eF-site ID 6br1-ABCDEF PDB Code 6br1 Chain A, B, C, D, E, F click to enlarge Title Tubulin-RB3_SLD-TTL in complex with heterocyclic pyrimidine compound 4a Classification CELL CYCLE/INHIBITOR 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 RFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLLTVPELT QQMFDSKNMMAACDPRHGRYLTVAAIFRGRMSMKEVDEQM LNVQNKNSSYFVEWIPNNVKTAVCDIPPRGLKMSATFIGN STAIQELFKRISEQFTAMFRRKAFLHWYTGEGMDEMEFTE AESNMNDLVSEYQQYQDATAD E:  MEVIELNKCTSGQSFEVILKPPSDPSLEEIQKKLEAAEER RKYQEAELLKHLAEKREHEREVIQKAIEENNNFIKMAKEK LAQKMESNKENREAHLAAMLERLQEKDKHAEEVRKNKELK E F:  MYTFVVRDENSSVYAEVSRLLLATGQWKRLRKDNPRFNLM LGERNRLPFGRLGHEPGLVQLVNYYRGADKLCRKASLVKL IKTSPELSESCTWFPESYVIYPTREVFLAAYNRRREGREG NVWIALISSEASELLDFIDEQGQVHVIQKYLEKPLLLEPG HRKFDIRSWVLVDHLYNIYLYREGVLRTSSEPYNSANFQD KTCHLTNHCIQKNYGRYEEGNEMFFEEFNQYLMDALNTTL ENSILLQIKHIIRSCLMCIEPAISTKHLHYQSFQLFGFDF MVDEELKVWLIEVNGAPACAQKLYAELCQGIVDVAISSVF PLATSIFIKLHH Description Functional site 1) chain A residue 10 type sequence G description binding site for residue GTP A 501 source : AC1 2) chain A residue 11 type sequence Q description binding site for residue GTP A 501 source : AC1 3) chain A residue 12 type sequence A description binding site for residue GTP A 501 source : AC1 4) chain A residue 15 type sequence Q description binding site for residue GTP A 501 source : AC1 5) chain A residue 98 type sequence D description binding site for residue GTP A 501 source : AC1 6) chain A residue 99 type sequence A description binding site for residue GTP A 501 source : AC1 7) chain A residue 101 type sequence N description binding site for residue GTP A 501 source : AC1 8) chain A residue 140 type sequence S description binding site for residue GTP A 501 source : AC1 9) chain A residue 143 type sequence G description binding site for residue GTP A 501 source : AC1 10) chain A residue 144 type sequence G description binding site for residue GTP A 501 source : AC1 11) chain A residue 145 type sequence T description binding site for residue GTP A 501 source : AC1 12) chain A residue 146 type sequence G description binding site for residue GTP A 501 source : AC1 13) chain A residue 177 type sequence V description binding site for residue GTP A 501 source : AC1 14) chain A residue 178 type sequence S description binding site for residue GTP A 501 source : AC1 15) chain A residue 179 type sequence T description binding site for residue GTP A 501 source : AC1 16) chain A residue 183 type sequence E description binding site for residue GTP A 501 source : AC1 17) chain A residue 206 type sequence N description binding site for residue GTP A 501 source : AC1 18) chain A residue 224 type sequence Y description binding site for residue GTP A 501 source : AC1 19) chain A residue 228 type sequence N description binding site for residue GTP A 501 source : AC1 20) chain A residue 231 type sequence I description binding site for residue GTP A 501 source : AC1 21) chain A residue 39 type sequence D description binding site for residue CA A 502 source : AC2 22) chain A residue 41 type sequence T description binding site for residue CA A 502 source : AC2 23) chain A residue 44 type sequence G description binding site for residue CA A 502 source : AC2 24) chain A residue 55 type sequence E description binding site for residue CA A 502 source : AC2 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 138 type sequence S description binding site for residue GDP B 501 source : AC4 30) chain B residue 141 type sequence G description binding site for residue GDP B 501 source : AC4 31) chain B residue 142 type sequence G description binding site for residue GDP B 501 source : AC4 32) chain B residue 143 type sequence T description binding site for residue GDP B 501 source : AC4 33) chain B residue 144 type sequence G description binding site for residue GDP B 501 source : AC4 34) chain B residue 175 type sequence V description binding site for residue GDP B 501 source : AC4 35) chain B residue 177 type sequence D description binding site for residue GDP B 501 source : AC4 36) chain B residue 181 type sequence E description binding site for residue GDP B 501 source : AC4 37) chain B residue 204 type sequence N description binding site for residue GDP B 501 source : AC4 38) chain B residue 222 type sequence Y description binding site for residue GDP B 501 source : AC4 39) chain B residue 226 type sequence N description binding site for residue GDP B 501 source : AC4 40) chain B residue 156 type sequence R description binding site for residue MES B 502 source : AC5 41) chain B residue 160 type sequence P description binding site for residue MES B 502 source : AC5 42) chain B residue 161 type sequence D description binding site for residue MES B 502 source : AC5 43) chain B residue 162 type sequence R description binding site for residue MES B 502 source : AC5 44) chain B residue 195 type sequence N description binding site for residue MES B 502 source : AC5 45) chain B residue 197 type sequence D description binding site for residue MES B 502 source : AC5 46) chain B residue 