><br /><b>SecStrScore: 1.409</b><br /><b>TotalScore: 1.873</b><br /><b>TotalScoreP-value: </b></b><br />LIG_FHA_1<b>[1,7]</b><br /><b>MSTSSLR</b><br /><b><br /><b>BestStruct: d1h0aa_</b><br /><b>AccessScore: 0.57</b><br /><b>SecStrScore: 0.686</b><br /><b>TotalScore: 1.256</b><br /><b>TotalScoreP-value: </b></b><br />LIG_FHA_1<b>[45,51]</b><br /><b>DLTYNVV</b><br /><b><br /><b>BestStruct: d1h0aa_</b><br /><b>AccessScore: 0.486</b><br /><b>SecStrScore: 0.957</b><br /><b>TotalScore: 1.443</b><br /><b>TotalScoreP-value: </b></b><br />ConscoredConscoredLIG_TYR_ITIM<b>[46,51]</b><br /><b>LTYNVV</b><br /><b><br /><b>BestStruct: d1h0aa_</b><br /><b>AccessScore: 0.448</b><br /><b>SecStrScore: 1.025</b><br /><b>TotalScore: 1.473</b><br /><b>TotalScoreP-value: </b></b><br />Smart: ENTH: 
<b>[18,144]</b><br /><b>SEAEIKVREATSNDPWGPSS
SLMSEIADLTYNVVAFSEIM
SMIWKRLNDHGKNWRHVYKA
MTLMEYLIKTGSERVSQQCK
ENMYAVQTLKDFQYVDRDGK
DQGVNVREKAKQLVALLRDE
DRLREER</b><br /><b></b><br />Smart: low_complexity_region: 
<b>[157,174]</b><br /><b>TATASSAAVGSGPPPEAE</b><br /><b></b><br />Smart: UIM: 
<b>[183,202]</b><br /><b>EEELQLQLALAMSKEEADQP
</b><br /><b></b><br />Smart: UIM: 
<b>[208,227]</b><br /><b>EDDAQLQLALSLSREEHDKE
</b><br /><b></b><br />Smart: UIM: 
<b>[233,252]</b><br /><b>GDDLRLQMAIEESKRETGGK
</b><br /><b></b><br />Smart: low_complexity_region: 
<b>[265,316]</b><br /><b>TAPAPAPTTDPWGGPAPMAA
AVPTAAPTSDPWGGPPVPPA
ADPWGGPAPTPA</b><br /><b></b><br />Smart: low_complexity_region: 
<b>[332,368]</b><br /><b>DPWGGTPAPAAGEGPTPDPW
GSSDGGVPVSGPSASDP</b><br /><b></b><br />Smart: low_complexity_region: 
<b>[455,467]</b><br /><b>PPPAATPTPTPPT</b><br /><b></b><br />Smart: low_complexity_region: 
<b>[537,546]</b><br /><b>PVPPVPGAPP</b><br /><b></b><br />Smart: low_complexity_region: 
<b>[551,567]</b><br /><b>PLGGGPGLPPMMPPGPP</b><br /><b></b><br />CLV_PCSK_SKI1_1<b>[8,12]</b><br /><b>RQMKN</b><br /><b><br /><b>BestStruct: d1h0aa_</b><br /><b>AccessScore: 0.356</b><br /><b>SecStrScore: 0.55</b><br /><b>TotalScore: 0.906</b><br /><b>TotalScoreP-value: </b></b><br />CLV_PCSK_SKI1_1<b>[25,29]</b><br /><b>REATS</b><br /><b><br /><b>BestStruct: d1h0aa_</b><br /><b>AccessScore: 0.092</b><br /><b>SecStrScore: 0.93</b><br /><b>TotalScore: 1.022</b><br /><b>TotalScoreP-value: </b></b><br />CLV_PCSK_SKI1_1<b>[76,80]</b><br /><b>KAMTL</b><br /><b><br /><b>BestStruct: d1h0aa_</b><br /><b>AccessScore: 0.054</b><br /><b>SecStrScore: 0.55</b><br /><b>TotalScore: 0.604</b><br /><b>TotalScoreP-value: </b></b><br />ConscoredLIG_LIR_Gen_1<b>[45,51]</b><br /><b>DLTYNVV</b><br /><b><br /><b>BestStruct: d1h0aa_</b><br /><b>AccessScore: 0.486</b><br /><b>SecStrScore: 0.957</b><br /><b>TotalScore: 1.443</b><br /><b>TotalScoreP-value: </b></b><br />LIG_LIR_Gen_1<b>[47,51]</b><br /><b>TYNVV</b><br /><b><br /><b>BestStruct: d1h0aa_</b><br /><b>AccessScore: 0.478</b><br /><b>SecStrScore: 1.12</b><br /><b>TotalScore: 1.598</b><br /><b>TotalScoreP-value: </b></b><br />LIG_LIR_Gen_1<b>[58,64]</b><br /><b>SMIWKRL</b><br /><b><br /><b>BestStruct: d1h0aa_</b><br /><b>AccessScore: 0.25</b><br /><b>SecStrScore: 0.55</b><br /><b>TotalScore: 0.8</b><br /><b>TotalScoreP-value: </b></b><br />LIG_LIR_Gen_1<b>[108,112]</b><br /><b>DFQYV</b><br /><b><br /><b>BestStruct: d1h0aa_</b><br /><b>AccessScore: 0.478</b><br /><b>SecStrScore: 1.466</b><br /><b>TotalScore: 1.944</b><br /><b>TotalScoreP-value: </b></b><br />ConscoredConscoredConscoredConscoredConscoredLIG_NRBOX<b>[129,135]</b><br /><b>QLVALLR</b><br /><b><br /><b>BestStruct: d1h0aa_</b><br /><b>AccessScore: 0.253</b><br /><b>SecStrScore: 0.686</b><br /><b>TotalScore: 0.939</b><br /><b>TotalScoreP-value: </b></b><br />CLV_NRD_NRD_1<b>[7,9]</b><br /><b>RRQ</b><br /><b><br /><b>BestStruct: d1h0aa_</b><br /><b>AccessScore: 0.487</b><br /><b>SecStrScore: 0.55</b><br /><b>TotalScore: 1.037</b><br /><b>TotalScoreP-value: </b></b><br />ConscoredConscoredConscoredConscoredConscoredConscoredConscoredLIG_Pex14_1<b>[71,75]</b><br /><b>WRHVY</b><br /><b><br /><b>BestStruct: d1h0aa_</b><br /><b>AccessScore: 0.162</b><br /><b>SecStrScore: 0.55</b><br /><b>TotalScore: 0.712</b><br /><b>TotalScoreP-value: </b></b><br />ConscoredConscoredDOC_MAPK_gen_1<b>[114,123]</b><br /><b>RDGKDQGVNV</b><br /><b><br /><b>BestStruct: d1h0aa_</b><br /><b>AccessScore: 0.461</b><br /><b>SecStrScore: 1.215</b><br /><b>TotalScore: 1.676</b><br /><b>TotalScoreP-value: </b></b><br />DOC_MAPK_gen_1<b>[124,133]</b><br /><b>REKAKQLVAL</b><br /><b><br /><b>BestStruct: d1h0aa_</b><br /><b>AccessScore: 0.241</b><br /><b>SecStrScore: 0.55</b><br /><b>TotalScore: 0.791</b><br /><b>TotalScoreP-value: </b></b><br />DOC_MAPK_gen_1<b>[126,133]</b><br /><b>KAKQLVAL</b><br /><b><br /><b>BestStruct: d1h0aa_</b><br /><b>AccessScore: 0.211</b><br /><b>SecStrScore: 0.55</b><br /><b>TotalScore: 0.761</b><br /><b>TotalScoreP-value: </b></b><br />ConscoredConscoredMOD_PIKK_1<b>[90,96]</b><br /><b>ERVSQQC</b><br /><b><br /><b>BestStruct: d1h0aa_</b><br /><b>AccessScore: 0.287</b><br /><b>SecStrScore: 0.55</b><br /><b>TotalScore: 0.837</b><br /><b>TotalScoreP-value: </b></b><br />ConscoredConscoredConscoredConscoredDisOrder: <b>[28,39]</b><br /><b>TSNDPWGPSSSL</b><br /><b></b><br />DisOrder: <b>[162,177]</b><br /><b>SAAVGSGPPPEAEQAW</b><br /><b></b><br />DisOrder: <b>[199,209]</b><br /><b>ADQPPSCGPED</b><br /><b></b><br />DisOrder: <b>[265,404]</b><br /><b>TAPAPAPTTDPWGGPAPMAA
AVPTAAPTSDPWGGPPVPPA
ADPWGGPAPTPASGDPWRPA
APAGPSVDPWGGTPAPAAGE
GPTPDPWGSSDGGVPVSGPS
ASDPWTPAPAFSDPWGGSPA
KPSTNGTTAAGGFDTEPDEF
</b><br /><b></b><br />DisOrder: <b>[433,475]</b><br /><b>ARSPGAFDMSGVRGSLAEAV
GSPPPAATPTPTPPTRKTPE
SFL</b><br /><b></b><br />DisOrder: <b>[486,526]</b><br /><b>SLVSRPGPTPPGAKASNPFL
PGGGPATGPSVTNPFQPAPP
A</b><br /><b></b><br />DisOrder: <b>[534,572]</b><br /><b>RLSPVPPVPGAPPTYISPLG
GGPGLPPMMPPGPPAPNTN</b><br /><b></b><br />GlobDom: <b>[40,161]</b><br /><b>MSEIADLTYNVVAFSEIMSM
IWKRLNDHGKNWRHVYKAMT
LMEYLIKTGSERVSQQCKEN
MYAVQTLKDFQYVDRDGKDQ
GVNVREKAKQLVALLRDEDR
LREERAHALKTKEKLAQTAT
AS</b><br /><b></b><br />DEG_APCC_KENBOX_2<b>[96,100]</b><br /><b>CKENM</b><br /><b><br /><b>BestStruct: d1h0aa_</b><br /><b>AccessScore: 0.382</b><br /><b>SecStrScore: 0.74</b><br /><b>TotalScore: 1.122</b><br /><b>TotalScoreP-value: </b></b><br />LIG_BIR_II_1<b>[1,5]</b><br /><b>MSTSS</b><br /><b><br /><b>BestStruct: d1h0aa_</b><br /><b>AccessScore: 0.524</b><br /><b>SecStrScore: 0.74</b><br /><b>TotalScore: 1.264</b><br /><b>TotalScoreP-value: </b></b><br />MOD_N-GLC_1<b>[15,20]</b><br /><b>HNYSEA</b><br /><b><br /><b>BestStruct: