eF-site ID 5zxh-ABCDEF PDB Code 5zxh Chain A, B, C, D, E, F click to enlarge Title The structure of MT189-tubulin complex Classification STRUCTURAL PROTEIN Compound Tubulin alpha-1B chain Source (E1BQ43_CHICK) Sequence A:  MRECISIHVGQAGVQIGNACWELYCLEHGIQPDGQMPSDK TIGGGDDSFNTFFSETGAGKHVPRAVFVDLEPTVIDEVRT GTYRQLFHPEQLITGKEDAANNYARGHYTIGKEIIDLVLD RIRKLADQCTGLQGFLVFHSFGGGTGSGFTSLLMERLSVD YGKKSKLEFSIYPAPQVSTAVVEPYNSILTTHTTLEHSDC AFMVDNEAIYDICRRNLDIERPTYTNLNRLISQIVSSITA SLRFDGALNVDLTEFQTNLVPYPRIHFPLATYAPVISAEK AYHEQLSVAEITNACFEPANQMVKCDPRHGKYMACCLLYR GDVVPKDVNAAIATIKTKRSIQFVDWCPTGFKVGINYQPP TVVPGGDLAKVQRAVCMLSNTTAIAEAWARLDHKFDLMYA KRAFVHWYVGEGMEEGEFSEAREDMAALEKDYEEVGV B:  MREIVHIQAGQCGNQIGAKFWEVISDEHGIDPTGSYHGDS DLQLERINVYYNEATGNKYVPRAILVDLEPGTMDSVRSGP FGQIFRPDNFVFGQSGAGNNWAKGHYTEGAELVDSVLDVV RKESESCDCLQGFQLTHSLGGGTGSGMGTLLISKIREEYP DRIMNTFSVVPSPKVSDTVVEPYNATLSVHQLVENTDETY CIDNEALYDICFRTLKLTTPTYGDLNHLVSATMSGVTTCL RFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTSQYRAL TVPELTQQMFDSKNMMAACDPRHGRYLTVAAVFRGRMSMK EVDEQMLNVQNKNSSYFVEWIPNNVKTAVCDIPPRGLKMS ATFIGNSTAIQELFKRISEQFTAMFRRKAFLHWYTGEGMD EMEFTEAESNMNDLVSEYQQYQDA C:  MRECISIHVGQAGVQIGNACWELYCLEHGIQPDGQMPSDK TIGGGDDSFNTFFSETGAGKHVPRAVFVDLEPTVIDEVRT GTYRQLFHPEQLITGKEDAANNYARGHYTIGKEIIDLVLD RIRKLADQCTGLQGFLVFHSFGGGTGSGFTSLLMERLSVD YGKKSKLEFSIYPAPQVSTAVVEPYNSILTTHTTLEHSDC AFMVDNEAIYDICRRNLDIERPTYTNLNRLISQIVSSITA SLRFDGALNVDLTEFQTNLVPYPRIHFPLATYAPVISAEK AYHEQLSVAEITNACFEPANQMVKCDPRHGKYMACCLLYR GDVVPKDVNAAIATIKTKRSIQFVDWCPTGFKVGINYQPP TVVPGGDLAKVQRAVCMLSNTTAIAEAWARLDHKFDLMYA KRAFVHWYVGEGMEEGEFSEAREDMAALEKDYEEVGVDSV D:  MREIVHIQAGQCGNQIGAKFWEVISDEHGIDPTGSYHGDS DLQLERINVYYNEATGNKYVPRAILVDLEPGTMDSVRSGP FGQIFRPDNFVFGQSGAGNNWAKGHYTEGAELVDSVLDVV RKESESCDCLQGFQLTHSLGGGTGSGMGTLLISKIREEYP DRIMNTFSVVPSPKVSDTVVEPYNATLSVHQLVENTDETY CIDNEALYDICFRTLKLTTPTYGDLNHLVSATMSGVTTCL RFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLLTVPELT QQMFDSKNMMAACDPRHGRYLTVAAVFRGRMSMKEVDEQM LNVQNKNSSYFVEWIPNNVKTAVCDIPPRGLKMSATFIGN STAIQELFKRISEQFTAMFRRKAFLHWYTGEGMDEMEFTE AESNMNDLVSEYQQYQDATAD E:  MEVIELNKCTSGQSFEVILKPPDPSLEEIQKKLEAAEERR KYQEAELLKHLAEKREHEREVIQKAIEENNNFIKMAKEKL AQKMESNKENREAHLAAMLERLQEKDKHAEEVRKNKELKE F:  MYTFVVRDENSSVYAEVSRLLLATGQWKRLRKDNPRFNLM LGERNRLPFGRLGHEPGLVQLVNYYRGADKLCRKASLVKL IKTSPELSESCTWFPESYVIYPGNVWIAKSGILISSEAHV IQKYLEKPLLLEPGHRKFDIRSWVLVDHLYNIYLYREGVL RTSSEPYNSANFQDKTCHLTNHCIQKNYGRYEEGNEMFFE EFNQYLMDALNTTLENSILLQIKHIIRSCLMCIEPAISTK HLHYQSFQLFGFDFMVDEELKVWLIEVNGAPACAQKLYAE LCQGIVDVAISSVFPLASIFIKLHHHHHH Description Functional site 1) chain A residue 10 type sequence G description binding site for residue GTP A 501 source : AC1 2) chain A residue 11 type sequence Q description binding site for residue GTP A 501 source : AC1 3) chain A residue 12 type sequence A description binding site for residue GTP A 501 source : AC1 4) chain A residue 15 type sequence Q description binding site for residue GTP A 501 source : AC1 5) chain A residue 98 type sequence D description binding site for residue GTP A 501 source : AC1 6) chain A residue 99 type sequence A description binding site for residue GTP A 501 source : AC1 7) chain A residue 101 type sequence N description binding site for residue GTP A 501 source : AC1 8) chain A residue 140 type sequence S description binding site for residue GTP A 501 source : AC1 9) chain A residue 143 type sequence G description binding site for residue GTP A 501 source : AC1 10) chain A residue 144 type sequence G description binding site for residue GTP A 501 source : AC1 11) chain A residue 145 type sequence T description binding site for residue GTP A 501 source : AC1 12) chain A residue 146 type sequence G description binding site for residue GTP A 501 source : AC1 13) chain A residue 177 type sequence V description binding site for residue GTP A 501 source : AC1 14) chain A residue 183 type sequence E description binding site for residue GTP A 501 source : AC1 15) chain A residue 