eF-site ID 5cpi-ABCDEFGHIJ PDB Code 5cpi Chain A, B, C, D, E, F, G, H, I, J click to enlarge Title Nucleosome containing unmethylated Sat2R DNA Classification STRUCTURAL PROTEIN/DNA Compound Histone H3.1 Source (5CPI) Sequence A:  PHRYRPGTVALREIRRYQKSTELLIRKLPFQRLVREIAQD FKTDLRFQSSAVMALQEACEAYLVGLFEDTNLCAIHAKRV TIMPKDIQLARRIRGER B:  NIQGITKPAIRRLARRGGVKRISGLIYEETRGVLKVFLEN VIRDAVTYTEHAKRKTVTAMDVVYALKRQGRTLYGFGG C:  RAKAKTRSSRAGLQFPVGRVHRLLRKGNYSERVGAGAPVY LAAVLEYLTAEILELAGNAARDNKKTRIIPRHLQLAIRND EELNKLLGRVTIAQGGVLPNIQAVLLPK D:  SRKESYSIYVYKVLKQVHPDTGISSKAMGIMNSFVNDIFE RIAGEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHAV SEGTKAVTKYTSA E:  PHRYRPGTVALREIRRYQKSTELLIRKLPFQRLVREIAQD FKTDLRFQSSAVMALQEACEAYLVGLFEDTNLCAIHAKRV TIMPKDIQLARRIRGERA F:  RKVLRDNIQGITKPAIRRLARRGGVKRISGLIYEETRGVL KVFLENVIRDAVTYTEHAKRKTVTAMDVVYALKRQGRTLY GFG G:  KTRSSRAGLQFPVGRVHRLLRKGNYSERVGAGAPVYLAAV LEYLTAEILELAGNAARDNKKTRIIPRHLQLAIRNDEELN KLLGRVTIAQGGVLPNIQAVLLPK H:  RKESYSIYVYKVLKQVHPDTGISSKAMGIMNSFVNDIFER IAGEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHAVS EGTKAVTKYTS I:  ATCCAAATGGATTCGAATGGAATCATTGAATGGAAATGAA TGGAATCATTGGTTGGACTCAAATGGAATTTTCGAACAGG CTCAAATGGAATCTTCGAATGGATTCGAATGTAATCATTT TCGAATGGATTCGAATGGAATCTGAT J:  ATCAGATTCCATTCGAATCCATTCGAAAATGATTACATTC GAATCCATTCGAAGATTCCATTTGAGCCTGTTCGAAAATT CCATTTGAGTCCAACCAATGATTCCATTCATTTCCATTCA ATGATTCCATTCGAATCCATTTGGAT Description Functional site 1) chain D residue 92-114 type prosite sequence REIQTAVRLLLPGELAKHAVSEG description HISTONE_H2B Histone H2B signature. REIQTavRlLLpGELaKHAVSEG source prosite : PS00357 2) chain A residue 79 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000269|PubMed:22389435, ECO:0000269|PubMed:29211711 source Swiss-Prot : SWS_FT_FI21 3) chain E residue 79 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000269|PubMed:22389435, ECO:0000269|PubMed:29211711 source Swiss-Prot : SWS_FT_FI21 4) chain A residue 80 type MOD_RES sequence T description Phosphothreonine => ECO:0000269|PubMed:20850016 source Swiss-Prot : SWS_FT_FI22 5) chain E residue 80 type MOD_RES sequence T description Phosphothreonine => ECO:0000269|PubMed:20850016 source Swiss-Prot : SWS_FT_FI22 6) chain A residue 86 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P84243 source Swiss-Prot : SWS_FT_FI23 7) chain E residue 86 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P84243 source Swiss-Prot : SWS_FT_FI23 8) chain A residue 107 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI24 9) chain E residue 107 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI24 10) chain A residue 115 type MOD_RES sequence K description N6-glutaryllysine; alternate => ECO:0000269|PubMed:31542297 source Swiss-Prot : SWS_FT_FI25 11) chain E residue 115 type MOD_RES sequence K description N6-glutaryllysine; alternate => ECO:0000269|PubMed:31542297 source Swiss-Prot : SWS_FT_FI25 12) chain A residue 122 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000269|PubMed:22389435, ECO:0000269|PubMed:27436229 source Swiss-Prot : SWS_FT_FI26 13) chain E residue 122 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000269|PubMed:22389435, ECO:0000269|PubMed:27436229 source Swiss-Prot : SWS_FT_FI26 14) chain D residue 112 type CARBOHYD sequence S description O-linked (GlcNAc) serine => ECO:0000250|UniProtKB:P62807 source Swiss-Prot : SWS_FT_FI16 15) chain B residue 79 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250|UniProtKB:P62807 source