d1h0aa_</b><br /><b>AccessScore: 0.422</b><br /><b>SecStrScore: 1.025</b><br /><b>TotalScore: 1.447</b><br /><b>TotalScoreP-value: </b></b><br />Conscored<b>Pos: 417<br>Residue: S</b><br /><b>S</b><br /><b>Phospho-ELM</b><br /><b>Pos: 357<br>Residue: S</b><br /><b>G</b><br /><b>Phospho-ELM</b><br /><b>Pos: 429<br>Residue: S</b><br /><b>G</b><br /><b>Phospho-ELM</b><br /><b>Pos: 435<br>Residue: T</b><br /><b>S</b><br /><b>Phospho-ELM</b><br /><b>Pos: 437<br>Residue: T</b><br /><b>G</b><br /><b>Phospho-ELM</b><br /><b>Pos: 439<br>Residue: T</b><br /><b>F</b><br /><b>Phospho-ELM</b><br /><b>Pos: 410<br>Residue: S</b><br /><b>L</b><br /><b>Phospho-ELM</b><br /><b>Pos: 469<br>Residue: T</b><br /><b>K</b><br /><b>Phospho-ELM</b><br />ConscoredLIG_eIF4E_1<b>[75,81]</b><br /><b>YKAMTLM</b><br /><b><br /><b>BestStruct: d1h0aa_</b><br /><b>AccessScore: 0.086</b><br /><b>SecStrScore: 0.55</b><br /><b>TotalScore: 0.636</b><br /><b>TotalScoreP-value: </b></b><br />LIG_UBA3_1<b>[56,62]</b><br /><b>IMSMIWK</b><br /><b><br /><b>BestStruct: d1h0aa_</b><br /><b>AccessScore: 0.229</b><br /><b>SecStrScore: 0.55</b><br /><b>TotalScore: 0.779</b><br /><b>TotalScoreP-value: </b></b><br />LIG_UBA3_1<b>[80,86]</b><br /><b>LMEYLIK</b><br /><b><br /><b>BestStruct: d1h0aa_</b><br /><b>AccessScore: 0.099</b><br /><b>SecStrScore: 0.55</b><br /><b>TotalScore: 0.649</b><br /><b>TotalScoreP-value: </b></b><br />LIG_LIR_Nem_3<b>[45,51]</b><br /><b>DLTYNVV</b><br /><b><br /><b>BestStruct: d1h0aa_</b><br /><b>AccessScore: 0.486</b><br /><b>SecStrScore: 0.957</b><br /><b>TotalScore: 1.443</b><br /><b>TotalScoreP-value: </b></b><br />LIG_LIR_Nem_3<b>[47,51]</b><br /><b>TYNVV</b><br /><b><br /><b>BestStruct: d1h0aa_</b><br /><b>AccessScore: 0.478</b><br /><b>SecStrScore: 1.12</b><br /><b>TotalScore: 1.598</b><br /><b>TotalScoreP-value: </b></b><br />LIG_LIR_Nem_3<b>[58,64]</b><br /><b>SMIWKRL</b><br /><b><br /><b>BestStruct: d1h0aa_</b><br /><b>AccessScore: 0.25</b><br /><b>SecStrScore: 0.55</b><br /><b>TotalScore: 0.8</b><br /><b>TotalScoreP-value: </b></b><br />LIG_LIR_Nem_3<b>[108,112]</b><br /><b>DFQYV</b><br /><b><br /><b>BestStruct: d1h0aa_</b><br /><b>AccessScore: 0.478</b><br /><b>SecStrScore: 1.466</b><br /><b>TotalScore: 1.944</b><br /><b>TotalScoreP-value: </b></b><br />ConscoredConscoredConscoredConscoredTRG_ER_diArg_1<b>[6,8]</b><br /><b>LRR</b><br /><b><br /><b>BestStruct: d1h0aa_</b><br /><b>AccessScore: 0.497</b><br /><b>SecStrScore: 0.55</b><br /><b>TotalScore: 1.047</b><br /><b>TotalScoreP-value: </b></b><br />ConscoredConscoredTRG_LysEnd_APsAcLL_1<b>[129,134]</b><br /><b>QLVALL</b><br /><b><br /><b>BestStruct: d1h0aa_</b><br /><b>AccessScore: 0.167</b><br /><b>SecStrScore: 0.55</b><br /><b>TotalScore: 0.717</b><br /><b>TotalScoreP-value: </b></b><br />ConscoredDOC_CYCLIN_1<b>[128,131]</b><br /><b>KQLV</b><br /><b><br /><b>BestStruct: d1h0aa_</b><br /><b>AccessScore: 0.28</b><br /><b>SecStrScore: 0.55</b><br /><b>TotalScore: 0.83</b><br /><b>TotalScoreP-value: </b></b><br />ConscoredConscoredDOC_USP7_UBL2_3<b>[149,153]</b><br /><b>KTKEK</b><br /><b><br /><b>BestStruct: d1h0aa_</b><br /><b>AccessScore: 0.578</b><br /><b>SecStrScore: 0.55</b><br /><b>TotalScore: 1.128</b><br /><b>TotalScoreP-value: </b></b><br /> QiKTqYptdG.png


