eF-site ID 3wkj-ABCDEFGH PDB Code 3wkj Chain A, B, C, D, E, F, G, H click to enlarge Title The nucleosome containing human TSH2B Classification STRUCTURAL PROTEIN/DNA Compound Histone H3.1 Source (3WKJ) Sequence A:  PHRYRPGTVALREIRRYQKSTELLIRKLPFQRLVREIAQD FKTDLRFQSSAVMALQEACEAYLVGLFEDTNLCAIHAKRV TIMPKDIQLARRIRGER B:  NIQGITKPAIRRLARRGGVKRISGLIYEETRGVLKVFLEN VIRDAVTYTEHAKRKTVTAMDVVYALKRQGRTLYGFGG C:  AKAKTRSSRAGLQFPVGRVHRLLRKGNYSERVGAGAPVYL AAVLEYLTAEILELAGNAARDNKKTRIIPRHLQLAIRNDE ELNKLLGRVTIAQGGVLPNIQAVLLPK D:  TRKESYSIYIYKVLKQVHPDTGISSKAMSIMNSFVTDIFE RIASEASRLAHYSKRSTISSREIQTAVRLLLPGELAKHAV SEGTKAVTKYTSS E:  PHRYRPGTVALREIRRYQKSTELLIRKLPFQRLVREIAQD FKTDLRFQSSAVMALQEACEAYLVGLFEDTNLCAIHAKRV TIMPKDIQLARRIRGERA F:  RKVLRDNIQGITKPAIRRLARRGGVKRISGLIYEETRGVL KVFLENVIRDAVTYTEHAKRKTVTAMDVVYALKRQGRTLY GFGG G:  KTRSSRAGLQFPVGRVHRLLRKGNYSERVGAGAPVYLAAV LEYLTAEILELAGNAARDNKKTRIIPRHLQLAIRNDEELN KLLGRVTIAQGGVLPNIQAVLLPK H:  RKESYSIYIYKVLKQVHPDTGISSKAMSIMNSFVTDIFER IASEASRLAHYSKRSTISSREIQTAVRLLLPGELAKHAVS EGTKAVTKYTSS Description Functional site 1) chain A residue 121 type sequence P description BINDING SITE FOR RESIDUE CL A 201 source : AC1 2) chain A residue 122 type sequence K description BINDING SITE FOR RESIDUE CL A 201 source : AC1 3) chain C residue 46 type sequence G description BINDING SITE FOR RESIDUE CL C 201 source : AC2 4) chain C residue 47 type sequence A description BINDING SITE FOR RESIDUE CL C 201 source : AC2 5) chain D residue 91 type sequence S description BINDING SITE FOR RESIDUE CL C 201 source : AC2 6) chain D residue 92 type sequence S description BINDING SITE FOR RESIDUE CL C 201 source : AC2 7) chain E residue 121 type sequence P description BINDING SITE FOR RESIDUE CL E 201 source : AC3 8) chain E residue 122 type sequence K description BINDING SITE FOR RESIDUE CL E 201 source : AC3 9) chain G residue 44 type sequence G description BINDING SITE FOR RESIDUE CL G 201 source : AC4 10) chain G residue 45 type sequence A description BINDING SITE FOR RESIDUE CL G 201 source : AC4 11) chain G residue 46 type sequence G description BINDING SITE FOR RESIDUE CL G 201 source : AC4 12) chain H residue 91 type sequence S description BINDING SITE FOR RESIDUE CL G 201 source : AC4 13) chain H residue 92 type sequence S description BINDING SITE FOR RESIDUE CL G 201 source : AC4 14) chain D residue 35 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000250|UniProtKB:P33778 source Swiss-Prot : SWS_FT_FI15 15) chain H residue 35 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000250|UniProtKB:P33778 source Swiss-Prot : SWS_FT_FI15 16) chain F residue 91 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000250|UniProtKB:P33778 source Swiss-Prot : SWS_FT_FI15 17) chain B residue 59 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0007744|PubMed:28112733 source Swiss-Prot : SWS_FT_FI16 18) chain B residue 79 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0007744|PubMed:28112733 source Swiss-Prot : SWS_FT_FI16 19) chain F residue 20 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0007744|PubMed:28112733 source Swiss-Prot : SWS_FT_FI16 20) chain F residue 59 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0007744|PubMed:28112733 source Swiss-Prot : SWS_FT_FI16 21) chain F residue 79 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0007744|PubMed:28112733 source Swiss-Prot : SWS_FT_FI16 22) chain C residue 15 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000269|PubMed:16307923, ECO:0000269|PubMed:16713563 source Swiss-Prot : SWS_FT_FI13 23) chain D residue 121 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000269|PubMed:16307923, ECO:0000269|PubMed:16713563 source Swiss-Prot : SWS_FT_FI13 24) chain H residue 121 