eF-site ID 3jar-ABCDEFGHIJKLMN PDB Code 3jar Chain A, B, C, D, E, F, G, H, I, J, K, L, M, N Title Cryo-EM structure of GDP-microtubule co-polymerized with EB3 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 GEGMEEGEFSEAREDMAALEKDYEEVGVDSVE B:  MREIVHIQAGQCGNQIGAKFWEVISDEHGIDPTGSYHGDS DLQLERINVYYNEAAGNKYVPRAILVDLEPGTMDSVRSGP FGQIFRPDNFVFGQSGAGNNWAKGHYTEGAELVDSVLDVV RKESESCDCLQGFQLTHSLGGGTGSGMGTLLISKIREEYP DRIMNTFSVVPSPKVSDTVVEPYNATLSVHQLVENTDETY CIDNEALYDICFRTLKLTTPTYGDLNHLVSATMSGVTTCL RFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTSRGSQQ YRALTVPELTQQMFDAKNMMAACDPRHGRYLTVAAVFRGR MSMKEVDEQMLNVQNKNSSYFVEWIPNNVKTAVCDIPPRG LKMSATFIGNSTAIQELFKRISEQFTAMFRRKAFLHWYTG EGMDEMEFTEAESNMNDLVSEYQQYQDAT C:  MRECISIHVGQAGVQIGNACWELYCLEHGIQPDGQMPDSF NTFFSETGAGKHVPRAVFVDLEPTVIDEVRTGTYRQLFHP EQLITGKEDAANNYARGHYTIGKEIIDLVLDRIRKLADQC TGLQGFLVFHSFGGGTGSGFTSLLMERLSVDYGKKSKLEF SIYPAPQVSTAVVEPYNSILTTHTTLEHSDCAFMVDNEAI YDICRRNLDIERPTYTNLNRLISQIVSSITASLRFDGALN VDLTEFQTNLVPYPRIHFPLATYAPVISAEKAYHEQLSVA EITNACFEPANQMVKCDPRHGKYMACCLLYRGDVVPKDVN AAIATIKTKRSIQFVDWCPTGFKVGINYQPPTVVPGGDLA KVQRAVCMLSNTTAIAEAWARLDHKFDLMYAKRAFVHWYV GEGMEEGEFSEAREDMAALEKDYEEVGVDSVE D:  MREIVHIQAGQCGNQIGAKFWEVISDEHGIDPTGSYHGDS DLQLERINVYYNEAAGNKYVPRAILVDLEPGTMDSVRSGP FGQIFRPDNFVFGQSGAGNNWAKGHYTEGAELVDSVLDVV RKESESCDCLQGFQLTHSLGGGTGSGMGTLLISKIREEYP DRIMNTFSVVPSPKVSDTVVEPYNATLSVHQLVENTDETY CIDNEALYDICFRTLKLTTPTYGDLNHLVSATMSGVTTCL RFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTSRGSQQ YRALTVPELTQQMFDAKNMMAACDPRHGRYLTVAAVFRGR MSMKEVDEQMLNVQNKNSSYFVEWIPNNVKTAVCDIPPRG LKMSATFIGNSTAIQELFKRISEQFTAMFRRKAFLHWYTG EGMDEMEFTEAESNMNDLVSEYQQYQDAT E:  MRECISIHVGQAGVQIGNACWELYCLEHGIQPDGQMPDSF NTFFSETGAGKHVPRAVFVDLEPTVIDEVRTGTYRQLFHP EQLITGKEDAANNYARGHYTIGKEIIDLVLDRIRKLADQC TGLQGFLVFHSFGGGTGSGFTSLLMERLSVDYGKKSKLEF SIYPAPQVSTAVVEPYNSILTTHTTLEHSDCAFMVDNEAI YDICRRNLDIERPTYTNLNRLISQIVSSITASLRFDGALN VDLTEFQTNLVPYPRIHFPLATYAPVISAEKAYHEQLSVA EITNACFEPANQMVKCDPRHGKYMACCLLYRGDVVPKDVN AAIATIKTKRSIQFVDWCPTGFKVGINYQPPTVVPGGDLA KVQRAVCMLSNTTAIAEAWARLDHKFDLMYAKRAFVHWYV GEGMEEGEFSEAREDMAALEKDYEEVGVDSVE F:  MREIVHIQAGQCGNQIGAKFWEVISDEHGIDPTGSYHGDS DLQLERINVYYNEAAGNKYVPRAILVDLEPGTMDSVRSGP FGQIFRPDNFVFGQSGAGNNWAKGHYTEGAELVDSVLDVV RKESESCDCLQGFQLTHSLGGGTGSGMGTLLISKIREEYP DRIMNTFSVVPSPKVSDTVVEPYNATLSVHQLVENTDETY CIDNEALYDICFRTLKLTTPTYGDLNHLVSATMSGVTTCL RFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTSRGSQQ YRALTVPELTQQMFDAKNMMAACDPRHGRYLTVAAVFRGR MSMKEVDEQMLNVQNKNSSYFVEWIPNNVKTAVCDIPPRG LKMSATFIGNSTAIQELFKRISEQFTAMFRRKAFLHWYTG EGMDEMEFTEAESNMNDLVSEYQQYQDAT G:  MREIVHIQAGQCGNQIGAKFWEVISDEHGIDPTGSYHGDS DLQLERINVYYNEAAGNKYVPRAILVDLEPGTMDSVRSGP FGQIFRPDNFVFGQSGAGNNWAKGHYTEGAELVDSVLDVV RKESESCDCLQGFQLTHSLGGGTGSGMGTLLISKIREEYP DRIMNTFSVVPSPKVSDTVVEPYNATLSVHQLVENTDETY CIDNEALYDICFRTLKLTTPTYGDLNHLVSATMSGVTTCL RFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTSRGSQQ YRALTVPELTQQMFDAKNMMAACDPRHGRYLTVAAVFRGR MSMKEVDEQMLNVQNKNSSYFVEWIPNNVKTAVCDIPPRG LKMSATFIGNSTAIQELFKRISEQFTAMFRRKAFLHWYTG EGMDEMEFTEAESNMNDLVSEYQQYQDAT H:  MREIVHIQAGQCGNQIGAKFWEVISDEHGIDPTGSYHGDS DLQLERINVYYNEAAGNKYVPRAILVDLEPGTMDSVRSGP FGQIFRPDNFVFGQSGAGNNWAKGHYTEGAELVDSVLDVV RKESESCDCLQGFQLTHSLGGGTGSGMGTLLISKIREEYP DRIMNTFSVVPSPKVSDTVVEPYNATLSVHQLVENTDETY CIDNEALYDICFRTLKLTTPTYGDLNHLVSATMSGVTTCL RFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTSRGSQQ YRALTVPELTQQMFDAKNMMAACDPRHGRYLTVAAVFRGR MSMKEVDEQMLNVQNKNSSYFVEWIPNNVKTAVCDIPPRG LKMSATFIGNSTAIQELFKRISEQFTAMFRRKAFLHWYTG EGMDEMEFTEAESNMNDLVSEYQQYQDAT I:  MREIVHIQAGQCGNQIGAKFWEVISDEHGIDPTGSYHGDS DLQLERINVYYNEAAGNKYVPRAILVDLEPGTMDSVRSGP FGQIFRPDNFVFGQSGAGNNWAKGHYTEGAELVDSVLDVV RKESESCDCLQGFQLTHSLGGGTGSGMGTLLISKIREEYP DRIMNTFSVVPSPKVSDTVVEPYNATLSVHQLVENTDETY CIDNEALYDICFRTLKLTTPTYGDLNHLVSATMSGVTTCL RFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTSRGSQQ YRALTVPELTQQMFDAKNMMAACDPRHGRYLTVAAVFRGR MSMKEVDEQMLNVQNKNSSYFVEWIPNNVKTAVCDIPPRG LKMSATFIGNSTAIQELFKRISEQFTAMFRRKAFLHWYTG EGMDEMEFTEAESNMNDLVSEYQQYQDAT J:  MRECISIHVGQAGVQIGNACWELYCLEHGIQPDGQMPDSF NTFFSETGAGKHVPRAVFVDLEPTVIDEVRTGTYRQLFHP EQLITGKEDAANNYARGHYTIGKEIIDLVLDRIRKLADQC TGLQGFLVFHSFGGGTGSGFTSLLMERLSVDYGKKSKLEF SIYPAPQVSTAVVEPYNSILTTHTTLEHSDCAFMVDNEAI YDICRRNLDIERPTYTNLNRLISQIVSSITASLRFDGALN VDLTEFQTNLVPYPRIHFPLATYAPVISAEKAYHEQLSVA EITNACFEPANQMVKCDPRHGKYMACCLLYRGDVVPKDVN AAIATIKTKRSIQFVDWCPTGFKVGINYQPPTVVPGGDLA KVQRAVCMLSNTTAIAEAWARLDHKFDLMYAKRAFVHWYV GEGMEEGEFSEAREDMAALEKDYEEVGVDSVE K:  MRECISIHVGQAGVQIGNACWELYCLEHGIQPDGQMPDSF NTFFSETGAGKHVPRAVFVDLEPTVIDEVRTGTYRQLFHP EQLITGKEDAANNYARGHYTIGKEIIDLVLDRIRKLADQC TGLQGFLVFHSFGGGTGSGFTSLLMERLSVDYGKKSKLEF SIYPAPQVSTAVVEPYNSILTTHTTLEHSDCAFMVDNEAI YDICRRNLDIERPTYTNLNRLISQIVSSITASLRFDGALN VDLTEFQTNLVPYPRIHFPLATYAPVISAEKAYHEQLSVA EITNACFEPANQMVKCDPRHGKYMACCLLYRGDVVPKDVN AAIATIKTKRSIQFVDWCPTGFKVGINYQPPTVVPGGDLA KVQRAVCMLSNTTAIAEAWARLDHKFDLMYAKRAFVHWYV GEGMEEGEFSEAREDMAALEKDYEEVGVDSVE L:  MRECISIHVGQAGVQIGNACWELYCLEHGIQPDGQMPDSF NTFFSETGAGKHVPRAVFVDLEPTVIDEVRTGTYRQLFHP EQLITGKEDAANNYARGHYTIGKEIIDLVLDRIRKLADQC TGLQGFLVFHSFGGGTGSGFTSLLMERLSVDYGKKSKLEF SIYPAPQVSTAVVEPYNSILTTHTTLEHSDCAFMVDNEAI YDICRRNLDIERPTYTNLNRLISQIVSSITASLRFDGALN VDLTEFQTNLVPYPRIHFPLATYAPVISAEKAYHEQLSVA EITNACFEPANQMVKCDPRHGKYMACCLLYRGDVVPKDVN AAIATIKTKRSIQFVDWCPTGFKVGINYQPPTVVPGGDLA KVQRAVCMLSNTTAIAEAWARLDHKFDLMYAKRAFVHWYV GEGMEEGEFSEAREDMAALEKDYEEVGVDSVE M:  MAVNVYSTSVTSENLSRHDMLAWVNDSLHLNYTKIEQLCS