Homologous sequences were used to calculate a multiple sequence alignment visualizing the conservation of individual short linear motifs.
Click here to enable the multiple sequence alignment viewer Jalview (requires Java browser plugin) (unsigned version)
Alternatively, you can download the alignment, conservation features, and phosphosite features to load into Jalview Desktop.


o Filtering summary

No user supplied cellular location.
User supplied taxon: root

(An ELM is listed as filtered when all its matching instances have been filtered out.)

ElmsInstances
FILTERED BY: Species00
Cellular location (counts only those ELMs not already excluded by species.)00
Structural score (below medium threshold score)1230
Smart (in a domain and no structural filter info available)517
TOTAL FILTERED:1747
RETAINED BY:Smart (outside domain and no structural filter info available)2657
Structural score (at or above medium threshold score)1320
TOTAL RETAINED:3977
TOTALall found
(before filtering)
56124
   
Query sequence:
>EPN1_HUMAN
MSTSSLRRQMKNIVHNYSEAEIKVREATSNDPWGPSSSLMSEIADLTYNVVAFSEIMSMI
WKRLNDHGKNWRHVYKAMTLMEYLIKTGSERVSQQCKENMYAVQTLKDFQYVDRDGKDQG
VNVREKAKQLVALLRDEDRLREERAHALKTKEKLAQTATASSAAVGSGPPPEAEQAWPQS
SGEEELQLQLALAMSKEEADQPPSCGPEDDAQLQLALSLSREEHDKEERIRRGDDLRLQM
AIEESKRETGGKEESSLMDLADVFTAPAPAPTTDPWGGPAPMAAAVPTAAPTSDPWGGPP
VPPAADPWGGPAPTPASGDPWRPAAPAGPSVDPWGGTPAPAAGEGPTPDPWGSSDGGVPV
SGPSASDPWTPAPAFSDPWGGSPAKPSTNGTTAAGGFDTEPDEFSDFDRLRTALPTSGSS
AGELELLAGEVPARSPGAFDMSGVRGSLAEAVGSPPPAATPTPTPPTRKTPESFLGPNAA
LVDLDSLVSRPGPTPPGAKASNPFLPGGGPATGPSVTNPFQPAPPATLTLNQLRLSPVPP
VPGAPPTYISPLGGGPGLPPMMPPGPPAPNTNPFLL


o Globular domains/ TM domains and signal peptide detected by the SMART server

Domain Start End
ENTH 18 144
UIM 183 202
UIM 208 227
UIM 233 252

o The ELMs in the following table are known instances annotated from the literature.

Click on the link at positions to see experimental evidence.

Elm Name Instances
(Matched Sequence)
Positions Logic Elm Description Cell Compartment Pattern
LIG_EH_1
SNPFL
TNPFQ
TNPFL
501-505
517-521
571-575
true positive
true positive
true positive
NPF motif interacting with EH domains, usually during regulation of endocytotic processes cytosol,
plasma membrane
.NPF.
TRG_AP2beta_CARGO_1
DEFSDFDRLR
402-411
true positive
AP-2 beta appendage platform subdomain (top surface) binding motif used in targeting cargo for internalisation. cytosol,
extrinsic to endosome membrane
[DE].{1,2}F[^P][^P][FL][^P][^P][^P]R


o Results of ELM motif search after globular domain filtering, structural filtering and context filtering.

Matches falling inside globular protein domains are excluded from this list unless having an acceptable structural score (if the structural filter (BETA version) is applicable). If the structural filter (BETA version)is applicable it is possible to view these structures with Jmol