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000269|PubMed:16307923, ECO:0000269|PubMed:16713563 source Swiss-Prot : SWS_FT_FI13 25) chain B residue 31 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in UFM1); alternate => ECO:0000269|PubMed:30886146 source Swiss-Prot : SWS_FT_FI17 26) chain F residue 31 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in UFM1); alternate => ECO:0000269|PubMed:30886146 source Swiss-Prot : SWS_FT_FI17 27) chain A residue 41 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000269|PubMed:19783980 source Swiss-Prot : SWS_FT_FI19 28) chain E residue 41 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000269|PubMed:19783980 source Swiss-Prot : SWS_FT_FI19 29) chain A residue 57 type MOD_RES sequence S description Phosphoserine => ECO:0000269|PubMed:20850016 source Swiss-Prot : SWS_FT_FI20 30) chain E residue 57 type MOD_RES sequence S description Phosphoserine => ECO:0000269|PubMed:20850016 source Swiss-Prot : SWS_FT_FI20 31) 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 32) 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 33) chain A residue 80 type MOD_RES sequence T description Phosphothreonine => ECO:0000269|PubMed:20850016 source Swiss-Prot : SWS_FT_FI22 34) chain E residue 80 type MOD_RES sequence T description Phosphothreonine => ECO:0000269|PubMed:20850016 source Swiss-Prot : SWS_FT_FI22 35) chain A residue 86 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P84243 source Swiss-Prot : SWS_FT_FI23 36) chain E residue 86 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P84243 source Swiss-Prot : SWS_FT_FI23 37) chain A residue 107 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI24 38) chain E residue 107 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI24 39) chain A residue 115 type MOD_RES sequence K description N6-glutaryllysine; alternate => ECO:0000269|PubMed:31542297 source Swiss-Prot : SWS_FT_FI25 40) chain E residue 115 type MOD_RES sequence K description N6-glutaryllysine; alternate => ECO:0000269|PubMed:31542297 source Swiss-Prot : SWS_FT_FI25 41) 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 42) 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 43) chain D residue 80 type MOD_RES sequence R description Dimethylated arginine => ECO:0000269|PubMed:21249133 source Swiss-Prot : SWS_FT_FI8 44) chain H residue 80 type MOD_RES sequence R description Dimethylated arginine => ECO:0000269|PubMed:21249133 source Swiss-Prot : SWS_FT_FI8 45) chain D residue 85 type MOD_RES sequence S description Phosphoserine => ECO:0000269|PubMed:21249133 source Swiss-Prot : SWS_FT_FI9 46) chain H residue 85 type MOD_RES sequence S description Phosphoserine => ECO:0000269|PubMed:21249133 source Swiss-Prot : SWS_FT_FI9 47) chain G residue 118 type MOD_RES sequence K description Phosphoserine => ECO:0000269|PubMed:21249133 source Swiss-Prot : SWS_FT_FI9 48) chain A residue 66-74 type prosite sequence PFQRLVREI description HISTONE_H3_2 Histone H3 signature 2. PFqRLVREI source prosite : PS00959 49) chain D residue 93-115 type prosite sequence REIQTAVRLLLPGELAKHAVSEG description HISTONE_H2B Histone H2B signature. REIQTavRlLLpGELaKHAVSEG source prosite : PS00357 50) chain C residue 21-27 type prosite sequence AGLQFPV description HISTONE_H2A Histone H2A signature. AGLqFPV source prosite : PS00046 51) chain D residue 87 type MOD_RES sequence R description Omega-N-methylarginine => ECO:0000269|PubMed:21249133 source Swiss-Prot : SWS_FT_FI10 52) chain D residue 93 type MOD_RES sequence R description Omega-N-methylarginine => ECO:0000269|PubMed:21249133 source Swiss-Prot : SWS_FT_FI10 53) chain H residue 87 type MOD_RES sequence R description Omega-N-methylarginine => ECO:0000269|PubMed:21249133 source Swiss-Prot : SWS_FT_FI10 54) chain