eF-site ID 2vnf-A PDB Code 2vnf Chain A click to enlarge Title MOLECULAR BASIS OF HISTONE H3K4ME3 RECOGNITION BY ING4 Classification CELL CYCLE Compound INHIBITOR OF GROWTH PROTEIN 4 Source Homo sapiens (Human) (Q5TEC6_HUMAN) Sequence A:  EPTYCLCHQVSYGEMIGCDNPDCSIEWFHFACVGLTTKPR GKWFCPRCSQ Description Functional site 1) chain A residue 244 type sequence Q description BINDING SITE FOR RESIDUE NA A 300 source : AC1 2) chain A residue 199 type sequence C description BINDING SITE FOR RESIDUE DTT A 1245 source : AC2 3) chain A residue 202 type sequence H description BINDING SITE FOR RESIDUE DTT A 1245 source : AC2 4) chain A residue 219 type sequence I description BINDING SITE FOR RESIDUE DTT A 1245 source : AC2 5) chain A residue 199 type sequence C description BINDING SITE FOR RESIDUE ZN A 1246 source : AC4 6) chain A residue 201 type sequence C description BINDING SITE FOR RESIDUE ZN A 1246 source : AC4 7) chain A residue 223 type sequence H description BINDING SITE FOR RESIDUE ZN A 1246 source : AC4 8) chain A residue 226 type sequence C description BINDING SITE FOR RESIDUE ZN A 1246 source : AC4 9) chain A residue 212 type sequence C description BINDING SITE FOR RESIDUE ZN A 1247 source : AC7 10) chain A residue 217 type sequence C description BINDING SITE FOR RESIDUE ZN A 1247 source : AC7 11) chain A residue 239 type sequence C description BINDING SITE FOR RESIDUE ZN A 1247 source : AC7 12) chain A residue 242 type sequence C description BINDING SITE FOR RESIDUE ZN A 1247 source : AC7 13) chain A residue 199-242 type prosite sequence CLCHQVSYGEMIGCDNPDCSIEWFHFACVGLTTKPRGKWF CPRC description ZF_PHD_1 Zinc finger PHD-type signature. Cl.Chqvsygem.....................................IgCdnpdCsiewFHfaCvglttkprgk...................................WfCprC source prosite : PS01359 14) chain A residue 212 type MOD_RES sequence C description Phosphothreonine; by HASPIN and VRK1 => ECO:0000269|PubMed:15681610, ECO:0000269|PubMed:16185088, ECO:0000269|PubMed:31527692 source Swiss-Prot : SWS_FT_FI2 15) chain A residue 217 type MOD_RES sequence C description Phosphothreonine; by HASPIN and VRK1 => ECO:0000269|PubMed:15681610, ECO:0000269|PubMed:16185088, ECO:0000269|PubMed:31527692 source Swiss-Prot : SWS_FT_FI2 16) chain A residue 223 type MOD_RES sequence H description Phosphothreonine; by HASPIN and VRK1 => ECO:0000269|PubMed:15681610, ECO:0000269|PubMed:16185088, ECO:0000269|PubMed:31527692 source Swiss-Prot : SWS_FT_FI2 17) chain A residue 226 type MOD_RES sequence C description Phosphothreonine; by HASPIN and VRK1 => ECO:0000269|PubMed:15681610, ECO:0000269|PubMed:16185088, ECO:0000269|PubMed:31527692 source Swiss-Prot : SWS_FT_FI2 18) chain A residue 239 type MOD_RES sequence C description Phosphothreonine; by HASPIN and VRK1 => ECO:0000269|PubMed:15681610, ECO:0000269|PubMed:16185088, ECO:0000269|PubMed:31527692 source Swiss-Prot : SWS_FT_FI2 19) chain A residue 242 type MOD_RES sequence C description Phosphothreonine; by HASPIN and VRK1 => ECO:0000269|PubMed:15681610, ECO:0000269|PubMed:16185088, ECO:0000269|PubMed:31527692 source Swiss-Prot : SWS_FT_FI2 20) chain A residue 213 type MOD_RES sequence D description N6-methyllysine; alternate => ECO:0000269|PubMed:16267050, ECO:0000269|PubMed:16457588, ECO:0000269|PubMed:17194708 source Swiss-Prot : SWS_FT_FI3 21) chain A residue 221 type MOD_RES sequence W description N6-methyllysine; alternate => ECO:0000269|PubMed:16267050, ECO:0000269|PubMed:16457588, ECO:0000269|PubMed:17194708 source Swiss-Prot : SWS_FT_FI3

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