eF-site ID 3jat-ABCDEFGHIJKL PDB Code 3jat Chain A, B, C, D, E, F, G, H, I, J, K, L Title Cryo-EM structure of GMPCPP-microtubule (14 protofilaments) decorated with kinesin Classification STRUCTURAL PROTEIN Compound Tubulin alpha-1B chain Source ORGANISM_COMMON: pig; ORGANISM_SCIENTIFIC: Sus scrofa; Sequence A:  MRECISIHVGQAGVQIGNACWELYCLEHGIQPDGQMPDSF NTFFSETGAGKHVPRAVFVDLEPTVIDEVRTGTYRQLFHP EQLITGKEDAANNYARGHYTIGKEIIDLVLDRIRKLADQC TGLQGFLVFHSFGGGTGSGFTSLLMERLSVDYGKKSKLEF SIYPAPQVSTAVVEPYNSILTTHTTLEHSDCAFMVDNEAI YDICRRNLDIERPTYTNLNRLISQIVSSITASLRFDGALN VDLTEFQTNLVPYPRIHFPLATYAPVISAEKAYHEQLSVA EITNACFEPANQMVKCDPRHGKYMACCLLYRGDVVPKDVN AAIATIKTKRSIQFVDWCPTGFKVGINYQPPTVVPGGDLA KVQRAVCMLSNTTAIAEAWARLDHKFDLMYAKRAFVHWYV GEGMEEGEFSEAREDMAALEKDYEEVGV B:  MREIVHIQAGQCGNQIGAKFWEVISDEHGIDPTGSYHGDS DLQLERINVYYNEAAGNKYVPRAILVDLEPGTMDSVRSGP FGQIFRPDNFVFGQSGAGNNWAKGHYTEGAELVDSVLDVV RKESESCDCLQGFQLTHSLGGGTGSGMGTLLISKIREEYP DRIMNTFSVVPSPKVSDTVVEPYNATLSVHQLVENTDETY CIDNEALYDICFRTLKLTTPTYGDLNHLVSATMSGVTTCL RFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTSRGSQQ YRALTVPELTQQMFDAKNMMAACDPRHGRYLTVAAVFRGR MSMKEVDEQMLNVQNKNSSYFVEWIPNNVKTAVCDIPPRG LKMSATFIGNSTAIQELFKRISEQFTAMFRRKAFLHWYTG EGMDEMEFTEAESNMNDLVSEYQQYQ C:  MRECISIHVGQAGVQIGNACWELYCLEHGIQPDGQMPDSF NTFFSETGAGKHVPRAVFVDLEPTVIDEVRTGTYRQLFHP EQLITGKEDAANNYARGHYTIGKEIIDLVLDRIRKLADQC TGLQGFLVFHSFGGGTGSGFTSLLMERLSVDYGKKSKLEF SIYPAPQVSTAVVEPYNSILTTHTTLEHSDCAFMVDNEAI YDICRRNLDIERPTYTNLNRLISQIVSSITASLRFDGALN VDLTEFQTNLVPYPRIHFPLATYAPVISAEKAYHEQLSVA EITNACFEPANQMVKCDPRHGKYMACCLLYRGDVVPKDVN AAIATIKTKRSIQFVDWCPTGFKVGINYQPPTVVPGGDLA KVQRAVCMLSNTTAIAEAWARLDHKFDLMYAKRAFVHWYV GEGMEEGEFSEAREDMAALEKDYEEVGV D:  MREIVHIQAGQCGNQIGAKFWEVISDEHGIDPTGSYHGDS DLQLERINVYYNEAAGNKYVPRAILVDLEPGTMDSVRSGP FGQIFRPDNFVFGQSGAGNNWAKGHYTEGAELVDSVLDVV RKESESCDCLQGFQLTHSLGGGTGSGMGTLLISKIREEYP DRIMNTFSVVPSPKVSDTVVEPYNATLSVHQLVENTDETY CIDNEALYDICFRTLKLTTPTYGDLNHLVSATMSGVTTCL RFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTSRGSQQ YRALTVPELTQQMFDAKNMMAACDPRHGRYLTVAAVFRGR MSMKEVDEQMLNVQNKNSSYFVEWIPNNVKTAVCDIPPRG LKMSATFIGNSTAIQELFKRISEQFTAMFRRKAFLHWYTG EGMDEMEFTEAESNMNDLVSEYQQYQ E:  MRECISIHVGQAGVQIGNACWELYCLEHGIQPDGQMPDSF NTFFSETGAGKHVPRAVFVDLEPTVIDEVRTGTYRQLFHP EQLITGKEDAANNYARGHYTIGKEIIDLVLDRIRKLADQC TGLQGFLVFHSFGGGTGSGFTSLLMERLSVDYGKKSKLEF SIYPAPQVSTAVVEPYNSILTTHTTLEHSDCAFMVDNEAI YDICRRNLDIERPTYTNLNRLISQIVSSITASLRFDGALN VDLTEFQTNLVPYPRIHFPLATYAPVISAEKAYHEQLSVA EITNACFEPANQMVKCDPRHGKYMACCLLYRGDVVPKDVN AAIATIKTKRSIQFVDWCPTGFKVGINYQPPTVVPGGDLA KVQRAVCMLSNTTAIAEAWARLDHKFDLMYAKRAFVHWYV GEGMEEGEFSEAREDMAALEKDYEEVGV F:  MREIVHIQAGQCGNQIGAKFWEVISDEHGIDPTGSYHGDS DLQLERINVYYNEAAGNKYVPRAILVDLEPGTMDSVRSGP FGQIFRPDNFVFGQSGAGNNWAKGHYTEGAELVDSVLDVV RKESESCDCLQGFQLTHSLGGGTGSGMGTLLISKIREEYP DRIMNTFSVVPSPKVSDTVVEPYNATLSVHQLVENTDETY CIDNEALYDICFRTLKLTTPTYGDLNHLVSATMSGVTTCL RFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTSRGSQQ YRALTVPELTQQMFDAKNMMAACDPRHGRYLTVAAVFRGR MSMKEVDEQMLNVQNKNSSYFVEWIPNNVKTAVCDIPPRG LKMSATFIGNSTAIQELFKRISEQFTAMFRRKAFLHWYTG EGMDEMEFTEAESNMNDLVSEYQQYQ G:  MREIVHIQAGQCGNQIGAKFWEVISDEHGIDPTGSYHGDS DLQLERINVYYNEAAGNKYVPRAILVDLEPGTMDSVRSGP FGQIFRPDNFVFGQSGAGNNWAKGHYTEGAELVDSVLDVV RKESESCDCLQGFQLTHSLGGGTGSGMGTLLISKIREEYP DRIMNTFSVVPSPKVSDTVVEPYNATLSVHQLVENTDETY CIDNEALYDICFRTLKLTTPTYGDLNHLVSATMSGVTTCL RFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTSRGSQQ YRALTVPELTQQMFDAKNMMAACDPRHGRYLTVAAVFRGR MSMKEVDEQMLNVQNKNSSYFVEWIPNNVKTAVCDIPPRG LKMSATFIGNSTAIQELFKRISEQFTAMFRRKAFLHWYTG EGMDEMEFTEAESNMNDLVSEYQQYQ H:  MREIVHIQAGQCGNQIGAKFWEVISDEHGIDPTGSYHGDS DLQLERINVYYNEAAGNKYVPRAILVDLEPGTMDSVRSGP FGQIFRPDNFVFGQSGAGNNWAKGHYTEGAELVDSVLDVV RKESESCDCLQGFQLTHSLGGGTGSGMGTLLISKIREEYP DRIMNTFSVVPSPKVSDTVVEPYNATLSVHQLVENTDETY CIDNEALYDICFRTLKLTTPTYGDLNHLVSATMSGVTTCL RFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTSRGSQQ YRALTVPELTQQMFDAKNMMAACDPRHGRYLTVAAVFRGR MSMKEVDEQMLNVQNKNSSYFVEWIPNNVKTAVCDIPPRG LKMSATFIGNSTAIQELFKRISEQFTAMFRRKAFLHWYTG EGMDEMEFTEAESNMNDLVSEYQQYQ I:  MREIVHIQAGQCGNQIGAKFWEVISDEHGIDPTGSYHGDS DLQLERINVYYNEAAGNKYVPRAILVDLEPGTMDSVRSGP FGQIFRPDNFVFGQSGAGNNWAKGHYTEGAELVDSVLDVV RKESESCDCLQGFQLTHSLGGGTGSGMGTLLISKIREEYP DRIMNTFSVVPSPKVSDTVVEPYNATLSVHQLVENTDETY CIDNEALYDICFRTLKLTTPTYGDLNHLVSATMSGVTTCL RFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTSRGSQQ YRALTVPELTQQMFDAKNMMAACDPRHGRYLTVAAVFRGR MSMKEVDEQMLNVQNKNSSYFVEWIPNNVKTAVCDIPPRG LKMSATFIGNSTAIQELFKRISEQFTAMFRRKAFLHWYTG EGMDEMEFTEAESNMNDLVSEYQQYQ J:  MRECISIHVGQAGVQIGNACWELYCLEHGIQPDGQMPDSF NTFFSETGAGKHVPRAVFVDLEPTVIDEVRTGTYRQLFHP EQLITGKEDAANNYARGHYTIGKEIIDLVLDRIRKLADQC TGLQGFLVFHSFGGGTGSGFTSLLMERLSVDYGKKSKLEF SIYPAPQVSTAVVEPYNSILTTHTTLEHSDCAFMVDNEAI YDICRRNLDIERPTYTNLNRLISQIVSSITASLRFDGALN VDLTEFQTNLVPYPRIHFPLATYAPVISAEKAYHEQLSVA EITNACFEPANQMVKCDPRHGKYMACCLLYRGDVVPKDVN AAIATIKTKRSIQFVDWCPTGFKVGINYQPPTVVPGGDLA KVQRAVCMLSNTTAIAEAWARLDHKFDLMYAKRAFVHWYV GEGMEEGEFSEAREDMAALEKDYEEVGV K:  MRECISIHVGQAGVQIGNACWELYCLEHGIQPDGQMPDSF NTFFSETGAGKHVPRAVFVDLEPTVIDEVRTGTYRQLFHP EQLITGKEDAANNYARGHYTIGKEIIDLVLDRIRKLADQC TGLQGFLVFHSFGGGTGSGFTSLLMERLSVDYGKKSKLEF SIYPAPQVSTAVVEPYNSILTTHTTLEHSDCAFMVDNEAI YDICRRNLDIERPTYTNLNRLISQIVSSITASLRFDGALN VDLTEFQTNLVPYPRIHFPLATYAPVISAEKAYHEQLSVA EITNACFEPANQMVKCDPRHGKYMACCLLYRGDVVPKDVN AAIATIKTKRSIQFVDWCPTGFKVGINYQPPTVVPGGDLA KVQRAVCMLSNTTAIAEAWARLDHKFDLMYAKRAFVHWYV GEGMEEGEFSEAREDMAALEKDYEEVGV L:  MRECISIHVGQAGVQIGNACWELYCLEHGIQPDGQMPDSF NTFFSETGAGKHVPRAVFVDLEPTVIDEVRTGTYRQLFHP EQLITGKEDAANNYARGHYTIGKEIIDLVLDRIRKLADQC TGLQGFLVFHSFGGGTGSGFTSLLMERLSVDYGKKSKLEF SIYPAPQVSTAVVEPYNSILTTHTTLEHSDCAFMVDNEAI