Elm Name Instances
(Matched Sequence)
Positions View in Jmol Elm Description Cell Compartment Pattern PHI-Blast Instance Mapping Structural Filter Info Probability
CLV_NRD_NRD_1
TRK
467-469 [A]
-
N-Arg dibasic convertase (NRD/Nardilysin) cleavage site (X-|-R-K or R-|-R-X). extracellular,
Golgi apparatus,
cell surface
(.RK)|(RR[^KR]) - - 7.465e-03
CLV_PCSK_SKI1_1
RTALP
411-415 [A]
-
Subtilisin/kexin isozyme-1 (SKI1) cleavage site ([RK]-X-[hydrophobic]-[LTKF]-|-X). endoplasmic reticulum lumen,
endoplasmic reticulum,
Golgi apparatus,
extracellular
[RK].[AILMFV][LTKF]. - - 6.821e-03
DEG_SCF_FBW7_1
PAATPTPT
457-464 [A]
-
The TPxxS phospho-dependent degron binds the FBW7 F box proteins of the SCF (Skp1_Cullin-Fbox) complex. cytosol,
nucleus
[LIVMP].{0,2}(T)P..([ST]) - - 7.138e-04
DOC_CKS1_1
PWTPAP
368-373 [A]
-
Phospho-dependent motif that mediates docking of CDK substrates and regulators to cyclin-CDK-bound Cks1. cytosol,
nucleus
[MPVLIFWYQ].(T)P.. - - 1.991e-03
DOC_MAPK_gen_1
RDGKDQGVNV
114-123 [A]
114-123
MAPK 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. nucleus,
cytosol
[KR]{0,2}[KR].{0,2}[KR].{2,4}[ILVM].[ILVF] - Output 4.324e-03
LIG_AP2alpha_2
DPW
DPW
DPW
DPW
DPW
DPW
DPW
DPW
DPW
31-33 [A]
274-276 [A]
294-296 [A]
306-308 [A]
319-321 [A]
332-334 [A]
349-351 [A]
367-369 [A]
377-379 [A]
31-33
-
-
-
-
-
-
-
-
DPF/W motif binds alpha and beta subunits of AP2 adaptor complex. clathrin-coated endocytic vesicle,
cytosol
DP[FW] Output
Summary
Output 1.192e-04
LIG_BIR_II_1
MSTSS
1-5 [A]
1-5
These 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. cytosol,
mitochondrion
^M{0,1}[AS]... - Output 3.252e-04
LIG_BRCT_BRCA1_1
ASNPF
500-504 [A]
-
Phosphopeptide motif which directly interacts with the BRCT (carboxy-terminal) domain of the Breast Cancer Gene BRCA1 with low affinity nucleus,
BRCA1-BARD1 complex
.(S)..F - - 1.912e-03
LIG_CaM_IQ_9
LKDFQYVDRDGKDQGV
106-121 [A]
106-121
Helical peptide motif responsible for Ca2+-independent binding of the CaM . The motif is manly characterized by a hydrophobic residue at position 1, a highly conserved Gln at position 2, basic charges at positions 6 and 11, and a variable Gly at position 7 intracellular,
cytosol
[ACLIVTM][^P][^P][ILVMFCT]Q[^P][^P][^P][RK][^P]{4,5}[RKQ][^P][^P] - Output 6.368e-05
LIG_Clathr_ClatBox_1
LVDLD
481-485 [A]
-
Clathrin box motif found on cargo adaptor proteins, it interacts with the beta propeller structure located at the N-terminus of Clathrin heavy chain. cytosol,
Golgi apparatus,
cytoskeleton,
clathrin-coated endocytic vesicle,
Golgi trans-face
L[IVLMF].[IVLMF][DE] Output
Summary
- 3.406e-04
LIG_CSL_BTD_1
PWTP
368-371 [A]
-
The motif mediates the interaction between a Notch-like protein and the transcription factor CSL by placing two amino acids (W and P) into a hydrophobic pocket of the BTD domain of CSL. Transcription factor complex,
chromatin,
nucleus
[AFILMPTVW]W[FHILMPSTVW]P - - 1.278e-04
LIG_EH_1
SNPFL
TNPFQ
TNPFL
501-505
517-521
571-575
-
-
-
NPF motif interacting with EH domains, usually during regulation of endocytotic processes cytosol,
plasma membrane
.NPF. Output
Summary
- 5.860e-05
LIG_FHA_1
MSTSSLR
DLTYNVV
PATLTLN
1-7 [A]
45-51 [A]
525-531 [A]
1-7
45-51
-
Phosphothreonine motif binding a subset of FHA domains that show a preference for a large aliphatic amino acid at the pT+3 position. nucleus ..(T)..[ILV]. - Output 8.662e-03
LIG_FHA_2
EATSNDP
VQTLKDF
FDTEPDE
26-32 [A]
103-109 [A]
397-403 [A]
26-32
103-109
-
Phosphothreonine motif binding a subset of FHA domains that have a preference for an acidic amino acid at the pT+3 position. nucleus,
Replication fork
..(T)..[DE]. - Output 8.286e-03
LIG_LIR_Apic_2
DVFTAP
TDPWGGP
DPWGGP
SDPWGGP
DPWGGP
DPWGGP
ESFLGP
SFLGP
TYISP
262-267 [A]
273-279 [A]
274-279 [A]
293-299 [A]
294-299 [A]
306-311 [A]
472-477 [A]
473-477 [A]
547-551 [A]
-
-
-
-
-
-
-
-
-
Apicomplexa specific variant of the canonical LIR motif that binds to Atg8 protein family members to mediate processes involved in autophagy. cytosol,
cytoplasmic side of late endosome membrane
[EDST].{0,2}[WFY]..P - - 3.371e-03
LIG_LIR_Gen_1
DLTYNVV
TYNVV
DFQYV
SDFDRL
DFDRL
45-51 [A]
47-51 [A]
108-112 [A]
405-410 [A]
406-410 [A]
45-51
47-51
108-112
-
-
Canonical LIR motif that binds to Atg8 protein family members to mediate processes involved in autophagy. cytosol,
cytoplasmic side of late endosome membrane
[EDST].{0,2}[WFY]..[ILV] - Output 5.200e-03
LIG_LIR_Nem_3
DLTYNVV
TYNVV
DFQYV
DEFSDF
EFSDF
SDFDRL
DFDRL
45-51 [A]
47-51 [A]
108-112 [A]
402-407 [A]
403-407 [A]
405-410 [A]
406-410 [A]
45-51
47-51
108-112
-
-
-
-
Nematode-specific variant of the canonical LIR motif that binds to Atg8 protein family members to mediate processes involved in autophagy. cytosol,
cytoplasmic side of late endosome membrane
[EDST].{0,2}[WFY]..[ILVFY] - Output 6.362e-03
LIG_MYND_1
PGLPP
556-560 [A]
-