206 type sequence N description binding site for residue GTP A 501 source : AC1 16) chain A residue 224 type sequence Y description binding site for residue GTP A 501 source : AC1 17) chain A residue 228 type sequence N description binding site for residue GTP A 501 source : AC1 18) chain A residue 231 type sequence I description binding site for residue GTP A 501 source : AC1 19) chain B residue 252 type sequence K description binding site for residue GTP A 501 source : AC1 20) chain A residue 39 type sequence D description binding site for residue CA A 503 source : AC3 21) chain A residue 41 type sequence T description binding site for residue CA A 503 source : AC3 22) chain A residue 44 type sequence G description binding site for residue CA A 503 source : AC3 23) chain A residue 55 type sequence E description binding site for residue CA A 503 source : AC3 24) chain B residue 10 type sequence G description binding site for residue GDP B 501 source : AC4 25) chain B residue 11 type sequence Q description binding site for residue GDP B 501 source : AC4 26) chain B residue 12 type sequence C description binding site for residue GDP B 501 source : AC4 27) chain B residue 15 type sequence Q description binding site for residue GDP B 501 source : AC4 28) chain B residue 138 type sequence S description binding site for residue GDP B 501 source : AC4 29) chain B residue 141 type sequence G description binding site for residue GDP B 501 source : AC4 30) chain B residue 142 type sequence G description binding site for residue GDP B 501 source : AC4 31) chain B residue 143 type sequence T description binding site for residue GDP B 501 source : AC4 32) chain B residue 144 type sequence G description binding site for residue GDP B 501 source : AC4 33) chain B residue 171 type sequence P description binding site for residue GDP B 501 source : AC4 34) chain B residue 175 type sequence V description binding site for residue GDP B 501 source : AC4 35) chain B residue 177 type sequence D description binding site for residue GDP B 501 source : AC4 36) chain B residue 181 type sequence E description binding site for residue GDP B 501 source : AC4 37) chain B residue 204 type sequence N description binding site for residue GDP B 501 source : AC4 38) chain B residue 222 type sequence Y description binding site for residue GDP B 501 source : AC4 39) chain B residue 226 type sequence N description binding site for residue GDP B 501 source : AC4 40) chain B residue 11 type sequence Q description binding site for residue MG B 502 source : AC5 41) chain B residue 177 type sequence D description binding site for residue MG B 502 source : AC5 42) chain B residue 156 type sequence R description binding site for residue MES B 503 source : AC6 43) chain B residue 160 type sequence P description binding site for residue MES B 503 source : AC6 44) chain B residue 161 type sequence D description binding site for residue MES B 503 source : AC6 45) chain B residue 162 type sequence R description binding site for residue MES B 503 source : AC6 46) chain B residue 195 type sequence N description binding site for residue MES B 503 source : AC6 47) chain B residue 197 type sequence D description binding site for residue MES B 503 source : AC6 48) chain B residue 251 type sequence R description binding site for residue MES B 503 source : AC6 49) chain B residue 111 type sequence E description binding site for residue CA B 504 source : AC7 50) chain B residue 294 type sequence F description binding site for residue MES B 505 source : AC8 51) chain B residue 295 type sequence D description binding site for residue MES B 505 source : AC8 52) chain B residue 296 type sequence S description binding site for residue MES B 505 source : AC8 53) chain B residue 305 type sequence P description binding site for residue MES B 505 source : AC8 54) chain B residue 306 type sequence R description binding