YDICRRNLDIERPTYTNLNRLISQIVSSITASLRFDGALN VDLTEFQTNLVPYPRIHFPLATYAPVISAEKAYHEQLSVA EITNACFEPANQMVKCDPRHGKYMACCLLYRGDVVPKDVN AAIATIKTKRSIQFVDWCPTGFKVGINYQPPTVVPGGDLA KVQRAVCMLSNTTAIAEAWARLDHKFDLMYAKRAFVHWYV GEGMEEGEFSEAREDMAALEKDYEEVGV Description Functional site 1) chain E residue 10 type sequence G description BINDING SITE FOR RESIDUE GTP E 501 source : AC1 2) chain E residue 11 type sequence Q description BINDING SITE FOR RESIDUE GTP E 501 source : AC1 3) chain E residue 12 type sequence A description BINDING SITE FOR RESIDUE GTP E 501 source : AC1 4) chain E residue 15 type sequence Q description BINDING SITE FOR RESIDUE GTP E 501 source : AC1 5) chain E residue 99 type sequence A description BINDING SITE FOR RESIDUE GTP E 501 source : AC1 6) chain E residue 100 type sequence A description BINDING SITE FOR RESIDUE GTP E 501 source : AC1 7) chain E residue 101 type sequence N description BINDING SITE FOR RESIDUE GTP E 501 source : AC1 8) chain E residue 140 type sequence S description BINDING SITE FOR RESIDUE GTP E 501 source : AC1 9) chain E residue 143 type sequence G description BINDING SITE FOR RESIDUE GTP E 501 source : AC1 10) chain E residue 144 type sequence G description BINDING SITE FOR RESIDUE GTP E 501 source : AC1 11) chain E residue 145 type sequence T description BINDING SITE FOR RESIDUE GTP E 501 source : AC1 12) chain E residue 146 type sequence G description BINDING SITE FOR RESIDUE GTP E 501 source : AC1 13) chain E residue 171 type sequence I description BINDING SITE FOR RESIDUE GTP E 501 source : AC1 14) chain E residue 179 type sequence T description BINDING SITE FOR RESIDUE GTP E 501 source : AC1 15) chain E residue 183 type sequence E description BINDING SITE FOR RESIDUE GTP E 501 source : AC1 16) chain E residue 206 type sequence N description BINDING SITE FOR RESIDUE GTP E 501 source : AC1 17) chain E residue 224 type sequence Y description BINDING SITE FOR RESIDUE GTP E 501 source : AC1 18) chain E residue 228 type sequence N description BINDING SITE FOR RESIDUE GTP E 501 source : AC1 19) chain G residue 254 type sequence K description BINDING SITE FOR RESIDUE GTP E 501 source : AC1 20) chain E residue 71 type sequence E description BINDING SITE FOR RESIDUE MG E 502 source : AC2 21) chain E residue 254 type sequence E description BINDING SITE FOR RESIDUE G2P F 501 source : AC3 22) chain F residue 10 type sequence G description BINDING SITE FOR RESIDUE G2P F 501 source : AC3 23) chain F residue 11 type sequence Q description BINDING SITE FOR RESIDUE G2P F 501 source : AC3 24) chain F residue 12 type sequence C description BINDING SITE FOR RESIDUE G2P F 501 source : AC3 25) chain F residue 15 type sequence Q description BINDING SITE FOR RESIDUE G2P F 501 source : AC3 26) chain F residue 99 type sequence A description BINDING SITE FOR RESIDUE G2P F 501 source : AC3 27) chain F residue 101 type sequence N description BINDING SITE FOR RESIDUE G2P F 501 source : AC3 28) chain F residue 144 type sequence G description BINDING SITE FOR RESIDUE G2P F 501 source : AC3 29) chain F residue 145 type sequence T description BINDING SITE FOR RESIDUE G2P F 501 source : AC3 30) chain F residue 146 type sequence G description BINDING SITE FOR RESIDUE G2P F 501 source : AC3 31) chain F residue 206 type sequence N description BINDING SITE FOR RESIDUE G2P F 501 source : AC3 32) chain F residue 224 type sequence Y description BINDING SITE FOR RESIDUE G2P F 501 source : AC3 33) chain F residue 228 type sequence N description BINDING SITE FOR RESIDUE G2P F 501 source : AC3 34) chain F residue 254 type sequence K description BINDING SITE FOR RESIDUE GTP J 501 source : AC5 35) chain J residue 10 type sequence G description BINDING SITE FOR RESIDUE GTP J 501 source : AC5 36) chain J residue 11 type sequence Q description BINDING SITE FOR RESIDUE GTP J 501 source : AC5 37) chain J residue 12 type sequence A description BINDING SITE FOR RESIDUE GTP J 501 source : AC5 38) chain J residue 15 type sequence Q description BINDING SITE FOR RESIDUE GTP J 501 source : AC5 39) chain J residue 98 type sequence D description BINDING SITE FOR RESIDUE GTP J 501 source : AC5 40) chain J residue 99 type sequence A description BINDING SITE FOR RESIDUE GTP J 501 source : AC5 41) chain J residue 100 type sequence A description BINDING SITE FOR RESIDUE GTP J 501 source : AC5 42) chain J residue 101 type sequence N description BINDING SITE FOR RESIDUE GTP J 501 source : AC5 43) chain J residue 140 type sequence S description BINDING SITE FOR RESIDUE GTP J 501 source : AC5 44) chain J residue 144 type sequence G description BINDING SITE FOR RESIDUE GTP J 501 source : AC5 45) chain J residue 145 type sequence T description BINDING SITE FOR RESIDUE GTP J 501 source : AC5 46) chain J residue 146 type sequence G description BINDING SITE FOR RESIDUE GTP J 501 source : AC5 47) chain J residue 171 type sequence I description BINDING SITE FOR RESIDUE GTP J 501 source : AC5 48) chain J residue 179 type sequence T description BINDING SITE FOR RESIDUE GTP J 501 source : AC5 49) chain J residue 183 type sequence E description BINDING SITE FOR RESIDUE GTP J 501 source : AC5 50) chain J residue 206 type sequence N description BINDING SITE FOR RESIDUE GTP J 501 source : AC5 51) chain J residue 224 type sequence Y description BINDING SITE FOR RESIDUE GTP J 501 source : AC5 52) chain J residue 228 type sequence N description BINDING SITE FOR RESIDUE GTP J 501 source : AC5 53) chain G residue 10 type sequence G description BINDING SITE