eF-site ID 3p5t-ABCDEFLMNOPQ PDB Code 3p5t Chain A, B, C, D, E, F, L, M, N, O, P, Q click to enlarge Title CFIm25-CFIm68 complex Classification RNA BINDING PROTEIN Compound Cleavage and polyadenylation specificity factor subunit 5 Source Homo sapiens (Human) (CPSF6_HUMAN) Sequence A:  ERTINLYPLTNYTFGTKEPLYEKDSSVAARFQRMREEFDK IGMRRTVEGVLIVHEHRLPHVLLLQLGTTFFKLPGGELNP GEDEVEGLKRLMTEILGRQDGVLQDWVIDDCIGNWWRPNF EPPQYPYIPAHITKPKEHKKLFLVQLQEKALFAVPKNYKL VAAPLFELYDNAPGYGPIISSLPQLLSRFNFIYNLE B:  ERTINLYPLTNYTFGTKEPLYEKDSSVAARFQRMREEFDK IGMRRTVEGVLIVHEHRLPHVLLLQLGTTFFKLPGGELNP GEDEVEGLKRLMTEILGRQDGVLQDWVIDDCIGNWWRPNF EPPQYPYIPAHITKPKEHKKLFLVQLQEKALFAVPKNYKL VAAPLFELYDNAPGYGPIISSLPQLLSRFNFIYNLEHH C:  ERTINLYPLTNYTFGTKEPLYEKDSSVAARFQRMREEFDK IGMRRTVEGVLIVHEHRLPHVLLLQLGTTFFKLPGGELNP GEDEVEGLKRLMTEILGRQDGVLQDWVIDDCIGNWWRPNF EPPQYPYIPAHITKPKEHKKLFLVQLQEKALFAVPKNYKL VAAPLFELYDNAPGYGPIISSLPQLLSRFNFIYNLE D:  ERTINLYPLTNYTFGTKEPLYEKDSSVAARFQRMREEFDK IGMRRTVEGVLIVHEHRLPHVLLLQLGTTFFKLPGGELNP GEDEVEGLKRLMTEILGRQDGVLQDWVIDDCIGNWWRPNF EPPQYPYIPAHITKPKEHKKLFLVQLQEKALFAVPKNYKL VAAPLFELYDNAPGYGPIISSLPQLLSRFNFIYNLEHH E:  ERTINLYPLTNYTFGTKEPLYEKDSSVAARFQRMREEFDK IGMRRTVEGVLIVHEHRLPHVLLLQLGTTFFKLPGGELNP GEDEVEGLKRLMTEILGVLQDWVIDDCIGNWWRPNFEPPQ YPYIPAHITKPKEHKKLFLVQLQEKALFAVPKNYKLVAAP LFELYDNAPGYGPIISSLPQLLSRFNFIYNL F:  ERTINLYPLTNYTFGTKEPLYEKDSSVAARFQRMREEFDK IGMRRTVEGVLIVHEHRLPHVLLLQLGTTFFKLPGGELNP GEDEVEGLKRLMTEILGRQDGVLQDWVIDDCIGNWWRPNF EPPQYPYIPAHITKPKEHKKLFLVQLQEKALFAVPKNYKL VAAPLFELYDNAPGYGPIISSLPQLLSRFNFIYNLEH L:  LYIGNLTWWTTDEDLTEAVHSLGVNDILEIKFFENRANGQ SKGFALVGVSEASSKKLMDLLPKRELHGQNPVVTPS M:  IALYIGNLTWWTTDEDLTEAVHSLGVNDILEIKFFENRAN GQSKGFALVGVGSEASSKKLMDLLPKRELHGQNPVVTPSN K N:  RIALYIGNLTWWTTDEDLTEAVHSLGVNDILEIKFFENRA NGQSKGFALVGVGSEASSKKLMDLLPKRELHGQNPVVTPS O:  RIALYIGNLTWWTTDEDLTEAVHSLGVNDILEIKFFENRA NGQSKGFALVGVGSEASSKKLMDLLPKRELHGQNPVVTPS N P:  IALYIGNLTWWTTDEDLTEAVHSLGVNDILEIKFFENRAN GQSKGFALVGVGSEASSKKLMDLLPKRELHGQNPVVTPS Q:  ALYIGNLTWWTTDEDLTEAVHSLGVNDILEIKFFENRANG QSKGFALVGVGSEASSKKLMDLLPKRELHGQNPVVTPSNK Description Functional site 1) chain L residue 157 type MOD_RES sequence T description Phosphothreonine => ECO:0000269|PubMed:30916345 source Swiss-Prot : SWS_FT_FI1 2) chain E residue 63 type MOD_RES sequence R description Phosphothreonine => ECO:0000269|PubMed:30916345 source Swiss-Prot : SWS_FT_FI1 3) chain F residue 55 type MOD_RES sequence E description Phosphothreonine => ECO:0000269|PubMed:30916345 source Swiss-Prot : SWS_FT_FI1 4) chain F residue 63 type MOD_RES sequence R description