site for residue MES B 505 source : AC8 55) chain B residue 310 type sequence Y description binding site for residue MES B 505 source : AC8 56) chain B residue 337 type sequence N description binding site for residue MES B 505 source : AC8 57) chain A residue 179 type sequence T description binding site for residue 9LX B 506 source : AC9 58) chain A residue 181 type sequence V description binding site for residue 9LX B 506 source : AC9 59) chain B residue 236 type sequence V description binding site for residue 9LX B 506 source : AC9 60) chain B residue 239 type sequence C description binding site for residue 9LX B 506 source : AC9 61) chain B residue 246 type sequence L description binding site for residue 9LX B 506 source : AC9 62) chain B residue 249 type sequence D description binding site for residue 9LX B 506 source : AC9 63) chain B residue 253 type sequence L description binding site for residue 9LX B 506 source : AC9 64) chain B residue 256 type sequence N description binding site for residue 9LX B 506 source : AC9 65) chain B residue 257 type sequence M description binding site for residue 9LX B 506 source : AC9 66) chain B residue 313 type sequence V description binding site for residue 9LX B 506 source : AC9 67) chain B residue 314 type sequence A description binding site for residue 9LX B 506 source : AC9 68) chain B residue 316 type sequence V description binding site for residue 9LX B 506 source : AC9 69) chain B residue 348 type sequence N description binding site for residue 9LX B 506 source : AC9 70) chain B residue 350 type sequence K description binding site for residue 9LX B 506 source : AC9 71) chain B residue 351 type sequence T description binding site for residue 9LX B 506 source : AC9 72) chain B residue 352 type sequence A description binding site for residue 9LX B 506 source : AC9 73) chain C residue 11 type sequence Q description binding site for residue GTP C 501 source : AD1 74) chain C residue 12 type sequence A description binding site for residue GTP C 501 source : AD1 75) chain C residue 15 type sequence Q description binding site for residue GTP C 501 source : AD1 76) chain C residue 98 type sequence D description binding site for residue GTP C 501 source : AD1 77) chain C residue 99 type sequence A description binding site for residue GTP C 501 source : AD1 78) chain C residue 100 type sequence A description binding site for residue GTP C 501 source : AD1 79) chain C residue 101 type sequence N description binding site for residue GTP C 501 source : AD1 80) chain C residue 140 type sequence S description binding site for residue GTP C 501 source : AD1 81) chain C residue 143 type sequence G description binding site for residue GTP C 501 source : AD1 82) chain C residue 144 type sequence G description binding site for residue GTP C 501 source : AD1 83) chain C residue 145 type sequence T description binding site for residue GTP C 501 source : AD1 84) chain C residue 146 type sequence G description binding site for residue GTP C 501 source : AD1 85) chain C residue 177 type sequence V description binding site for residue GTP C 501 source : AD1 86) chain C residue 183 type sequence E description binding site for residue GTP C 501 source : AD1 87) chain C residue 206 type sequence N description binding site for residue GTP C 501 source : AD1 88) chain C residue 224 type sequence Y description binding site for residue GTP C 501 source : AD1 89) chain C residue 228 type sequence N description binding site for residue GTP C 501 source : AD1 90) chain C residue 231 type sequence I description binding site for residue GTP C 501 source : AD1 91) chain D residue 252 type sequence K description binding site for residue GTP C 501 source : AD1 92) chain C residue 39 type sequence D description binding site for residue CA C 503 source : AD3 93) chain C residue 41 type sequence T description binding site for residue CA C 503 source : AD3 94) chain C residue 44 type sequence G description binding site for residue CA C 503 source : AD3 95) chain C residue 55 type sequence E description binding site for residue CA C 503 source : AD3 96) chain D residue 10 type sequence G description binding site for residue GTP D 501 source : AD4 97) chain D residue 11 type sequence Q description binding site for residue GTP D 501 source : AD4 98) chain D residue 12 type sequence C description binding site for residue GTP D 501 source : AD4 99) chain D residue 97 type sequence A description binding site for residue GTP D 501 source : AD4 100) chain D residue 98 type sequence G description binding site for residue GTP D 501 source : AD4 101) chain D residue 99 type sequence N description binding site for residue GTP D 501 source : AD4 102) chain D residue 138 type sequence S description binding site for residue GTP D 501 source : AD4 103) chain D residue 141 type sequence G description binding site for residue GTP D 501 source : AD4 104) chain D residue 142 type sequence G description binding site for residue GTP D 501 source : AD4 105) chain D residue 143 type sequence T description binding site for residue GTP D 501 source : AD4 106) chain D residue 144 type sequence G description binding site for residue GTP D 501 source : AD4 107) chain D residue 175 type sequence V description binding site for residue GTP D 501 source : AD4 108) chain D residue 176 type sequence S description binding site for residue GTP D 501 source : AD4 109) chain D residue 181 type sequence E description binding site for residue GTP D 501 source : AD4 110) chain D residue 204 type sequence N description binding site for residue GTP D 501 source : AD4 111) chain D residue 222 type sequence Y description binding site for residue GTP D 501 source : AD4 112) chain D residue 226 type sequence N description binding site for residue GTP D 501 source : AD4 113) chain C residue 179 type sequence T description binding site for residue 9LX D 503 source : AD6 114) chain C residue 181 type sequence V description binding site for residue 9LX D 503 source : AD6 115) chain D residue 236 type sequence V description binding site for residue 9LX D 503 source : AD6 116) chain D residue 239 type sequence C description binding site for residue 9LX D 503 source : AD6 117) chain D residue 240 type sequence L description binding site for residue 9LX D 503 source : AD6 118) chain D residue 246 type sequence L description binding site for residue 9LX D 503 source : AD6 119) chain D residue 249 type sequence D description binding site for residue 9LX D 503 source : AD6 120) chain D residue 252 type sequence K description binding site for residue 9LX D 503 source : AD6 121) chain D residue 253 type sequence L description binding site for residue 9LX D 503 source : AD6 122) chain D residue 256 type sequence N description binding site for residue 9LX D 503 source : AD6 123) chain D residue 313 type sequence V description binding site for residue 9LX D 503 source : AD6 124) chain D residue 316 type sequence V description binding site for residue 9LX D 503 source : AD6 125) chain D residue 350 type sequence K description binding site for residue 9LX D 503 source : AD6 126) chain D residue 351 type sequence T description binding site for residue 9LX D 503 source : AD6 127) chain D residue 352 type sequence A description binding site for residue 9LX D 503 source : AD6 128) chain F residue 74 type sequence K description binding site for residue ACP F 401 source : AD7 129) chain F residue 150 type sequence K description binding site for residue ACP F 401 source : AD7 130) chain F residue 183 type sequence Q description binding site for residue ACP F 401 source : AD7 131) chain F residue 184 type sequence K description binding site for residue ACP F 401 source : AD7 132) chain F residue 186 type sequence L description binding site for residue ACP F 401 source : AD7 133) chain F residue 198 type sequence K description binding site for residue ACP F 401 source : AD7 134) chain F residue 200 type sequence D description binding site for residue ACP F 401 source : AD7 135) chain F residue 202 type sequence R description binding site for residue ACP F 401 source : AD7 136) chain F residue 222 type sequence R description binding site for residue ACP F 401 source : AD7 137) chain F residue 241 type sequence T description binding site for residue ACP F 401 source : AD7 138) chain F residue 242 type sequence N description binding site for residue ACP F 401 source : AD7 139) chain F residue 318 type sequence D description binding site for residue ACP F 401 source : AD7 140) chain F residue 320 type sequence M description binding site for residue ACP F 401 source : AD7 141) chain F residue 330 type sequence I description binding site for residue ACP F 401 source : AD7 142) chain F residue 331 type sequence E description binding site for residue ACP F 401 source : AD7 143) chain F residue 333 type sequence N description binding site for residue ACP F 401 source : AD7 144) chain E residue 46 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:22673903 source Swiss-Prot : SWS_FT_FI1 145) chain D residue 142 type MOD_RES sequence G description Phosphoserine => ECO:0007744|PubMed:22673903 source Swiss-Prot : SWS_FT_FI1 146) chain D residue 143 type MOD_RES sequence T description Phosphoserine => ECO:0007744|PubMed:22673903 source Swiss-Prot : SWS_FT_FI1 147) chain D residue 144 type MOD_RES sequence G description Phosphoserine => ECO:0007744|PubMed:22673903 source Swiss-Prot : SWS_FT_FI1 148) chain D residue 204 type MOD_RES sequence N description Phosphoserine => ECO:0007744|PubMed:22673903 source Swiss-Prot : SWS_FT_FI1 149) chain D residue 226 type MOD_RES sequence N description Phosphoserine => ECO:0007744|PubMed:22673903 source Swiss-Prot : SWS_FT_FI1 150) chain B residue 138 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:22673903 source Swiss-Prot : SWS_FT_FI1 151) chain B residue 142 type MOD_RES sequence G description Phosphoserine => ECO:0007744|PubMed:22673903 source Swiss-Prot : SWS_FT_FI1 152) chain B residue 143 type MOD_RES sequence T description Phosphoserine => ECO:0007744|PubMed:22673903 source Swiss-Prot : SWS_FT_FI1 153) chain B residue 144 type MOD_RES sequence G description Phosphoserine => ECO:0007744|PubMed:22673903 source Swiss-Prot : SWS_FT_FI1 154) chain B residue 204 type MOD_RES sequence N description Phosphoserine => ECO:0007744|PubMed:22673903 source Swiss-Prot : SWS_FT_FI1 155) chain B residue 226 type MOD_RES sequence N description Phosphoserine => ECO:0007744|PubMed:22673903 source Swiss-Prot : SWS_FT_FI1 156) chain D residue 11 type MOD_RES sequence Q description Phosphoserine => ECO:0007744|PubMed:22673903 source Swiss-Prot : SWS_FT_FI1 157) chain D residue 138 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:22673903 source Swiss-Prot : SWS_FT_FI1 158) chain B residue 58 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_FI10 159) chain D residue 58 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_FI10 160) chain A residue 370 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_FI10 161) chain C residue 326 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_FI10 162) chain C residue 370 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_FI10 163) chain B residue 324 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_FI11 164) chain D residue 324 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_FI11 165) chain B residue 285 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:P07437 source Swiss-Prot : SWS_FT_FI7 166) chain B residue 290 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:P07437 source Swiss-Prot : SWS_FT_FI7 167) chain D residue 285 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:P07437 source Swiss-Prot : SWS_FT_FI7 168) chain