Swiss-Prot : SWS_FT_FI16 16) chain F residue 20 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250|UniProtKB:P62807 source Swiss-Prot : SWS_FT_FI16 17) chain F residue 59 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250|UniProtKB:P62807 source Swiss-Prot : SWS_FT_FI16 18) chain F residue 79 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250|UniProtKB:P62807 source Swiss-Prot : SWS_FT_FI16 19) chain H residue 112 type CARBOHYD sequence S description O-linked (GlcNAc) serine => ECO:0000250|UniProtKB:P62807 source Swiss-Prot : SWS_FT_FI16 20) 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 source Swiss-Prot : SWS_FT_FI18 21) 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 source Swiss-Prot : SWS_FT_FI18 22) 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 23) chain H 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 24) chain H residue 43 type MOD_RES sequence K description N6-lactoyllysine; alternate => ECO:0000269|PubMed:31645732 source Swiss-Prot : SWS_FT_FI3 25) chain H residue 85 type MOD_RES sequence K description N6-lactoyllysine; alternate => ECO:0000269|PubMed:31645732 source Swiss-Prot : SWS_FT_FI3 26) chain D residue 43 type MOD_RES sequence K description N6-lactoyllysine; alternate => ECO:0000269|PubMed:31645732 source Swiss-Prot : SWS_FT_FI3 27) chain D residue 85 type MOD_RES sequence K description N6-lactoyllysine; alternate => ECO:0000269|PubMed:31645732 source Swiss-Prot : SWS_FT_FI3 28) chain G residue 95 type MOD_RES sequence K description ADP-ribosylserine => ECO:0000269|PubMed:34874266 source Swiss-Prot : SWS_FT_FI4 29) chain B residue 44 type MOD_RES sequence K description N6-crotonyllysine; alternate => ECO:0000269|PubMed:21925322 source Swiss-Prot : SWS_FT_FI5 30) chain F residue 44 type MOD_RES sequence K description N6-crotonyllysine; alternate => ECO:0000269|PubMed:21925322 source Swiss-Prot : SWS_FT_FI5 31) chain B residue 77 type MOD_RES sequence K description Phosphoserine; by STK4/MST1 => ECO:0000269|PubMed:12757711 source Swiss-Prot : SWS_FT_FI6 32) chain B residue 91 type MOD_RES sequence K description Phosphoserine; by STK4/MST1 => ECO:0000269|PubMed:12757711 source Swiss-Prot : SWS_FT_FI6 33) chain F residue 31 type MOD_RES sequence K description Phosphoserine; by STK4/MST1 => ECO:0000269|PubMed:12757711 source Swiss-Prot : SWS_FT_FI6 34) chain F residue 77 type MOD_RES sequence K description Phosphoserine; by STK4/MST1 => ECO:0000269|PubMed:12757711 source Swiss-Prot : SWS_FT_FI6 35) chain F residue 91 type MOD_RES sequence K description Phosphoserine; by STK4/MST1 => ECO:0000269|PubMed:12757711 source Swiss-Prot : SWS_FT_FI6 36) chain G residue 74 type MOD_RES sequence K description N6-(2-hydroxyisobutyryl)lysine => ECO:0000269|PubMed:24681537 source Swiss-Prot : SWS_FT_FI7 37) chain G residue 75 type MOD_RES sequence K description N6-(2-hydroxyisobutyryl)lysine => ECO:0000269|PubMed:24681537 source Swiss-Prot : SWS_FT_FI7 38) chain H residue 116 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000269|PubMed:22389435 source Swiss-Prot : SWS_FT_FI8 39) chain H residue 120 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000269|PubMed:22389435 source Swiss-Prot : SWS_FT_FI8 40) chain D residue 116 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000269|PubMed:22389435 source Swiss-Prot : SWS_FT_FI8 41) chain D residue 120 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000269|PubMed:22389435 source