eF-site ID 5mf4-ABCDEF PDB Code 5mf4 Chain A, B, C, D, E, F click to enlarge Title Tubulin-Dictyostatin complex Classification CELL CYCLE Compound Tubulin alpha-1B chain Source ORGANISM_COMMON: Cattle; ORGANISM_SCIENTIFIC: Bos taurus; Sequence A:  RECISIHVGQAGVQIGNACWELYCLEHGIQPDGQMPSDKT IGGGDDSFNTFFSETGAGKHVPRAVFVDLEPTVIDEVRTG TYRQLFHPEQLITGKEDAANNYARGHYTIGKEIIDLVLDR IRKLADQCTGLQGFLVFHSFGGGTGSGFTSLLMERLSVDY GKKSKLEFSIYPAPQVSTAVVEPYNSILTTHTTLEHSDCA FMVDNEAIYDICRRNLDIERPTYTNLNRLISQIVSSITAS LRFDGALNVDLTEFQTNLVPYPRIHFPLATYAPVISAEKH EQLSVAEITNACFEPANQMVKCDPRHGKYMACCLLYRGDV VPKDVNAAIATIKTKRSIQFVDWCPTGFKVGINYQPPTVV PGGDLAKVQRAVCMLSNTTAIAEAWARLDHKFDLMYAKRA FVHWYVGEGMEEGEFSEAREDMAALEKDYEEVGVD B:  REIVHIQAGQCGNQIGAKFWEVISDEHGIDPTGSYHGDSD LQLERINVYYNEATGNKYVPRAILVDLEPGTMDSVRSGPF GQIFRPDNFVFGQSGAGNNWAKGHYTEGAELVDSVLDVVR KESESCDCLQGFQLTHSLGGGTGSGMGTLLISKIREEYPD RIMNTFSVMPSPKVSDTVVEPYNATLSVHQLVENTDETYC IDNEALYDICFRTLKLTTPTYGDLNHLVSATMSGVTTCLR FPGADLRKLAVNMVPFPRLHFFMPGFAPLTSRGSQQYRAL TVPELTQQMFDSKNMMAACDPRHGRYLTVAAIFRGRMSMK EVDEQMLNVQNKNSSYFVEWIPNNVKTAVCDIPPRGLKMS ATFIGNSTAIQELFKRISEQFTAMFRRKAFLHWYTGEGMD EMEFTEAESNMNDLVSEYQQYQDATAD C:  MRECISIHVGQAGVQIGNACWELYCLEHGIQPDGQMPSDK TIGGGDDSFNTFFSETGAGKHVPRAVFVDLEPTVIDEVRT GTYRQLFHPEQLITGKEDAANNYARGHYTIGKEIIDLVLD RIRKLADQCTGLQGFLVFHSFGGGTGSGFTSLLMERLSVD YGKKSKLEFSIYPAPQVSTAVVEPYNSILTTHTTLEHSDC AFMVDNEAIYDICRRNLDIERPTYTNLNRLISQIVSSITA SLRFDGALNVDLTEFQTNLVPYPRIHFPLATYAPVISAEK AYHEQLSVAEITNACFEPANQMVKCDPRHGKYMACCLLYR GDVVPKDVNAAIATIKTKRSIQFVDWCPTGFKVGINYQPP TVVPGGDLAKVQRAVCMLSNTTAIAEAWARLDHKFDLMYA KRAFVHWYVGEGMEEGEFSEAREDMAALEKDYEEVGVDSV D:  REIVHIQAGQCGNQIGAKFWEVISDEHGIDPTGSYHGDSD LQLERINVYYNEATGNKYVPRAILVDLEPGTMDSVRSGPF GQIFRPDNFVFGQSGAGNNWAKGHYTEGAELVDSVLDVVR KESESCDCLQGFQLTHSLGGGTGSGMGTLLISKIREEYPD RIMNTFSVMPSPKVSDTVVEPYNATLSVHQLVENTDETYC IDNEALYDICFRTLKLTTPTYGDLNHLVSATMSGVTTCLR FPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTSRGSLTV PELTQQMFDSKNMMAACDPRHGRYLTVAAIFRGRMSMKEV DEQMLNVQNKNSSYFVEWIPNNVKTAVCDIPPRGLKMSAT FIGNSTAIQELFKRISEQFTAMFRRKAFLHWYTGEGMDEM EFTEAESNMNDLVSEYQQYQDATAD E:  MEVIELNKCTSGQSFEVILKPPSDPSLEEIQKKLEAAEER RKYQEAELLKHLAEKREHEREVIQKAIEENNNFIKMAKEK LAQKMESNKENREAHLAAMLERLQEKDKHAEEVRKNKELK EE F:  MYTFVVRDENSSVYAEVSRLLLATGQWKRLRKDNPRFNLM LGERNRLPFGRLGHEPGLVQLVNYYRGADKLCRKASLVKL IKTSPELSESCTWFPESYVIYPTDEREVFLAAYNRRREGR EGNVWIAKGILISSEASELLDFIDVHVIQKYLEKPLLLEP GHRKFDIRSWVLVDHLYNIYLYREGVLRTSPYNSDKTCHL TNHCIQKYGRYEEGNEMFFEEFNQYLMDALNTTLENSILL QIKHIIRSCLMCIEPAISTKHLHYQSFQLFGFDFMVDEEL KVWLIEVNGAPACAQKLYAELCQGIVDVAISSVFPLATSI FIKLHH 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 71 type sequence E description binding site for residue MG A 502 source : AC2 22) chain A residue 39 type sequence D description binding site for residue CA A 503 source : AC3 23) chain A residue 41 type sequence T description binding site for residue CA A 503 source : AC3 24) chain A residue 44 type sequence G description binding site for residue CA A 503 source : AC3 25) chain A residue 55 type sequence E description binding site for residue CA A 503 source : AC3 26) chain A residue 216 type sequence N description binding site for residue GOL A 505 source : AC4 27) chain A residue 274 type sequence P description binding site for residue GOL A 505 source : AC4 28) chain A residue 275 type sequence V description binding site for residue GOL A 505 source : AC4 29) chain A residue 294 type sequence A description binding site for residue GOL A 505 source : AC4 30) chain A residue 300 type sequence N description binding site for residue GOL A 505 source : AC4 31) chain B residue 10 type sequence G description binding site for residue GDP B 501 source : AC5 32) chain B residue 11 type sequence Q description binding site for residue GDP B 501 source : AC5 33) chain B residue 12 type sequence C description binding site for residue GDP B 501 source : AC5 34) chain B residue 15 type sequence Q description binding site for residue GDP B 501 source : AC5 35) chain B residue 140 type sequence S description binding site for residue GDP B 501 source : AC5 36) chain B residue 143 type sequence G description binding site for residue GDP B 501 source : AC5 37) chain B residue 144 type sequence G description binding site for residue GDP B 501 source : AC5 38) chain B residue 145 