eF-site ID 4yj3-ABCDEF PDB Code 4yj3 Chain A, B, C, D, E, F click to enlarge Title Crystal structure of tubulin bound to compound 2 Classification CELL CYCLE Compound Tubulin alpha-1B chain Source ORGANISM_COMMON: Bovine; ORGANISM_SCIENTIFIC: Bos taurus; 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:  DMEVIELNKCTSGQSWEVILKPPDPSLEEIQKKLEAAEER RKYQEAELLKHLAEKREHEREVIQKAIEENNNFIKMAKEK LAQKMESNKENREAHLAAMLERLQEKDKHAEEVRKNKELK E F:  MYTFVVRDENSSVYAEVSRLLLATGQWKRLRKDNPRFNLM LGERNRLPFGRLGHEPGLVQLVNYYRGADKLCRKASLVKL IKTSPELSESCTWFPESYVIYDEREVFLAAYNGNVWIAKS ISSEASELLDFIVIQKYLEKPLLLEPGHRKFDIRSWVLVD HLYNIYLYREGVLRTMFFEEFNQYLMDALNTTLENSILLQ IKHIIRSCLMCIEPAISTKHLHYQSFQLFGFDFMVDEELK VWLIEVNGAPACAQKLYAELCQGIVDVAISSVFPLASIFI KL Description Functional site 1) chain A residue 71 type sequence E description binding site for residue MG A 501 source : AC1 2) chain A residue 10 type sequence G description binding site for residue GTP A 502 source : AC2 3) chain A residue 11 type sequence Q description binding site for residue GTP A 502 source : AC2 4) chain A residue 12 type sequence A description binding site for residue GTP A 502 source : AC2 5) chain A residue 15 type sequence Q description binding site for residue GTP A 502 source : AC2 6) chain A residue 98 type sequence D description binding site for residue GTP A 502 source : AC2 7) chain A residue 99 type sequence A description binding site for residue GTP A 502 source : AC2 8) chain A residue 100 type sequence A description binding site for residue GTP A 502 source : AC2 9) chain A residue 101 type sequence N description binding site for residue GTP A 502 source : AC2 10) chain A residue 140 type sequence S description binding site for residue GTP A 502 source : AC2 11) chain A residue 143 type sequence G description binding site for residue GTP A 502 source : AC2 12) chain A residue 144 type sequence G description binding site for residue GTP A 502 source : AC2 13) chain A residue 145 type sequence T description binding site for residue GTP A 502 source : AC2 14) chain A residue 177 type sequence V description binding site for residue GTP A 502 source : AC2 15) chain A residue 178 type sequence S description binding site for residue GTP A 502 source : AC2 16) chain A residue 179 type sequence T description binding site for residue GTP A 502 source : AC2 17) chain A residue 183 type sequence E description binding site for residue GTP A 502 source : AC2 18) chain A residue 206 type sequence N description binding site for residue GTP A 502 source : AC2 19) chain A residue 224 type sequence Y description binding site for residue GTP A 502 source : AC2 20) chain A residue 228 type sequence N description binding site for residue GTP A 502 source : AC2 21) chain A residue 231 type sequence I description binding site for residue GTP A 502 source : AC2 22) chain B residue 254 type sequence K description binding site for residue GTP A 502 source : AC2 23) chain A residue 39 type sequence D description binding site for residue CA A 503 source : AC3 24) chain A residue 41 type sequence T description binding site for residue CA A 503 source : AC3 25) chain A residue 44 type sequence G description binding site for residue CA A 503 source : AC3 26) chain A residue 45 type sequence G description binding site for residue CA A 503 source : AC3 27) chain A residue 55 type sequence E description binding site for residue CA A 503 source : AC3 28) chain B residue 10 type sequence G description binding site for residue GDP B 501 source : AC4 29) chain B residue 11 type sequence Q description binding site for residue GDP B 501 source : AC4 30) chain B residue 12 type sequence C description binding site for residue GDP B 501 source : AC4 31) chain B residue 15 type sequence Q description binding site for residue GDP B 501 source : AC4 32) chain B residue 140 type sequence S description binding site for residue GDP B 501 source : AC4 33) chain B residue 143 type sequence G description binding site for residue GDP B 501 source : AC4 34) chain B residue 144 type sequence G description binding site for residue GDP B 501 source : AC4 35) chain B residue 145 type sequence T description binding site for residue GDP B 501 source : AC4 36) chain B residue 146 type sequence G description binding site for residue GDP B 501 source : AC4 37) chain B residue 177 type sequence V description binding site for residue GDP B 501 source : AC4 38) chain B residue 179 type sequence D description binding site for residue GDP B 501 source : AC4 39) chain B residue 183 type sequence E description binding site for residue GDP B 501 source : AC4 40) chain B residue 206 type sequence N description binding site for residue GDP B 501 source : AC4 41) chain B residue 224 type sequence Y description binding site for residue GDP B 501 source : AC4 42) chain B residue 228 type sequence N description binding site for residue GDP B 501 source : AC4 43) chain B residue 11 type sequence Q description binding site for residue MG B 502 source : AC5 44) chain A residue 179 type sequence T description binding site for residue 4EE B 503 source : AC6 45) chain A residue 181 type sequence V description binding site for