Swiss-Prot : SWS_FT_FI8 42) chain H residue 34 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000269|PubMed:22389435 source Swiss-Prot : SWS_FT_FI8 43) chain D residue 34 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000269|PubMed:22389435 source Swiss-Prot : SWS_FT_FI8 44) chain H residue 35 type MOD_RES sequence E description PolyADP-ribosyl glutamic acid => ECO:0000250|UniProtKB:Q64475 source Swiss-Prot : SWS_FT_FI9 45) chain D residue 35 type MOD_RES sequence E description PolyADP-ribosyl glutamic acid => ECO:0000250|UniProtKB:Q64475 source Swiss-Prot : SWS_FT_FI9 46) chain G residue 118 type MOD_RES sequence K description PolyADP-ribosyl glutamic acid => ECO:0000250|UniProtKB:Q64475 source Swiss-Prot : SWS_FT_FI9 47) chain E residue 56 type MOD_RES sequence K description Phosphoserine; by AMPK => ECO:0000250|UniProtKB:Q64475 source Swiss-Prot : SWS_FT_FI10 48) chain D residue 36 type MOD_RES sequence S description Phosphoserine; by AMPK => ECO:0000250|UniProtKB:Q64475 source Swiss-Prot : SWS_FT_FI10 49) chain H residue 36 type MOD_RES sequence S description Phosphoserine; by AMPK => ECO:0000250|UniProtKB:Q64475 source Swiss-Prot : SWS_FT_FI10 50) chain H residue 46 type MOD_RES sequence K description N6-methyllysine; alternate => ECO:0000269|PubMed:16627869 source Swiss-Prot : SWS_FT_FI11 51) chain H residue 108 type MOD_RES sequence K description N6-methyllysine; alternate => ECO:0000269|PubMed:16627869 source Swiss-Prot : SWS_FT_FI11 52) chain D residue 46 type MOD_RES sequence K description N6-methyllysine; alternate => ECO:0000269|PubMed:16627869 source Swiss-Prot : SWS_FT_FI11 53) chain D residue 108 type MOD_RES sequence K description N6-methyllysine; alternate => ECO:0000269|PubMed:16627869 source Swiss-Prot : SWS_FT_FI11 54) 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 55) 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 56) chain D residue 79 type MOD_RES sequence R description Dimethylated arginine => ECO:0000250|UniProtKB:Q96A08 source Swiss-Prot : SWS_FT_FI13 57) chain H residue 79 type MOD_RES sequence R description Dimethylated arginine => ECO:0000250|UniProtKB:Q96A08 source Swiss-Prot : SWS_FT_FI13 58) chain H residue 86 type MOD_RES sequence R description Omega-N-methylarginine => ECO:0000250|UniProtKB:Q96A08 source Swiss-Prot : SWS_FT_FI14 59) chain H residue 92 type MOD_RES sequence R description Omega-N-methylarginine => ECO:0000250|UniProtKB:Q96A08 source Swiss-Prot : SWS_FT_FI14 60) chain D residue 86 type MOD_RES sequence R description Omega-N-methylarginine => ECO:0000250|UniProtKB:Q96A08 source Swiss-Prot : SWS_FT_FI14 61) chain D residue 92 type MOD_RES sequence R description Omega-N-methylarginine => ECO:0000250|UniProtKB:Q96A08 source Swiss-Prot : SWS_FT_FI14 62) chain F residue 91 type MOD_RES sequence K description Phosphothreonine => ECO:0000250|UniProtKB:Q00729 source Swiss-Prot : SWS_FT_FI15 63) chain D residue 115 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:Q00729 source Swiss-Prot : SWS_FT_FI15 64) chain H residue 115 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:Q00729 source Swiss-Prot : SWS_FT_FI15 65) chain A residue 66-74 type prosite sequence PFQRLVREI description HISTONE_H3_2 Histone H3 signature 2. PFqRLVREI source prosite : PS00959 66) chain C residue 21-27 type prosite sequence AGLQFPV description HISTONE_H2A Histone H2A signature. AGLqFPV source prosite : PS00046

Display surface Download Links