FOR RESIDUE G2P G 501 source : AC7 54) chain G residue 11 type sequence Q description BINDING SITE FOR RESIDUE G2P G 501 source : AC7 55) chain G residue 12 type sequence C description BINDING SITE FOR RESIDUE G2P G 501 source : AC7 56) chain G residue 15 type sequence Q description BINDING SITE FOR RESIDUE G2P G 501 source : AC7 57) chain G residue 99 type sequence A description BINDING SITE FOR RESIDUE G2P G 501 source : AC7 58) chain G residue 101 type sequence N description BINDING SITE FOR RESIDUE G2P G 501 source : AC7 59) chain G residue 144 type sequence G description BINDING SITE FOR RESIDUE G2P G 501 source : AC7 60) chain G residue 145 type sequence T description BINDING SITE FOR RESIDUE G2P G 501 source : AC7 61) chain G residue 146 type sequence G description BINDING SITE FOR RESIDUE G2P G 501 source : AC7 62) chain G residue 183 type sequence E description BINDING SITE FOR RESIDUE G2P G 501 source : AC7 63) chain G residue 206 type sequence N description BINDING SITE FOR RESIDUE G2P G 501 source : AC7 64) chain G residue 224 type sequence Y description BINDING SITE FOR RESIDUE G2P G 501 source : AC7 65) chain G residue 228 type sequence N description BINDING SITE FOR RESIDUE G2P G 501 source : AC7 66) chain C residue 10 type sequence G description BINDING SITE FOR RESIDUE GTP C 501 source : AC9 67) chain C residue 11 type sequence Q description BINDING SITE FOR RESIDUE GTP C 501 source : AC9 68) chain C residue 12 type sequence A description BINDING SITE FOR RESIDUE GTP C 501 source : AC9 69) chain C residue 15 type sequence Q description BINDING SITE FOR RESIDUE GTP C 501 source : AC9 70) chain C residue 99 type sequence A description BINDING SITE FOR RESIDUE GTP C 501 source : AC9 71) chain C residue 100 type sequence A description BINDING SITE FOR RESIDUE GTP C 501 source : AC9 72) chain C residue 101 type sequence N description BINDING SITE FOR RESIDUE GTP C 501 source : AC9 73) chain C residue 140 type sequence S description BINDING SITE FOR RESIDUE GTP C 501 source : AC9 74) chain C residue 143 type sequence G description BINDING SITE FOR RESIDUE GTP C 501 source : AC9 75) chain C residue 144 type sequence G description BINDING SITE FOR RESIDUE GTP C 501 source : AC9 76) chain C residue 145 type sequence T description BINDING SITE FOR RESIDUE GTP C 501 source : AC9 77) chain C residue 146 type sequence G description BINDING SITE FOR RESIDUE GTP C 501 source : AC9 78) chain C residue 179 type sequence T description BINDING SITE FOR RESIDUE GTP C 501 source : AC9 79) chain C residue 183 type sequence E description BINDING SITE FOR RESIDUE GTP C 501 source : AC9 80) chain C residue 206 type sequence N description BINDING SITE FOR RESIDUE GTP C 501 source : AC9 81) chain C residue 224 type sequence Y description BINDING SITE FOR RESIDUE GTP C 501 source : AC9 82) chain C residue 228 type sequence N description BINDING SITE FOR RESIDUE GTP C 501 source : AC9 83) chain I residue 254 type sequence K description BINDING SITE FOR RESIDUE GTP C 501 source : AC9 84) chain C residue 71 type sequence E description BINDING SITE FOR RESIDUE MG C 502 source : BC1 85) chain C residue 254 type sequence E description BINDING SITE FOR RESIDUE G2P D 501 source : BC2 86) chain D residue 10 type sequence G description BINDING SITE FOR RESIDUE G2P D 501 source : BC2 87) chain D residue 11 type sequence Q description BINDING SITE FOR RESIDUE G2P D 501 source : BC2 88) chain D residue 12 type sequence C description BINDING SITE FOR RESIDUE G2P D 501 source : BC2 89) chain D residue 15 type sequence Q description BINDING SITE FOR RESIDUE G2P D 501 source : BC2 90) chain D residue 99 type sequence A description BINDING SITE FOR RESIDUE G2P D 501 source : BC2 91) chain D residue 101 type sequence N description BINDING SITE FOR RESIDUE G2P D 501 source : BC2 92) chain D residue 144 type sequence G description BINDING SITE FOR RESIDUE G2P D 501 source : BC2 93) chain D residue 145 type sequence T description BINDING SITE FOR RESIDUE G2P D 501 source : BC2 94) chain D residue 146 type sequence G description BINDING SITE FOR RESIDUE G2P D 501 source : BC2 95) chain D residue 179 type sequence D description BINDING SITE FOR RESIDUE G2P D 501 source : BC2 96) chain D residue 183 type sequence E description BINDING SITE FOR RESIDUE G2P D 501 source : BC2 97) chain D residue 206 type sequence N description BINDING SITE FOR RESIDUE G2P D 501 source : BC2 98) chain D residue 224 type sequence Y description BINDING SITE FOR RESIDUE G2P D 501 source : BC2 99) chain D residue 228 type sequence N description BINDING SITE FOR RESIDUE G2P D 501 source : BC2 100) chain D residue 254 type sequence K description BINDING SITE FOR RESIDUE GTP L 501 source : BC4 101) chain L residue 10 type sequence G description BINDING SITE FOR RESIDUE GTP L 501 source : BC4 102) chain L residue 11 type sequence Q description BINDING SITE FOR RESIDUE GTP L 501 source : BC4 103) chain L residue 12 type sequence A description BINDING SITE FOR RESIDUE GTP L 501 source : BC4 104) chain L residue 15 type sequence Q description BINDING SITE FOR RESIDUE GTP L 501 source : BC4 105) chain L residue 99 type sequence A description BINDING SITE FOR RESIDUE GTP L 501 source : BC4 106) chain L residue 100 type sequence A description BINDING SITE FOR RESIDUE GTP L 501 source : BC4 107) chain L residue 101 type sequence N description BINDING SITE FOR RESIDUE GTP L 501 source : BC4 108) chain L residue 140 type sequence S description BINDING SITE FOR RESIDUE GTP