eF-site ID 5xkg-ABCDEF PDB Code 5xkg Chain A, B, C, D, E, F click to enlarge Title Crystal structure of T2R-TTL-CH1 complex Classification STRUCTURAL PROTEIN Compound Tubulin alpha-1B chain Source Sus scrofa (Pig) (E1BQ43_CHICK) Sequence A:  MRECISIHVGQAGVQIGNACWELYCLEHGIQPDGQMPSDK TIGGGDDSFNTFFSETGAGKHVPRAVFVDLEPTVIDEVRT GTYRQLFHPEQLITGKEDAANNYARGHYTIGKEIIDLVLD RIRKLADQCTGLQGFLVFHSFGGGTGSGFTSLLMERLSVD YGKKSKLEFSIYPAPQVSTAVVEPYNSILTTHTTLEHSDC AFMVDNEAIYDICRRNLDIERPTYTNLNRLISQIVSSITA SLRFDGALNVDLTEFQTNLVPYPRIHFPLATYAPVISAEK AYHEQLSVAEITNACFEPANQMVKCDPRHGKYMACCLLYR GDVVPKDVNAAIATIKTKRSIQFVDWCPTGFKVGINYQPP TVVPGGDLAKVQRAVCMLSNTTAIAEAWARLDHKFDLMYA KRAFVHWYVGEGMEEGEFSEAREDMAALEKDYEEVGV B:  MREIVHIQAGQCGNQIGAKFWEVISDEHGIDPTGSYHGDS DLQLERINVYYNEATGNKYVPRAILVDLEPGTMDSVRSGP FGQIFRPDNFVFGQSGAGNNWAKGHYTEGAELVDSVLDVV RKESESCDCLQGFQLTHSLGGGTGSGMGTLLISKIREEYP DRIMNTFSVMPSPKVSDTVVEPYNATLSVHQLVENTDETY CIDNEALYDICFRTLKLTTPTYGDLNHLVSATMSGVTTCL RFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTSRGSQQ YRALTVPELTQQMFDSKNMMAACDPRHGRYLTVAAIFRGR MSMKEVDEQMLNVQNKNSSYFVEWIPNNVKTAVCDIPPRG LKMSATFIGNSTAIQELFKRISEQFTAMFRRKAFLHWYTG EGMDEMEFTEAESNMNDLVSEYQQYQDA C:  MRECISIHVGQAGVQIGNACWELYCLEHGIQPDGQMPSDK TIGGGDDSFNTFFSETGAGKHVPRAVFVDLEPTVIDEVRT GTYRQLFHPEQLITGKEDAANNYARGHYTIGKEIIDLVLD RIRKLADQCTGLQGFLVFHSFGGGTGSGFTSLLMERLSVD YGKKSKLEFSIYPAPQVSTAVVEPYNSILTTHTTLEHSDC AFMVDNEAIYDICRRNLDIERPTYTNLNRLISQIVSSITA SLRFDGALNVDLTEFQTNLVPYPRIHFPLATYAPVISAEK AYHEQLSVAEITNACFEPANQMVKCDPRHGKYMACCLLYR GDVVPKDVNAAIATIKTKRSIQFVDWCPTGFKVGINYQPP TVVPGGDLAKVQRAVCMLSNTTAIAEAWARLDHKFDLMYA KRAFVHWYVGEGMEEGEFSEAREDMAALEKDYEEVGVDSV D:  MREIVHIQAGQCGNQIGAKFWEVISDEHGIDPTGSYHGDS DLQLERINVYYNEATGNKYVPRAILVDLEPGTMDSVRSGP FGQIFRPDNFVFGQSGAGNNWAKGHYTEGAELVDSVLDVV RKESESCDCLQGFQLTHSLGGGTGSGMGTLLISKIREEYP DRIMNTFSVMPSPKVSDTVVEPYNATLSVHQLVENTDETY CIDNEALYDICFRTLKLTTPTYGDLNHLVSATMSGVTTCL RFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLLTVPELT QQMFDSKNMMAACDPRHGRYLTVAAIFRGRMSMKEVDEQM LNVQNKNSSYFVEWIPNNVKTAVCDIPPRGLKMSATFIGN STAIQELFKRISEQFTAMFRRKAFLHWYTGEGMDEMEFTE AESNMNDLVSEYQQYQDATAD E:  MEVIELNKCTSGQSFEVILKPPSDPSLEEIQKKLEAAEER RKYQEAELLKHLAEKREHEREVIQKAIEENNNFIKMAKEK LAQKMESNKENREAHLAAMLERLQEKDKHAEEVRKNKELK E F:  MYTFVVRDENSSVYAEVSRLLLATGQWKRLRKDNPRFNLM LGERNRLPFGRLGHEPGLVQLVNYYRGADKLCRKASLVKL IKTSPELSESCTWFPESYVIYPTDEREVFLAAYNRRREGR EGNVWIALISSEASELLDFIDEQGQVHVIQKYLEKPLLLE PGHRKFDIRSWVLVDHLYNIYLYREGVLRTSSEPYNSANF QDKTCHLTNHCIQKNYGRYEEGNEMFFEEFNQYLMDALNT TLENSILLQIKHIIRSCLMCIEPAISTKHLHYQSFQLFGF DFMVDEELKVWLIEVNGAPACAQKLYAELCQGIVDVAISS VFPLATSIFIKLHH 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 179 type sequence T 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 A residue 39 type sequence D description binding site for residue CA A 503 source : AC3 21) chain A residue 41 type sequence T description binding site for residue CA A 503 source : AC3 22) chain A residue 44 type sequence G description binding site for residue CA A 503 source : AC3 23) chain A residue 55 type sequence E description binding site for residue CA A 503 source : AC3 24) chain A residue 216 type sequence N description binding site for residue GOL A 504 source : AC4 25) chain A residue 274 type sequence P description binding site for residue GOL A 504 source : AC4 26) chain A residue 275 type sequence V description binding site for residue GOL A 504 source : AC4 27) chain A residue 276 type sequence I description binding site for residue GOL A 504 source : AC4 28) chain A residue 300 type sequence N description binding site for residue GOL A 504 source : AC4 29) chain B residue 10 type sequence G description binding site for residue GDP B 501 source : AC5 30) chain B residue 11 type sequence Q description binding site for residue GDP B 501 source : AC5 31) chain B residue 12 type sequence C description binding site for residue GDP B 501 source : AC5 32) chain B residue 15 type sequence Q description binding site for residue GDP B 501 source : AC5 33) chain B residue 138 type sequence S description binding site for residue GDP B 501 source : AC5 34) chain B residue 141 type sequence G description binding site for residue GDP B 501 source : AC5 35) chain B residue 142 type sequence G description binding site for residue GDP B 501 source : AC5 36) chain B residue 143 type sequence T 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 175 type sequence V description binding site for residue GDP B 501 source : AC5 39) chain B residue 177 type sequence D description binding site for residue GDP B 501 source : AC5 40) chain B residue 181 