GAAYCQFMDMLFPGCVHLRKVKFQAKLEHEYIHNFKVLQA AFKKMGVDKIIPVEKLVKGKFQDNFEFIQWFKKFFDANYD GKDYNPLLARQ N:  MAVNVYSTSVTSENLSRHDMLAWVNDSLHLNYTKIEQLCS GAAYCQFMDMLFPGCVHLRKVKFQAKLEHEYIHNFKVLQA AFKKMGVDKIIPVEKLVKGKFQDNFEFIQWFKKFFDANYD GKDYNPLLARQ 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 98 type sequence D description BINDING SITE FOR RESIDUE GTP E 501 source : AC1 6) chain E residue 99 type sequence A description BINDING SITE FOR RESIDUE GTP E 501 source : AC1 7) chain E residue 100 type sequence A description BINDING SITE FOR RESIDUE GTP E 501 source : AC1 8) chain E residue 101 type sequence N description BINDING SITE FOR RESIDUE GTP E 501 source : AC1 9) chain E residue 140 type sequence S description BINDING SITE FOR RESIDUE GTP E 501 source : AC1 10) chain E residue 143 type sequence G description BINDING SITE FOR RESIDUE GTP E 501 source : AC1 11) chain E residue 144 type sequence G description BINDING SITE FOR RESIDUE GTP E 501 source : AC1 12) chain E residue 145 type sequence T description BINDING SITE FOR RESIDUE GTP E 501 source : AC1 13) chain E residue 146 type sequence G description BINDING SITE FOR RESIDUE GTP E 501 source : AC1 14) chain E residue 171 type sequence I description BINDING SITE FOR RESIDUE GTP E 501 source : AC1 15) chain E residue 179 type sequence T description BINDING SITE FOR RESIDUE GTP E 501 source : AC1 16) chain E residue 183 type sequence E description BINDING SITE FOR RESIDUE GTP E 501 source : AC1 17) chain E residue 206 type sequence N description BINDING SITE FOR RESIDUE GTP E 501 source : AC1 18) chain E residue 224 type sequence Y description BINDING SITE FOR RESIDUE GTP E 501 source : AC1 19) chain E residue 228 type sequence N description BINDING SITE FOR RESIDUE GTP E 501 source : AC1 20) chain G residue 248 type sequence L description BINDING SITE FOR RESIDUE GTP E 501 source : AC1 21) chain G residue 254 type sequence K description BINDING SITE FOR RESIDUE GTP E 501 source : AC1 22) chain E residue 71 type sequence E description BINDING SITE FOR RESIDUE MG E 502 source : AC2 23) chain F residue 11 type sequence Q description BINDING SITE FOR RESIDUE GDP F 501 source : AC3 24) chain F residue 12 type sequence C description BINDING SITE FOR RESIDUE GDP F 501 source : AC3 25) chain F residue 15 type sequence Q description BINDING SITE FOR RESIDUE GDP F 501 source : AC3 26) chain F residue 140 type sequence S description BINDING SITE FOR RESIDUE GDP F 501 source : AC3 27) chain F residue 143 type sequence G description BINDING SITE FOR RESIDUE GDP F 501 source : AC3 28) chain F residue 144 type sequence G description BINDING SITE FOR RESIDUE GDP F 501 source : AC3 29) chain F residue 145 type sequence T description BINDING SITE FOR RESIDUE GDP F 501 source : AC3 30) chain F residue 146 type sequence G description BINDING SITE FOR RESIDUE GDP F 501 source : AC3 31) chain F residue 179 type sequence D description BINDING SITE FOR RESIDUE GDP F 501 source : AC3 32) chain F residue 206 type sequence N description BINDING SITE FOR RESIDUE GDP F 501 source : AC3 33) chain F residue 224 type sequence Y description BINDING SITE FOR RESIDUE GDP F 501 source : AC3 34) chain F residue 228 type sequence N description BINDING SITE FOR RESIDUE GDP F 501 source : AC3 35) chain F residue 248 type sequence L description BINDING SITE FOR RESIDUE GTP J 501 source : AC4 36) chain F residue 254 type sequence K description BINDING SITE FOR RESIDUE GTP J 501 source : AC4 37) chain J residue 11 type sequence Q description BINDING SITE FOR RESIDUE GTP J 501 source : AC4 38) chain J residue 12 type sequence A description BINDING SITE FOR RESIDUE GTP J 501 source : AC4 39) chain J residue 15 type sequence Q description BINDING SITE FOR RESIDUE GTP J 501 source : AC4 40) chain J residue 99 type sequence A description BINDING SITE FOR RESIDUE GTP J 501 source : AC4 41) chain J residue 101 type sequence N description BINDING SITE FOR RESIDUE GTP J 501 source : AC4 42) chain J residue 140 type sequence S description BINDING SITE FOR RESIDUE GTP J 501 source : AC4 43) chain J residue 143 type sequence G description BINDING SITE FOR RESIDUE GTP J 501 source : AC4 44) chain J residue 144 type sequence G description BINDING SITE FOR RESIDUE GTP J 501 source : AC4 45) chain J residue 145 type sequence T description BINDING SITE FOR RESIDUE GTP J 501 source : AC4 46) chain J residue 146 type sequence G description BINDING SITE FOR RESIDUE GTP J 501 source : AC4 47) chain J residue 171 type sequence I description BINDING SITE FOR RESIDUE GTP J 501 source : AC4 48) chain J residue 179 type sequence T description BINDING SITE FOR RESIDUE GTP J 501 source : AC4 49) chain J residue 183 type sequence E description BINDING SITE FOR RESIDUE GTP J 501 source : AC4 50) chain J residue 206 type sequence N description BINDING SITE FOR RESIDUE GTP J 501 source : AC4 51) chain J residue 224 type sequence Y description BINDING SITE FOR RESIDUE GTP J 501 source : AC4 52) chain J residue 228 type sequence N description BINDING SITE FOR RESIDUE GTP J 501 source : AC4 53) chain J residue 71 type sequence E description BINDING SITE FOR RESIDUE MG J 502 source : AC5 54) chain G residue 11 type sequence Q description BINDING SITE FOR RESIDUE GDP G 501 source : AC6 55) chain G residue 12 type sequence C description BINDING SITE FOR RESIDUE