eF-site ID 5xaf-ABCDEF PDB Code 5xaf Chain A, B, C, D, E, F click to enlarge Title Crystal structure of tubulin-stathmin-TTL-Compound Z1 complex Classification STRUCTURAL PROTEIN Compound Tubulin alpha-1B chain Source Bos taurus (Bovine) (E1BQ43_CHICK) Sequence A:  MRECISIHVGQAGVQIGNACWELYCLEHGIQPDGQMPSDK TIGGGDDSFNTFFSETGAGKHVPRAVFVDLEPTVIDEVRT GTYRQLFHPEQLITGKEDAANNYARGHYTIGKEIIDLVLD RIRKLADQCTGLQGFLVFHSFGGGTGSGFTSLLMERLSVD YGKKSKLEFSIYPAPQVSTAVVEPYNSILTTHTTLEHSDC AFMVDNEAIYDICRRNLDIERPTYTNLNRLISQIVSSITA SLRFDGALNVDLTEFQTNLVPYPRIHFPLATYAPVISAEK AYHEQLSVAEITNACFEPANQMVKCDPRHGKYMACCLLYR GDVVPKDVNAAIATIKTKRSIQFVDWCPTGFKVGINYQPP TVVPGGDLAKVQRAVCMLSNTTAIAEAWARLDHKFDLMYA KRAFVHWYVGEGMEEGEFSEAREDMAALEKDYEEVGVD B:  MREIVHIQAGQCGNQIGAKFWEVISDEHGIDPTGSYHGDS DLQLERINVYYNEATGNKYVPRAILVDLEPGTMDSVRSGP FGQIFRPDNFVFGQSGAGNNWAKGHYTEGAELVDSVLDVV RKESESCDCLQGFQLTHSLGGGTGSGMGTLLISKIREEYP DRIMNTFSVMPSPKVSDTVVEPYNATLSVHQLVENTDETY CIDNEALYDICFRTLKLTTPTYGDLNHLVSATMSGVTTCL RFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLQYRALTV PELTQQMFDSKNMMAACDPRHGRYLTVAAIFRGRMSMKEV DEQMLNVQNKNSSYFVEWIPNNVKTAVCDIPPRGLKMSAT FIGNSTAIQELFKRISEQFTAMFRRKAFLHWYTGEGMDEM EFTEAESNMNDLVSEYQQYQDA C:  MRECISIHVGQAGVQIGNACWELYCLEHGIQPDGQMPSDK TIGGGDDSFNTFFSETGAGKHVPRAVFVDLEPTVIDEVRT GTYRQLFHPEQLITGKEDAANNYARGHYTIGKEIIDLVLD RIRKLADQCTGLQGFLVFHSFGGGTGSGFTSLLMERLSVD YGKKSKLEFSIYPAPQVSTAVVEPYNSILTTHTTLEHSDC AFMVDNEAIYDICRRNLDIERPTYTNLNRLISQIVSSITA SLRFDGALNVDLTEFQTNLVPYPRIHFPLATYAPVISAEK AYHEQLSVAEITNACFEPANQMVKCDPRHGKYMACCLLYR GDVVPKDVNAAIATIKTKRSIQFVDWCPTGFKVGINYQPP TVVPGGDLAKVQRAVCMLSNTTAIAEAWARLDHKFDLMYA KRAFVHWYVGEGMEEGEFSEAREDMAALEKDYEEVGVDSV D:  MREIVHIQAGQCGNQIGAKFWEVISDEHGIDPTGSYHGDS DLQLERINVYYNEATGNKYVPRAILVDLEPGTMDSVRSGP FGQIFRPDNFVFGQSGAGNNWAKGHYTEGAELVDSVLDVV RKESESCDCLQGFQLTHSLGGGTGSGMGTLLISKIREEYP DRIMNTFSVMPSPKVSDTVVEPYNATLSVHQLVENTDETY CIDNEALYDICFRTLKLTTPTYGDLNHLVSATMSGVTTCL RFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLLTVPELT QQMFDSKNMMAACDPRHGRYLTVAAIFRGRMSMKEVDEQM LNVQNKNSSYFVEWIPNNVKTAVCDIPPRGLKMSATFIGN STAIQELFKRISEQFTAMFRRKAFLHWYTGEGMDEMEFTE AESNMNDLVSEYQQYQDATAD E:  MEVIELNKCTSGQSFEVILKPPSDPSLEEIQKKLEAAEER RKYQEAELLKHLAEKREHEREVIQKAIEENNNFIKMAKEK LAQKMESNKENREAHLAAMLERLQEKDKHAEEVRKNKELK E F:  MYTFVVRDENSSVYAEVSRLLLATGQWKRLRKDNPRFNLM LGERNRLPFGRLGHEPGLVQLVNYYRGADKLCRKASLVKL IKTSPELSCTWFPESYVIYPTDEREVFLAAYNGNVWIAKS ISSEASELLDFIHVIQKYLEKPLLLEPGHRKFDIRSWVLV DHLYNIYLYREGVLRTSSEPYNSADKTCHLTNHCIQKEYS NYGRYEEGNEMFFEEFNQYLMDALNTTLENSILLQIKHII RSCLMCIEPAISTKHLHYQSFQLFGFDFMVDEELKVWLIE VNGAPACAQKLYAELCQGIVDVAISSVFPLASIFIKL 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 171 type sequence I description binding site for residue GTP A 501 source : AC1 14) chain A residue 177 type sequence V description binding site for residue GTP A 501 source : AC1 15) chain A residue 179 type sequence T description binding site for residue GTP A 501 source : AC1 16) chain A residue 183 type sequence E description binding site for residue GTP A 501 source : AC1 17) chain A residue 206 type sequence N description binding site for residue GTP A 501 source : AC1 18) chain A residue 224 type sequence Y description binding site for residue GTP A 501 source : AC1 19) chain A residue 228 type sequence N description binding site for residue GTP A 501 source : AC1 20) chain A residue 231 type sequence I description binding site for residue GTP A 501 source : AC1 21) chain A residue 71 type sequence E description binding site for residue MG A 502 source : AC2 22) chain A residue 216 type sequence N description binding site for residue GOL A 503 source : AC3 23) chain A residue 274 type sequence P description binding site for residue GOL A 503 source : AC3 24) chain A residue 275 type sequence V description binding site for residue GOL A 503 source : AC3 25) chain A residue 294 type sequence A description binding site for residue GOL A 503 source : AC3 26) chain A residue 300 type sequence N description binding site for residue GOL A 503 source : AC3 27) chain A residue 309 type sequence H description binding site for residue GOL A 504 source : AC4 28) chain A residue 382 type sequence T description binding site for residue GOL A 504 source : AC4 29) chain A residue 383 type sequence A description binding site for residue GOL A 504 source : AC4 30) chain A residue 386 type sequence E description binding site for residue GOL A 504 source : AC4 31) chain A residue 433 type sequence