PxLxP motif is recognized by a subset of MYND domain containing proteins. nucleus P.L.P - - 6.499e-04
LIG_PDZ_Class_2
TNPFLL
571-576 [A]
-
The C-terminal class 2 PDZ-binding motif is classically represented by a pattern such as (VYF)X(VIL)* cytosol,
internal side of plasma membrane
...[VLIFY].[ACVILF]$ - - 7.889e-05
LIG_Pex14_2
FSDPW
375-379 [A]
-
Fxxx[WF] motifs are present in Pex19 and S. cerevisiae Pex5 cytosolic receptors that bind to peroxisomal membrane docking member, Pex14 cytosol,
peroxisome,
glycosome
F...[WF] - - 4.628e-04
LIG_SH2_PTP2
YISP
548-551 [A]
-
SH-PTP2 and phospholipase C-gamma Src Homology 2 (SH2) domains binding motif. cytosol (Y)[IV].[VILP] - - 2.454e-04
LIG_SH2_STAT5
YVDR
YISP
111-114 [A]
548-551 [A]
111-114
-
STAT5 Src Homology 2 (SH2) domain binding motif. cytosol (Y)[VLTFIC].. - Output 3.296e-03
LIG_SH3_1
RPGPTPP
RLSPVPP
490-496 [A]
534-540 [A]
-
-
This is the motif recognized by class I SH3 domains plasma membrane,
focal adhesion,
cytosol
[RKY]..P..P - - 1.237e-03
LIG_SH3_2
PTPPTR
463-468 [A]
-
This is the motif recognized by class II SH3 domains cytosol,
plasma membrane,
focal adhesion
P..P.[KR] - - 1.111e-03
LIG_SUMO_SIM_anti_2
ELELLA
423-428 [A]
-
Motif for the antiparallel beta augmentation mode of non-covalent binding to SUMO protein. PML body,
nucleus,
nuclear body
[DEST]{1,10}.{0,1}[VIL][DESTVILMA][VIL][VILM].[DEST]{0,5} - - 2.349e-03
LIG_SUMO_SIM_par_1
ALVDLDS
480-486 [A]
-
Motif for the parallel beta augmentation mode of non-covalent binding to SUMO protein. PML body,
nucleus,
nuclear body
[DEST]{0,5}.[VILPTM][VIL][DESTVILMA][VIL].{0,1}[DEST]{1,10} - - 4.545e-03
LIG_TRAF6
TEPDEFSDF
399-407 [A]
-
TRAF6 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. cytosol ..P.E..[FYWHDE]. - - 1.715e-03
LIG_TYR_ITIM
LTYNVV
46-51 [A]
46-51
ITIM (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. cytosol [ILV].(Y)..[ILV] - Output 2.992e-04
LIG_WW_1
PPTY
545-548 [A]
-
PPXY is the motif recognized by WW domains of Group I cytosol,
integral plasma membrane protein,
integral membrane protein,
plasma membrane
PP.Y - - 1.257e-04
MOD_CDK_SPxK_1
WGGSPAK
379-385 [A]
-
Canonical version of the CDK phosphorylation site which shows specificity towards a lysine/arginine residue at the [ST]+3 position. nucleus,
cycloplasmic cyclin-dependent protein kinase holoenzyme complex,
cytosol
...([ST])P.[KR] - - 1.929e-03
MOD_CDK_SPxxK_3
PTPTPPTR
461-468 [A]
-
Longer version of the CDK phosphorylation site which shows specificity towards a lysine/arginine residue at position +4 after the phospho-Ser/Thr cycloplasmic cyclin-dependent protein kinase holoenzyme complex,
origin recognition complex,
spindle,
microtubule,
cytosol,
nucleus
...([ST])P..[RK] - - 1.929e-03
MOD_N-GLC_1
HNYSEA
TNGTTA
15-20 [A]
388-393 [A]
15-20
-
Generic motif for N-glycosylation. It was shown 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. extracellular,
Golgi apparatus,
endoplasmic reticulum
.(N)[^P][ST].. - Output 5.018e-03
MOD_NEK2_1
MSTSSL
LAQTAT
FDMSGV
1-6 [A]
154-159 [A]
439-444 [A]
1-6
154-159
-
NEK2 phosphorylation motif with preferred Phe, Leu or Met in the -3 position to compensate for less favorable residues in the +1 and +2 position. centrosome,
Ndc80 complex,
condensed nuclear chromosome outer kinetochore,
cytosol,
nucleus
[FLM][^P][^P]([ST])[^DEP][^DE] - Output 9.798e-03
MOD_PKA_2
VRGSLAE
444-450 [A]
-
Secondary preference for PKA-type AGC kinase phosphorylation. cytosol,
nucleus,
cAMP-dependent protein kinase complex
.R.([ST])[^P].. - - 9.458e-03
MOD_PLK
EESSLMD
253-259 [A]
-
Site phosphorylated by the Polo-like kinase. nucleus,
cytosol
.[DE].([ST])[ILFWMVA].. - - 6.015e-03
TRG_AP2beta_CARGO_1
DEFSDFDRLR
402-411
-
AP-2 beta appendage platform subdomain (top surface) binding motif used in targeting cargo for internalisation. cytosol,
extrinsic to endosome membrane
[DE].{1,2}F[^P][^P][FL][^P][^P][^P]R Output
Summary
- 1.817e-05
TRG_ENDOCYTIC_2
YNVV
48-51 [A]
48-51
Tyrosine-based sorting signal responsible for the interaction with mu subunit of AP (Adaptor Protein) complex plasma membrane,
clathrin-coated endocytic vesicle,
cytosol
Y..[LMVIF] - Output 2.587e-03
TRG_ER_diArg_1
RIRR
IRR
229-232 [A]
230-232 [A]
-
-
The di-Arg ER retention motif is defined by two consecutive arginine residues (RR) or with a single residue insertion (RXR). The motif is completed by an adjacent hydrophobic/arginine residue which may be on either side of the Arg pair. cytosol,
endoplasmic reticulum membrane, integral protein,
ER-Golgi transport vesicle membrane,
endoplasmic reticulum membrane,
Golgi-ER transport vesicle membrane,
rough endoplasmic reticulum,
endoplasmic reticulum cisterna
([LIVMFYWPR]R[^YFWDE]{0,1}R)|(R[^YFWDE]{0,1}R[LIVMFYWPR]) - - 5.369e-03
TRG_LysEnd_APsAcLL_1
DLDSLV
483-488 [A]
-
Sorting 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 cytosol,
Endocytic vesicle
[DERQ]...L[LVI] - - 2.758e-03


