eF-site ID 4o4l-ABCDEF PDB Code 4o4l Chain A, B, C, D, E, F click to enlarge Title Tubulin-Peloruside A-Epothilone A complex Classification CELL CYCLE/INHIBITOR Compound Tubulin alpha-1B chain Source ORGANISM_COMMON: bovine,cow,domestic cattle,domestic cow; ORGANISM_SCIENTIFIC: Bos taurus; Sequence A:  MRECISIHVGQAGVQIGNACWELYCLEHGIQPDGQMPSDK TIGGGDDSFNTFFSETGAGKHVPRAVFVDLEPTVIDEVRT GTYRQLFHPEQLITGKEDAANNYARGHYTIGKEIIDLVLD RIRKLADQCTGLQGFLVFHSFGGGTGSGFTSLLMERLSVD YGKKSKLEFSIYPAPQVSTAVVEPYNSILTTHTTLEHSDC AFMVDNEAIYDICRRNLDIERPTYTNLNRLISQIVSSITA SLRFDGALNVDLTEFQTNLVPYPRIHFPLATYAPVISAEK AYHEQLSVAEITNACFEPANQMVKCDPRHGKYMACCLLYR GDVVPKDVNAAIATIKTKRSIQFVDWCPTGFKVGINYQPP TVVPGGDLAKVQRAVCMLSNTTAIAEAWARLDHKFDLMYA KRAFVHWYVGEGMEEGEFSEAREDMAALEKDYEEVGVDS B:  MREIVHIQAGQCGNQIGAKFWEVISDEHGIDPTGSYHGDS DLQLERINVYYNEATGNKYVPRAILVDLEPGTMDSVRSGP FGQIFRPDNFVFGQSGAGNNWAKGHYTEGAELVDSVLDVV RKESESCDCLQGFQLTHSLGGGTGSGMGTLLISKIREEYP DRIMNTFSVMPSPKVSDTVVEPYNATLSVHQLVENTDETY CIDNEALYDICFRTLKLTTPTYGDLNHLVSATMSGVTTCL RFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTSRGSQQ YRALTVPELTQQMFDSKNMMAACDPRHGRYLTVAAIFRGR MSMKEVDEQMLNVQNKNSSYFVEWIPNNVKTAVCDIPPRG LKMSATFIGNSTAIQELFKRISEQFTAMFRRKAFLHWYTG EGMDEMEFTEAESNMNDLVSEYQQYQDA C:  MRECISIHVGQAGVQIGNACWELYCLEHGIQPDGQMPSDK TIGGGDDSFNTFFSETGAGKHVPRAVFVDLEPTVIDEVRT GTYRQLFHPEQLITGKEDAANNYARGHYTIGKEIIDLVLD RIRKLADQCTGLQGFLVFHSFGGGTGSGFTSLLMERLSVD YGKKSKLEFSIYPAPQVSTAVVEPYNSILTTHTTLEHSDC AFMVDNEAIYDICRRNLDIERPTYTNLNRLISQIVSSITA SLRFDGALNVDLTEFQTNLVPYPRIHFPLATYAPVISAEK AYHEQLSVAEITNACFEPANQMVKCDPRHGKYMACCLLYR GDVVPKDVNAAIATIKTKRSIQFVDWCPTGFKVGINYQPP TVVPGGDLAKVQRAVCMLSNTTAIAEAWARLDHKFDLMYA KRAFVHWYVGEGMEEGEFSEAREDMAALEKDYEEVGVDSV D:  MREIVHIQAGQCGNQIGAKFWEVISDEHGIDPTGSYHGDS DLQLERINVYYNEATGNKYVPRAILVDLEPGTMDSVRSGP FGQIFRPDNFVFGQSGAGNNWAKGHYTEGAELVDSVLDVV RKESESCDCLQGFQLTHSLGGGTGSGMGTLLISKIREEYP DRIMNTFSVMPSPKVSDTVVEPYNATLSVHQLVENTDETY CIDNEALYDICFRTLKLTTPTYGDLNHLVSATMSGVTTCL RFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTSRGSQQ YRALTVPELTQQMFDSKNMMAACDPRHGRYLTVAAIFRGR MSMKEVDEQMLNVQNKNSSYFVEWIPNNVKTAVCDIPPRG LKMSATFIGNSTAIQELFKRISEQFTAMFRRKAFLHWYTG EGMDEMEFTEAESNMNDLVSEYQQYQDATAD E:  MEVIELNKCTSGQSFEVILKPPSDPSLEEIQKKLEAAEER RKYQEAELLKHLAEKREHEREVIQKAIEENNNFIKMAKEK LAQKMESNKENREAHLAAMLERLQEKDKHAEEVRKNKELK EEA F:  MYTFVVRDENSSVYAEVSRLLLATGQWKRLRKDNPRFNLM LGERNRLPFGRLGHEPGLVQLVNYYRGADKLCRKASLVKL IKTSPELSESCTWFPESYVIYPTNLTDEREVFLAAYNRRR EGREGNVWIAKSSAGAKGEGILISSEASELLDFIDEQGQV HVIQKYLEKPLLLEPGHRKFDIRSWVLVDHLYNIYLYREG VLRTSSEPYNSANFQDKTCHLTNHCIQKEYSKNYGRYEEG NEMFFEEFNQYLMDALNTTLENSILLQIKHIIRSCLMCIE PAISTKHLHYQSFQLFGFDFMVDEELKVWLIEVNGAPACA QKLYAELCQGIVDVAISSVFPLAPTSIFIKL 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 100 type sequence A description BINDING SITE FOR RESIDUE GTP A 501 source : AC1 8) chain A residue 101 type sequence N description BINDING SITE FOR RESIDUE GTP A 501 source : AC1 9) chain A residue 140 type sequence S description BINDING SITE FOR RESIDUE GTP A 501 source : AC1 10) chain A residue 143 type sequence G description BINDING SITE FOR RESIDUE GTP A 501 source : AC1 11) chain A residue 144 type sequence G description BINDING SITE FOR RESIDUE GTP A 501 source : AC1 12) chain A residue 145 type sequence T description BINDING SITE FOR RESIDUE GTP A 501 source : AC1 13) chain A residue 146 type sequence G 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 183 type sequence E description BINDING SITE FOR RESIDUE GTP A 501 source : AC1 16) chain