residue 4EE B 503 source : AC6 46) chain B residue 241 type sequence C description binding site for residue 4EE B 503 source : AC6 47) chain B residue 250 type sequence A description binding site for residue 4EE B 503 source : AC6 48) chain B residue 255 type sequence L description binding site for residue 4EE B 503 source : AC6 49) chain B residue 258 type sequence N description binding site for residue 4EE B 503 source : AC6 50) chain B residue 314 type sequence T description binding site for residue 4EE B 503 source : AC6 51) chain B residue 315 type sequence V description binding site for residue 4EE B 503 source : AC6 52) chain B residue 316 type sequence A description binding site for residue 4EE B 503 source : AC6 53) chain B residue 317 type sequence A description binding site for residue 4EE B 503 source : AC6 54) chain B residue 318 type sequence I description binding site for residue 4EE B 503 source : AC6 55) chain B residue 350 type sequence N description binding site for residue 4EE B 503 source : AC6 56) chain B residue 352 type sequence K description binding site for residue 4EE B 503 source : AC6 57) chain B residue 354 type sequence A description binding site for residue 4EE B 503 source : AC6 58) chain B residue 378 type sequence I description binding site for residue 4EE B 503 source : AC6 59) chain B residue 110 type sequence E description binding site for residue CA B 504 source : AC7 60) chain B residue 113 type sequence E description binding site for residue CA B 504 source : AC7 61) chain C residue 282 type sequence Y description binding site for residue CA B 504 source : AC7 62) chain A residue 407 type sequence W description binding site for residue MES B 505 source : AC8 63) chain B residue 158 type sequence R description binding site for residue MES B 505 source : AC8 64) chain B residue 162 type sequence P description binding site for residue MES B 505 source : AC8 65) chain B residue 163 type sequence D description binding site for residue MES B 505 source : AC8 66) chain B residue 164 type sequence R description binding site for residue MES B 505 source : AC8 67) chain B residue 165 type sequence I description binding site for residue MES B 505 source : AC8 68) chain B residue 197 type sequence N description binding site for residue MES B 505 source : AC8 69) chain B residue 199 type sequence D description binding site for residue MES B 505 source : AC8 70) chain B residue 253 type sequence R description binding site for residue MES B 505 source : AC8 71) chain C residue 11 type sequence Q description binding site for residue MG C 501 source : AC9 72) chain C residue 71 type sequence E description binding site for residue MG C 501 source : AC9 73) chain C residue 10 type sequence G description binding site for residue GTP C 502 source : AD1 74) chain C residue 11 type sequence Q description binding site for residue GTP C 502 source : AD1 75) chain C residue 12 type sequence A description binding site for residue GTP C 502 source : AD1 76) chain C residue 15 type sequence Q description binding site for residue GTP C 502 source : AD1 77) chain C residue 98 type sequence D description binding site for residue GTP C 502 source : AD1 78) chain C residue 99 type sequence A description binding site for residue GTP C 502 source : AD1 79) chain C residue 100 type sequence A description binding site for residue GTP C 502 source : AD1 80) chain C residue 101 type sequence N description binding site for residue GTP C 502 source : AD1 81) chain C residue 140 type sequence S description binding site for residue GTP C 502 source : AD1 82) chain C residue 143 type sequence G description binding site for residue GTP C 502 source : AD1 83) chain C residue 144 type sequence G description binding site for residue GTP C 502 source : AD1 84) chain C residue 145 type sequence T description binding site for residue GTP C 502 source : AD1 85) chain C residue 146 type sequence G description binding site for residue GTP C 502 source : AD1 86) chain C residue 171 type sequence I description binding site for residue GTP C 502 source : AD1 87) chain C residue 179 type sequence T description binding site for residue GTP C 502 source : AD1 88) chain C residue 183 type sequence E description binding site for residue GTP C 502 source : AD1 89) chain C residue 206 type sequence N description binding site for residue GTP C 502 source : AD1 90) chain C residue 224 type sequence Y description binding site for residue GTP C 502 source : AD1 91) chain C residue 228 type sequence N description binding site for residue GTP C 502 source : AD1 92) chain D residue 254 type sequence K description binding site for residue GTP C 502 source : AD1 93) chain C residue 39 type sequence D description binding site for residue CA C 503 source : AD2 94) chain C residue 41 type sequence T description binding site for residue CA C 503 source : AD2 95) chain C residue 44 type sequence G description binding site for residue CA C 503 source : AD2 96) chain C residue 55 type sequence E description binding site for residue CA C 503 source : AD2 97) chain C residue 262 type sequence Y description binding site for residue IMD C 504 