o  List of excluded ELMs falling inside SMART/PFAM domains and/or scoring poorly with the structural filter (if applicable).

Matches in this list are only likely to be of interest if they are in accessible surface-exposed loops. Motif matches buried in stably folded cores of globular domains are not plausible candidates.
If the structural filter (BETA version) is applicable it is possible to view these structures with Jmol. For more info consult the PDB structure entry used for structure filtering or the SMART or PFAM entries for useful links to solved 3D structures.

Elm Name Positions View in Jmol Elm Description Cell Compartment Pattern PHI-Blast Instance Mapping Structural Filter Info Probability
CLV_NRD_NRD_1
7-9 [A]
231-233 [A]
7-9
-
N-Arg dibasic convertase (NRD/Nardilysin) cleavage site (X-|-R-K or R-|-R-X). extracellular,
Golgi apparatus,
cell surface
(.RK)|(RR[^KR]) - Output 7.465e-03
CLV_PCSK_FUR_1
229-233 [A]
-
Furin (PACE) cleavage site (R-X-[RK]-R-|-X). extracellular,
Golgi apparatus,
Golgi membrane
R.[RK]R. - - 5.087e-04
CLV_PCSK_KEX2_1
7-9 [A]
62-64 [A]
231-233 [A]
246-248 [A]
7-9
62-64
-
-
Yeast kexin 2 cleavage site (K-R-|-X or R-R-|-X). extracellular,
Golgi apparatus
[KR]R. - Output 7.973e-03
CLV_PCSK_PC1ET2_1
62-64 [A]
246-248 [A]
62-64
-
NEC1/NEC2 cleavage site (K-R-|-X). extracellular,
Golgi apparatus,
Golgi membrane
KR. - Output 3.903e-03
CLV_PCSK_SKI1_1
8-12 [A]
25-29 [A]
76-80 [A]
8-12
25-29
76-80
Subtilisin/kexin isozyme-1 (SKI1) cleavage site ([RK]-X-[hydrophobic]-[LTKF]-|-X). endoplasmic reticulum lumen,
endoplasmic reticulum,
Golgi apparatus,
extracellular
[RK].[AILMFV][LTKF]. - Output 6.821e-03
DEG_APCC_KENBOX_2
96-100 [A]
96-100
Motif conserving the exact sequence KEN that binds to the APC/C subunit Cdh1 causing the protein to be targeted for 26S proteasome mediated degradation. nucleus,
cytosol
.KEN. - Output 1.843e-04
DOC_CYCLIN_1
128-131 [A]
128-131
Substrate recognition site that interacts with cyclin and thereby increases phosphorylation by cyclin/cdk complexes. Predicted proteins should have a CDK phosphorylation site. Also used by cyclin/cdk inhibitors. cytosol,
nucleus
[RK].L.{0,1}[FYLIVMP] - Output 5.324e-03
DOC_MAPK_gen_1
124-133 [A]
126-133 [A]
229-238 [A]
231-238 [A]
124-133
126-133
-
-
MAPK 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. nucleus,
cytosol
[KR]{0,2}[KR].{0,2}[KR].{2,4}[ILVM].[ILVF] - Output 4.324e-03
DOC_MAPK_MEF2A_6
231-240 [A]
232-240 [A]
-
-
A kinase docking motif that mediates interaction towards the ERK1/2 and p38 subfamilies of MAP kinases. cytosol,
Transcription factor complex,
nucleus
[RK].{2,4}[LIVMP].[LIV].[LIVMF] - - 2.584e-03
DOC_USP7_UBL2_3
149-153 [A]
149-153
The USP7 CTD domain binding motif variant based on the ICP0 and DNMT1 interactions nucleus K...K - Output 3.742e-03
LIG_eIF4E_1
75-81 [A]
75-81
Motif binding to the dorsal surface of eIF4E. cytosol Y....L[VILMF] - Output 1.891e-04
LIG_FHA_2
77-83 [A]
85-91 [A]
77-83
85-91
Phosphothreonine motif binding a subset of FHA domains that have a preference for an acidic amino acid at the pT+3 position. nucleus,
Replication fork
..(T)..[DE]. - Output 8.286e-03
LIG_LIR_Gen_1
58-64 [A]
58-64
Canonical LIR motif that binds to Atg8 protein family members to mediate processes involved in autophagy. cytosol,
cytoplasmic side of late endosome membrane
[EDST].{0,2}[WFY]..[ILV] - Output 5.200e-03
LIG_LIR_Nem_3
58-64 [A]
58-64