L 501 source : BC4 109) chain L residue 143 type sequence G description BINDING SITE FOR RESIDUE GTP L 501 source : BC4 110) chain L residue 144 type sequence G description BINDING SITE FOR RESIDUE GTP L 501 source : BC4 111) chain L residue 145 type sequence T description BINDING SITE FOR RESIDUE GTP L 501 source : BC4 112) chain L residue 146 type sequence G description BINDING SITE FOR RESIDUE GTP L 501 source : BC4 113) chain L residue 171 type sequence I description BINDING SITE FOR RESIDUE GTP L 501 source : BC4 114) chain L residue 179 type sequence T description BINDING SITE FOR RESIDUE GTP L 501 source : BC4 115) chain L residue 183 type sequence E description BINDING SITE FOR RESIDUE GTP L 501 source : BC4 116) chain L residue 206 type sequence N description BINDING SITE FOR RESIDUE GTP L 501 source : BC4 117) chain L residue 224 type sequence Y description BINDING SITE FOR RESIDUE GTP L 501 source : BC4 118) chain L residue 228 type sequence N description BINDING SITE FOR RESIDUE GTP L 501 source : BC4 119) chain L residue 71 type sequence E description BINDING SITE FOR RESIDUE MG L 502 source : BC5 120) chain I residue 10 type sequence G description BINDING SITE FOR RESIDUE G2P I 501 source : BC6 121) chain I residue 11 type sequence Q description BINDING SITE FOR RESIDUE G2P I 501 source : BC6 122) chain I residue 12 type sequence C description BINDING SITE FOR RESIDUE G2P I 501 source : BC6 123) chain I residue 15 type sequence Q description BINDING SITE FOR RESIDUE G2P I 501 source : BC6 124) chain I residue 99 type sequence A description BINDING SITE FOR RESIDUE G2P I 501 source : BC6 125) chain I residue 101 type sequence N description BINDING SITE FOR RESIDUE G2P I 501 source : BC6 126) chain I residue 144 type sequence G description BINDING SITE FOR RESIDUE G2P I 501 source : BC6 127) chain I residue 145 type sequence T description BINDING SITE FOR RESIDUE G2P I 501 source : BC6 128) chain I residue 146 type sequence G description BINDING SITE FOR RESIDUE G2P I 501 source : BC6 129) chain I residue 183 type sequence E description BINDING SITE FOR RESIDUE G2P I 501 source : BC6 130) chain I residue 206 type sequence N description BINDING SITE FOR RESIDUE G2P I 501 source : BC6 131) chain I residue 224 type sequence Y description BINDING SITE FOR RESIDUE G2P I 501 source : BC6 132) chain I residue 228 type sequence N description BINDING SITE FOR RESIDUE G2P I 501 source : BC6 133) chain A residue 10 type sequence G description BINDING SITE FOR RESIDUE GTP A 501 source : BC8 134) chain A residue 11 type sequence Q description BINDING SITE FOR RESIDUE GTP A 501 source : BC8 135) chain A residue 12 type sequence A description BINDING SITE FOR RESIDUE GTP A 501 source : BC8 136) chain A residue 15 type sequence Q description BINDING SITE FOR RESIDUE GTP A 501 source : BC8 137) chain A residue 99 type sequence A description BINDING SITE FOR RESIDUE GTP A 501 source : BC8 138) chain A residue 101 type sequence N description BINDING SITE FOR RESIDUE GTP A 501 source : BC8 139) chain A residue 140 type sequence S description BINDING SITE FOR RESIDUE GTP A 501 source : BC8 140) chain A residue 143 type sequence G description BINDING SITE FOR RESIDUE GTP A 501 source : BC8 141) chain A residue 144 type sequence G description BINDING SITE FOR RESIDUE GTP A 501 source : BC8 142) chain A residue 145 type sequence T description BINDING SITE FOR RESIDUE GTP A 501 source : BC8 143) chain A residue 146 type sequence G description BINDING SITE FOR RESIDUE GTP A 501 source : BC8 144) chain A residue 171 type sequence I description BINDING SITE FOR RESIDUE GTP A 501 source : BC8 145) chain A residue 179 type sequence T description BINDING SITE FOR RESIDUE GTP A 501 source : BC8 146) chain A residue 183 type sequence E description BINDING SITE FOR RESIDUE GTP A 501 source : BC8 147) chain A residue 206 type sequence N description BINDING SITE FOR RESIDUE GTP A 501 source : BC8 148) chain A residue 224 type sequence Y description BINDING SITE FOR RESIDUE GTP A 501 source : BC8 149) chain A residue 228 type sequence N description BINDING SITE FOR RESIDUE GTP A 501 source : BC8 150) chain H residue 254 type sequence K description BINDING SITE FOR RESIDUE GTP A 501 source : BC8 151) chain A residue 71 type sequence E description BINDING SITE FOR RESIDUE MG A 502 source : BC9 152) chain A residue 254 type sequence E description BINDING SITE FOR RESIDUE G2P B 501 source : CC1 153) chain B residue 10 type sequence G description BINDING SITE FOR RESIDUE G2P B 501 source : CC1 154) chain B residue 11 type sequence Q description BINDING SITE FOR RESIDUE G2P B 501 source : CC1 155) chain B residue 12 type sequence C description BINDING SITE FOR RESIDUE G2P B 501 source : CC1 156) chain B residue 15 type sequence Q description BINDING SITE FOR RESIDUE G2P B 501 source : CC1 157) chain B residue 99 type sequence A description BINDING SITE FOR RESIDUE G2P B 501 source : CC1 158) chain B residue 101 type sequence N description BINDING SITE FOR RESIDUE G2P B 501 source : CC1 159) chain B residue 144 type sequence G description BINDING SITE FOR RESIDUE G2P B 501 source : CC1 160) chain B residue 145 type sequence T description BINDING SITE FOR RESIDUE G2P B 501 source : CC1 161) chain B residue 146 type sequence G description BINDING SITE FOR RESIDUE G2P B 501 source : CC1 162) chain B residue 179 type sequence D description BINDING SITE FOR RESIDUE G2P B 501 source : CC1 163) chain B residue 183 type sequence E description