E description binding site for residue GOL A 504 source : AC4 32) chain F residue 66 type sequence R description binding site for residue GOL A 504 source : AC4 33) chain A residue 39 type sequence D description binding site for residue CA A 505 source : AC5 34) chain A residue 41 type sequence T description binding site for residue CA A 505 source : AC5 35) chain A residue 44 type sequence G description binding site for residue CA A 505 source : AC5 36) chain A residue 55 type sequence E description binding site for residue CA A 505 source : AC5 37) chain A residue 162 type sequence G description binding site for residue GOL A 506 source : AC6 38) chain A residue 164 type sequence K description binding site for residue GOL A 506 source : AC6 39) chain A residue 166 type sequence K description binding site for residue GOL A 506 source : AC6 40) chain A residue 196 type sequence E description binding site for residue GOL A 506 source : AC6 41) chain A residue 197 type sequence H description binding site for residue GOL A 506 source : AC6 42) chain A residue 199 type sequence D description binding site for residue GOL A 506 source : AC6 43) chain E residue 44 type sequence D description binding site for residue GOL A 506 source : AC6 44) chain B residue 10 type sequence G description binding site for residue GDP B 501 source : AC7 45) chain B residue 11 type sequence Q description binding site for residue GDP B 501 source : AC7 46) chain B residue 12 type sequence C description binding site for residue GDP B 501 source : AC7 47) chain B residue 15 type sequence Q description binding site for residue GDP B 501 source : AC7 48) chain B residue 140 type sequence S description binding site for residue GDP B 501 source : AC7 49) chain B residue 143 type sequence G description binding site for residue GDP B 501 source : AC7 50) chain B residue 144 type sequence G description binding site for residue GDP B 501 source : AC7 51) chain B residue 145 type sequence T description binding site for residue GDP B 501 source : AC7 52) chain B residue 146 type sequence G description binding site for residue GDP B 501 source : AC7 53) chain B residue 177 type sequence V description binding site for residue GDP B 501 source : AC7 54) chain B residue 179 type sequence D description binding site for residue GDP B 501 source : AC7 55) chain B residue 183 type sequence E description binding site for residue GDP B 501 source : AC7 56) chain B residue 206 type sequence N description binding site for residue GDP B 501 source : AC7 57) chain B residue 224 type sequence Y description binding site for residue GDP B 501 source : AC7 58) chain B residue 228 type sequence N description binding site for residue GDP B 501 source : AC7 59) chain B residue 11 type sequence Q description binding site for residue MG B 502 source : AC8 60) chain B residue 179 type sequence D description binding site for residue MG B 502 source : AC8 61) chain B residue 401 type sequence R description binding site for residue GOL B 503 source : AC9 62) chain C residue 262 type sequence Y description binding site for residue GOL B 503 source : AC9 63) chain C residue 434 type sequence E description binding site for residue GOL B 503 source : AC9 64) chain C residue 435 type sequence V description binding site for residue GOL B 503 source : AC9 65) chain B residue 177 type sequence V description binding site for residue GOL B 504 source : AD1 66) chain B residue 178 type sequence S description binding site for residue GOL B 504 source : AD1 67) chain B residue 222 type sequence P description binding site for residue GOL B 504 source : AD1 68) chain B residue 224 type sequence Y description binding site for residue GOL B 504 source : AD1 69) chain B residue 233 type sequence A description binding site for residue GOL B 505 source : AD2 70) chain B residue 236 type sequence S description binding site for residue GOL B 505 source : AD2 71) chain B residue 237 type sequence G description binding site for residue GOL B 505 source : AD2 72) chain B residue 272 type sequence F description binding site for residue GOL B 505 source : AD2 73) chain B residue 320 type sequence R description binding site for residue GOL B 505 source : AD2 74) chain B residue 360 type sequence P description binding site for residue GOL B 505 source : AD2 75) chain B residue 374 type sequence S description binding site