source : AD3 98) chain C residue 431 type sequence D description binding site for residue IMD C 504 source : AD3 99) chain C residue 434 type sequence E description binding site for residue IMD C 504 source : AD3 100) chain D residue 10 type sequence G description binding site for residue GDP D 501 source : AD4 101) chain D residue 11 type sequence Q description binding site for residue GDP D 501 source : AD4 102) chain D residue 12 type sequence C description binding site for residue GDP D 501 source : AD4 103) chain D residue 15 type sequence Q description binding site for residue GDP D 501 source : AD4 104) chain D residue 101 type sequence N description binding site for residue GDP D 501 source : AD4 105) chain D residue 140 type sequence S description binding site for residue GDP D 501 source : AD4 106) chain D residue 143 type sequence G description binding site for residue GDP D 501 source : AD4 107) chain D residue 144 type sequence G description binding site for residue GDP D 501 source : AD4 108) chain D residue 145 type sequence T description binding site for residue GDP D 501 source : AD4 109) chain D residue 146 type sequence G description binding site for residue GDP D 501 source : AD4 110) chain D residue 177 type sequence V description binding site for residue GDP D 501 source : AD4 111) chain D residue 179 type sequence D description binding site for residue GDP D 501 source : AD4 112) chain D residue 183 type sequence E description binding site for residue GDP D 501 source : AD4 113) chain D residue 206 type sequence N description binding site for residue GDP D 501 source : AD4 114) chain D residue 224 type sequence Y description binding site for residue GDP D 501 source : AD4 115) chain D residue 228 type sequence N description binding site for residue GDP D 501 source : AD4 116) chain D residue 11 type sequence Q description binding site for residue MG D 502 source : AD5 117) chain D residue 101 type sequence N description binding site for residue MG D 502 source : AD5 118) chain D residue 179 type sequence D description binding site for residue MG D 502 source : AD5 119) chain C residue 180 type sequence A description binding site for residue 4EE D 503 source : AD6 120) chain C residue 181 type sequence V description binding site for residue 4EE D 503 source : AD6 121) chain D residue 241 type sequence C description binding site for residue 4EE D 503 source : AD6 122) chain D residue 242 type sequence L description binding site for residue 4EE D 503 source : AD6 123) chain D residue 250 type sequence A description binding site for residue 4EE D 503 source : AD6 124) chain D residue 254 type sequence K description binding site for residue 4EE D 503 source : AD6 125) chain D residue 255 type sequence L description binding site for residue 4EE D 503 source : AD6 126) chain D residue 258 type sequence N description binding site for residue 4EE D 503 source : AD6 127) chain D residue 314 type sequence T description binding site for residue 4EE D 503 source : AD6 128) chain D residue 315 type sequence V description binding site for residue 4EE D 503 source : AD6 129) chain D residue 316 type sequence A description binding site for residue 4EE D 503 source : AD6 130) chain D residue 317 type sequence A description binding site for residue 4EE D 503 source : AD6 131) chain D residue 318 type sequence I description binding site for residue 4EE D 503 source : AD6 132) chain D residue 350 type sequence N description binding site for residue 4EE D 503 source : AD6 133) chain D residue 352 type sequence K description binding site for residue 4EE D 503 source : AD6 134) chain D residue 354 type sequence A description binding site for residue 4EE D 503 source : AD6 135) chain D residue 378 type sequence I description binding site for residue 4EE D 503 source : AD6 136) chain B residue 142-148 type prosite sequence GGGTGSG description TUBULIN Tubulin subunits alpha, beta, and gamma signature. GGGTGSG source prosite : PS00227 137) chain A residue 142-148 type prosite sequence GGGTGSG description TUBULIN Tubulin subunits alpha, beta, and gamma signature. GGGTGSG source prosite : PS00227 138) chain B residue 1-4 type prosite sequence MREI description TUBULIN_B_AUTOREG Tubulin-beta mRNA autoregulation signal. MREI source prosite : PS00228 139) chain E residue 73-82 type prosite sequence AEKREHEREV description STATHMIN_2 Stathmin family signature 2. AEKREHEREV source prosite : PS01041 140) chain E residue 19 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:22673903 source Swiss-Prot : SWS_FT_FI1 141) chain D residue 144 type MOD_RES sequence G description Phosphoserine => ECO:0007744|PubMed:22673903 source Swiss-Prot : SWS_FT_FI1 142) chain D residue 145 type MOD_RES sequence T description Phosphoserine => ECO:0007744|PubMed:22673903 source Swiss-Prot : SWS_FT_FI1 143) chain D residue 146 type MOD_RES sequence G description Phosphoserine => ECO:0007744|PubMed:22673903 source Swiss-Prot : SWS_FT_FI1 144) chain D residue 206 type MOD_RES sequence N description Phosphoserine => ECO:0007744|PubMed:22673903 source Swiss-Prot : SWS_FT_FI1 145) chain D residue 228 type MOD_RES sequence N description