BINDING SITE FOR RESIDUE G2P B 501 source : CC1 164) chain B residue 206 type sequence N description BINDING SITE FOR RESIDUE G2P B 501 source : CC1 165) chain B residue 224 type sequence Y description BINDING SITE FOR RESIDUE G2P B 501 source : CC1 166) chain B residue 228 type sequence N description BINDING SITE FOR RESIDUE G2P B 501 source : CC1 167) chain B residue 254 type sequence K description BINDING SITE FOR RESIDUE GTP K 501 source : CC3 168) chain K residue 10 type sequence G description BINDING SITE FOR RESIDUE GTP K 501 source : CC3 169) chain K residue 11 type sequence Q description BINDING SITE FOR RESIDUE GTP K 501 source : CC3 170) chain K residue 12 type sequence A description BINDING SITE FOR RESIDUE GTP K 501 source : CC3 171) chain K residue 15 type sequence Q description BINDING SITE FOR RESIDUE GTP K 501 source : CC3 172) chain K residue 99 type sequence A description BINDING SITE FOR RESIDUE GTP K 501 source : CC3 173) chain K residue 100 type sequence A description BINDING SITE FOR RESIDUE GTP K 501 source : CC3 174) chain K residue 101 type sequence N description BINDING SITE FOR RESIDUE GTP K 501 source : CC3 175) chain K residue 140 type sequence S description BINDING SITE FOR RESIDUE GTP K 501 source : CC3 176) chain K residue 143 type sequence G description BINDING SITE FOR RESIDUE GTP K 501 source : CC3 177) chain K residue 144 type sequence G description BINDING SITE FOR RESIDUE GTP K 501 source : CC3 178) chain K residue 145 type sequence T description BINDING SITE FOR RESIDUE GTP K 501 source : CC3 179) chain K residue 146 type sequence G description BINDING SITE FOR RESIDUE GTP K 501 source : CC3 180) chain K residue 171 type sequence I description BINDING SITE FOR RESIDUE GTP K 501 source : CC3 181) chain K residue 179 type sequence T description BINDING SITE FOR RESIDUE GTP K 501 source : CC3 182) chain K residue 183 type sequence E description BINDING SITE FOR RESIDUE GTP K 501 source : CC3 183) chain K residue 206 type sequence N description BINDING SITE FOR RESIDUE GTP K 501 source : CC3 184) chain K residue 224 type sequence Y description BINDING SITE FOR RESIDUE GTP K 501 source : CC3 185) chain K residue 228 type sequence N description BINDING SITE FOR RESIDUE GTP K 501 source : CC3 186) chain H residue 10 type sequence G description BINDING SITE FOR RESIDUE G2P H 501 source : CC5 187) chain H residue 11 type sequence Q description BINDING SITE FOR RESIDUE G2P H 501 source : CC5 188) chain H residue 12 type sequence C description BINDING SITE FOR RESIDUE G2P H 501 source : CC5 189) chain H residue 15 type sequence Q description BINDING SITE FOR RESIDUE G2P H 501 source : CC5 190) chain H residue 99 type sequence A description BINDING SITE FOR RESIDUE G2P H 501 source : CC5 191) chain H residue 101 type sequence N description BINDING SITE FOR RESIDUE G2P H 501 source : CC5 192) chain H residue 144 type sequence G description BINDING SITE FOR RESIDUE G2P H 501 source : CC5 193) chain H residue 145 type sequence T description BINDING SITE FOR RESIDUE G2P H 501 source : CC5 194) chain H residue 146 type sequence G description BINDING SITE FOR RESIDUE G2P H 501 source : CC5 195) chain H residue 183 type sequence E description BINDING SITE FOR RESIDUE G2P H 501 source : CC5 196) chain H residue 206 type sequence N description BINDING SITE FOR RESIDUE G2P H 501 source : CC5 197) chain H residue 224 type sequence Y description BINDING SITE FOR RESIDUE G2P H 501 source : CC5 198) chain H residue 228 type sequence N description BINDING SITE FOR RESIDUE G2P H 501 source : CC5 199) chain B residue 326 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P07437 source Swiss-Prot : SWS_FT_FI10 200) chain H residue 326 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P07437 source Swiss-Prot : SWS_FT_FI10 201) chain I residue 326 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P07437 source Swiss-Prot : SWS_FT_FI10 202) chain F residue 326 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P07437 source Swiss-Prot : SWS_FT_FI10 203) chain G residue 326 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P07437 source Swiss-Prot : SWS_FT_FI10 204) chain D residue 326 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P07437 source Swiss-Prot : SWS_FT_FI10 205) chain E residue 326 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI12 206) chain L residue 326 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI12 207) chain L residue 370 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI12 208) chain A residue 326 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI12 209) chain A residue 370 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI12 210) chain K residue 326 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI12 211) chain K residue 370 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI12 212) chain E residue 370 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI12 213) chain J residue 326 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI12 214) chain J residue 370 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI12 215) chain C residue 326 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI12 216) chain C residue 370 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI12 217) chain F residue 60 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000250|UniProtKB:P07437 source Swiss-Prot : SWS_FT_FI9 218) chain G residue 60 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000250|UniProtKB:P07437 source