GDP G 501 source : AC6 56) chain G residue 15 type sequence Q description BINDING SITE FOR RESIDUE GDP G 501 source : AC6 57) chain G residue 140 type sequence S description BINDING SITE FOR RESIDUE GDP G 501 source : AC6 58) chain G residue 143 type sequence G description BINDING SITE FOR RESIDUE GDP G 501 source : AC6 59) chain G residue 144 type sequence G description BINDING SITE FOR RESIDUE GDP G 501 source : AC6 60) chain G residue 145 type sequence T description BINDING SITE FOR RESIDUE GDP G 501 source : AC6 61) chain G residue 146 type sequence G description BINDING SITE FOR RESIDUE GDP G 501 source : AC6 62) chain G residue 179 type sequence D description BINDING SITE FOR RESIDUE GDP G 501 source : AC6 63) chain G residue 206 type sequence N description BINDING SITE FOR RESIDUE GDP G 501 source : AC6 64) chain G residue 224 type sequence Y description BINDING SITE FOR RESIDUE GDP G 501 source : AC6 65) chain G residue 228 type sequence N description BINDING SITE FOR RESIDUE GDP G 501 source : AC6 66) chain C residue 11 type sequence Q description BINDING SITE FOR RESIDUE GTP C 501 source : AC7 67) chain C residue 12 type sequence A description BINDING SITE FOR RESIDUE GTP C 501 source : AC7 68) chain C residue 15 type sequence Q description BINDING SITE FOR RESIDUE GTP C 501 source : AC7 69) chain C residue 99 type sequence A description BINDING SITE FOR RESIDUE GTP C 501 source : AC7 70) chain C residue 100 type sequence A description BINDING SITE FOR RESIDUE GTP C 501 source : AC7 71) chain C residue 101 type sequence N description BINDING SITE FOR RESIDUE GTP C 501 source : AC7 72) chain C residue 140 type sequence S description BINDING SITE FOR RESIDUE GTP C 501 source : AC7 73) chain C residue 143 type sequence G description BINDING SITE FOR RESIDUE GTP C 501 source : AC7 74) chain C residue 144 type sequence G description BINDING SITE FOR RESIDUE GTP C 501 source : AC7 75) chain C residue 145 type sequence T description BINDING SITE FOR RESIDUE GTP C 501 source : AC7 76) chain C residue 146 type sequence G description BINDING SITE FOR RESIDUE GTP C 501 source : AC7 77) chain C residue 171 type sequence I description BINDING SITE FOR RESIDUE GTP C 501 source : AC7 78) chain C residue 179 type sequence T description BINDING SITE FOR RESIDUE GTP C 501 source : AC7 79) chain C residue 183 type sequence E description BINDING SITE FOR RESIDUE GTP C 501 source : AC7 80) chain C residue 206 type sequence N description BINDING SITE FOR RESIDUE GTP C 501 source : AC7 81) chain C residue 224 type sequence Y description BINDING SITE FOR RESIDUE GTP C 501 source : AC7 82) chain C residue 228 type sequence N description BINDING SITE FOR RESIDUE GTP C 501 source : AC7 83) chain I residue 248 type sequence L description BINDING SITE FOR RESIDUE GTP C 501 source : AC7 84) chain I residue 254 type sequence K description BINDING SITE FOR RESIDUE GTP C 501 source : AC7 85) chain C residue 71 type sequence E description BINDING SITE FOR RESIDUE MG C 502 source : AC8 86) chain D residue 11 type sequence Q description BINDING SITE FOR RESIDUE GDP D 501 source : AC9 87) chain D residue 12 type sequence C description BINDING SITE FOR RESIDUE GDP D 501 source : AC9 88) chain D residue 15 type sequence Q description BINDING SITE FOR RESIDUE GDP D 501 source : AC9 89) chain D residue 140 type sequence S description BINDING SITE FOR RESIDUE GDP D 501 source : AC9 90) chain D residue 143 type sequence G description BINDING SITE FOR RESIDUE GDP D 501 source : AC9 91) chain D residue 144 type sequence G description BINDING SITE FOR RESIDUE GDP D 501 source : AC9 92) chain D residue 145 type sequence T description BINDING SITE FOR RESIDUE GDP D 501 source : AC9 93) chain D residue 146 type sequence G description BINDING SITE FOR RESIDUE GDP D 501 source : AC9 94) chain D residue 179 type sequence D description BINDING SITE FOR RESIDUE GDP D 501 source : AC9 95) chain D residue 206 type sequence N description BINDING SITE FOR RESIDUE GDP D 501 source : AC9 96) chain D residue 224 type sequence Y description BINDING SITE FOR RESIDUE GDP D 501 source : AC9 97) chain D residue 228 type sequence N description BINDING SITE FOR RESIDUE GDP D 501 source : AC9 98) chain D residue 248 type sequence L description BINDING SITE FOR RESIDUE GTP L 501 source : BC1 99) chain D residue 254 type sequence K description BINDING SITE FOR RESIDUE GTP L 501 source : BC1 100) chain L residue 11 type sequence Q description BINDING SITE FOR RESIDUE GTP L 501 source : BC1 101) chain L residue 12 type sequence A description BINDING SITE FOR RESIDUE GTP L 501 source : BC1 102) chain L residue 15 type sequence Q description BINDING SITE FOR RESIDUE GTP L 501 source : BC1 103) chain L residue 99 type sequence A description BINDING SITE FOR RESIDUE GTP L 501 source : BC1 104) chain L residue 101 type sequence N description BINDING SITE FOR RESIDUE GTP L 501 source : BC1 105) chain L residue 140 type sequence S description BINDING SITE FOR RESIDUE GTP L 501 source : BC1 106) chain L residue 143 type sequence G description BINDING SITE FOR RESIDUE GTP L 501 source : BC1 107) chain L residue 144 type sequence G description BINDING SITE FOR RESIDUE GTP L 501 source : BC1 108) chain L residue 145 type sequence T description BINDING SITE FOR RESIDUE GTP L 501 source : BC1 109) chain