A residue 206 type sequence N description BINDING SITE FOR RESIDUE GTP A 501 source : AC1 17) chain A residue 224 type sequence Y description BINDING SITE FOR RESIDUE GTP A 501 source : AC1 18) chain A residue 228 type sequence N description BINDING SITE FOR RESIDUE GTP A 501 source : AC1 19) chain A residue 231 type sequence I description BINDING SITE FOR RESIDUE GTP A 501 source : AC1 20) chain B residue 254 type sequence K description BINDING SITE FOR RESIDUE GTP A 501 source : AC1 21) chain A residue 39 type sequence D description BINDING SITE FOR RESIDUE CA A 503 source : AC3 22) chain A residue 41 type sequence T description BINDING SITE FOR RESIDUE CA A 503 source : AC3 23) chain A residue 44 type sequence G description BINDING SITE FOR RESIDUE CA A 503 source : AC3 24) chain A residue 55 type sequence E description BINDING SITE FOR RESIDUE CA A 503 source : AC3 25) chain B residue 10 type sequence G description BINDING SITE FOR RESIDUE GDP B 501 source : AC4 26) chain B residue 11 type sequence Q description BINDING SITE FOR RESIDUE GDP B 501 source : AC4 27) chain B residue 12 type sequence C description BINDING SITE FOR RESIDUE GDP B 501 source : AC4 28) chain B residue 15 type sequence Q description BINDING SITE FOR RESIDUE GDP B 501 source : AC4 29) chain B residue 140 type sequence S description BINDING SITE FOR RESIDUE GDP B 501 source : AC4 30) chain B residue 143 type sequence G description BINDING SITE FOR RESIDUE GDP B 501 source : AC4 31) chain B residue 144 type sequence G description BINDING SITE FOR RESIDUE GDP B 501 source : AC4 32) chain B residue 145 type sequence T description BINDING SITE FOR RESIDUE GDP B 501 source : AC4 33) chain B residue 146 type sequence G description BINDING SITE FOR RESIDUE GDP B 501 source : AC4 34) chain B residue 177 type sequence V description BINDING SITE FOR RESIDUE GDP B 501 source : AC4 35) chain B residue 179 type sequence D description BINDING SITE FOR RESIDUE GDP B 501 source : AC4 36) chain B residue 183 type sequence E description BINDING SITE FOR RESIDUE GDP B 501 source : AC4 37) chain B residue 206 type sequence N description BINDING SITE FOR RESIDUE GDP B 501 source : AC4 38) chain B residue 224 type sequence Y description BINDING SITE FOR RESIDUE GDP B 501 source : AC4 39) chain B residue 228 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 293 type sequence Q description BINDING SITE FOR RESIDUE POU B 503 source : AC6 42) chain B residue 296 type sequence F description BINDING SITE FOR RESIDUE POU B 503 source : AC6 43) chain B residue 297 type sequence D description BINDING SITE FOR RESIDUE POU B 503 source : AC6 44) chain B residue 298 type sequence S description BINDING SITE FOR RESIDUE POU B 503 source : AC6 45) chain B residue 308 type sequence R description BINDING SITE FOR RESIDUE POU B 503 source : AC6 46) chain B residue 312 type sequence Y description BINDING SITE FOR RESIDUE POU B 503 source : AC6 47) chain B residue 339 type sequence N description BINDING SITE FOR RESIDUE POU B 503 source : AC6 48) chain B residue 342 type sequence Y description BINDING SITE FOR RESIDUE POU B 503 source : AC6 49) chain B residue 217 type sequence L description BINDING SITE FOR RESIDUE EP B 504 source : AC7 50) chain B residue 219 type sequence L description BINDING SITE FOR RESIDUE EP B 504 source : AC7 51) chain B residue 226 type sequence D description BINDING SITE FOR RESIDUE EP B 504 source : AC7 52) chain B residue 