eF-site ID 5ezy-ABCDEF PDB Code 5ezy Chain A, B, C, D, E, F click to enlarge Title Crystal structure of T2R-TTL-taccalonolide AJ complex Classification STRUCTURAL PROTEIN Compound Tubulin alpha-1B chain Source ORGANISM_COMMON: Pig; ORGANISM_SCIENTIFIC: Sus scrofa; Sequence A:  MRECISIHVGQAGVQIGNACWELYCLEHGIQPDGQMPSDK TIGGGDDSFNTFFSETGAGKHVPRAVFVDLEPTVIDEVRT GTYRQLFHPEQLITGKEDAANNYARGHYTIGKEIIDLVLD RIRKLADQCTGLQGFLVFHSFGGGTGSGFTSLLMERLSVD YGKKSKLEFSIYPAPQVSTAVVEPYNSILTTHTTLEHSDC AFMVDNEAIYDICRRNLDIERPTYTNLNRLISQIVSSITA SLRFDGALNVDLTEFQTNLVPYPRIHFPLATYAPVISAEK AYHEQLSVAEITNACFEPANQMVKCDPRHGKYMACCLLYR GDVVPKDVNAAIATIKTKRSIQFVDWCPTGFKVGINYQPP TVVPGGDLAKVQRAVCMLSNTTAIAEAWARLDHKFDLMYA KRAFVHWYVGEGMEEGEFSEAREDMAALEKDYEEVGV B:  REIVHIQAGQCGNQIGAKFWEVISDEHGIDPTGSYHGDSD LQLERINVYYNEATGNKYVPRAILVDLEPGTMDSVRSGPF GQIFRPDNFVFGQSGAGNNWAKGHYTEGAELVDSVLDVVR KESESCDCLQGFQLTHSLGGGTGSGMGTLLISKIREEYPD RIMNTFSVMPSPKVSDTVVEPYNATLSVHQLVENTDETYC IDNEALYDICFRTLKLTTPTYGDLNHLVSATMSGVTTCLR FPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTSRGSQQY RALTVPELTQQMFDSKNMMAACDPRHGRYLTVAAIFRGRM SMKEVDEQMLNVQNKNSSYFVEWIPNNVKTAVCDIPPRGL KMSATFIGNSTAIQELFKRISEQFTAMFRRKAFLHWYTGE GMDEMEFTEAESNMNDLVSEYQQYQDA 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 E F:  MYTFVVRDENSSVYAEVSRLLLATGQWKRLRKDNPRFNLM LGERNRLPFGRLGHEPGLVQLVNYYRGADKLCRKASLVKL IKTSPELSESCTWFPESYVIYPTDEREVFLAAYNRRREGR EGNVWIAKSSGILISSEASELLDFIDEQGQVHVIQKYLEK PLLLEPGHRKFDIRSWVLVDHLYNIYLYREGVLRTSSEPY NSANFQDKTCHLTNHCIQKEYSKNYGRYEEGNEMFFEEFN QYLMDALNTTLENSILLQIKHIIRSCLMCIEPAISTKHLH YQSFQLFGFDFMVDEELKVWLIEVNGAPACAQKLYAELCQ GIVDVAISSVFPLATSIFIKLHHHHHH 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 173 type sequence P description binding site for residue GDP B 501 source : AC4 35) chain B residue 177 type sequence V description binding site for residue GDP B 501 source : AC4 36) chain B residue 179 type sequence D description binding site for residue GDP B 501 source : AC4 37) chain B residue 183 type sequence E description binding site for residue GDP B 501 source : AC4 38) chain B residue 206 type sequence N description binding site for residue GDP B 501 source : AC4 39) chain B residue 224 type sequence Y description binding site for residue GDP B 501 source : AC4 40) chain B residue 228 type sequence N description binding site for residue GDP B 501 source : AC4 41) chain B residue 11 type sequence Q description binding site for residue MG B 502 source : AC5 42) chain B residue 158 type sequence R description binding site for residue MES B 503 source : AC6 43) chain B residue 162 type sequence P description binding site for residue MES B 503 source : AC6 44) chain B residue 163 type sequence D description binding site for residue MES B 503 source : AC6 45) chain B residue 164 type sequence R description binding site for residue MES B 503 source : AC6 46) chain B residue 197 type sequence N description binding site for residue MES B 503 source : AC6 47) chain B residue 198 type sequence T description binding site for residue MES B 503 source : AC6 48) chain B residue 199 type sequence D description binding site for residue MES B 503 source : AC6 49) chain B residue 253 type sequence R description binding site for residue MES B 503 source : AC6 50) chain B residue 296 type sequence F description binding site for residue MES B 504 source : AC7 51) chain B residue 297 type sequence D description binding site for residue MES B 504 source : AC7 52) chain B residue 298 type sequence S description binding site for residue MES B 504 source : AC7 53) chain B residue 308 type sequence R description binding site for residue MES B 504 source : AC7 54) chain B residue 335 type sequence V description binding site for residue MES B 504 source : AC7 55) chain B residue 339 type sequence N description binding site for residue MES B 504 source : AC7 56) chain B residue 217 type sequence L description binding site for residue TAJ B 505 source : AC8 57) chain B residue 219 type sequence L description binding site for residue TAJ B 505 source : AC8 58) chain B residue 225 type sequence G description binding site for residue TAJ B 505 source : AC8 59) chain B residue 226 type sequence D description binding site for residue TAJ B 505 source : AC8 60) chain B residue 229 type sequence H description binding site for residue TAJ B 505 source : AC8 61) chain B residue 276 type sequence T description binding site for residue TAJ B 