L residue 146 type sequence G description BINDING SITE FOR RESIDUE GTP L 501 source : BC1 110) chain L residue 171 type sequence I description BINDING SITE FOR RESIDUE GTP L 501 source : BC1 111) chain L residue 179 type sequence T description BINDING SITE FOR RESIDUE GTP L 501 source : BC1 112) chain L residue 183 type sequence E description BINDING SITE FOR RESIDUE GTP L 501 source : BC1 113) chain L residue 206 type sequence N description BINDING SITE FOR RESIDUE GTP L 501 source : BC1 114) chain L residue 224 type sequence Y description BINDING SITE FOR RESIDUE GTP L 501 source : BC1 115) chain L residue 228 type sequence N description BINDING SITE FOR RESIDUE GTP L 501 source : BC1 116) chain L residue 71 type sequence E description BINDING SITE FOR RESIDUE MG L 502 source : BC2 117) chain I residue 11 type sequence Q description BINDING SITE FOR RESIDUE GDP I 501 source : BC3 118) chain I residue 12 type sequence C description BINDING SITE FOR RESIDUE GDP I 501 source : BC3 119) chain I residue 15 type sequence Q description BINDING SITE FOR RESIDUE GDP I 501 source : BC3 120) chain I residue 140 type sequence S description BINDING SITE FOR RESIDUE GDP I 501 source : BC3 121) chain I residue 143 type sequence G description BINDING SITE FOR RESIDUE GDP I 501 source : BC3 122) chain I residue 144 type sequence G description BINDING SITE FOR RESIDUE GDP I 501 source : BC3 123) chain I residue 145 type sequence T description BINDING SITE FOR RESIDUE GDP I 501 source : BC3 124) chain I residue 146 type sequence G description BINDING SITE FOR RESIDUE GDP I 501 source : BC3 125) chain I residue 179 type sequence D description BINDING SITE FOR RESIDUE GDP I 501 source : BC3 126) chain I residue 206 type sequence N description BINDING SITE FOR RESIDUE GDP I 501 source : BC3 127) chain I residue 224 type sequence Y description BINDING SITE FOR RESIDUE GDP I 501 source : BC3 128) chain I residue 228 type sequence N description BINDING SITE FOR RESIDUE GDP I 501 source : BC3 129) chain A residue 11 type sequence Q description BINDING SITE FOR RESIDUE GTP A 501 source : BC4 130) chain A residue 12 type sequence A description BINDING SITE FOR RESIDUE GTP A 501 source : BC4 131) chain A residue 15 type sequence Q description BINDING SITE FOR RESIDUE GTP A 501 source : BC4 132) chain A residue 98 type sequence D description BINDING SITE FOR RESIDUE GTP A 501 source : BC4 133) chain A residue 99 type sequence A description BINDING SITE FOR RESIDUE GTP A 501 source : BC4 134) chain A residue 100 type sequence A description BINDING SITE FOR RESIDUE GTP A 501 source : BC4 135) chain A residue 101 type sequence N description BINDING SITE FOR RESIDUE GTP A 501 source : BC4 136) chain A residue 140 type sequence S description BINDING SITE FOR RESIDUE GTP A 501 source : BC4 137) chain A residue 143 type sequence G description BINDING SITE FOR RESIDUE GTP A 501 source : BC4 138) chain A residue 144 type sequence G description BINDING SITE FOR RESIDUE GTP A 501 source : BC4 139) chain A residue 145 type sequence T description BINDING SITE FOR RESIDUE GTP A 501 source : BC4 140) chain A residue 146 type sequence G description BINDING SITE FOR RESIDUE GTP A 501 source : BC4 141) chain A residue 171 type sequence I description BINDING SITE FOR RESIDUE GTP A 501 source : BC4 142) chain A residue 179 type sequence T description BINDING SITE FOR RESIDUE GTP A 501 source : BC4 143) chain A residue 183 type sequence E description BINDING SITE FOR RESIDUE GTP A 501 source : BC4 144) chain A residue 206 type sequence N description BINDING SITE FOR RESIDUE GTP A 501 source : BC4 145) chain A residue 224 type sequence Y description BINDING SITE FOR RESIDUE GTP A 501 source : BC4 146) chain A residue 228 type sequence N description BINDING SITE FOR RESIDUE GTP A 501 source : BC4 147) chain H residue 248 type sequence L description BINDING SITE FOR RESIDUE GTP A 501 source : BC4 148) chain H residue 254 type sequence K description BINDING SITE FOR RESIDUE GTP A 501 source : BC4 149) chain A residue 71 type sequence E description BINDING SITE FOR RESIDUE MG A 502 source : BC5 150) chain B residue 11 type sequence Q description BINDING SITE FOR RESIDUE GDP B 501 source : BC6 151) chain B residue 12 type sequence C description BINDING SITE FOR RESIDUE GDP B 501 source : BC6 152) chain B residue 15 type sequence Q description BINDING SITE FOR RESIDUE GDP B 501 source : BC6 153) chain B residue 140 type sequence S description BINDING SITE FOR RESIDUE GDP B 501 source : BC6 154) chain B residue 143 type sequence G description BINDING SITE FOR RESIDUE GDP B 501 source : BC6 155) chain B residue 144 type sequence G description BINDING SITE FOR RESIDUE GDP B 501 source : BC6 156) chain B residue 145 type sequence T description BINDING SITE FOR RESIDUE GDP B 501 source : BC6 157) chain B residue 146 type sequence G description BINDING SITE FOR RESIDUE GDP B 501 source : BC6 158) chain B residue 179 type sequence D description BINDING SITE FOR RESIDUE GDP B 501 source : BC6 159) chain B residue 206 type sequence N description BINDING SITE FOR RESIDUE GDP B 501 source : BC6 160) chain B residue 224 type sequence Y description BINDING SITE FOR RESIDUE GDP B 501 source : BC6 161) chain B residue 228 type sequence N description BINDING SITE FOR RESIDUE GDP B 501 source : BC6 162) chain B residue 248 type sequence L description BINDING SITE FOR RESIDUE GTP K 501 source : BC7 163) chain B residue 254 type sequence K description BINDING SITE FOR RESIDUE GTP K 501 source : BC7 164) chain K residue 11 type sequence Q description BINDING SITE FOR RESIDUE GTP K 501 source : BC7 165) chain K residue 12 type sequence A description BINDING SITE FOR RESIDUE GTP K 501 source : BC7 166) chain K residue 15 type sequence Q description BINDING SITE FOR RESIDUE GTP K 501 source : BC7 167) chain K residue 98 type sequence D description BINDING SITE FOR RESIDUE GTP K 501 source : BC7 168) chain K residue 99 type sequence A description BINDING SITE FOR RESIDUE GTP K 501 source : BC7 169) chain K residue 100 type sequence A description BINDING SITE FOR RESIDUE GTP K 501 source : BC7 170) chain K residue 101 type sequence N description BINDING SITE FOR RESIDUE GTP K 501 source : BC7 171) chain K residue 140 type sequence S description BINDING SITE FOR RESIDUE GTP K 501 source : BC7 172) chain K residue 143 type sequence G description BINDING SITE FOR RESIDUE GTP K 501 source : BC7 173) chain K residue 144 type sequence G description BINDING SITE FOR RESIDUE GTP K 501 source : BC7 174) chain K residue 145 type sequence T description BINDING SITE FOR RESIDUE GTP K 501 source : BC7 175) chain K residue 146 type sequence G description BINDING SITE FOR RESIDUE GTP K 501 source : BC7 176) chain K residue 171 type sequence I description BINDING SITE FOR RESIDUE GTP K 501 source : BC7 177) chain K residue 179 type sequence T description BINDING SITE FOR RESIDUE GTP K 501 source : BC7 178) chain K residue 183 type sequence E description BINDING SITE FOR RESIDUE GTP K 501 source : BC7 179) chain K residue 206 type sequence N description BINDING SITE FOR RESIDUE GTP K 501 source : BC7 180) chain K residue 224 type sequence Y description BINDING SITE FOR RESIDUE GTP K 501 source : BC7 181) chain K residue 228 type sequence N description BINDING SITE FOR RESIDUE GTP K 501 source : BC7 182) chain K residue 71 type sequence E description BINDING SITE FOR RESIDUE MG K 502 source : BC8 183) chain H residue 11 type sequence Q description BINDING SITE FOR RESIDUE GDP H 501 source : BC9 184) chain H residue 12 type sequence C description BINDING SITE FOR RESIDUE GDP H 501 source : BC9 185) chain H residue 15 type sequence Q description BINDING SITE FOR RESIDUE GDP H 501 source : BC9 186) chain H residue 140 type sequence S description BINDING SITE FOR RESIDUE GDP H 501 source : BC9 187) chain H residue 143 type sequence G description BINDING SITE FOR RESIDUE GDP H 501 source : BC9 188) chain H residue 144 type sequence G description BINDING SITE FOR RESIDUE GDP H 501 source : BC9 189) chain H residue 145 type sequence T description BINDING SITE FOR RESIDUE GDP H 501 source : BC9 190) chain H residue 146 type sequence G description BINDING SITE FOR RESIDUE GDP H 501 source : BC9 191) chain H residue 179 type sequence D description BINDING SITE FOR RESIDUE GDP H 501 source : BC9 192) chain H residue 206 type sequence N description BINDING SITE FOR RESIDUE GDP H 501 source : BC9 193) chain H residue 224 type sequence Y description BINDING SITE FOR RESIDUE GDP H 501 source : BC9 194) chain H residue 228 type sequence N description BINDING SITE FOR RESIDUE GDP H 501 source : BC9 195) chain G residue 144 type MOD_RES sequence G description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI1 196) chain G residue 145 type MOD_RES sequence T description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI1 197) chain G residue 146 type MOD_RES sequence G description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI1 198) chain G residue 206 type MOD_RES sequence N description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI1 199) chain G residue 228 type MOD_RES sequence N description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI1 200) chain D residue 11 type MOD_RES sequence Q description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI1 201) chain D residue 140 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI1 202) chain D residue 144 type MOD_RES sequence G description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI1 203) chain D residue 145 type MOD_RES sequence T description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI1 204) chain D residue 146 type MOD_RES sequence G description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI1 205) chain D residue 206 type MOD_RES sequence N description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI1 206) chain D residue 228 type MOD_RES sequence N description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI1 207) chain I residue 11 type MOD_RES sequence Q description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI1 208) chain I residue 140 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI1 209) chain I residue 144 type MOD_RES sequence G description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI1 210) chain I residue 145 type MOD_RES sequence T description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI1 211) chain I residue 146 type MOD_RES sequence G description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI1 212) chain I residue 206 type MOD_RES sequence N description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI1 