229 type sequence H description BINDING SITE FOR RESIDUE EP B 504 source : AC7 53) chain B residue 272 type sequence F description BINDING SITE FOR RESIDUE EP B 504 source : AC7 54) chain B residue 274 type sequence P description BINDING SITE FOR RESIDUE EP B 504 source : AC7 55) chain B residue 275 type sequence L description BINDING SITE FOR RESIDUE EP B 504 source : AC7 56) chain B residue 276 type sequence T description BINDING SITE FOR RESIDUE EP B 504 source : AC7 57) chain B residue 281 type sequence Q description BINDING SITE FOR RESIDUE EP B 504 source : AC7 58) chain B residue 282 type sequence Q description BINDING SITE FOR RESIDUE EP B 504 source : AC7 59) chain B residue 371 type sequence L description BINDING SITE FOR RESIDUE EP B 504 source : AC7 60) chain B residue 113 type sequence E description BINDING SITE FOR RESIDUE CA B 506 source : AC9 61) chain B residue 158 type sequence R description BINDING SITE FOR RESIDUE MES B 507 source : BC1 62) chain B residue 162 type sequence P description BINDING SITE FOR RESIDUE MES B 507 source : BC1 63) chain B residue 163 type sequence D description BINDING SITE FOR RESIDUE MES B 507 source : BC1 64) chain B residue 164 type sequence R description BINDING SITE FOR RESIDUE MES B 507 source : BC1 65) chain B residue 197 type sequence N description BINDING SITE FOR RESIDUE MES B 507 source : BC1 66) chain B residue 199 type sequence D description BINDING SITE FOR RESIDUE MES B 507 source : BC1 67) chain B residue 253 type sequence R description BINDING SITE FOR RESIDUE MES B 507 source : BC1 68) chain C residue 10 type sequence G description BINDING SITE FOR RESIDUE GTP C 501 source : BC2 69) chain C residue 11 type sequence Q description BINDING SITE FOR RESIDUE GTP C 501 source : BC2 70) chain C residue 12 type sequence A description BINDING SITE FOR RESIDUE GTP C 501 source : BC2 71) chain C residue 15 type sequence Q description BINDING SITE FOR RESIDUE GTP C 501 source : BC2 72) chain C residue 98 type sequence D description BINDING SITE FOR RESIDUE GTP C 501 source : BC2 73) chain C residue 99 type sequence A description BINDING SITE FOR RESIDUE GTP C 501 source : BC2 74) chain C residue 100 type sequence A description BINDING SITE FOR RESIDUE GTP C 501 source : BC2 75) chain C residue 101 type sequence N description BINDING SITE FOR RESIDUE GTP C 501 source : BC2 76) chain C residue 140 type sequence S description BINDING SITE FOR RESIDUE GTP C 501 source : BC2 77) chain C residue 143 type sequence G description BINDING SITE FOR RESIDUE GTP C 501 source : BC2 78) chain C residue 144 type sequence G description BINDING SITE FOR RESIDUE GTP C 501 source : BC2 79) chain C residue 145 type sequence T description BINDING SITE FOR RESIDUE GTP C 501 source : BC2 80) chain C residue 146 type sequence G description BINDING SITE FOR RESIDUE GTP C 501 source : BC2 81) chain C residue 171 type sequence I description BINDING SITE FOR RESIDUE GTP C 501 source : BC2 82) chain C residue 177 type sequence V description BINDING SITE FOR RESIDUE GTP C 501 source : BC2 83) chain C residue 179 type sequence T description BINDING SITE FOR RESIDUE GTP C 501 source : BC2 84) chain C residue 183 type sequence E description BINDING SITE FOR RESIDUE GTP C 501 source : BC2 85) chain C residue 206 type sequence N description BINDING SITE FOR RESIDUE GTP C 501 source : BC2 86) chain C residue 224 type sequence Y description BINDING SITE FOR RESIDUE GTP C 501 