505 source : AC8 62) chain B residue 278 type sequence R description binding site for residue TAJ B 505 source : AC8 63) chain C residue 10 type sequence G description binding site for residue GTP C 501 source : AC9 64) chain C residue 11 type sequence Q description binding site for residue GTP C 501 source : AC9 65) chain C residue 12 type sequence A description binding site for residue GTP C 501 source : AC9 66) chain C residue 15 type sequence Q description binding site for residue GTP C 501 source : AC9 67) chain C residue 98 type sequence D description binding site for residue GTP C 501 source : AC9 68) chain C residue 99 type sequence A description binding site for residue GTP C 501 source : AC9 69) chain C residue 100 type sequence A description binding site for residue GTP C 501 source : AC9 70) chain C residue 101 type sequence N description binding site for residue GTP C 501 source : AC9 71) chain C residue 140 type sequence S description binding site for residue GTP C 501 source : AC9 72) chain C residue 143 type sequence G description binding site for residue GTP C 501 source : AC9 73) chain C residue 144 type sequence G description binding site for residue GTP C 501 source : AC9 74) chain C residue 145 type sequence T description binding site for residue GTP C 501 source : AC9 75) chain C residue 146 type sequence G description binding site for residue GTP C 501 source : AC9 76) chain C residue 171 type sequence I description binding site for residue GTP C 501 source : AC9 77) chain C residue 177 type sequence V description binding site for residue GTP C 501 source : AC9 78) chain C residue 183 type sequence E description binding site for residue GTP C 501 source : AC9 79) chain C residue 206 type sequence N description binding site for residue GTP C 501 source : AC9 80) chain C residue 224 type sequence Y description binding site for residue GTP C 501 source : AC9 81) chain C residue 228 type sequence N description binding site for residue GTP C 501 source : AC9 82) chain C residue 231 type sequence I description binding site for residue GTP C 501 source : AC9 83) chain D residue 254 type sequence K description binding site for residue GTP C 501 source : AC9 84) chain C residue 39 type sequence D description binding site for residue CA C 503 source : AD2 85) chain C residue 41 type sequence T description binding site for residue CA C 503 source : AD2 86) chain C residue 44 type sequence G description binding site for residue CA C 503 source : AD2 87) chain C residue 55 type sequence E description binding site for residue CA C 503 source : AD2 88) chain D residue 10 type sequence G description binding site for residue GTP D 501 source : AD3 89) chain D residue 11 type sequence Q description binding site for residue GTP D 501 source : AD3 90) chain D residue 12 type sequence C description binding site for residue GTP D 501 source : AD3 91) chain D residue 15 type sequence Q description binding site for residue GTP D 501 source : AD3 92) chain D residue 98 type sequence G description binding site for residue GTP D 501 source : AD3 93) chain D residue 99 type sequence A description binding site for residue GTP D 501 source : AD3 94) chain D residue 100 type sequence G description binding site for residue GTP D 501 source : AD3 95) chain D residue 101 type sequence N description binding site for residue GTP D 501 source : AD3 96) chain D residue 140 type sequence S description binding site for residue GTP D 501 source : AD3 97) chain D residue 143 type sequence G description binding site for residue GTP D 501 source : AD3 98) chain D residue 144 type sequence G description binding site for residue GTP D 501 source : AD3 99) chain D residue 145 type sequence T description binding site for residue GTP D 501 source : AD3 100) chain D residue 146 type sequence G description binding site for residue GTP D 501 source : AD3 101) chain D residue 177 type sequence V description binding site for residue GTP D 501 source : AD3 102) chain D residue 178 type sequence S description binding site for residue GTP D 501 source : AD3 103) chain D residue 183 type sequence E description binding site for residue GTP D 501 source : AD3 104) chain D residue 206 type sequence N description binding site for residue GTP D 501 source : AD3 105) chain D residue 224 type sequence Y description binding site for residue GTP D 501 source : AD3 106) chain D residue 