251 type sequence R description binding site for residue MES B 502 source : AC5 47) chain B residue 294 type sequence F description binding site for residue MES B 503 source : AC6 48) chain B residue 295 type sequence D description binding site for residue MES B 503 source : AC6 49) chain B residue 296 type sequence S description binding site for residue MES B 503 source : AC6 50) chain B residue 306 type sequence R description binding site for residue MES B 503 source : AC6 51) chain B residue 337 type sequence N description binding site for residue MES B 503 source : AC6 52) chain B residue 11 type sequence Q description binding site for residue MG B 504 source : AC7 53) chain A residue 179 type sequence T description binding site for residue E3Y B 505 source : AC8 54) chain B residue 239 type sequence C description binding site for residue E3Y B 505 source : AC8 55) chain B residue 240 type sequence L description binding site for residue E3Y B 505 source : AC8 56) chain B residue 246 type sequence L description binding site for residue E3Y B 505 source : AC8 57) chain B residue 248 type sequence A description binding site for residue E3Y B 505 source : AC8 58) chain B residue 253 type sequence L description binding site for residue E3Y B 505 source : AC8 59) chain B residue 256 type sequence N description binding site for residue E3Y B 505 source : AC8 60) chain B residue 257 type sequence M description binding site for residue E3Y B 505 source : AC8 61) chain B residue 313 type sequence V description binding site for residue E3Y B 505 source : AC8 62) chain B residue 314 type sequence A description binding site for residue E3Y B 505 source : AC8 63) chain B residue 315 type sequence A description binding site for residue E3Y B 505 source : AC8 64) chain B residue 348 type sequence N description binding site for residue E3Y B 505 source : AC8 65) chain B residue 350 type sequence K description binding site for residue E3Y B 505 source : AC8 66) chain C residue 10 type sequence G description binding site for residue GTP C 501 source : AC9 67) chain C residue 11 type sequence Q description binding site for residue GTP C 501 source : AC9 68) chain C residue 12 type sequence A description binding site for residue GTP C 501 source : AC9 69) chain C residue 15 type sequence Q description binding site for residue GTP C 501 source : AC9 70) chain C residue 98 type sequence D description binding site for residue GTP C 501 source : AC9 71) chain C residue 99 type sequence A description binding site for residue GTP C 501 source : AC9 72) chain C residue 101 type sequence N description binding site for residue GTP C 501 source : AC9 73) chain C residue 140 type sequence S description binding site for residue GTP C 501 source : AC9 74) chain C residue 143 type sequence G description binding site for residue GTP C 501 source : AC9 75) chain C residue 144 type sequence G description binding site for residue GTP C 501 source : AC9 76) chain C residue 145 type sequence T description binding site for residue GTP C 501 source : AC9 77) chain C residue 146 type sequence G description binding site for residue GTP C 501 source : AC9 78) chain C residue 171 type sequence I description binding site for residue GTP C 501 source : AC9 79) chain C residue 177 type sequence V description binding site for residue GTP C 501 source : AC9 80) chain C residue 179 type sequence T description binding site for residue GTP C 501 source : AC9 81) chain C residue 183 type sequence E description binding site for residue GTP C 501 source : AC9 82) chain C residue 206 type sequence N description binding site for residue GTP C 501 source : AC9 83) chain C residue 224 type sequence Y description binding site for residue GTP C 501 source : AC9 84) chain C residue 228 type sequence N description binding site for residue GTP C 501 source : AC9 85) chain C residue 231 type sequence I description binding site for residue GTP C 501 source : AC9 86) chain C residue 39 type sequence D description binding site for residue CA C 502 source : AD1 87) chain C residue 41 type sequence T description binding site for residue CA C 502 source : AD1 88) chain C residue 44 type sequence G description binding site for residue CA C 502 source : AD1 89) chain C residue 55 type sequence E description binding site for residue CA C 502 source : AD1 90) chain D residue 10 type sequence G description binding site for residue GDP D 501 source : AD3 91) chain D residue 11 type sequence Q description binding site for residue GDP D 501 source : AD3 92) chain D residue 12 type sequence C description binding site for residue GDP D 501 source : AD3 93) chain D residue 15 type sequence Q description binding site for residue GDP D 501 source : AD3 94) chain D residue 138 type sequence S description binding site for residue GDP D 501 source : AD3 95) chain D residue 141 type sequence G description binding site for residue GDP D 501 source : AD3 96) chain D residue 143 type sequence T description binding site for residue GDP D 501 source : AD3 97) chain D residue 144 type