eF-site ID 6fuy-A PDB Code 6fuy Chain A click to enlarge Title Crystal structure of human full-length vinculin-T12-A974K (residues 1-1066) Classification CELL ADHESION Compound Vinculin Source Homo sapiens (Human) (VINC_HUMAN) Sequence A:  MPVFHTRTIESILEPVAQQISHLVIMHEEGEVDGKAIPDL TAPVAAVQAAVSNLVRVGKETVQTTEDQILKRDMPPAFIK VENACTKLVQAAQMLQSDPYSVPARDYLIDGSRGILSGTS DLLLTFDEAEVRKIIRVCKGILEYLTVAEVVETMEDLVTY TKNLGPGMTKMAKMIDERQQELTHQEHRVMLVNSMNTVKE LLPVLISAMKIFVTTKNSKNQGIEEALKNRNFTVEKMSAE INEIIRVLQLTSWDEDAWASKDTEAMKRALASIDSKLNQA KGWLRDPSASPGDAGEQAIRQILDEAGKVGELCAGKERRE ILGTCKMLGQMTDQVADLRARGQGSSPVAMQKAQQVSQGL DVLTAKVENAARKLEAMTNSKQSIAKKIDAAQNWLADPEG EEQIRGALAEAAKQVATALQNLQTKTNRAVANSRPAKAAV HLEGKIEQAQRWIDNPTVDDRGVGQAAIRGLVAEGHRLAN VMMGPYRQDLLAKCDRVDQLTAQLADLAARGEGESPQARA LASQLQDSLKDLKARMQEAMTQEVSDVFSDTTTPIKLLAV AATAPPDAPNREEVFDERAANFENHSGKLGATAEKAAAVG TANKSTVEGIQASVKTARELTPQVVSAARILLRNPGNQAA YEHFETMKNQWIDNVEKMTGLVDEAIDTKSLLDASEEAIK KDLDKCKVAMANIQPQMLVAGATSIARRANRILLVAKREV ENSEDPKFREAVKAASDELSKTISPMVMDAKAVAGNISDP GLQKSFLDSGYRILGAVAKVREAFEKDEEFPEQKANQPMM MAARQLHDEARKWSSKGNDIIAAAKRMALLMAEMSRLVRG GSGTKRALIQCAKDIAKASDEVTRLAKEVAKQCTKAAIAT NLLQVCERIPTISTQLKILSTVKATMLGRTNISDEESEQA TEMLVHNAQNLMQSVKETVREAEAASIKFTLRWVRKTPWY Q Description Functional site 1) chain A residue 800 type sequence D description binding site for residue CA A 1101 source : AC1 2) chain A residue 162-182 type prosite sequence KNLGPGMTKMAKMIDERQQEL description VINCULIN_1 Vinculin family talin-binding region signature. KnLgpgMtkMakmideRQQEL source prosite : PS00663 3) chain A residue 277-287 type prosite sequence LNQAKGWLRDP description VINCULIN_2 Vinculin repeated domain signature. LnQAkgWLrDP source prosite : PS00664 4) chain A residue 497-507 type prosite sequence IEQAQRWIDNP description VINCULIN_2 Vinculin repeated domain signature. LnQAkgWLrDP source prosite : PS00664 5) chain A residue 97 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P85972 source Swiss-Prot : SWS_FT_FI1 6) chain A residue 272 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P85972 source Swiss-Prot : SWS_FT_FI1 7) chain A residue 574 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P85972 source Swiss-Prot : SWS_FT_FI1 8) chain A residue 672 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI10 9) chain A residue 721 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI11 10) chain A residue 822 type MOD_RES sequence Y description Phosphotyrosine => ECO:0007744|PubMed:18669648 source Swiss-Prot : SWS_FT_FI12 11) chain A residue 173 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI2 12) chain A residue 496 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI2 13) chain A residue 260 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI3 14) chain A residue 275 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI3 15) chain A residue 579 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI3 16) chain A residue 600 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI3 17) chain A residue 795 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI3 18) chain A residue 809 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI3 19) chain A residue 288 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI4 20) chain A residue 290 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI5 21) chain A residue 346 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI6 22) chain A residue 537 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000305 source Swiss-Prot : SWS_FT_FI8 23) chain A residue 604 type MOD_RES sequence T description Phosphothreonine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI9

Display surface Download Links