for residue GOL B 505 source : AD2 76) chain B residue 375 type sequence A description binding site for residue GOL B 505 source : AD2 77) chain B residue 376 type sequence T description binding site for residue GOL B 505 source : AD2 78) chain B residue 110 type sequence E description binding site for residue CA B 506 source : AD3 79) chain B residue 113 type sequence E description binding site for residue CA B 506 source : AD3 80) chain B residue 158 type sequence R description binding site for residue MES B 507 source : AD4 81) chain B residue 162 type sequence P description binding site for residue MES B 507 source : AD4 82) chain B residue 163 type sequence D description binding site for residue MES B 507 source : AD4 83) chain B residue 164 type sequence R description binding site for residue MES B 507 source : AD4 84) chain B residue 166 type sequence M description binding site for residue MES B 507 source : AD4 85) chain B residue 197 type sequence N description binding site for residue MES B 507 source : AD4 86) chain B residue 199 type sequence D description binding site for residue MES B 507 source : AD4 87) chain B residue 253 type sequence R description binding site for residue MES B 507 source : AD4 88) chain A residue 179 type sequence T description binding site for residue 84F B 508 source : AD5 89) chain A residue 180 type sequence A description binding site for residue 84F B 508 source : AD5 90) chain A residue 181 type sequence V description binding site for residue 84F B 508 source : AD5 91) chain B residue 237 type sequence G description binding site for residue 84F B 508 source : AD5 92) chain B residue 238 type sequence V description binding site for residue 84F B 508 source : AD5 93) chain B residue 241 type sequence C description binding site for residue 84F B 508 source : AD5 94) chain B residue 242 type sequence L description binding site for residue 84F B 508 source : AD5 95) chain B residue 250 type sequence A description binding site for residue 84F B 508 source : AD5 96) chain B residue 251 type sequence D description binding site for residue 84F B 508 source : AD5 97) chain B residue 255 type sequence L description binding site for residue 84F B 508 source : AD5 98) chain B residue 258 type sequence N description binding site for residue 84F B 508 source : AD5 99) chain B residue 315 type sequence V description binding site for residue 84F B 508 source : AD5 100) chain B residue 316 type sequence A description binding site for residue 84F B 508 source : AD5 101) chain B residue 317 type sequence A description binding site for residue 84F B 508 source : AD5 102) chain B residue 318 type sequence I description binding site for residue 84F B 508 source : AD5 103) chain B residue 350 type sequence N description binding site for residue 84F B 508 source : AD5 104) chain B residue 352 type sequence K description binding site for residue 84F B 508 source : AD5 105) chain B residue 100 type sequence G description binding site for residue GOL C 501 source : AD6 106) chain B residue 105 type sequence K description binding site for residue GOL C 501 source : AD6 107) chain C residue 253 type sequence T description binding site for residue GOL C 501 source : AD6 108) chain C residue 257 type sequence T description binding site for residue GOL C 501 source : AD6 109) chain C residue 10 type sequence G description binding site for residue GTP C 502 source : AD7 110) chain C residue 11 type sequence Q description binding site for residue GTP C 502 source : AD7 111) chain C residue 12 type sequence A description binding site for residue GTP C 502 source : AD7 112) chain C residue 15 type sequence Q description binding site for residue GTP C 502 source : AD7 113) chain C residue 98 type sequence D description binding site for residue GTP C 502 source : AD7 114) chain C residue 99 type sequence A description binding site for residue GTP C 502 source : AD7 115) chain C residue 101 type sequence N description binding site for residue GTP C 502 source : AD7 116) chain C residue 140 type sequence S description binding site for residue GTP C 502 source : AD7 117) chain C residue 143 type sequence G description binding site for residue GTP C 502 source : AD7 118) chain C residue 144 type sequence G description binding site for residue GTP C 502 source : AD7 119) chain C residue 145 type sequence T description binding site for