type sequence T description binding site for residue GDP B 501 source : AC5 39) chain B residue 146 type sequence G description binding site for residue GDP B 501 source : AC5 40) chain B residue 177 type sequence V description binding site for residue GDP B 501 source : AC5 41) chain B residue 179 type sequence D description binding site for residue GDP B 501 source : AC5 42) chain B residue 183 type sequence E description binding site for residue GDP B 501 source : AC5 43) chain B residue 206 type sequence N description binding site for residue GDP B 501 source : AC5 44) chain B residue 224 type sequence Y description binding site for residue GDP B 501 source : AC5 45) chain B residue 228 type sequence N description binding site for residue GDP B 501 source : AC5 46) chain B residue 11 type sequence Q description binding site for residue MG B 502 source : AC6 47) chain B residue 179 type sequence D description binding site for residue MG B 502 source : AC6 48) chain B residue 217 type sequence L description binding site for residue 7LZ B 503 source : AC7 49) chain B residue 226 type sequence D description binding site for residue 7LZ B 503 source : AC7 50) chain B residue 229 type sequence H description binding site for residue 7LZ B 503 source : AC7 51) chain B residue 274 type sequence P description binding site for residue 7LZ B 503 source : AC7 52) chain B residue 275 type sequence L description binding site for residue 7LZ B 503 source : AC7 53) chain B residue 276 type sequence T description binding site for residue 7LZ B 503 source : AC7 54) chain B residue 278 type sequence R description binding site for residue 7LZ B 503 source : AC7 55) chain B residue 282 type sequence Q description binding site for residue 7LZ B 503 source : AC7 56) chain B residue 369 type sequence R description binding site for residue 7LZ B 503 source : AC7 57) chain B residue 370 type sequence G description binding site for residue 7LZ B 503 source : AC7 58) chain C residue 10 type sequence G description binding site for residue GTP C 501 source : AC8 59) chain C residue 11 type sequence Q description binding site for residue GTP C 501 source : AC8 60) chain C residue 12 type sequence A description binding site for residue GTP C 501 source : AC8 61) chain C residue 15 type sequence Q description binding site for residue GTP C 501 source : AC8 62) chain C residue 98 type sequence D description binding site for residue GTP C 501 source : AC8 63) chain C residue 99 type sequence A description binding site for residue GTP C 501 source : AC8 64) chain C residue 101 type sequence N description binding site for residue GTP C 501 source : AC8 65) chain C residue 140 type sequence S description binding site for residue GTP C 501 source : AC8 66) chain C residue 143 type sequence G description binding site for residue GTP C 501 source : AC8 67) chain C residue 144 type sequence G description binding site for residue GTP C 501 source : AC8 68) chain C residue 145 type sequence T description binding site for residue GTP C 501 source : AC8 69) chain C residue 146 type sequence G description binding site for residue GTP C 501 source : AC8 70) chain C residue 171 type sequence I description binding site for residue GTP C 501 source : AC8 71) chain C residue 177 type sequence V description binding site for residue GTP C 501 source : AC8 72) chain C residue 179 type sequence T description binding site for residue GTP C 501 source : AC8 73) chain C residue 183 type sequence E description binding site for residue GTP C 501 source : AC8 74) chain C residue 206 type sequence N description binding site for residue GTP C 501 source : AC8 75) chain C residue 224 type sequence Y description binding site for residue GTP C 501 source : AC8 76) chain C residue 228 type sequence N description binding site for residue GTP C 501 source : AC8 77) chain C residue 231 type sequence I description binding site for residue GTP C 501 source : AC8 78) chain D residue 254 type sequence K description binding site for residue GTP C 501 source : AC8 79) chain C residue 39 type sequence D description binding site for residue CA C 503 source : AD1 80) chain C residue 41 type sequence T description binding site for residue CA C 503 source : AD1 81) chain