eF-site ID 6se6-ABCDEFGHV PDB Code 6se6 Chain A, B, C, D, E, F, G, H, V click to enlarge Title Class2 : CENP-A nucleosome in complex with CENP-C central region Classification NUCLEAR PROTEIN Compound Histone H3-like centromeric protein A Source (CENPC_HUMAN) Sequence A:  RRRQGWLKEIRKLQKSTHLLIRKLPFSRLAREICVKFTRG VDFNWQAQALLALQEAAEAFLVHLFEDAYLLTLHAGRVTL FPKDVQLARRIRGLEEGL B:  VLRDNIQGITKPAIRRLARRGGVKRISGLIYEETRGVLKV FLENVIRDAVTYTEHAKRKTVTAMDVVYALKRQGRTLYGF GG C:  SRSSRAGLQFPVGRVHRLLRKGNYAERVGAGAPVYMAAVL EYLTAEILELAGNAARDNKKTRIIPRHLQLAIRNDEELNK LLGKVTIAQGGVLPNIQAVLL D:  RKESYSVYVYKVLKQVHPDTGISSKAMGIMNSFVNDIFER IAGEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHAVS EGTKAVTKYTSS E:  RRRQGWLKEIRKLQKSTHLLIRKLPFSRLAREICVKFTRG VDFNWQAQALLALQEAAEAFLVHLFEDAYLLTLHAGRVTL FPKDVQLARRIRGLEEGL F:  RKVLRDNIQGITKPAIRRLARRGGVKRISGLIYEETRGVL KVFLENVIRDAVTYTEHAKRKTVTAMDVVYALKRQGRTLY GFGG G:  ARAKAKSRSSRAGLQFPVGRVHRLLRKGNYAERVGAGAPV YMAAVLEYLTAEILELAGNAARDNKKTRIIPRHLQLAIRN DEELNKLLGKVTIAQGGVLPNIQAVLLP H:  ESYSVYVYKVLKQVHPDTGISSKAMGIMNSFVNDIFERIA GEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHAVSEG TKAVTKYTSS V:  KSRRISRRPSDWWVVKSE Description (1)  Histone H3-like centromeric protein A, Histone H4, Histone H2A type 2-A, Histone H2B type 1-C/E/F/G/I, Centromere protein C/DNA Complex Functional site 1) chain D residue 120 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000269|PubMed:16307923, ECO:0000269|PubMed:16627869, ECO:0000269|PubMed:16713563, ECO:0000269|PubMed:22121020 source Swiss-Prot : SWS_FT_FI18 2) chain H residue 120 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000269|PubMed:16307923, ECO:0000269|PubMed:16627869, ECO:0000269|PubMed:16713563, ECO:0000269|PubMed:22121020 source Swiss-Prot : SWS_FT_FI18 3) chain D residue 34 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000269|PubMed:21726816 source Swiss-Prot : SWS_FT_FI20 4) chain D residue 112 type CARBOHYD sequence S description O-linked (GlcNAc) serine => ECO:0000269|PubMed:22121020 source Swiss-Prot : SWS_FT_FI16 5) chain H residue 112 type CARBOHYD sequence S description O-linked (GlcNAc) serine => ECO:0000269|PubMed:22121020 source Swiss-Prot : SWS_FT_FI16 6) chain B residue 79 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000269|PubMed:22121020 source Swiss-Prot : SWS_FT_FI16 7) chain F residue 20 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000269|PubMed:22121020 source Swiss-Prot : SWS_FT_FI16 8) chain F residue 59 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000269|PubMed:22121020 source Swiss-Prot : SWS_FT_FI16 9) chain F residue 79 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000269|PubMed:22121020 source Swiss-Prot : SWS_FT_FI16 10) chain D residue 92-114 type prosite sequence REIQTAVRLLLPGELAKHAVSEG description HISTONE_H2B Histone H2B signature. REIQTavRlLLpGELaKHAVSEG source prosite : PS00357 11) chain C residue 21-27 type prosite sequence AGLQFPV description HISTONE_H2A Histone H2A signature. AGLqFPV source prosite : PS00046 12) chain A residue 66-74 type prosite sequence PFSRLAREI description HISTONE_H3_2 Histone H3 signature 2. PFsRLAREI source prosite : PS00959 13) chain V residue 528 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI2 14) chain H residue 43 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733 source Swiss-Prot : SWS_FT_FI3 15) chain H residue 85 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733 source Swiss-Prot : SWS_FT_FI3 16) chain D residue 43 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733 source Swiss-Prot : SWS_FT_FI3 17) chain D residue 85 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733 source Swiss-Prot : SWS_FT_FI3 18) chain V residue 534 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733 source Swiss-Prot : SWS_FT_FI3 19) chain G residue 95 type MOD_RES sequence K description ADP-ribosylserine => ECO:0000269|PubMed:34874266 source Swiss-Prot : SWS_FT_FI4 20) chain B residue 44 type MOD_RES sequence K description N6-crotonyllysine; alternate => ECO:0000269|PubMed:21925322 source Swiss-Prot : SWS_FT_FI5 21) chain F residue 44 type MOD_RES sequence K description N6-crotonyllysine; alternate => ECO:0000269|PubMed:21925322 source Swiss-Prot : SWS_FT_FI5 22) chain B residue 77 type MOD_RES sequence K description Phosphoserine; by STK4/MST1 => ECO:0000269|PubMed:12757711 source Swiss-Prot : SWS_FT_FI6 23) chain