sequence G description binding site for residue GDP D 501 source : AD3 98) chain D residue 176 type sequence S description binding site for residue GDP D 501 source : AD3 99) chain D residue 181 type sequence E description binding site for residue GDP D 501 source : AD3 100) chain D residue 204 type sequence N description binding site for residue GDP D 501 source : AD3 101) chain D residue 222 type sequence Y description binding site for residue GDP D 501 source : AD3 102) chain D residue 226 type sequence N description binding site for residue GDP D 501 source : AD3 103) chain C residue 179 type sequence T description binding site for residue E3Y D 502 source : AD4 104) chain D residue 239 type sequence C description binding site for residue E3Y D 502 source : AD4 105) chain D residue 240 type sequence L description binding site for residue E3Y D 502 source : AD4 106) chain D residue 248 type sequence A description binding site for residue E3Y D 502 source : AD4 107) chain D residue 253 type sequence L description binding site for residue E3Y D 502 source : AD4 108) chain D residue 256 type sequence N description binding site for residue E3Y D 502 source : AD4 109) chain D residue 257 type sequence M description binding site for residue E3Y D 502 source : AD4 110) chain D residue 313 type sequence V description binding site for residue E3Y D 502 source : AD4 111) chain D residue 314 type sequence A description binding site for residue E3Y D 502 source : AD4 112) chain D residue 315 type sequence A description binding site for residue E3Y D 502 source : AD4 113) chain D residue 316 type sequence I description binding site for residue E3Y D 502 source : AD4 114) chain D residue 348 type sequence N description binding site for residue E3Y D 502 source : AD4 115) chain D residue 350 type sequence K description binding site for residue E3Y D 502 source : AD4 116) chain F residue 74 type sequence K description binding site for residue MG F 401 source : AD5 117) chain F residue 331 type sequence E description binding site for residue MG F 401 source : AD5 118) chain F residue 333 type sequence N description binding site for residue MG F 401 source : AD5 119) chain F residue 74 type sequence K description binding site for residue ACP F 402 source : AD6 120) chain F residue 148 type sequence I description binding site for residue ACP F 402 source : AD6 121) chain F residue 183 type sequence Q description binding site for residue ACP F 402 source : AD6 122) chain F residue 184 type sequence K description binding site for residue ACP F 402 source : AD6 123) chain F residue 185 type sequence Y description binding site for residue ACP F 402 source : AD6 124) chain F residue 186 type sequence L description binding site for residue ACP F 402 source : AD6 125) chain F residue 198 type sequence K description binding site for residue ACP F 402 source : AD6 126) chain F residue 200 type sequence D description binding site for residue ACP F 402 source : AD6 127) chain F residue 202 type sequence R description binding site for residue ACP F 402 source : AD6 128) chain F residue 222 type sequence R description binding site for residue ACP F 402 source : AD6 129) chain F residue 239 type sequence H description binding site for residue ACP F 402 source : AD6 130) chain F residue 241 type sequence T description binding site for residue ACP F 402 source : AD6 131) chain F residue 242 type sequence N description binding site for residue ACP F 402 source : AD6 132) chain F residue 318 type sequence D description binding site for residue ACP F 402 source : AD6 133) chain F residue 330 type sequence I description binding site for residue ACP F 402 source : AD6 134) chain F residue 331 type sequence E description binding site for residue ACP F 402 source : AD6 135) chain F residue 333 type sequence N description binding site for residue ACP F 402 source : AD6 136) chain A residue 142-148 type prosite sequence GGGTGSG description TUBULIN Tubulin subunits alpha, beta, and gamma signature. GGGTGSG source prosite : PS00227 137) chain B residue 140-146 type prosite sequence GGGTGSG description TUBULIN Tubulin subunits alpha, beta, and gamma signature. GGGTGSG source prosite : PS00227 138) chain E residue 73-82 type prosite sequence AEKREHEREV description STATHMIN_2 Stathmin family signature 2. AEKREHEREV source prosite : PS01041 139) chain B residue 11 type BINDING sequence Q description BINDING => ECO:0000250|UniProtKB:Q13509 source Swiss-Prot : SWS_FT_FI1 140) chain D residue 142 type BINDING sequence G description BINDING => ECO:0000250|UniProtKB:Q13509 source Swiss-Prot : SWS_FT_FI1 141) chain D residue 143 type BINDING sequence T description BINDING => ECO:0000250|UniProtKB:Q13509 source Swiss-Prot : SWS_FT_FI1 142) chain D residue 144 type BINDING sequence G description BINDING => ECO:0000250|UniProtKB:Q13509 source Swiss-Prot : SWS_FT_FI1 143) chain D residue 204 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:Q13509 source Swiss-Prot : SWS_FT_FI1 144) chain D residue 226 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:Q13509 