Nematode-specific variant of the canonical LIR motif that binds to Atg8 protein family members to mediate processes involved in autophagy. cytosol,
cytoplasmic side of late endosome membrane
[EDST].{0,2}[WFY]..[ILVFY] - Output 6.362e-03
LIG_NRBOX
129-135 [A]
129-135
The nuclear receptor box motif (LXXLL) confers binding to nuclear receptors. nucleus [^P]L[^P][^P]LL[^P] - Output 2.628e-04
LIG_Pex14_1
71-75 [A]
71-75
Wxxx[FY] motifs present in N-terminal half of Pex5 bind to Pex13 and Pex14 at peroxisomal and glycosomal membranes to facilitate entrance of PTS1 cargo proteins into the organellar lumen. peroxisome,
cytosol,
glycosome
W...[FY] - Output 2.226e-04
LIG_RGD
232-234 [A]
-
The 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 lo extracellular,
integrin
RGD - - 2.366e-04
LIG_SH2_STAT3
101-104 [A]
101-104
YXXQ motif found in the cytoplasmic region of cytokine receptors that bind STAT3 SH2 domain. cytosol (Y)..Q - Output 7.975e-04
LIG_SH2_STAT5
83-86 [A]
83-86
STAT5 Src Homology 2 (SH2) domain binding motif. cytosol (Y)[VLTFIC].. - Output 3.296e-03
LIG_TRAF2_1
181-184 [A]
195-198 [A]
220-223 [A]
241-244 [A]
-
-
-
-
Major 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. cytosol [PSAT].[QE]E - - 4.300e-03
LIG_UBA3_1
56-62 [A]
80-86 [A]
56-62
80-86
UBA3 adenylation domain binding motif variant based on the UBE2M and UBE2F interactions. nucleus [ILM][ILMF].{1,2}[ILM].{0,4}K - Output 1.196e-03
MOD_NEK2_1
84-89 [A]
215-220 [A]
84-89
-
NEK2 phosphorylation motif with preferred Phe, Leu or Met in the -3 position to compensate for less favorable residues in the +1 and +2 position. centrosome,
Ndc80 complex,
condensed nuclear chromosome outer kinetochore,
cytosol,
nucleus
[FLM][^P][^P]([ST])[^DEP][^DE] - Output 9.798e-03
MOD_NEK2_2
102-107 [A]
102-107
NEK2 phosphorylation motif with specific set of residues in the +1 and +2 position to compensate for less favorable residues in the -3 position. centrosome,
Ndc80 complex,
condensed nuclear chromosome outer kinetochore,
cytosol,
nucleus
[WYPCAG][^P][^P]([ST])[IFCVML][KRHYF] - Output 1.295e-03
MOD_PIKK_1
90-96 [A]
90-96
(ST)Q motif which is phosphorylated by PIKK family members. nucleus ...([ST])Q.. - Output 9.230e-03
MOD_PKA_1
246-252 [A]
-
Main preference for PKA-type AGC kinase phosphorylation. cAMP-dependent protein kinase complex,
cytosol,
nucleus
[RK][RK].([ST])[^P].. - - 2.315e-03
MOD_PKA_2
90-96 [A]
246-252 [A]
90-96
-
Secondary preference for PKA-type AGC kinase phosphorylation. cytosol,
nucleus,
cAMP-dependent protein kinase complex
.R.([ST])[^P].. - Output 9.458e-03
TRG_ENDOCYTIC_2
75-78 [A]
75-78
Tyrosine-based sorting signal responsible for the interaction with mu subunit of AP (Adaptor Protein) complex plasma membrane,
clathrin-coated endocytic vesicle,
cytosol
Y..[LMVIF] - Output 2.587e-03
TRG_ER_diArg_1
6-8 [A]
6-8
The di-Arg ER retention motif is defined by two consecutive arginine residues (RR) or with a single residue insertion (RXR). The motif is completed by an adjacent hydrophobic/arginine residue which may be on either side of the Arg pair. cytosol,
endoplasmic reticulum membrane, integral protein,
ER-Golgi transport vesicle membrane,
endoplasmic reticulum membrane,
Golgi-ER transport vesicle membrane,
rough endoplasmic reticulum,
endoplasmic reticulum cisterna
([LIVMFYWPR]R[^YFWDE]{0,1}R)|(R[^YFWDE]{0,1}R[LIVMFYWPR]) - Output 5.369e-03
TRG_LysEnd_APsAcLL_1
129-134 [A]
129-134
Sorting 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 cytosol,
Endocytic vesicle
[DERQ]...L[LVI] - Output 2.758e-03