228 type sequence N description binding site for residue GTP D 501 source : AD3 107) chain D residue 217 type sequence L description binding site for residue TAJ D 503 source : AD5 108) chain D residue 219 type sequence L description binding site for residue TAJ D 503 source : AD5 109) chain D residue 225 type sequence G description binding site for residue TAJ D 503 source : AD5 110) chain D residue 226 type sequence D description binding site for residue TAJ D 503 source : AD5 111) chain D residue 229 type sequence H description binding site for residue TAJ D 503 source : AD5 112) chain D residue 278 type sequence R description binding site for residue TAJ D 503 source : AD5 113) chain D residue 282 type sequence Q description binding site for residue TAJ D 503 source : AD5 114) chain D residue 370 type sequence G description binding site for residue TAJ D 503 source : AD5 115) chain F residue 74 type sequence K description binding site for residue ACP F 401 source : AD6 116) chain F residue 150 type sequence K description binding site for residue ACP F 401 source : AD6 117) chain F residue 183 type sequence Q description binding site for residue ACP F 401 source : AD6 118) chain F residue 184 type sequence K description binding site for residue ACP F 401 source : AD6 119) chain F residue 185 type sequence Y description binding site for residue ACP F 401 source : AD6 120) chain F residue 186 type sequence L description binding site for residue ACP F 401 source : AD6 121) chain F residue 198 type sequence K description binding site for residue ACP F 401 source : AD6 122) chain F residue 202 type sequence R description binding site for residue ACP F 401 source : AD6 123) chain F residue 240 type sequence L description binding site for residue ACP F 401 source : AD6 124) chain F residue 241 type sequence T description binding site for residue ACP F 401 source : AD6 125) chain F residue 242 type sequence N description binding site for residue ACP F 401 source : AD6 126) chain F residue 318 type sequence D description binding site for residue ACP F 401 source : AD6 127) chain F residue 330 type sequence I description binding site for residue ACP F 401 source : AD6 128) chain F residue 331 type sequence E description binding site for residue ACP F 401 source : AD6 129) chain A residue 142-148 type prosite sequence GGGTGSG description TUBULIN Tubulin subunits alpha, beta, and gamma signature. GGGTGSG source prosite : PS00227 130) chain B residue 142-148 type prosite sequence GGGTGSG description TUBULIN Tubulin subunits alpha, beta, and gamma signature. GGGTGSG source prosite : PS00227 131) chain E residue 73-82 type prosite sequence AEKREHEREV description STATHMIN_2 Stathmin family signature 2. AEKREHEREV source prosite : PS01041 132) chain E residue 46 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:22673903 source Swiss-Prot : SWS_FT_FI1 133) chain D residue 144 type MOD_RES sequence G description Phosphoserine => ECO:0007744|PubMed:22673903 source Swiss-Prot : SWS_FT_FI1 134) chain D residue 145 type MOD_RES sequence T description Phosphoserine => ECO:0007744|PubMed:22673903 source Swiss-Prot : SWS_FT_FI1 135) chain D residue 146 type MOD_RES sequence G description Phosphoserine => ECO:0007744|PubMed:22673903 source Swiss-Prot : SWS_FT_FI1 136) chain D residue 206 type MOD_RES sequence N description Phosphoserine => ECO:0007744|PubMed:22673903 source Swiss-Prot : SWS_FT_FI1 137) chain D residue 228 type MOD_RES sequence N description Phosphoserine => ECO:0007744|PubMed:22673903 source Swiss-Prot : SWS_FT_FI1 138) chain B residue 140 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:22673903 source Swiss-Prot : SWS_FT_FI1 139) chain B residue 144 type MOD_RES sequence G description Phosphoserine => ECO:0007744|PubMed:22673903 source Swiss-Prot : SWS_FT_FI1 140) chain B residue 145 type MOD_RES sequence T description Phosphoserine => ECO:0007744|PubMed:22673903 source Swiss-Prot : SWS_FT_FI1 141) chain B residue 146 type MOD_RES sequence G description Phosphoserine => ECO:0007744|PubMed:22673903 source Swiss-Prot : SWS_FT_FI1 142) chain B residue 206 type MOD_RES sequence N description Phosphoserine => ECO:0007744|PubMed:22673903 source Swiss-Prot : SWS_FT_FI1 143) chain B residue 228 type MOD_RES sequence N description Phosphoserine => ECO:0007744|PubMed:22673903 source Swiss-Prot : SWS_FT_FI1 144) chain D residue 11 type MOD_RES