Phosphoserine => ECO:0007744|PubMed:22673903 source Swiss-Prot : SWS_FT_FI1 146) chain B residue 140 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:22673903 source Swiss-Prot : SWS_FT_FI1 147) chain B residue 144 type MOD_RES sequence G description Phosphoserine => ECO:0007744|PubMed:22673903 source Swiss-Prot : SWS_FT_FI1 148) chain B residue 145 type MOD_RES sequence T description Phosphoserine => ECO:0007744|PubMed:22673903 source Swiss-Prot : SWS_FT_FI1 149) chain B residue 146 type MOD_RES sequence G description Phosphoserine => ECO:0007744|PubMed:22673903 source Swiss-Prot : SWS_FT_FI1 150) chain B residue 206 type MOD_RES sequence N description Phosphoserine => ECO:0007744|PubMed:22673903 source Swiss-Prot : SWS_FT_FI1 151) chain B residue 228 type MOD_RES sequence N description Phosphoserine => ECO:0007744|PubMed:22673903 source Swiss-Prot : SWS_FT_FI1 152) chain D residue 11 type MOD_RES sequence Q description Phosphoserine => ECO:0007744|PubMed:22673903 source Swiss-Prot : SWS_FT_FI1 153) chain D residue 140 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:22673903 source Swiss-Prot : SWS_FT_FI1 154) 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 155) 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 156) 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 157) 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 158) 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 159) 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 160) 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 161) 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 162) chain B residue 71 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 163) chain C residue 71 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 164) chain C residue 140 type BINDING sequence S description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 165) chain C residue 144 type BINDING sequence G description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 166) chain C residue 145 type BINDING sequence T description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 167) chain C residue 179 type BINDING sequence T description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 168) chain C residue 206 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 169) chain C residue 228 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 170) chain D residue 71 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 171) chain A residue 140 type BINDING sequence S description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 172) chain A residue 144 type BINDING sequence G description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 173) chain A residue 145 type BINDING sequence T description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 174) chain A residue 179 type BINDING sequence T description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 175) chain A residue 206 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 176) chain A residue 228 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 177) chain C residue 11 type BINDING sequence Q description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 178) chain B residue 40 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P99024 source Swiss-Prot : SWS_FT_FI3 179) chain D residue 40 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P99024 source Swiss-Prot : SWS_FT_FI3 180) chain B residue 57 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:Q3KRE8 source Swiss-Prot : SWS_FT_FI4 181) chain D residue 57 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:Q3KRE8 source Swiss-Prot : SWS_FT_FI4 182) chain B residue 60 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P99024 source Swiss-Prot : SWS_FT_FI5 183) chain D residue 60 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P99024 source Swiss-Prot : SWS_FT_FI5 184) chain C residue 48 type MOD_RES sequence S description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P99024 source Swiss-Prot : SWS_FT_FI5 185) chain C residue 232 type MOD_RES sequence S description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P99024 source Swiss-Prot : SWS_FT_FI5 186) chain B residue 174 type MOD_RES sequence S description Phosphoserine; by CDK1 => ECO:0000250|UniProtKB:Q9BVA1 source Swiss-Prot : SWS_FT_FI6 187) chain D residue 174 type MOD_RES sequence S description Phosphoserine; by CDK1 => ECO:0000250|UniProtKB:Q9BVA1 source Swiss-Prot : SWS_FT_FI6 188) chain B residue 287 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:P07437 source Swiss-Prot : SWS_FT_FI7 189) chain B residue 292 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:P07437 source Swiss-Prot : SWS_FT_FI7 190) chain D residue 287 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:P07437 source Swiss-Prot : SWS_FT_FI7 191) chain D residue 292 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:P07437 source Swiss-Prot : SWS_FT_FI7 192) chain B residue 320 type MOD_RES sequence R description Omega-N-methylarginine => ECO:0000250|UniProtKB:P07437 source Swiss-Prot : SWS_FT_FI8 193) 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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