H residue 93 type MOD_RES sequence R description Omega-N-methylarginine => ECO:0000269|PubMed:21249133 source Swiss-Prot : SWS_FT_FI10 55) chain D residue 116 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:Q00729 source Swiss-Prot : SWS_FT_FI11 56) chain H residue 116 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:Q00729 source Swiss-Prot : SWS_FT_FI11 57) chain H residue 44 type MOD_RES sequence K description N6-lactoyllysine; alternate => ECO:0000269|PubMed:31645732 source Swiss-Prot : SWS_FT_FI2 58) chain H residue 86 type MOD_RES sequence K description N6-lactoyllysine; alternate => ECO:0000269|PubMed:31645732 source Swiss-Prot : SWS_FT_FI2 59) chain D residue 44 type MOD_RES sequence K description N6-lactoyllysine; alternate => ECO:0000269|PubMed:31645732 source Swiss-Prot : SWS_FT_FI2 60) chain D residue 86 type MOD_RES sequence K description N6-lactoyllysine; alternate => ECO:0000269|PubMed:31645732 source Swiss-Prot : SWS_FT_FI2 61) chain D residue 35 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P33778 source Swiss-Prot : SWS_FT_FI4 62) chain D residue 117 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P33778 source Swiss-Prot : SWS_FT_FI4 63) chain D residue 121 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P33778 source Swiss-Prot : SWS_FT_FI4 64) chain H residue 35 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P33778 source Swiss-Prot : SWS_FT_FI4 65) chain H residue 117 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P33778 source Swiss-Prot : SWS_FT_FI4 66) chain H residue 121 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P33778 source Swiss-Prot : SWS_FT_FI4 67) chain D residue 37 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:Q64475 source Swiss-Prot : SWS_FT_FI5 68) chain H residue 37 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:Q64475 source Swiss-Prot : SWS_FT_FI5 69) chain B residue 44 type MOD_RES sequence K description Phosphoserine => ECO:0000250|UniProtKB:Q64475 source Swiss-Prot : SWS_FT_FI5 70) chain F residue 44 type MOD_RES sequence K description Phosphoserine => ECO:0000250|UniProtKB:Q64475 source Swiss-Prot : SWS_FT_FI5 71) chain D residue 47 type MOD_RES sequence K description N6-methyllysine => ECO:0000250|UniProtKB:P62807 source Swiss-Prot : SWS_FT_FI6 72) chain D residue 109 type MOD_RES sequence K description N6-methyllysine => ECO:0000250|UniProtKB:P62807 source Swiss-Prot : SWS_FT_FI6 73) chain H residue 47 type MOD_RES sequence K description N6-methyllysine => ECO:0000250|UniProtKB:P62807 source Swiss-Prot : SWS_FT_FI6 74) chain H residue 109 type MOD_RES sequence K description N6-methyllysine => ECO:0000250|UniProtKB:P62807 source Swiss-Prot : SWS_FT_FI6 75) chain F residue 31 type MOD_RES sequence K description N6-methyllysine => ECO:0000250|UniProtKB:P62807 source Swiss-Prot : SWS_FT_FI6 76) chain F residue 77 type MOD_RES sequence K description N6-methyllysine => ECO:0000250|UniProtKB:P62807 source Swiss-Prot : SWS_FT_FI6 77) chain F residue 91 type MOD_RES sequence K description N6-methyllysine => ECO:0000250|UniProtKB:P62807 source Swiss-Prot : SWS_FT_FI6 78) chain D residue 58 type MOD_RES sequence K description N6,N6-dimethyllysine => ECO:0000250|UniProtKB:P62807 source Swiss-Prot : SWS_FT_FI7 79) chain H residue 58 type MOD_RES sequence K description N6,N6-dimethyllysine => ECO:0000250|UniProtKB:P62807 source Swiss-Prot : SWS_FT_FI7 80) chain G residue 74 type MOD_RES sequence K description N6,N6-dimethyllysine => ECO:0000250|UniProtKB:P62807 source Swiss-Prot : SWS_FT_FI7 81) chain G residue 75 type MOD_RES sequence K description N6,N6-dimethyllysine => ECO:0000250|UniProtKB:P62807 source Swiss-Prot : SWS_FT_FI7

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