Swiss-Prot : SWS_FT_FI9 219) chain D residue 60 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000250|UniProtKB:P07437 source Swiss-Prot : SWS_FT_FI9 220) chain I residue 60 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000250|UniProtKB:P07437 source Swiss-Prot : SWS_FT_FI9 221) chain B residue 60 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000250|UniProtKB:P07437 source Swiss-Prot : SWS_FT_FI9 222) chain H residue 60 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000250|UniProtKB:P07437 source Swiss-Prot : SWS_FT_FI9 223) chain G residue 144 type BINDING sequence G description BINDING => ECO:0000250|UniProtKB:Q13509 source Swiss-Prot : SWS_FT_FI1 224) chain G residue 145 type BINDING sequence T description BINDING => ECO:0000250|UniProtKB:Q13509 source Swiss-Prot : SWS_FT_FI1 225) chain G residue 146 type BINDING sequence G description BINDING => ECO:0000250|UniProtKB:Q13509 source Swiss-Prot : SWS_FT_FI1 226) chain G residue 206 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:Q13509 source Swiss-Prot : SWS_FT_FI1 227) chain G residue 228 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:Q13509 source Swiss-Prot : SWS_FT_FI1 228) chain D residue 11 type BINDING sequence Q description BINDING => ECO:0000250|UniProtKB:Q13509 source Swiss-Prot : SWS_FT_FI1 229) chain D residue 140 type BINDING sequence S description BINDING => ECO:0000250|UniProtKB:Q13509 source Swiss-Prot : SWS_FT_FI1 230) chain D residue 144 type BINDING sequence G description BINDING => ECO:0000250|UniProtKB:Q13509 source Swiss-Prot : SWS_FT_FI1 231) chain D residue 145 type BINDING sequence T description BINDING => ECO:0000250|UniProtKB:Q13509 source Swiss-Prot : SWS_FT_FI1 232) chain D residue 146 type BINDING sequence G description BINDING => ECO:0000250|UniProtKB:Q13509 source Swiss-Prot : SWS_FT_FI1 233) chain D residue 206 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:Q13509 source Swiss-Prot : SWS_FT_FI1 234) chain D residue 228 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:Q13509 source Swiss-Prot : SWS_FT_FI1 235) chain I residue 11 type BINDING sequence Q description BINDING => ECO:0000250|UniProtKB:Q13509 source Swiss-Prot : SWS_FT_FI1 236) chain I residue 140 type BINDING sequence S description BINDING => ECO:0000250|UniProtKB:Q13509 source Swiss-Prot : SWS_FT_FI1 237) chain I residue 144 type BINDING sequence G description BINDING => ECO:0000250|UniProtKB:Q13509 source Swiss-Prot : SWS_FT_FI1 238) chain I residue 145 type BINDING sequence T description BINDING => ECO:0000250|UniProtKB:Q13509 source Swiss-Prot : SWS_FT_FI1 239) chain I residue 146 type BINDING sequence G description BINDING => ECO:0000250|UniProtKB:Q13509 source Swiss-Prot : SWS_FT_FI1 240) chain I residue 206 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:Q13509 source Swiss-Prot : SWS_FT_FI1 241) chain I residue 228 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:Q13509 source Swiss-Prot : SWS_FT_FI1 242) chain B residue 11 type BINDING sequence Q description BINDING => ECO:0000250|UniProtKB:Q13509 source Swiss-Prot : SWS_FT_FI1 243) chain B residue 140 type BINDING sequence S description BINDING => ECO:0000250|UniProtKB:Q13509 source Swiss-Prot : SWS_FT_FI1 244) chain B residue 144 type BINDING sequence G description BINDING => ECO:0000250|UniProtKB:Q13509 source Swiss-Prot : SWS_FT_FI1 245) chain B residue 145 type BINDING sequence T description BINDING => ECO:0000250|UniProtKB:Q13509 source Swiss-Prot : SWS_FT_FI1 246) chain B residue 146 type BINDING sequence G description BINDING => ECO:0000250|UniProtKB:Q13509 source Swiss-Prot : SWS_FT_FI1 247) chain B residue 206 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:Q13509 source Swiss-Prot : SWS_FT_FI1 248) chain B residue 228 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:Q13509 source Swiss-Prot : SWS_FT_FI1 249) chain H residue 11 type BINDING sequence Q description BINDING => ECO:0000250|UniProtKB:Q13509 source Swiss-Prot : SWS_FT_FI1 250) chain H residue 140 type BINDING sequence S description BINDING => ECO:0000250|UniProtKB:Q13509 source Swiss-Prot : SWS_FT_FI1 251) chain H residue 144 type BINDING sequence G description BINDING => ECO:0000250|UniProtKB:Q13509 source Swiss-Prot : SWS_FT_FI1 252) chain H residue 145 type BINDING sequence T description BINDING => ECO:0000250|UniProtKB:Q13509 source Swiss-Prot : SWS_FT_FI1 253) chain H residue 146 type BINDING sequence G description BINDING => ECO:0000250|UniProtKB:Q13509 source Swiss-Prot : SWS_FT_FI1 254) chain H residue 206 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:Q13509 source Swiss-Prot : SWS_FT_FI1 255) chain H residue 228 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:Q13509 source Swiss-Prot : SWS_FT_FI1 256) chain F residue 228 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:Q13509 source Swiss-Prot : SWS_FT_FI1 257) chain G residue 11 type BINDING sequence Q description BINDING => ECO:0000250|UniProtKB:Q13509 source Swiss-Prot : SWS_FT_FI1 258) chain G residue 140 type BINDING sequence S description BINDING => ECO:0000250|UniProtKB:Q13509 source Swiss-Prot : SWS_FT_FI1 259) chain F residue 11 type BINDING sequence Q description BINDING => ECO:0000250|UniProtKB:Q13509 source Swiss-Prot : SWS_FT_FI1 260) chain F residue 140 type BINDING sequence S description BINDING => ECO:0000250|UniProtKB:Q13509 source Swiss-Prot : SWS_FT_FI1 261) chain F residue 144 type BINDING sequence G description BINDING => ECO:0000250|UniProtKB:Q13509 source