sequence Q description Phosphoserine => ECO:0007744|PubMed:22673903 source Swiss-Prot : SWS_FT_FI1 145) chain D residue 140 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:22673903 source Swiss-Prot : SWS_FT_FI1 146) 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 147) 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 148) chain A residue 370 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000250|UniProtKB:P07437 source Swiss-Prot : SWS_FT_FI10 149) chain C residue 326 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000250|UniProtKB:P07437 source Swiss-Prot : SWS_FT_FI10 150) chain C residue 370 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000250|UniProtKB:P07437 source Swiss-Prot : SWS_FT_FI10 151) 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 152) 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 153) chain B residue 71 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 154) chain C residue 71 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 155) chain C residue 140 type BINDING sequence S description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 156) chain C residue 144 type BINDING sequence G description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 157) chain C residue 145 type BINDING sequence T description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 158) chain C residue 179 type BINDING sequence T description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 159) chain C residue 206 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 160) chain C residue 228 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 161) chain D residue 71 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 162) chain A residue 140 type BINDING sequence S description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 163) chain A residue 144 type BINDING sequence G description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 164) chain A residue 145 type BINDING sequence T description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 165) chain A residue 179 type BINDING sequence T description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 166) chain A residue 206 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 167) chain A residue 228 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 168) chain C residue 11 type BINDING sequence Q description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 169) chain B residue 40 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P99024 source Swiss-Prot : SWS_FT_FI3 170) chain D residue 40 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P99024 source Swiss-Prot : SWS_FT_FI3 171) chain B residue 57 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:Q3KRE8 source Swiss-Prot : SWS_FT_FI4 172) chain D residue 57 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:Q3KRE8 source Swiss-Prot : SWS_FT_FI4 173) chain C residue 48 type MOD_RES sequence S description Phosphothreonine => ECO:0000250|UniProtKB:Q3KRE8 source Swiss-Prot : SWS_FT_FI4 174) chain C residue 232 type MOD_RES sequence S description Phosphothreonine => ECO:0000250|UniProtKB:Q3KRE8 source Swiss-Prot : SWS_FT_FI4 175) chain B residue 60 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P99024 source Swiss-Prot : SWS_FT_FI5 176) chain D residue 60 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P99024 source Swiss-Prot : SWS_FT_FI5 177) chain B residue 174 type MOD_RES sequence S description Phosphoserine; by CDK1 => ECO:0000250|UniProtKB:Q9BVA1 source Swiss-Prot : SWS_FT_FI6 178) chain D residue 174 type MOD_RES sequence S description Phosphoserine; by CDK1 => ECO:0000250|UniProtKB:Q9BVA1 source Swiss-Prot : SWS_FT_FI6 179) chain B residue 287 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:P07437 source Swiss-Prot : SWS_FT_FI7 180) chain B residue 292 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:P07437 source Swiss-Prot : SWS_FT_FI7 181) chain D residue 287 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:P07437 source Swiss-Prot : SWS_FT_FI7 182) chain D residue 292 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:P07437 source Swiss-Prot : SWS_FT_FI7 183) chain B residue 320 type MOD_RES sequence R description Omega-N-methylarginine => ECO:0000250|UniProtKB:P07437 source Swiss-Prot : SWS_FT_FI8 184) 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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