type sequence E description binding site for residue GDP B 501 source : AC5 41) chain B residue 204 type sequence N description binding site for residue GDP B 501 source : AC5 42) chain B residue 222 type sequence Y description binding site for residue GDP B 501 source : AC5 43) chain B residue 226 type sequence N description binding site for residue GDP B 501 source : AC5 44) chain B residue 11 type sequence Q description binding site for residue MG B 502 source : AC6 45) chain B residue 156 type sequence R description binding site for residue MES B 503 source : AC7 46) chain B residue 161 type sequence D description binding site for residue MES B 503 source : AC7 47) chain B residue 162 type sequence R description binding site for residue MES B 503 source : AC7 48) chain B residue 195 type sequence N description binding site for residue MES B 503 source : AC7 49) chain B residue 197 type sequence D description binding site for residue MES B 503 source : AC7 50) chain B residue 251 type sequence R description binding site for residue MES B 503 source : AC7 51) chain A residue 179 type sequence T description binding site for residue 890 B 504 source : AC8 52) chain A residue 180 type sequence A description binding site for residue 890 B 504 source : AC8 53) chain A residue 181 type sequence V description binding site for residue 890 B 504 source : AC8 54) chain B residue 239 type sequence C description binding site for residue 890 B 504 source : AC8 55) chain B residue 240 type sequence L description binding site for residue 890 B 504 source : AC8 56) chain B residue 246 type sequence L description binding site for residue 890 B 504 source : AC8 57) chain B residue 248 type sequence A description binding site for residue 890 B 504 source : AC8 58) chain B residue 252 type sequence K description binding site for residue 890 B 504 source : AC8 59) chain B residue 253 type sequence L description binding site for residue 890 B 504 source : AC8 60) chain B residue 256 type sequence N description binding site for residue 890 B 504 source : AC8 61) chain B residue 257 type sequence M description binding site for residue 890 B 504 source : AC8 62) chain B residue 315 type sequence A description binding site for residue 890 B 504 source : AC8 63) chain B residue 316 type sequence I description binding site for residue 890 B 504 source : AC8 64) chain B residue 348 type sequence N description binding site for residue 890 B 504 source : AC8 65) chain B residue 350 type sequence K description binding site for residue 890 B 504 source : AC8 66) chain B residue 352 type sequence A description binding site for residue 890 B 504 source : AC8 67) chain C residue 10 type sequence G description binding site for residue GTP C 501 source : AC9 68) chain C residue 11 type sequence Q description binding site for residue GTP C 501 source : AC9 69) chain C residue 12 type sequence A description binding site for residue GTP C 501 source : AC9 70) chain C residue 15 type sequence Q description binding site for residue GTP C 501 source : AC9 71) chain C residue 98 type sequence D description binding site for residue GTP C 501 source : AC9 72) chain C residue 99 type sequence A description binding site for residue GTP C 501 source : AC9 73) chain C residue 101 type sequence N description binding site for residue GTP C 501 source : AC9 74) chain C residue 140 type sequence S description binding site for residue GTP C 501 source : AC9 75) chain C residue 143 type sequence G description binding site for residue GTP C 501 source : AC9 76) chain C residue 144 type sequence G description binding site for residue GTP C 501 source : AC9 77) chain C residue 145 type sequence T description binding site for residue GTP C 501 source : AC9 78) chain C residue 146 type sequence G 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 D residue 252 type sequence K description binding site for residue GTP C 501 source : AC9 87) chain C residue 39 type sequence D description binding site for residue CA C 503 source : AD2 88) chain C residue 41 type sequence T description binding site for residue CA C 503 source : AD2 89) chain C residue 44 type sequence G description binding site for residue CA C 503 source : AD2 90) chain C residue 55 type sequence E description binding site for residue CA C 503 source : AD2 91) chain D residue 10 type sequence G description binding site for residue GTP D 501 source : AD3 92) chain D residue 11 type sequence Q description binding site for residue GTP D 501 source : AD3 93) chain D