C residue 44 type sequence G description binding site for residue CA C 503 source : AD1 82) chain C residue 55 type sequence E description binding site for residue CA C 503 source : AD1 83) chain D residue 10 type sequence G description binding site for residue GDP D 501 source : AD2 84) chain D residue 11 type sequence Q description binding site for residue GDP D 501 source : AD2 85) chain D residue 12 type sequence C description binding site for residue GDP D 501 source : AD2 86) chain D residue 15 type sequence Q description binding site for residue GDP D 501 source : AD2 87) chain D residue 101 type sequence N description binding site for residue GDP D 501 source : AD2 88) chain D residue 140 type sequence S description binding site for residue GDP D 501 source : AD2 89) chain D residue 143 type sequence G description binding site for residue GDP D 501 source : AD2 90) chain D residue 144 type sequence G description binding site for residue GDP D 501 source : AD2 91) chain D residue 145 type sequence T description binding site for residue GDP D 501 source : AD2 92) chain D residue 146 type sequence G description binding site for residue GDP D 501 source : AD2 93) chain D residue 177 type sequence V description binding site for residue GDP D 501 source : AD2 94) chain D residue 179 type sequence D description binding site for residue GDP D 501 source : AD2 95) chain D residue 183 type sequence E description binding site for residue GDP D 501 source : AD2 96) chain D residue 206 type sequence N description binding site for residue GDP D 501 source : AD2 97) chain D residue 224 type sequence Y description binding site for residue GDP D 501 source : AD2 98) chain D residue 228 type sequence N description binding site for residue GDP D 501 source : AD2 99) chain D residue 11 type sequence Q description binding site for residue MG D 502 source : AD3 100) chain D residue 179 type sequence D description binding site for residue MG D 502 source : AD3 101) chain D residue 217 type sequence L description binding site for residue 7LZ D 503 source : AD4 102) chain D residue 219 type sequence L description binding site for residue 7LZ D 503 source : AD4 103) chain D residue 226 type sequence D description binding site for residue 7LZ D 503 source : AD4 104) chain D residue 229 type sequence H description binding site for residue 7LZ D 503 source : AD4 105) chain D residue 274 type sequence P description binding site for residue 7LZ D 503 source : AD4 106) chain D residue 275 type sequence L description binding site for residue 7LZ D 503 source : AD4 107) chain D residue 276 type sequence T description binding site for residue 7LZ D 503 source : AD4 108) chain D residue 278 type sequence R description binding site for residue 7LZ D 503 source : AD4 109) chain D residue 369 type sequence R description binding site for residue 7LZ D 503 source : AD4 110) chain D residue 370 type sequence G description binding site for residue 7LZ D 503 source : AD4 111) chain D residue 371 type sequence L description binding site for residue 7LZ D 503 source : AD4 112) chain D residue 158 type sequence R description binding site for residue MES D 504 source : AD5 113) chain D residue 162 type sequence P description binding site for residue MES D 504 source : AD5 114) chain D residue 163 type sequence D description binding site for residue MES D 504 source : AD5 115) chain D residue 164 type sequence R description binding site for residue MES D 504 source : AD5 116) chain D residue 197 type sequence N description binding site for residue MES D 504 source : AD5 117) chain D residue 199 type sequence D description binding site for residue MES D 504 source : AD5 118) chain D residue 253 type sequence R description binding site for residue MES D 504 source : AD5 119) chain F residue 331 type sequence E description binding site for residue CA F 401 source : AD6 120) chain F residue 333 type sequence N description binding site for residue CA F 401 source : AD6 121) chain F residue 74 type sequence K description binding site for residue ACP F 402 source : AD7 122) chain F residue 150 type sequence K description binding site for residue ACP F 402 source : AD7 123) chain F residue 183 type sequence Q description binding site