source : BC2 87) chain C residue 228 type sequence N description BINDING SITE FOR RESIDUE GTP C 501 source : BC2 88) chain C residue 231 type sequence I description BINDING SITE FOR RESIDUE GTP C 501 source : BC2 89) chain D residue 254 type sequence K description BINDING SITE FOR RESIDUE GTP C 501 source : BC2 90) chain D residue 10 type sequence G description BINDING SITE FOR RESIDUE GDP D 501 source : BC4 91) chain D residue 11 type sequence Q description BINDING SITE FOR RESIDUE GDP D 501 source : BC4 92) chain D residue 12 type sequence C description BINDING SITE FOR RESIDUE GDP D 501 source : BC4 93) chain D residue 15 type sequence Q description BINDING SITE FOR RESIDUE GDP D 501 source : BC4 94) chain D residue 140 type sequence S description BINDING SITE FOR RESIDUE GDP D 501 source : BC4 95) chain D residue 143 type sequence G description BINDING SITE FOR RESIDUE GDP D 501 source : BC4 96) chain D residue 144 type sequence G description BINDING SITE FOR RESIDUE GDP D 501 source : BC4 97) chain D residue 145 type sequence T description BINDING SITE FOR RESIDUE GDP D 501 source : BC4 98) chain D residue 146 type sequence G description BINDING SITE FOR RESIDUE GDP D 501 source : BC4 99) chain D residue 178 type sequence S description BINDING SITE FOR RESIDUE GDP D 501 source : BC4 100) chain D residue 183 type sequence E description BINDING SITE FOR RESIDUE GDP D 501 source : BC4 101) chain D residue 206 type sequence N description BINDING SITE FOR RESIDUE GDP D 501 source : BC4 102) chain D residue 224 type sequence Y description BINDING SITE FOR RESIDUE GDP D 501 source : BC4 103) chain D residue 228 type sequence N description BINDING SITE FOR RESIDUE GDP D 501 source : BC4 104) chain D residue 11 type sequence Q description BINDING SITE FOR RESIDUE MG D 502 source : BC5 105) chain D residue 293 type sequence Q description BINDING SITE FOR RESIDUE POU D 503 source : BC6 106) chain D residue 296 type sequence F description BINDING SITE FOR RESIDUE POU D 503 source : BC6 107) chain D residue 297 type sequence D description BINDING SITE FOR RESIDUE POU D 503 source : BC6 108) chain D residue 298 type sequence S description BINDING SITE FOR RESIDUE POU D 503 source : BC6 109) chain D residue 307 type sequence P description BINDING SITE FOR RESIDUE POU D 503 source : BC6 110) chain D residue 308 type sequence R description BINDING SITE FOR RESIDUE POU D 503 source : BC6 111) chain D residue 312 type sequence Y description BINDING SITE FOR RESIDUE POU D 503 source : BC6 112) chain D residue 335 type sequence V description BINDING SITE FOR RESIDUE POU D 503 source : BC6 113) chain D residue 339 type sequence N description BINDING SITE FOR RESIDUE POU D 503 source : BC6 114) chain D residue 342 type sequence Y description BINDING SITE FOR RESIDUE POU D 503 source : BC6 115) chain D residue 217 type sequence L description BINDING SITE FOR RESIDUE EP D 504 source : BC7 116) chain D residue 226 type sequence D description BINDING SITE FOR RESIDUE EP D 504 source : BC7 117) chain D residue 229 type sequence H description BINDING SITE FOR RESIDUE EP D 504 source : BC7 118) chain D residue 272 type sequence F description BINDING SITE FOR RESIDUE EP D 504 source : BC7 119) chain D residue 274 type sequence P description BINDING SITE FOR RESIDUE EP D 504 source : BC7 120) chain D residue 275 type sequence L description BINDING SITE FOR RESIDUE EP D 504 source : BC7 121) chain D residue 276 type