eF-site ID 4nft-A PDB Code 4nft Chain A click to enlarge Title Crystal structure of human lnkH2B-h2A.Z-Anp32e Classification CHAPERONE Compound Histone H2B type 2-E, Histone H2A.Z Source Homo sapiens (Human) (AN32E_HUMAN) Sequence A:  MRKESYSIYVYKVLKQVHPDTGISSKAMGIMNSFVNDIFE RIAGEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHAV SEGTKAVTKYTSSKKSRSQRAGLQFPVGRIHRHLKSRTTS HGRVGATAAVYSAAILEYLTAEVLELAGNASKDLKVKRIT PRHLQLAIRGDEELDSLIKATIAG Description Functional site 1) chain A residue 103-109 type prosite sequence AGLQFPV description HISTONE_H2A Histone H2A signature. AGLqFPV source prosite : PS00046 2) chain A residue 61-83 type prosite sequence REIQTAVRLLLPGELAKHAVSEG description HISTONE_H2B Histone H2B signature. REIQTavRlLLpGELaKHAVSEG source prosite : PS00357 3) chain A residue 3 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000269|PubMed:22389435 source Swiss-Prot : SWS_FT_FI1 4) chain A residue 85 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000269|PubMed:22389435 source Swiss-Prot : SWS_FT_FI1 5) chain A residue 89 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000269|PubMed:22389435 source Swiss-Prot : SWS_FT_FI1 6) chain A residue 81 type CARBOHYD sequence S description O-linked (GlcNAc) serine => ECO:0000250|UniProtKB:P62807 source Swiss-Prot : SWS_FT_FI10 7) chain A residue 3 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_FI11 8) chain A residue 89 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_FI12 9) chain A residue 4 type MOD_RES sequence E description PolyADP-ribosyl glutamic acid => ECO:0000250|UniProtKB:Q64475 source Swiss-Prot : SWS_FT_FI2 10) chain A residue 5 type MOD_RES sequence S description Phosphoserine; by AMPK => ECO:0000250|UniProtKB:Q64524 source Swiss-Prot : SWS_FT_FI3 11) chain A residue 12 type MOD_RES sequence K description N6-lactoyllysine; alternate => ECO:0000269|PubMed:31645732 source Swiss-Prot : SWS_FT_FI4 12) chain A residue 54 type MOD_RES sequence K description N6-lactoyllysine; alternate => ECO:0000269|PubMed:31645732 source Swiss-Prot : SWS_FT_FI4 13) chain A residue 15 type MOD_RES sequence K description N6-methyllysine; alternate => ECO:0000269|PubMed:16627869 source Swiss-Prot : SWS_FT_FI5 14) chain A residue 77 type MOD_RES sequence K description N6-methyllysine; alternate => ECO:0000269|PubMed:16627869 source Swiss-Prot : SWS_FT_FI5 15) chain A residue 26 type MOD_RES sequence K description N6-(2-hydroxyisobutyryl)lysine; alternate => ECO:0000269|PubMed:24681537 source Swiss-Prot : SWS_FT_FI6 16) chain A residue 48 type MOD_RES sequence R description Dimethylated arginine => ECO:0000250|UniProtKB:Q96A08 source Swiss-Prot : SWS_FT_FI7 17) chain A residue 55 type MOD_RES sequence R description Omega-N-methylarginine => ECO:0000250|UniProtKB:Q96A08 source Swiss-Prot : SWS_FT_FI8 18) chain A residue 61 type MOD_RES sequence R description Omega-N-methylarginine => ECO:0000250|UniProtKB:Q96A08 source Swiss-Prot : SWS_FT_FI8 19) chain A residue 84 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:Q00729 source Swiss-Prot : SWS_FT_FI9

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