source Swiss-Prot : SWS_FT_FI1 145) chain B residue 138 type BINDING sequence S description BINDING => ECO:0000250|UniProtKB:Q13509 source Swiss-Prot : SWS_FT_FI1 146) chain B residue 142 type BINDING sequence G description BINDING => ECO:0000250|UniProtKB:Q13509 source Swiss-Prot : SWS_FT_FI1 147) chain B residue 143 type BINDING sequence T description BINDING => ECO:0000250|UniProtKB:Q13509 source Swiss-Prot : SWS_FT_FI1 148) chain B residue 144 type BINDING sequence G description BINDING => ECO:0000250|UniProtKB:Q13509 source Swiss-Prot : SWS_FT_FI1 149) chain B residue 204 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:Q13509 source Swiss-Prot : SWS_FT_FI1 150) chain B residue 226 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:Q13509 source Swiss-Prot : SWS_FT_FI1 151) chain D residue 11 type BINDING sequence Q description BINDING => ECO:0000250|UniProtKB:Q13509 source Swiss-Prot : SWS_FT_FI1 152) chain D residue 138 type BINDING sequence S description BINDING => ECO:0000250|UniProtKB:Q13509 source Swiss-Prot : SWS_FT_FI1 153) chain A 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_FI10 154) chain B residue 324 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_FI10 155) chain A residue 370 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_FI10 156) chain D residue 324 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_FI10 157) chain C residue 370 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_FI10 158) chain B residue 69 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 159) chain C residue 71 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 160) chain C residue 140 type BINDING sequence S description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 161) chain C residue 144 type BINDING sequence G description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 162) chain C residue 145 type BINDING sequence T description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 163) chain C residue 179 type BINDING sequence T description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 164) chain C residue 206 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 165) chain C residue 228 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 166) chain D residue 69 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 167) chain A residue 140 type BINDING sequence S description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 168) chain A residue 144 type BINDING sequence G description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 169) chain A residue 145 type BINDING sequence T description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 170) chain A residue 179 type BINDING sequence T description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 171) chain A residue 206 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 172) chain A residue 228 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 173) chain C residue 11 type BINDING sequence Q description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 174) chain B residue 40 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P99024 source Swiss-Prot : SWS_FT_FI3 175) chain D residue 40 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P99024 source Swiss-Prot : SWS_FT_FI3 176) chain B residue 58 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P99024 source Swiss-Prot : SWS_FT_FI4 177) chain D residue 58 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P99024 source Swiss-Prot : SWS_FT_FI4 178) chain C residue 48 type MOD_RES sequence S description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P99024 source Swiss-Prot : SWS_FT_FI4 179) chain C residue 232 type MOD_RES sequence S description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P99024 source Swiss-Prot : SWS_FT_FI4 180) chain B residue 172 type MOD_RES sequence S description Phosphoserine; by CDK1 => ECO:0000250|UniProtKB:Q13885 source Swiss-Prot : SWS_FT_FI5 181) chain D residue 172 type MOD_RES sequence S description Phosphoserine; by CDK1 => ECO:0000250|UniProtKB:Q13885 source Swiss-Prot : SWS_FT_FI5 182) chain B residue 285 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:P07437 source Swiss-Prot : SWS_FT_FI6 183) chain B residue 290 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:P07437 source Swiss-Prot : SWS_FT_FI6 184) chain D residue 285 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:P07437 source Swiss-Prot : SWS_FT_FI6 185) chain D residue 290 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:P07437 source Swiss-Prot : SWS_FT_FI6 186) chain B residue 318 type MOD_RES sequence R description Omega-N-methylarginine => ECO:0000250|UniProtKB:P07437 source Swiss-Prot : SWS_FT_FI7 187) chain D residue 318 type MOD_RES sequence R description Omega-N-methylarginine => ECO:0000250|UniProtKB:P07437 source Swiss-Prot : SWS_FT_FI7 188) chain B residue 58 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_FI9 189) chain D residue 58 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_FI9

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