residue GTP C 502 source : AD7 120) chain C residue 146 type sequence G description binding site for residue GTP C 502 source : AD7 121) chain C residue 177 type sequence V description binding site for residue GTP C 502 source : AD7 122) chain C residue 179 type sequence T description binding site for residue GTP C 502 source : AD7 123) chain C residue 183 type sequence E description binding site for residue GTP C 502 source : AD7 124) chain C residue 206 type sequence N description binding site for residue GTP C 502 source : AD7 125) chain C residue 224 type sequence Y description binding site for residue GTP C 502 source : AD7 126) chain C residue 228 type sequence N description binding site for residue GTP C 502 source : AD7 127) chain C residue 98 type sequence D description binding site for residue MG C 503 source : AD8 128) chain C residue 221 type sequence R description binding site for residue GOL C 504 source : AD9 129) chain C residue 222 type sequence P description binding site for residue GOL C 504 source : AD9 130) chain C residue 224 type sequence Y description binding site for residue GOL C 504 source : AD9 131) chain D residue 247 type sequence Q description binding site for residue GOL C 504 source : AD9 132) chain C residue 288 type sequence V description binding site for residue GOL C 505 source : AE1 133) chain C residue 322 type sequence D description binding site for residue GOL C 505 source : AE1 134) chain C residue 327 type sequence D description binding site for residue GOL C 505 source : AE1 135) chain C residue 373 type sequence R description binding site for residue GOL C 505 source : AE1 136) chain C residue 163 type sequence K description binding site for residue GOL C 506 source : AE2 137) chain C residue 164 type sequence K description binding site for residue GOL C 506 source : AE2 138) chain C residue 166 type sequence K description binding site for residue GOL C 506 source : AE2 139) chain C residue 196 type sequence E description binding site for residue GOL C 506 source : AE2 140) chain C residue 197 type sequence H description binding site for residue GOL C 506 source : AE2 141) chain C residue 199 type sequence D description binding site for residue GOL C 506 source : AE2 142) chain E residue 93 type sequence F description binding site for residue GOL C 506 source : AE2 143) chain B residue 113 type sequence E description binding site for residue CA C 507 source : AE3 144) chain C residue 282 type sequence Y description binding site for residue CA C 507 source : AE3 145) chain C residue 262 type sequence Y description binding site for residue IMD C 508 source : AE4 146) chain C residue 431 type sequence D description binding site for residue IMD C 508 source : AE4 147) chain C residue 4 type sequence C description binding site for residue IMD C 509 source : AE5 148) chain C residue 133 type sequence Q description binding site for residue IMD C 509 source : AE5 149) chain C residue 165 type sequence S description binding site for residue IMD C 509 source : AE5 150) chain C residue 167 type sequence L description binding site for residue IMD C 509 source : AE5 151) chain C residue 253 type sequence T description binding site for residue IMD C 509 source : AE5 152) chain C residue 256 type sequence Q description binding site for residue IMD C 509 source : AE5 153) chain D residue 10 type sequence G description binding site for residue GDP D 501 source : AE6 154) chain D residue 11 type sequence Q description binding site for residue GDP D 501 source : AE6 155) chain D residue 12 type sequence C description binding site for residue GDP D 501 source : AE6 156) chain D residue 15 type sequence Q description binding site for residue GDP D 501 source : AE6 157) chain D residue 99 type sequence A description binding site for residue GDP D 501 source : AE6 158) chain D residue 140 type sequence S description binding site for residue GDP D 501 source : AE6 159) chain D residue 143 type sequence G description binding site for residue GDP D 501 source : AE6 160) chain D residue 144 type sequence G description binding site for residue GDP D 501 source : AE6 161) chain D residue 145 type sequence T description binding site for residue GDP D 501 source : AE6 162) chain D residue 146 type sequence G description binding site for residue GDP D 501 source : AE6 163) chain D residue 177 type sequence V description