Phosphothreonine => ECO:0000269|PubMed:30916345 source Swiss-Prot : SWS_FT_FI1 5) chain M residue 157 type MOD_RES sequence T description Phosphothreonine => ECO:0000269|PubMed:30916345 source Swiss-Prot : SWS_FT_FI1 6) chain N residue 157 type MOD_RES sequence T description Phosphothreonine => ECO:0000269|PubMed:30916345 source Swiss-Prot : SWS_FT_FI1 7) chain O residue 157 type MOD_RES sequence T description Phosphothreonine => ECO:0000269|PubMed:30916345 source Swiss-Prot : SWS_FT_FI1 8) chain P residue 157 type MOD_RES sequence T description Phosphothreonine => ECO:0000269|PubMed:30916345 source Swiss-Prot : SWS_FT_FI1 9) chain Q residue 157 type MOD_RES sequence T description Phosphothreonine => ECO:0000269|PubMed:30916345 source Swiss-Prot : SWS_FT_FI1 10) chain D residue 55 type MOD_RES sequence E description Phosphothreonine => ECO:0000269|PubMed:30916345 source Swiss-Prot : SWS_FT_FI1 11) chain D residue 63 type MOD_RES sequence R description Phosphothreonine => ECO:0000269|PubMed:30916345 source Swiss-Prot : SWS_FT_FI1 12) chain E residue 55 type MOD_RES sequence E description Phosphothreonine => ECO:0000269|PubMed:30916345 source Swiss-Prot : SWS_FT_FI1 13) chain A residue 40 type MOD_RES sequence Y description Phosphotyrosine => ECO:0007744|PubMed:15592455 source Swiss-Prot : SWS_FT_FI2 14) chain B residue 40 type MOD_RES sequence Y description Phosphotyrosine => ECO:0007744|PubMed:15592455 source Swiss-Prot : SWS_FT_FI2 15) chain C residue 40 type MOD_RES sequence Y description Phosphotyrosine => ECO:0007744|PubMed:15592455 source Swiss-Prot : SWS_FT_FI2 16) chain D residue 40 type MOD_RES sequence Y description Phosphotyrosine => ECO:0007744|PubMed:15592455 source Swiss-Prot : SWS_FT_FI2 17) chain E residue 40 type MOD_RES sequence Y description Phosphotyrosine => ECO:0007744|PubMed:15592455 source Swiss-Prot : SWS_FT_FI2 18) chain F residue 40 type MOD_RES sequence Y description Phosphotyrosine => ECO:0007744|PubMed:15592455 source Swiss-Prot : SWS_FT_FI2 19) chain A residue 56 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI3 20) chain B residue 56 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI3 21) chain C residue 56 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI3 22) chain D residue 56 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI3 23) chain E residue 56 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI3 24) chain F residue 56 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI3

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