213) chain I residue 228 type MOD_RES sequence N description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI1 214) chain B residue 11 type MOD_RES sequence Q description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI1 215) chain F residue 144 type MOD_RES sequence G description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI1 216) chain B residue 140 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI1 217) chain B residue 144 type MOD_RES sequence G description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI1 218) chain B residue 145 type MOD_RES sequence T description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI1 219) chain B residue 146 type MOD_RES sequence G description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI1 220) chain B residue 206 type MOD_RES sequence N description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI1 221) chain B residue 228 type MOD_RES sequence N description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI1 222) chain H residue 11 type MOD_RES sequence Q description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI1 223) chain H residue 140 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI1 224) chain H residue 144 type MOD_RES sequence G description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI1 225) chain H residue 145 type MOD_RES sequence T description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI1 226) chain F residue 145 type MOD_RES sequence T description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI1 227) chain H residue 146 type MOD_RES sequence G description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI1 228) chain H residue 206 type MOD_RES sequence N description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI1 229) chain H residue 228 type MOD_RES sequence N description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI1 230) chain F residue 146 type MOD_RES sequence G description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI1 231) chain F residue 206 type MOD_RES sequence N description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI1 232) chain F residue 228 type MOD_RES sequence N description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI1 233) chain G residue 11 type MOD_RES sequence Q description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI1 234) chain G residue 140 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI1 235) chain J residue 71 type MOD_RES sequence E description Phosphoserine => ECO:0000250|UniProtKB:Q6PER3 source Swiss-Prot : SWS_FT_FI2 236) chain J residue 140 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:Q6PER3 source Swiss-Prot : SWS_FT_FI2 237) chain J residue 144 type MOD_RES sequence G description Phosphoserine => ECO:0000250|UniProtKB:Q6PER3 source Swiss-Prot : SWS_FT_FI2 238) chain J residue 145 type MOD_RES sequence T description Phosphoserine => ECO:0000250|UniProtKB:Q6PER3 source Swiss-Prot : SWS_FT_FI2 239) chain J residue 179 type MOD_RES sequence T description Phosphoserine => ECO:0000250|UniProtKB:Q6PER3 source Swiss-Prot : SWS_FT_FI2 240) chain J residue 206 type MOD_RES sequence N description Phosphoserine => ECO:0000250|UniProtKB:Q6PER3 source Swiss-Prot : SWS_FT_FI2 241) chain J residue 228 type MOD_RES sequence N description Phosphoserine => ECO:0000250|UniProtKB:Q6PER3 source Swiss-Prot : SWS_FT_FI2 242) chain C residue 11 type MOD_RES sequence Q description Phosphoserine => ECO:0000250|UniProtKB:Q6PER3 source Swiss-Prot : SWS_FT_FI2 243) chain C residue 71 type MOD_RES sequence E description Phosphoserine => ECO:0000250|UniProtKB:Q6PER3 source Swiss-Prot : SWS_FT_FI2 244) chain C residue 140 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:Q6PER3 source Swiss-Prot : SWS_FT_FI2 245) chain C residue 144 type MOD_RES sequence G description Phosphoserine => ECO:0000250|UniProtKB:Q6PER3 source Swiss-Prot : SWS_FT_FI2 246) chain C residue 145 type MOD_RES sequence T description Phosphoserine => ECO:0000250|UniProtKB:Q6PER3 source Swiss-Prot : SWS_FT_FI2 247) chain C residue 179 type MOD_RES sequence T description Phosphoserine => ECO:0000250|UniProtKB:Q6PER3 source Swiss-Prot : SWS_FT_FI2 248) chain C residue 206 type MOD_RES sequence N description Phosphoserine => ECO:0000250|UniProtKB:Q6PER3 source Swiss-Prot : SWS_FT_FI2 249) chain C residue 228 type MOD_RES sequence N description Phosphoserine => ECO:0000250|UniProtKB:Q6PER3 source Swiss-Prot : SWS_FT_FI2 250) chain L residue 11 type MOD_RES sequence Q description Phosphoserine => ECO:0000250|UniProtKB:Q6PER3 source Swiss-Prot : SWS_FT_FI2 251) chain L residue 71 type MOD_RES sequence E description Phosphoserine => ECO:0000250|UniProtKB:Q6PER3 source Swiss-Prot : SWS_FT_FI2 252) chain L residue 140 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:Q6PER3 source Swiss-Prot : SWS_FT_FI2 253) chain L residue 144 type MOD_RES sequence G description Phosphoserine => ECO:0000250|UniProtKB:Q6PER3 source Swiss-Prot : SWS_FT_FI2 254) chain L residue 145 type MOD_RES sequence T description Phosphoserine => ECO:0000250|UniProtKB:Q6PER3 source Swiss-Prot : SWS_FT_FI2 255) chain D residue 71 type MOD_RES sequence E description Phosphoserine => ECO:0000250|UniProtKB:Q6PER3 source Swiss-Prot : SWS_FT_FI2 256) chain L residue 179 type