sequence T description BINDING SITE FOR RESIDUE EP D 504 source : BC7 122) chain D residue 284 type sequence R description BINDING SITE FOR RESIDUE EP D 504 source : BC7 123) chain D residue 371 type sequence L description BINDING SITE FOR RESIDUE EP D 504 source : BC7 124) 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 125) 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 126) 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 127) 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 128) 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 129) 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 130) 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 131) 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 132) chain D residue 144 type MOD_RES sequence G description Phosphoserine => ECO:0007744|PubMed:22673903 source Swiss-Prot : SWS_FT_FI1 133) chain D residue 145 type MOD_RES sequence T description Phosphoserine => ECO:0007744|PubMed:22673903 source Swiss-Prot : SWS_FT_FI1 134) chain D residue 146 type MOD_RES sequence G description Phosphoserine => ECO:0007744|PubMed:22673903 source Swiss-Prot : SWS_FT_FI1 135) chain D residue 206 type MOD_RES sequence N description Phosphoserine => ECO:0007744|PubMed:22673903 source Swiss-Prot : SWS_FT_FI1 136) chain D residue 228 type MOD_RES sequence N description Phosphoserine => ECO:0007744|PubMed:22673903 source Swiss-Prot : SWS_FT_FI1 137) chain B residue 144 type MOD_RES sequence G description Phosphoserine => ECO:0007744|PubMed:22673903 source Swiss-Prot : SWS_FT_FI1 138) chain B residue 145 type MOD_RES sequence T description Phosphoserine => ECO:0007744|PubMed:22673903 source Swiss-Prot : SWS_FT_FI1 139) chain B residue 146 type MOD_RES sequence G description Phosphoserine => ECO:0007744|PubMed:22673903 source Swiss-Prot : SWS_FT_FI1 140) chain B residue 206 type MOD_RES sequence N description Phosphoserine => ECO:0007744|PubMed:22673903 source Swiss-Prot : SWS_FT_FI1 141) chain B residue 228 type MOD_RES sequence N description Phosphoserine => ECO:0007744|PubMed:22673903 source Swiss-Prot : SWS_FT_FI1 142) chain D residue 11 type MOD_RES sequence Q description Phosphoserine => ECO:0007744|PubMed:22673903 source Swiss-Prot : SWS_FT_FI1 143) chain D residue 140 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:22673903 source Swiss-Prot : SWS_FT_FI1 144) chain E residue 46 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:22673903 source Swiss-Prot : SWS_FT_FI1 145) chain B residue 140 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:22673903 source Swiss-Prot : SWS_FT_FI1 146) chain C residue 71 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 147) chain C residue 140 type BINDING sequence S description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 148) chain C residue 144 type BINDING sequence G description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 149) chain C residue 145 type BINDING sequence T description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 150) chain C residue 179 type BINDING sequence T description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 151) chain C residue 206 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 152) chain C residue 228 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 153) chain A residue 140 type BINDING sequence S description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 154) chain A residue 144 type BINDING sequence