D residue 290 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:P07437 source Swiss-Prot : SWS_FT_FI7 169) chain B residue 318 type MOD_RES sequence R description Omega-N-methylarginine => ECO:0000250|UniProtKB:P07437 source Swiss-Prot : SWS_FT_FI8 170) chain D residue 318 type MOD_RES sequence R description Omega-N-methylarginine => ECO:0000250|UniProtKB:P07437 source Swiss-Prot : SWS_FT_FI8 171) chain B residue 69 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 172) chain C residue 71 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 173) chain C residue 140 type BINDING sequence S description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 174) chain C residue 144 type BINDING sequence G description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 175) chain C residue 145 type BINDING sequence T description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 176) chain C residue 179 type BINDING sequence T description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 177) chain C residue 206 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 178) chain C residue 228 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 179) chain D residue 69 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 180) chain A residue 140 type BINDING sequence S description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 181) chain A residue 144 type BINDING sequence G description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 182) chain A residue 145 type BINDING sequence T description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 183) chain A residue 179 type BINDING sequence T description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 184) chain A residue 206 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 185) chain A residue 228 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 186) chain C residue 11 type BINDING sequence Q description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 187) chain B residue 40 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P99024 source Swiss-Prot : SWS_FT_FI3 188) chain D residue 40 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P99024 source Swiss-Prot : SWS_FT_FI3 189) chain B residue 55 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:Q3KRE8 source Swiss-Prot : SWS_FT_FI4 190) chain D residue 55 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:Q3KRE8 source Swiss-Prot : SWS_FT_FI4 191) chain C residue 48 type MOD_RES sequence S description Phosphothreonine => ECO:0000250|UniProtKB:Q3KRE8 source Swiss-Prot : SWS_FT_FI4 192) chain C residue 232 type MOD_RES sequence S description Phosphothreonine => ECO:0000250|UniProtKB:Q3KRE8 source Swiss-Prot : SWS_FT_FI4 193) chain B residue 58 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P99024 source Swiss-Prot : SWS_FT_FI5 194) chain D residue 58 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P99024 source Swiss-Prot : SWS_FT_FI5 195) chain B residue 172 type MOD_RES sequence S description Phosphoserine; by CDK1 => ECO:0000250|UniProtKB:Q9BVA1 source Swiss-Prot : SWS_FT_FI6 196) chain D residue 172 type MOD_RES sequence S description Phosphoserine; by CDK1 => ECO:0000250|UniProtKB:Q9BVA1 source Swiss-Prot : SWS_FT_FI6 197) chain B residue 140-146 type prosite sequence GGGTGSG description TUBULIN Tubulin subunits alpha, beta, and gamma signature. GGGTGSG source prosite : PS00227 198) chain A residue 142-148 type prosite sequence GGGTGSG description TUBULIN Tubulin subunits alpha, beta, and gamma signature. GGGTGSG source prosite : PS00227 199) chain B residue 1-4 type prosite sequence MREI description TUBULIN_B_AUTOREG Tubulin-beta mRNA autoregulation signal. MREI source prosite : PS00228 200) chain E residue 73-82 type prosite sequence AEKREHEREV description STATHMIN_2 Stathmin family signature 2. AEKREHEREV source prosite : PS01041

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