for residue ACP F 402 source : AD7 124) chain F residue 184 type sequence K description binding site for residue ACP F 402 source : AD7 125) chain F residue 185 type sequence Y description binding site for residue ACP F 402 source : AD7 126) chain F residue 186 type sequence L description binding site for residue ACP F 402 source : AD7 127) chain F residue 198 type sequence K description binding site for residue ACP F 402 source : AD7 128) chain F residue 200 type sequence D description binding site for residue ACP F 402 source : AD7 129) chain F residue 222 type sequence R description binding site for residue ACP F 402 source : AD7 130) chain F residue 240 type sequence L description binding site for residue ACP F 402 source : AD7 131) chain F residue 241 type sequence T description binding site for residue ACP F 402 source : AD7 132) chain F residue 242 type sequence N description binding site for residue ACP F 402 source : AD7 133) chain F residue 318 type sequence D description binding site for residue ACP F 402 source : AD7 134) chain F residue 331 type sequence E description binding site for residue ACP F 402 source : AD7 135) chain F residue 333 type sequence N description binding site for residue ACP F 402 source : AD7 136) chain A residue 105 type sequence R description binding site for residues GOL A 504 and MES B 504 source : AD8 137) chain A residue 411 type sequence E description binding site for residues GOL A 504 and MES B 504 source : AD8 138) chain B residue 158 type sequence R description binding site for residues GOL A 504 and MES B 504 source : AD8 139) chain B residue 162 type sequence P description binding site for residues GOL A 504 and MES B 504 source : AD8 140) chain B residue 163 type sequence D description binding site for residues GOL A 504 and MES B 504 source : AD8 141) chain B residue 164 type sequence R description binding site for residues GOL A 504 and MES B 504 source : AD8 142) chain B residue 197 type sequence N description binding site for residues GOL A 504 and MES B 504 source : AD8 143) chain B residue 198 type sequence T description binding site for residues GOL A 504 and MES B 504 source : AD8 144) chain B residue 199 type sequence D description binding site for residues GOL A 504 and MES B 504 source : AD8 145) chain B residue 253 type sequence R description binding site for residues GOL A 504 and MES B 504 source : AD8 146) 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 147) 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 148) 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 149) 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 150) chain B residue 71 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 151) chain C residue 71 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 152) chain C residue 140 type BINDING sequence S description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 153) chain C residue 144 type BINDING sequence G description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 154) chain C residue 145 type BINDING sequence T description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 155) chain C residue 179 type BINDING sequence T description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 156) chain C residue 206 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 157) chain C residue 228 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 158) chain D residue 71 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 159) chain A residue 140 type BINDING sequence S description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 160) chain A residue 144 type BINDING sequence G description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 161) chain A residue 145 type BINDING sequence T description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 162) chain A residue 179 type BINDING sequence T description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 163) chain A residue 206 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 164) chain A residue 228 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 165) chain C residue 11 type BINDING sequence Q description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 166) chain B residue 40 