MOD_RES sequence T description Phosphoserine => ECO:0000250|UniProtKB:Q6PER3 source Swiss-Prot : SWS_FT_FI2 257) chain L residue 206 type MOD_RES sequence N description Phosphoserine => ECO:0000250|UniProtKB:Q6PER3 source Swiss-Prot : SWS_FT_FI2 258) chain L residue 228 type MOD_RES sequence N description Phosphoserine => ECO:0000250|UniProtKB:Q6PER3 source Swiss-Prot : SWS_FT_FI2 259) chain A residue 11 type MOD_RES sequence Q description Phosphoserine => ECO:0000250|UniProtKB:Q6PER3 source Swiss-Prot : SWS_FT_FI2 260) chain A residue 71 type MOD_RES sequence E description Phosphoserine => ECO:0000250|UniProtKB:Q6PER3 source Swiss-Prot : SWS_FT_FI2 261) chain A residue 140 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:Q6PER3 source Swiss-Prot : SWS_FT_FI2 262) chain A residue 144 type MOD_RES sequence G description Phosphoserine => ECO:0000250|UniProtKB:Q6PER3 source Swiss-Prot : SWS_FT_FI2 263) chain A residue 145 type MOD_RES sequence T description Phosphoserine => ECO:0000250|UniProtKB:Q6PER3 source Swiss-Prot : SWS_FT_FI2 264) chain A residue 179 type MOD_RES sequence T description Phosphoserine => ECO:0000250|UniProtKB:Q6PER3 source Swiss-Prot : SWS_FT_FI2 265) chain A residue 206 type MOD_RES sequence N description Phosphoserine => ECO:0000250|UniProtKB:Q6PER3 source Swiss-Prot : SWS_FT_FI2 266) chain I residue 71 type MOD_RES sequence E description Phosphoserine => ECO:0000250|UniProtKB:Q6PER3 source Swiss-Prot : SWS_FT_FI2 267) chain A residue 228 type MOD_RES sequence N description Phosphoserine => ECO:0000250|UniProtKB:Q6PER3 source Swiss-Prot : SWS_FT_FI2 268) chain K residue 11 type MOD_RES sequence Q description Phosphoserine => ECO:0000250|UniProtKB:Q6PER3 source Swiss-Prot : SWS_FT_FI2 269) chain K residue 71 type MOD_RES sequence E description Phosphoserine => ECO:0000250|UniProtKB:Q6PER3 source Swiss-Prot : SWS_FT_FI2 270) chain K residue 140 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:Q6PER3 source Swiss-Prot : SWS_FT_FI2 271) chain K residue 144 type MOD_RES sequence G description Phosphoserine => ECO:0000250|UniProtKB:Q6PER3 source Swiss-Prot : SWS_FT_FI2 272) chain K residue 145 type MOD_RES sequence T description Phosphoserine => ECO:0000250|UniProtKB:Q6PER3 source Swiss-Prot : SWS_FT_FI2 273) chain K residue 179 type MOD_RES sequence T description Phosphoserine => ECO:0000250|UniProtKB:Q6PER3 source Swiss-Prot : SWS_FT_FI2 274) chain K residue 206 type MOD_RES sequence N description Phosphoserine => ECO:0000250|UniProtKB:Q6PER3 source Swiss-Prot : SWS_FT_FI2 275) chain K residue 228 type MOD_RES sequence N description Phosphoserine => ECO:0000250|UniProtKB:Q6PER3 source Swiss-Prot : SWS_FT_FI2 276) chain B residue 71 type MOD_RES sequence E description Phosphoserine => ECO:0000250|UniProtKB:Q6PER3 source Swiss-Prot : SWS_FT_FI2 277) chain H residue 71 type MOD_RES sequence E description Phosphoserine => ECO:0000250|UniProtKB:Q6PER3 source Swiss-Prot : SWS_FT_FI2 278) chain E residue 206 type MOD_RES sequence N description Phosphoserine => ECO:0000250|UniProtKB:Q6PER3 source Swiss-Prot : SWS_FT_FI2 279) chain E residue 228 type MOD_RES sequence N description Phosphoserine => ECO:0000250|UniProtKB:Q6PER3 source Swiss-Prot : SWS_FT_FI2 280) chain J residue 11 type MOD_RES sequence Q description Phosphoserine => ECO:0000250|UniProtKB:Q6PER3 source Swiss-Prot : SWS_FT_FI2 281) 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 282) 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 283) 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 284) 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 285) 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 286) 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 287) 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 288) 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 289) 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 290) 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 291) 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 292) 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 293) chain F residue 40 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P99024 source Swiss-Prot : SWS_FT_FI3 294) chain G residue 40 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P99024 source Swiss-Prot : SWS_FT_FI3 295) chain D residue 40 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P99024 source Swiss-Prot : SWS_FT_FI3 296) chain I residue 40 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P99024 source Swiss-Prot : SWS_FT_FI3 297) chain B residue 40 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P99024 source Swiss-Prot : SWS_FT_FI3 298) chain H residue 40 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P99024 source Swiss-Prot : SWS_FT_FI3 299) chain F residue 60 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P99024 source Swiss-Prot : SWS_FT_FI4 300) chain G residue 60 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P99024 source Swiss-Prot : SWS_FT_FI4 301) chain D residue 60 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P99024 source Swiss-Prot : SWS_FT_FI4 302) chain I residue 60 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P99024 source Swiss-Prot : SWS_FT_FI4 303) chain B residue 60 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P99024 source Swiss-Prot : SWS_FT_FI4 304) chain H residue 60 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P99024 source Swiss-Prot : SWS_FT_FI4 305) chain F residue 174 type MOD_RES sequence S description Phosphoserine; by CDK1 => ECO:0000250|UniProtKB:Q13885 source Swiss-Prot : SWS_FT_FI5 306) chain A residue 232 type MOD_RES sequence S description Phosphoserine; by CDK1 => ECO:0000250|UniProtKB:Q13885 source Swiss-Prot : SWS_FT_FI5 307) chain K residue 48 type MOD_RES sequence S description Phosphoserine; by CDK1 => ECO:0000250|UniProtKB:Q13885 source Swiss-Prot : SWS_FT_FI5 308) chain K residue 232 type MOD_RES sequence S description Phosphoserine; by CDK1 => ECO:0000250|UniProtKB:Q13885 source Swiss-Prot : SWS_FT_FI5 309) chain G residue 174 type MOD_RES sequence S description Phosphoserine; by CDK1 => ECO:0000250|UniProtKB:Q13885 source Swiss-Prot : SWS_FT_FI5 310) chain D residue 174 type MOD_RES sequence S description Phosphoserine; by CDK1 => ECO:0000250|UniProtKB:Q13885 source Swiss-Prot : SWS_FT_FI5 311) chain I residue 174 type MOD_RES sequence S description Phosphoserine; by CDK1 => ECO:0000250|UniProtKB:Q13885 source Swiss-Prot : SWS_FT_FI5 312) chain B residue 174 type MOD_RES sequence S description Phosphoserine; by CDK1 => ECO:0000250|UniProtKB:Q13885 source Swiss-Prot : SWS_FT_FI5 313) chain H residue 174 type MOD_RES sequence S description Phosphoserine; by CDK1 => ECO:0000250|UniProtKB:Q13885 source Swiss-Prot : SWS_FT_FI5 314) chain L residue 48 type MOD_RES sequence S description Phosphoserine; by CDK1 => ECO:0000250|UniProtKB:Q13885 source Swiss-Prot : SWS_FT_FI5 315) chain L residue 232 type MOD_RES sequence S description Phosphoserine; by CDK1 => ECO:0000250|UniProtKB:Q13885 source Swiss-Prot : SWS_FT_FI5 316) chain A residue 48 type MOD_RES sequence S description Phosphoserine; by CDK1 => ECO:0000250|UniProtKB:Q13885 source Swiss-Prot : SWS_FT_FI5 317) chain F residue 287 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:P07437 source Swiss-Prot : SWS_FT_FI6 318) chain B residue 292 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:P07437 source Swiss-Prot : SWS_FT_FI6 319) chain H residue 287 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:P07437 source Swiss-Prot : SWS_FT_FI6 320) chain H residue 292 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:P07437 source Swiss-Prot : SWS_FT_FI6 321) chain F residue 292 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:P07437 source Swiss-Prot : SWS_FT_FI6 322) chain G residue 287 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:P07437 source Swiss-Prot : SWS_FT_FI6 323) chain G residue 292 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:P07437 source Swiss-Prot : SWS_FT_FI6 324) chain D residue 287 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:P07437 source Swiss-Prot : SWS_FT_FI6 325) chain D residue 292 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:P07437 source Swiss-Prot : SWS_FT_FI6 326) chain I residue 287 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:P07437 source Swiss-Prot : SWS_FT_FI6 327) chain I residue 292 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:P07437 source Swiss-Prot : SWS_FT_FI6 328) chain B residue 287 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:P07437 source Swiss-Prot : SWS_FT_FI6 329) chain F residue 320 type MOD_RES sequence R description Omega-N-methylarginine => ECO:0000250|UniProtKB:P07437 source Swiss-Prot : SWS_FT_FI7 330) chain G residue 320 type MOD_RES sequence R description Omega-N-methylarginine => ECO:0000250|UniProtKB:P07437 source Swiss-Prot : SWS_FT_FI7 331) chain D residue 320 type MOD_RES sequence R description Omega-N-methylarginine => ECO:0000250|UniProtKB:P07437 source Swiss-Prot : SWS_FT_FI7 332) chain I residue 320 type MOD_RES sequence R description Omega-N-methylarginine => ECO:0000250|UniProtKB:P07437 source Swiss-Prot : SWS_FT_FI7 333) chain B residue 320 type MOD_RES sequence R description Omega-N-methylarginine => ECO:0000250|UniProtKB:P07437 source Swiss-Prot : SWS_FT_FI7 334) chain H residue 320 type MOD_RES sequence R description Omega-N-methylarginine => ECO:0000250|UniProtKB:P07437 source Swiss-Prot : SWS_FT_FI7 335) 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 336) 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 337) 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 338) 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 339) 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 340) 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 341) 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 342) 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 343) 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 344) 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 345) 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 346) 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 347) chain F residue 142-148 type prosite sequence GGGTGSG description TUBULIN Tubulin subunits alpha, beta, and gamma signature. GGGTGSG source prosite : PS00227 348) chain E residue 142-148 type prosite sequence GGGTGSG description TUBULIN Tubulin subunits alpha, beta, and gamma signature. GGGTGSG source prosite : PS00227 349) 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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