Swiss-Prot : SWS_FT_FI1 262) chain F residue 145 type BINDING sequence T description BINDING => ECO:0000250|UniProtKB:Q13509 source Swiss-Prot : SWS_FT_FI1 263) chain F residue 146 type BINDING sequence G description BINDING => ECO:0000250|UniProtKB:Q13509 source Swiss-Prot : SWS_FT_FI1 264) chain F residue 206 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:Q13509 source Swiss-Prot : SWS_FT_FI1 265) chain J residue 71 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 266) chain J residue 140 type BINDING sequence S description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 267) chain J residue 144 type BINDING sequence G description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 268) chain J residue 145 type BINDING sequence T description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 269) chain J residue 179 type BINDING sequence T description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 270) chain J residue 206 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 271) chain J residue 228 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 272) chain C residue 11 type BINDING sequence Q description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 273) chain C residue 71 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 274) chain C residue 140 type BINDING sequence S description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 275) chain C residue 144 type BINDING sequence G description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 276) chain C residue 145 type BINDING sequence T description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 277) chain C residue 179 type BINDING sequence T description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 278) chain C residue 206 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 279) chain C residue 228 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 280) chain L residue 11 type BINDING sequence Q description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 281) chain L residue 71 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 282) chain L residue 140 type BINDING sequence S description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 283) chain L residue 144 type BINDING sequence G description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 284) chain L residue 145 type BINDING sequence T description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 285) chain L residue 179 type BINDING sequence T description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 286) chain L residue 206 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 287) chain L residue 228 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 288) chain A residue 11 type BINDING sequence Q description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 289) chain A residue 71 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 290) chain A residue 140 type BINDING sequence S description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 291) chain A residue 144 type BINDING sequence G description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 292) chain A residue 145 type BINDING sequence T description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 293) chain A residue 179 type BINDING sequence T description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 294) chain A residue 206 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 295) chain A residue 228 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 296) chain K residue 11 type BINDING sequence Q description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 297) chain K residue 71 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 298) chain K residue 140 type BINDING sequence S description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 299) chain K residue 144 type BINDING sequence G description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 300) chain K residue 145 type BINDING sequence T description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 301) chain K residue 179 type BINDING sequence T description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 302) chain K residue 206 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 303) chain K residue 228 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 304) chain E residue 206 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 305) chain E residue 228 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 306) chain J residue 11 type BINDING sequence Q description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 307) chain F residue 71 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 308) chain G residue 71 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 309) chain D residue 71 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 310) chain I residue 71 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 311) chain B residue 71 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 312) chain H residue 71 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 313) chain F residue 40 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P99024 source Swiss-Prot : SWS_FT_FI3 314) chain G residue 40 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P99024 source Swiss-Prot : SWS_FT_FI3 315) chain D residue 40 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P99024 source Swiss-Prot : SWS_FT_FI3 316) chain I residue 40 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P99024 source Swiss-Prot : SWS_FT_FI3 