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P99024 source Swiss-Prot : SWS_FT_FI3 167) chain D residue 40 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P99024 source Swiss-Prot : SWS_FT_FI3 168) chain B residue 57 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:Q3KRE8 source Swiss-Prot : SWS_FT_FI4 169) chain D residue 57 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:Q3KRE8 source Swiss-Prot : SWS_FT_FI4 170) chain B residue 174 type MOD_RES sequence S description Phosphoserine; by CDK1 => ECO:0000250|UniProtKB:Q9BVA1 source Swiss-Prot : SWS_FT_FI6 171) chain D residue 174 type MOD_RES sequence S description Phosphoserine; by CDK1 => ECO:0000250|UniProtKB:Q9BVA1 source Swiss-Prot : SWS_FT_FI6 172) chain B residue 287 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:P07437 source Swiss-Prot : SWS_FT_FI7 173) chain B residue 292 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:P07437 source Swiss-Prot : SWS_FT_FI7 174) chain D residue 287 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:P07437 source Swiss-Prot : SWS_FT_FI7 175) chain D residue 292 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 19 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:22673903 source Swiss-Prot : SWS_FT_FI1 179) chain D residue 144 type MOD_RES sequence G description Phosphoserine => ECO:0007744|PubMed:22673903 source Swiss-Prot : SWS_FT_FI1 180) chain D residue 145 type MOD_RES sequence T description Phosphoserine => ECO:0007744|PubMed:22673903 source Swiss-Prot : SWS_FT_FI1 181) chain D residue 146 type MOD_RES sequence G description Phosphoserine => ECO:0007744|PubMed:22673903 source Swiss-Prot : SWS_FT_FI1 182) chain D residue 206 type MOD_RES sequence N description Phosphoserine => ECO:0007744|PubMed:22673903 source Swiss-Prot : SWS_FT_FI1 183) chain D residue 228 type MOD_RES sequence N description Phosphoserine => ECO:0007744|PubMed:22673903 source Swiss-Prot : SWS_FT_FI1 184) chain B residue 140 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:22673903 source Swiss-Prot : SWS_FT_FI1 185) chain B residue 144 type MOD_RES sequence G description Phosphoserine => ECO:0007744|PubMed:22673903 source Swiss-Prot : SWS_FT_FI1 186) chain B residue 145 type MOD_RES sequence T description Phosphoserine => ECO:0007744|PubMed:22673903 source Swiss-Prot : SWS_FT_FI1 187) chain B residue 146 type MOD_RES sequence G description Phosphoserine => ECO:0007744|PubMed:22673903 source Swiss-Prot : SWS_FT_FI1 188) chain B residue 206 type MOD_RES sequence N description Phosphoserine => ECO:0007744|PubMed:22673903 source Swiss-Prot : SWS_FT_FI1 189) chain B residue 228 type MOD_RES sequence N description Phosphoserine => ECO:0007744|PubMed:22673903 source Swiss-Prot : SWS_FT_FI1 190) chain D residue 11 type MOD_RES sequence Q description Phosphoserine => ECO:0007744|PubMed:22673903 source Swiss-Prot : SWS_FT_FI1 191) chain D residue 140 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:22673903 source Swiss-Prot : SWS_FT_FI1 192) 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 193) 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 194) 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 195) 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 196) chain B residue 142-148 type prosite sequence GGGTGSG description TUBULIN Tubulin subunits alpha, beta, and gamma signature. GGGTGSG source prosite : PS00227 197) chain A residue 142-148 type prosite sequence GGGTGSG description TUBULIN Tubulin subunits alpha, beta, and gamma signature. GGGTGSG source prosite : PS00227 198) chain E residue 73-82 type prosite sequence AEKREHEREV description STATHMIN_2 Stathmin family signature 2. AEKREHEREV source prosite : PS01041 199) chain B residue 60 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P99024 source Swiss-Prot : SWS_FT_FI5 200) chain D residue 60 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P99024 source Swiss-Prot : SWS_FT_FI5 201) chain C residue 48 type MOD_RES sequence S description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P99024 source Swiss-Prot : SWS_FT_FI5 202) chain C residue 232 type MOD_RES sequence S description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P99024 source Swiss-Prot : SWS_FT_FI5

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