binding site for residue GDP D 501 source : AE6 164) chain D residue 183 type sequence E description binding site for residue GDP D 501 source : AE6 165) chain D residue 206 type sequence N description binding site for residue GDP D 501 source : AE6 166) chain D residue 224 type sequence Y description binding site for residue GDP D 501 source : AE6 167) chain D residue 228 type sequence N description binding site for residue GDP D 501 source : AE6 168) chain D residue 11 type sequence Q description binding site for residue MG D 502 source : AE7 169) chain D residue 101 type sequence N description binding site for residue MG D 502 source : AE7 170) chain D residue 177 type sequence V description binding site for residue GOL D 503 source : AE8 171) chain D residue 222 type sequence P description binding site for residue GOL D 503 source : AE8 172) chain D residue 223 type sequence T description binding site for residue GOL D 503 source : AE8 173) chain D residue 224 type sequence Y description binding site for residue GOL D 503 source : AE8 174) chain C residue 179 type sequence T description binding site for residue 84F D 505 source : AE9 175) chain C residue 180 type sequence A description binding site for residue 84F D 505 source : AE9 176) chain C residue 181 type sequence V description binding site for residue 84F D 505 source : AE9 177) chain D residue 237 type sequence G description binding site for residue 84F D 505 source : AE9 178) chain D residue 238 type sequence V description binding site for residue 84F D 505 source : AE9 179) chain D residue 241 type sequence C description binding site for residue 84F D 505 source : AE9 180) chain D residue 250 type sequence A description binding site for residue 84F D 505 source : AE9 181) chain D residue 251 type sequence D description binding site for residue 84F D 505 source : AE9 182) chain D residue 254 type sequence K description binding site for residue 84F D 505 source : AE9 183) chain D residue 255 type sequence L description binding site for residue 84F D 505 source : AE9 184) chain D residue 258 type sequence N description binding site for residue 84F D 505 source : AE9 185) chain D residue 259 type sequence M description binding site for residue 84F D 505 source : AE9 186) chain D residue 317 type sequence A description binding site for residue 84F D 505 source : AE9 187) chain D residue 318 type sequence I description binding site for residue 84F D 505 source : AE9 188) chain D residue 352 type sequence K description binding site for residue 84F D 505 source : AE9 189) chain D residue 354 type sequence A description binding site for residue 84F D 505 source : AE9 190) chain D residue 378 type sequence I description binding site for residue 84F D 505 source : AE9 191) chain F residue 200 type sequence D description binding site for residue MG F 401 source : AF1 192) chain F residue 222 type sequence R description binding site for residue MG F 401 source : AF1 193) chain F residue 242 type sequence N description binding site for residue MG F 401 source : AF1 194) chain F residue 318 type sequence D description binding site for residue MG F 401 source : AF1 195) chain F residue 74 type sequence K description binding site for residue ACP F 402 source : AF2 196) chain F residue 95 type sequence P description binding site for residue ACP F 402 source : AF2 197) chain F residue 183 type sequence Q description binding site for residue ACP F 402 source : AF2 198) chain F residue 184 type sequence K description binding site for residue ACP F 402 source : AF2 199) chain F residue 186 type sequence L description binding site for residue ACP F 402 source : AF2 200) chain F residue 198 type sequence K description binding site for residue ACP F 402 source : AF2 201) chain F residue 239 type sequence H description binding site for residue ACP F 402 source : AF2 202) chain F residue 240 type sequence L description binding site for residue ACP F 402 source : AF2 203) chain F residue 241 type sequence T description binding site for residue ACP F 402 source : AF2 204) chain F residue 330 type sequence I description binding site for residue ACP F 402 source : AF2 205) chain F residue 331 type sequence E description binding site for residue ACP F 402 source : AF2 206) chain C residue 407 type sequence W description binding site for residues GOL D 504 and IMD E 201 source : AF3 207) chain C