residue 12 type sequence C description binding site for residue GTP D 501 source : AD3 94) chain D residue 15 type sequence Q description binding site for residue GTP D 501 source : AD3 95) chain D residue 97 type sequence A description binding site for residue GTP D 501 source : AD3 96) chain D residue 98 type sequence G description binding site for residue GTP D 501 source : AD3 97) chain D residue 99 type sequence N description binding site for residue GTP D 501 source : AD3 98) chain D residue 138 type sequence S description binding site for residue GTP D 501 source : AD3 99) chain D residue 141 type sequence G description binding site for residue GTP D 501 source : AD3 100) chain D residue 142 type sequence G description binding site for residue GTP D 501 source : AD3 101) chain D residue 143 type sequence T description binding site for residue GTP D 501 source : AD3 102) chain D residue 144 type sequence G description binding site for residue GTP D 501 source : AD3 103) chain D residue 175 type sequence V description binding site for residue GTP D 501 source : AD3 104) chain D residue 181 type sequence E description binding site for residue GTP D 501 source : AD3 105) chain D residue 204 type sequence N description binding site for residue GTP D 501 source : AD3 106) chain D residue 222 type sequence Y description binding site for residue GTP D 501 source : AD3 107) chain D residue 226 type sequence N description binding site for residue GTP D 501 source : AD3 108) chain D residue 11 type sequence Q description binding site for residue MG D 502 source : AD4 109) chain C residue 179 type sequence T description binding site for residue 890 D 503 source : AD5 110) chain C residue 180 type sequence A description binding site for residue 890 D 503 source : AD5 111) chain C residue 181 type sequence V description binding site for residue 890 D 503 source : AD5 112) chain D residue 239 type sequence C description binding site for residue 890 D 503 source : AD5 113) chain D residue 248 type sequence A description binding site for residue 890 D 503 source : AD5 114) chain D residue 252 type sequence K description binding site for residue 890 D 503 source : AD5 115) chain D residue 253 type sequence L description binding site for residue 890 D 503 source : AD5 116) chain D residue 256 type sequence N description binding site for residue 890 D 503 source : AD5 117) chain D residue 257 type sequence M description binding site for residue 890 D 503 source : AD5 118) chain D residue 315 type sequence A description binding site for residue 890 D 503 source : AD5 119) chain D residue 316 type sequence I description binding site for residue 890 D 503 source : AD5 120) chain D residue 348 type sequence N description binding site for residue 890 D 503 source : AD5 121) chain D residue 350 type sequence K description binding site for residue 890 D 503 source : AD5 122) 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 123) 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 124) chain A residue 326 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI12 125) chain A residue 370 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI12 126) chain C residue 326 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI12 127) chain C residue 370 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI12 128) chain E residue 73-82 type prosite sequence AEKREHEREV description STATHMIN_2 Stathmin family signature 2. AEKREHEREV source prosite : PS01041 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 140-146 type prosite sequence GGGTGSG description TUBULIN Tubulin subunits alpha, beta, and gamma signature. GGGTGSG source prosite : PS00227 131) chain B residue 1-4 type prosite sequence MREI description TUBULIN_B_AUTOREG Tubulin-beta mRNA autoregulation signal. MREI source prosite : PS00228 132) chain D residue 142 type BINDING sequence G description BINDING => ECO:0000250|UniProtKB:Q13509 source Swiss-Prot : SWS_FT_FI1 133) chain D residue 143 type BINDING sequence T description BINDING => ECO:0000250|UniProtKB:Q13509 source Swiss-Prot : SWS_FT_FI1 134) chain D residue 144 type BINDING sequence G description BINDING => ECO:0000250|UniProtKB:Q13509 source Swiss-Prot : SWS_FT_FI1 135) chain D residue 204 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:Q13509 source Swiss-Prot : SWS_FT_FI1 136) chain D residue 226 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:Q13509 source Swiss-Prot : SWS_FT_FI1 137) chain D residue 11 type BINDING sequence Q description BINDING => ECO:0000250|UniProtKB:Q13509 source Swiss-Prot : SWS_FT_FI1 138) chain D residue 138 type BINDING sequence S description BINDING => ECO:0000250|UniProtKB:Q13509 source Swiss-Prot : SWS_FT_FI1 139) chain B residue 142 type BINDING sequence G description BINDING => ECO:0000250|UniProtKB:Q13509 source Swiss-Prot : SWS_FT_FI1 140) chain B residue 143 type BINDING sequence T description BINDING => ECO:0000250|UniProtKB:Q13509 source Swiss-Prot : SWS_FT_FI1 141) chain B residue 144 type BINDING sequence G description BINDING => ECO:0000250|UniProtKB:Q13509 source Swiss-Prot : SWS_FT_FI1 142) chain B residue 204 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:Q13509 source Swiss-Prot : SWS_FT_FI1 143) chain B residue 226 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:Q13509 source Swiss-Prot : SWS_FT_FI1 144) chain B residue 11 type BINDING sequence Q 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 D residue 69 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 147) chain C residue 71 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 148) chain C residue 140 type BINDING sequence S description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 149) chain C residue 144 type BINDING sequence G description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 150) chain C residue 145 type BINDING sequence T description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 151) chain C residue 179 type BINDING sequence T description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 152) chain C residue 206 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 153) chain C residue 228 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 154) chain A residue 140 type BINDING sequence S description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 155) chain A residue 144 type BINDING sequence G description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 156) chain A residue 145 type BINDING sequence T description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 157) chain A residue 179 type BINDING sequence T description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 158) chain A residue 206 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 159) chain A residue 228 type BINDING sequence N description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 160) chain C residue 11 type BINDING sequence Q description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 161) chain B residue 69 type BINDING sequence E description BINDING => ECO:0000250|UniProtKB:P68363 source Swiss-Prot : SWS_FT_FI2 162) chain D residue 40 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P99024 source Swiss-Prot : SWS_FT_FI3 163) chain B residue 40 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P99024 source Swiss-Prot : SWS_FT_FI3 164) chain D residue 58 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P99024 source Swiss-Prot : SWS_FT_FI4 165) chain B residue 58 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P99024 source Swiss-Prot : SWS_FT_FI4 166) chain D residue 172 type MOD_RES sequence S description Phosphoserine; by CDK1 => ECO:0000250|UniProtKB:Q13885 source Swiss-Prot : SWS_FT_FI5 167) chain C residue 48 type MOD_RES sequence S description Phosphoserine; by CDK1 => ECO:0000250|UniProtKB:Q13885 source Swiss-Prot : SWS_FT_FI5 168) chain C residue 232 type MOD_RES sequence S description Phosphoserine; by CDK1 => ECO:0000250|UniProtKB:Q13885 source Swiss-Prot : SWS_FT_FI5 169) chain B residue 172 type MOD_RES sequence S description Phosphoserine; by CDK1 => ECO:0000250|UniProtKB:Q13885 source Swiss-Prot : SWS_FT_FI5 170) chain D residue 285 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:P07437 source Swiss-Prot : SWS_FT_FI6 171) chain D residue 290 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:P07437 source Swiss-Prot : SWS_FT_FI6 172) chain B residue 290 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:P07437 source Swiss-Prot : SWS_FT_FI6 173) chain B residue 285 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:P07437 source Swiss-Prot : SWS_FT_FI6 174) chain D residue 318 type MOD_RES sequence R description Omega-N-methylarginine => ECO:0000250|UniProtKB:P07437 source Swiss-Prot : SWS_FT_FI7 175) chain B residue 318 type MOD_RES sequence R description Omega-N-methylarginine => ECO:0000250|UniProtKB:P07437 source Swiss-Prot : SWS_FT_FI7 176) 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 177) 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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