eF-site ID 6nrc-H PDB Code 6nrc Chain H click to enlarge Title hTRiC-hPFD Class3 Classification CHAPERONE Compound Prefoldin subunit 1 Source (TCPQ_HUMAN) Sequence H:  MLKEGAKHFSGLEEAVYRNIQACKELAQTTRTAYGPNGMN KMVINHLEKLFVTNDAATILRELEVQHPAAKMIVMASHMQ EQEVGDGTNFVLVFAGALLELAEELLRIGLSVSEVIEGYE IACRKAHEILPNLVCCSAKNLRDIDEVSSLLRTSIMSKQY GNEVFLAKLIAQACVSIFPDSGHFNVDNIRVCKILGSGIS SSSVLHGMVFKKETEGDVTSVKDAKIAVYSCPFDGMITET KGTVLIKTAEELMNFSKGEENLMDAQVKAIADTGANVVVT GGKVADMALHYANKYNIMLVRLNSKWDLRRLCKTVGATAL PRLTPPVLEEMGHCDSVYLSEVGDTQVVVFKHEKEDGAIS TIVLRGSTDNLMDDIERAVDDGVNTFKVLTRDKRLVPGGG ATEIELAKQITSYGETCPGLEQYAIKKFAEAFEAIPRALA ENSGVKANEVISKLYAVHQEGNKNVGLDIEAEVPAVKDML EAGILDTYLGKYWAIKLATNAAVTVLRVDQ Description Functional site 1) chain H residue 224 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_FI6 2) chain H residue 254 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_FI6 3) chain H residue 260 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_FI6 4) chain H residue 459 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1) => ECO:0007744|PubMed:25114211 source Swiss-Prot : SWS_FT_FI7 5) chain H residue 282-293 type prosite sequence AIADTGANVVVT description ASP_PROTEASE Eukaryotic and viral aspartyl proteases active site. AIADTGANVVVT source prosite : PS00141 6) chain H residue 44-56 type prosite sequence RTAYGPNGMNKMV description TCP1_1 Chaperonins TCP-1 signature 1. RTnLGPkGtmKML source prosite : PS00750 7) chain H residue 65-81 type prosite sequence VTNDAATILRELEVQHP description TCP1_2 Chaperonins TCP-1 signature 2. LTKDGNVLLheMqIqHP source prosite : PS00751 8) chain H residue 93-101 type prosite sequence QEQEVGDGT description TCP1_3 Chaperonins TCP-1 signature 3. QDdiTGDGT source prosite : PS00995 9) chain H residue 23 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI1 10) chain H residue 30 type MOD_RES sequence Y description Phosphotyrosine => ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI2 11) chain H residue 269 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI3 12) chain H residue 162 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI3 13) chain H residue 213 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI3 14) chain H residue 317 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI3 15) chain H residue 318 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI4 16) chain H residue 400 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI4 17) chain H residue 466 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI4 18) chain H residue 505 type MOD_RES sequence Y description Phosphotyrosine => ECO:0007744|PubMed:15592455 source Swiss-Prot : SWS_FT_FI5

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