residue 410 type sequence G description binding site for residues GOL D 504 and IMD E 201 source : AF3 208) chain C residue 411 type sequence E description binding site for residues GOL D 504 and IMD E 201 source : AF3 209) chain D residue 162 type sequence P description binding site for residues GOL D 504 and IMD E 201 source : AF3 210) chain D residue 164 type sequence R description binding site for residues GOL D 504 and IMD E 201 source : AF3 211) chain D residue 168 type sequence T description binding site for residues GOL D 504 and IMD E 201 source : AF3 212) chain D residue 170 type sequence S description binding site for residues GOL D 504 and IMD E 201 source : AF3 213) chain D residue 198 type sequence T description binding site for residues GOL D 504 and IMD E 201 source : AF3 214) chain D residue 199 type sequence D description binding site for residues GOL D 504 and IMD E 201 source : AF3 215) chain D residue 200 type sequence E description binding site for residues GOL D 504 and IMD E 201 source : AF3 216) chain D residue 202 type sequence Y description binding site for residues GOL D 504 and IMD E 201 source : AF3 217) chain D residue 203 type sequence C description binding site for residues GOL D 504 and IMD E 201 source : AF3 218) chain D residue 253 type sequence R description binding site for residues GOL D 504 and IMD E 201 source : AF3 219) chain D residue 266 type sequence H description binding site for residues GOL D 504 and IMD E 201 source : AF3 220) chain D residue 267 type sequence F description binding site for residues GOL D 504 and IMD E 201 source : AF3 221) chain D residue 268 type sequence F description binding site for residues GOL D 504 and IMD E 201 source : AF3 222) chain E residue 112 type sequence R description binding site for residues GOL D 504 and IMD E 201 source : AF3 223) chain B residue 142-148 type prosite sequence GGGTGSG description TUBULIN Tubulin subunits alpha, beta, and gamma signature. GGGTGSG source prosite : PS00227 224) chain A residue 142-148 type prosite sequence GGGTGSG description TUBULIN Tubulin subunits alpha, beta, and gamma signature. GGGTGSG source prosite : PS00227 225) chain B residue 1-4 type prosite sequence MREI description TUBULIN_B_AUTOREG Tubulin-beta mRNA autoregulation signal. MREI source prosite : PS00228 226) chain E residue 73-82 type prosite sequence AEKREHEREV description STATHMIN_2 Stathmin family signature 2. AEKREHEREV source prosite : PS01041 227) chain E residue 46 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:22673903 source Swiss-Prot : SWS_FT_FI1 228) chain D residue 144 type MOD_RES sequence G description Phosphoserine => ECO:0007744|PubMed:22673903 source Swiss-Prot : SWS_FT_FI1 229) chain D residue 145 type MOD_RES sequence T description Phosphoserine => ECO:0007744|PubMed:22673903 source Swiss-Prot : SWS_FT_FI1 230) chain D residue 146 type MOD_RES sequence G description Phosphoserine => ECO:0007744|PubMed:22673903 source Swiss-Prot : SWS_FT_FI1 231) chain D residue 206 type MOD_RES sequence N description Phosphoserine => ECO:0007744|PubMed:22673903 source Swiss-Prot : SWS_FT_FI1 232) chain D residue 228 type MOD_RES sequence N description Phosphoserine => ECO:0007744|PubMed:22673903 source Swiss-Prot : SWS_FT_FI1 233) chain B residue 140 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:22673903 source Swiss-Prot : SWS_FT_FI1 234) chain B residue 144 type MOD_RES sequence G description Phosphoserine => ECO:0007744|PubMed:22673903 source Swiss-Prot : SWS_FT_FI1 235) chain B residue 145 type MOD_RES sequence T description Phosphoserine => ECO:0007744|PubMed:22673903 source Swiss-Prot : SWS_FT_FI1 236) chain B residue 146 type MOD_RES sequence G description Phosphoserine => ECO:0007744|PubMed:22673903 source Swiss-Prot : SWS_FT_FI1 237) chain B residue 206 type MOD_RES sequence N description Phosphoserine => ECO:0007744|PubMed:22673903 source Swiss-Prot : SWS_FT_FI1 238) chain B residue 228 type MOD_RES sequence N description Phosphoserine => ECO:0007744|PubMed:22673903 source Swiss-Prot : SWS_FT_FI1 239) chain D residue 11 type MOD_RES sequence Q description Phosphoserine => ECO:0007744|PubMed:22673903 source Swiss-Prot : SWS_FT_FI1 240) chain D residue 140 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:22673903 source Swiss-Prot : SWS_FT_FI1 241) 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_FI10 242) 