G description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 155) chain A residue 145 type BINDING sequence T description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 156) chain A residue 179 type BINDING sequence T description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 157) chain A residue 206 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 158) chain A residue 228 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 159) chain C residue 11 type BINDING sequence Q description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 160) chain D residue 71 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 161) chain B residue 71 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 162) chain D residue 40 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P99024 source Swiss-Prot : SWS_FT_FI3 163) chain B residue 40 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P99024 source Swiss-Prot : SWS_FT_FI3 164) chain D residue 57 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:Q3KRE8 source Swiss-Prot : SWS_FT_FI4 165) chain B residue 57 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:Q3KRE8 source Swiss-Prot : SWS_FT_FI4 166) chain D residue 60 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P99024 source Swiss-Prot : SWS_FT_FI5 167) chain C residue 48 type MOD_RES sequence S description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P99024 source Swiss-Prot : SWS_FT_FI5 168) chain C residue 232 type MOD_RES sequence S description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P99024 source Swiss-Prot : SWS_FT_FI5 169) chain B residue 60 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P99024 source Swiss-Prot : SWS_FT_FI5 170) chain D residue 174 type MOD_RES sequence S description Phosphoserine; by CDK1 => ECO:0000250|UniProtKB:Q9BVA1 source Swiss-Prot : SWS_FT_FI6 171) chain B residue 174 type MOD_RES sequence S description Phosphoserine; by CDK1 => ECO:0000250|UniProtKB:Q9BVA1 source Swiss-Prot : SWS_FT_FI6 172) chain D residue 287 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:P07437 source Swiss-Prot : SWS_FT_FI7 173) chain D residue 292 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:P07437 source Swiss-Prot : SWS_FT_FI7 174) chain B residue 292 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:P07437 source Swiss-Prot : SWS_FT_FI7 175) chain B residue 287 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:P07437 source Swiss-Prot : SWS_FT_FI7 176) chain B residue 320 type MOD_RES sequence R description Omega-N-methylarginine => ECO:0000250|UniProtKB:P07437 source Swiss-Prot : SWS_FT_FI8 177) chain D residue 320 type MOD_RES sequence R description Omega-N-methylarginine => ECO:0000250|UniProtKB:P07437 source Swiss-Prot : SWS_FT_FI8 178) chain E residue 73-82 type prosite sequence AEKREHEREV description STATHMIN_2 Stathmin family signature 2. AEKREHEREV source prosite : PS01041 179) chain B residue 142-148 type prosite sequence GGGTGSG description TUBULIN Tubulin subunits alpha, beta, and gamma signature. GGGTGSG source prosite : PS00227 180) chain A residue 142-148 type prosite sequence GGGTGSG description TUBULIN Tubulin subunits alpha, beta, and gamma signature. GGGTGSG source prosite : PS00227 181) chain B residue 1-4 type prosite sequence MREI description TUBULIN_B_AUTOREG Tubulin-beta mRNA autoregulation signal. MREI source prosite : PS00228

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