B residue 91 type MOD_RES sequence K description Phosphoserine; by STK4/MST1 => ECO:0000269|PubMed:12757711 source Swiss-Prot : SWS_FT_FI6 24) chain F residue 31 type MOD_RES sequence K description Phosphoserine; by STK4/MST1 => ECO:0000269|PubMed:12757711 source Swiss-Prot : SWS_FT_FI6 25) chain F residue 77 type MOD_RES sequence K description Phosphoserine; by STK4/MST1 => ECO:0000269|PubMed:12757711 source Swiss-Prot : SWS_FT_FI6 26) chain F residue 91 type MOD_RES sequence K description Phosphoserine; by STK4/MST1 => ECO:0000269|PubMed:12757711 source Swiss-Prot : SWS_FT_FI6 27) chain G residue 74 type MOD_RES sequence K description N6-(2-hydroxyisobutyryl)lysine => ECO:0000269|PubMed:24681537 source Swiss-Prot : SWS_FT_FI7 28) chain G residue 75 type MOD_RES sequence K description N6-(2-hydroxyisobutyryl)lysine => ECO:0000269|PubMed:24681537 source Swiss-Prot : SWS_FT_FI7 29) chain H residue 116 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000269|PubMed:22389435 source Swiss-Prot : SWS_FT_FI8 30) chain H residue 120 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000269|PubMed:22389435 source Swiss-Prot : SWS_FT_FI8 31) chain D residue 34 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000269|PubMed:22389435 source Swiss-Prot : SWS_FT_FI8 32) chain D residue 116 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000269|PubMed:22389435 source Swiss-Prot : SWS_FT_FI8 33) chain D residue 120 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000269|PubMed:22389435 source Swiss-Prot : SWS_FT_FI8 34) chain D residue 35 type MOD_RES sequence E description PolyADP-ribosyl glutamic acid => ECO:0000250|UniProtKB:Q64475 source Swiss-Prot : SWS_FT_FI9 35) chain H residue 35 type MOD_RES sequence E description PolyADP-ribosyl glutamic acid => ECO:0000250|UniProtKB:Q64475 source Swiss-Prot : SWS_FT_FI9 36) chain D residue 36 type MOD_RES sequence S description Phosphoserine; by AMPK => ECO:0000250|UniProtKB:Q6ZWY9 source Swiss-Prot : SWS_FT_FI10 37) chain H residue 36 type MOD_RES sequence S description Phosphoserine; by AMPK => ECO:0000250|UniProtKB:Q6ZWY9 source Swiss-Prot : SWS_FT_FI10 38) chain D residue 46 type MOD_RES sequence K description N6-methyllysine; alternate => ECO:0000269|PubMed:16627869 source Swiss-Prot : SWS_FT_FI11 39) chain D residue 108 type MOD_RES sequence K description N6-methyllysine; alternate => ECO:0000269|PubMed:16627869 source Swiss-Prot : SWS_FT_FI11 40) chain H residue 46 type MOD_RES sequence K description N6-methyllysine; alternate => ECO:0000269|PubMed:16627869 source Swiss-Prot : SWS_FT_FI11 41) chain H residue 108 type MOD_RES sequence K description N6-methyllysine; alternate => ECO:0000269|PubMed:16627869 source Swiss-Prot : SWS_FT_FI11 42) chain D residue 57 type MOD_RES sequence K description N6-(2-hydroxyisobutyryl)lysine; alternate => ECO:0000269|PubMed:24681537 source Swiss-Prot : SWS_FT_FI12 43) chain H residue 57 type MOD_RES sequence K description N6-(2-hydroxyisobutyryl)lysine; alternate => ECO:0000269|PubMed:24681537 source Swiss-Prot : SWS_FT_FI12 44) chain D residue 79 type MOD_RES sequence R description Dimethylated arginine => ECO:0000250|UniProtKB:Q96A08 source Swiss-Prot : SWS_FT_FI13 45) chain H residue 79 type MOD_RES sequence R description Dimethylated arginine => ECO:0000250|UniProtKB:Q96A08 source Swiss-Prot : SWS_FT_FI13 46) chain H residue 86 type MOD_RES sequence R description Omega-N-methylarginine => ECO:0000250|UniProtKB:Q96A08 source Swiss-Prot : SWS_FT_FI14 47) chain H residue 92 type MOD_RES sequence R description Omega-N-methylarginine => ECO:0000250|UniProtKB:Q96A08 source Swiss-Prot : SWS_FT_FI14 48) chain D residue 86 type MOD_RES sequence R description Omega-N-methylarginine => ECO:0000250|UniProtKB:Q96A08 source Swiss-Prot : SWS_FT_FI14 49) chain D residue 92 type MOD_RES sequence R description Omega-N-methylarginine => ECO:0000250|UniProtKB:Q96A08 source Swiss-Prot : SWS_FT_FI14 50) chain D residue 115 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:Q00729 source Swiss-Prot : SWS_FT_FI15 51) chain H residue 115 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:Q00729 source Swiss-Prot : SWS_FT_FI15 52) chain F residue 91 type MOD_RES sequence K description Phosphothreonine => ECO:0000250|UniProtKB:Q00729 source Swiss-Prot : SWS_FT_FI15

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