317) chain B residue 40 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P99024 source Swiss-Prot : SWS_FT_FI3 318) chain H residue 40 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P99024 source Swiss-Prot : SWS_FT_FI3 319) chain F residue 60 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P99024 source Swiss-Prot : SWS_FT_FI4 320) chain G residue 60 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P99024 source Swiss-Prot : SWS_FT_FI4 321) chain D residue 60 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P99024 source Swiss-Prot : SWS_FT_FI4 322) chain I residue 60 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P99024 source Swiss-Prot : SWS_FT_FI4 323) chain B residue 60 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P99024 source Swiss-Prot : SWS_FT_FI4 324) chain H residue 60 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P99024 source Swiss-Prot : SWS_FT_FI4 325) chain F residue 174 type MOD_RES sequence S description Phosphoserine; by CDK1 => ECO:0000250|UniProtKB:Q13885 source Swiss-Prot : SWS_FT_FI5 326) chain G residue 174 type MOD_RES sequence S description Phosphoserine; by CDK1 => ECO:0000250|UniProtKB:Q13885 source Swiss-Prot : SWS_FT_FI5 327) chain D residue 174 type MOD_RES sequence S description Phosphoserine; by CDK1 => ECO:0000250|UniProtKB:Q13885 source Swiss-Prot : SWS_FT_FI5 328) chain I residue 174 type MOD_RES sequence S description Phosphoserine; by CDK1 => ECO:0000250|UniProtKB:Q13885 source Swiss-Prot : SWS_FT_FI5 329) chain B residue 174 type MOD_RES sequence S description Phosphoserine; by CDK1 => ECO:0000250|UniProtKB:Q13885 source Swiss-Prot : SWS_FT_FI5 330) chain H residue 174 type MOD_RES sequence S description Phosphoserine; by CDK1 => ECO:0000250|UniProtKB:Q13885 source Swiss-Prot : SWS_FT_FI5 331) chain L residue 48 type MOD_RES sequence S description Phosphoserine; by CDK1 => ECO:0000250|UniProtKB:Q13885 source Swiss-Prot : SWS_FT_FI5 332) chain L residue 232 type MOD_RES sequence S description Phosphoserine; by CDK1 => ECO:0000250|UniProtKB:Q13885 source Swiss-Prot : SWS_FT_FI5 333) chain A residue 48 type MOD_RES sequence S description Phosphoserine; by CDK1 => ECO:0000250|UniProtKB:Q13885 source Swiss-Prot : SWS_FT_FI5 334) chain A residue 232 type MOD_RES sequence S description Phosphoserine; by CDK1 => ECO:0000250|UniProtKB:Q13885 source Swiss-Prot : SWS_FT_FI5 335) chain K residue 48 type MOD_RES sequence S description Phosphoserine; by CDK1 => ECO:0000250|UniProtKB:Q13885 source Swiss-Prot : SWS_FT_FI5 336) chain K residue 232 type MOD_RES sequence S description Phosphoserine; by CDK1 => ECO:0000250|UniProtKB:Q13885 source Swiss-Prot : SWS_FT_FI5 337) chain B residue 292 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:P07437 source Swiss-Prot : SWS_FT_FI6 338) chain H residue 287 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:P07437 source Swiss-Prot : SWS_FT_FI6 339) chain H residue 292 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:P07437 source Swiss-Prot : SWS_FT_FI6 340) chain I residue 287 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:P07437 source Swiss-Prot : SWS_FT_FI6 341) chain I residue 292 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:P07437 source Swiss-Prot : SWS_FT_FI6 342) chain B residue 287 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:P07437 source Swiss-Prot : SWS_FT_FI6 343) chain F residue 287 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:P07437 source Swiss-Prot : SWS_FT_FI6 344) chain F residue 292 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:P07437 source Swiss-Prot : SWS_FT_FI6 345) chain G residue 287 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:P07437 source Swiss-Prot : SWS_FT_FI6 346) chain G residue 292 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:P07437 source Swiss-Prot : SWS_FT_FI6 347) chain D residue 287 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:P07437 source Swiss-Prot : SWS_FT_FI6 348) chain D residue 292 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:P07437 source Swiss-Prot : SWS_FT_FI6 349) chain F residue 320 type MOD_RES sequence R description Omega-N-methylarginine => ECO:0000250|UniProtKB:P07437 source Swiss-Prot : SWS_FT_FI7 350) chain G residue 320 type MOD_RES sequence R description Omega-N-methylarginine => ECO:0000250|UniProtKB:P07437 source Swiss-Prot : SWS_FT_FI7 351) chain D residue 320 type MOD_RES sequence R description Omega-N-methylarginine => ECO:0000250|UniProtKB:P07437 source Swiss-Prot : SWS_FT_FI7 352) chain I residue 320 type MOD_RES sequence R description Omega-N-methylarginine => ECO:0000250|UniProtKB:P07437 source Swiss-Prot : SWS_FT_FI7 353) chain B residue 320 type MOD_RES sequence R description Omega-N-methylarginine => ECO:0000250|UniProtKB:P07437 source Swiss-Prot : SWS_FT_FI7 354) chain H residue 320 type MOD_RES sequence R description Omega-N-methylarginine => ECO:0000250|UniProtKB:P07437 source Swiss-Prot : SWS_FT_FI7 355) chain E residue 142-148 type prosite sequence GGGTGSG description TUBULIN Tubulin subunits alpha, beta, and gamma signature. GGGTGSG source prosite : PS00227 356) chain F residue 142-148 type prosite sequence GGGTGSG description TUBULIN Tubulin subunits alpha, beta, and gamma signature. GGGTGSG source prosite : PS00227 357) chain F residue 1-4 type prosite sequence MREI description TUBULIN_B_AUTOREG Tubulin-beta mRNA autoregulation signal. MREI source prosite : PS00228

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