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_FI10 243) 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_FI11 244) 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_FI11 245) 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 246) 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 247) 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 248) 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 249) chain C residue 71 type LIPID sequence E description S-palmitoyl cysteine => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 250) chain C residue 140 type LIPID sequence S description S-palmitoyl cysteine => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 251) chain C residue 144 type LIPID sequence G description S-palmitoyl cysteine => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 252) chain C residue 145 type LIPID sequence T description S-palmitoyl cysteine => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 253) chain C residue 179 type LIPID sequence T description S-palmitoyl cysteine => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 254) chain C residue 206 type LIPID sequence N description S-palmitoyl cysteine => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 255) chain C residue 228 type LIPID sequence N description S-palmitoyl cysteine => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 256) chain A residue 140 type LIPID sequence S description S-palmitoyl cysteine => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 257) chain A residue 144 type LIPID sequence G description S-palmitoyl cysteine => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 258) chain A residue 145 type LIPID sequence T description S-palmitoyl cysteine => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 259) chain A residue 179 type LIPID sequence T description S-palmitoyl cysteine => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 260) chain A residue 206 type LIPID sequence N description S-palmitoyl cysteine => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 261) chain A residue 228 type LIPID sequence N description S-palmitoyl cysteine => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 262) chain C residue 11 type LIPID sequence Q description S-palmitoyl cysteine => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 263) chain B residue 40 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P99024 source Swiss-Prot : SWS_FT_FI3 264) chain D residue 40 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P99024 source Swiss-Prot : SWS_FT_FI3 265) chain B residue 57 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:Q3KRE8 source Swiss-Prot : SWS_FT_FI4 266) chain D residue 57 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:Q3KRE8 source Swiss-Prot : SWS_FT_FI4 267) chain B residue 60 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P99024 source Swiss-Prot : SWS_FT_FI5 268) chain D residue 60 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P99024 source Swiss-Prot : SWS_FT_FI5 269) chain C residue 48 type MOD_RES sequence S description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P99024 source Swiss-Prot : SWS_FT_FI5 270) chain C residue 232 type MOD_RES sequence S description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P99024 source Swiss-Prot : SWS_FT_FI5 271) chain B residue 174 type MOD_RES sequence S description Phosphoserine; by CDK1 => ECO:0000250|UniProtKB:Q9BVA1 source Swiss-Prot : SWS_FT_FI6 272) chain D residue 174 type MOD_RES sequence S description Phosphoserine; by CDK1 => ECO:0000250|UniProtKB:Q9BVA1 source Swiss-Prot : SWS_FT_FI6 273) chain B residue 287 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:P07437 source Swiss-Prot : SWS_FT_FI7 274) chain B residue 292 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:P07437 source Swiss-Prot : SWS_FT_FI7 275) chain D residue 287 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:P07437 source Swiss-Prot : SWS_FT_FI7 276) chain D residue 292 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:P07437 source Swiss-Prot : SWS_FT_FI7 277) chain B residue 320 type MOD_RES sequence R description Omega-N-methylarginine => ECO:0000250|UniProtKB:P07437 source Swiss-Prot : SWS_FT_FI8 278) chain D residue 320 type MOD_RES sequence R description Omega-N-methylarginine => ECO:0000250|UniProtKB:P07437 source Swiss-Prot : SWS_FT_FI8

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