eF-site ID 6a5p-ABCDEFGHIJKLNPTabcdefgh PDB Code 6a5p Chain A, B, C, D, E, F, G, H, I, J, K, L, N, P, T, a, b, c, d, e, f, g, h Title RNA polymerase II elongation complex stalled at SHL(-5) of the nucleosome Classification TRANSCRIPTION/RNA/DNA Compound DNA-directed RNA polymerase subunit Source ORGANISM_COMMON: Yeast; ORGANISM_SCIENTIFIC: Komagataella phaffii (strain GS115 / ATCC 20864); Sequence A:  SQFPYSSAPLRSVKEVQFGLLSPEEIRAISVVKIEYPEIM DESRQRPREGGLNDPKLGSIDRNFKCQTCGEGMAECPGHF GHMELAKPVFHIGFIPKIKKVCECICMNCGKLLLDETNPT MAQAIRIRDPKKRFNAVWQLCKTKMVCEADAPKVVSRGGC GNTQPVVRKDGMKLWGTWKKSRDAQPERKLLTPGEILNVF KHISPEDCFRLGFNEDYARPEWMIITVLPVPPPQVRPSIA MDETTQGQDDLTHKLSDILKANINVQKLEMDGSPQHIINE VEQLLQFHVATYMDNDIAGQPQALQKSGRPVKAIRARLKG KEGRLRGNLMGKRVDFSARTVISGDPNLELDQVGVPISIA KTLSYPETVTQYNIHRLTEYVRNGPNEHPGAKYVIRDNGD RIDLRYHKRAGDIVLQYGWKVERHLMDDDPVLFNRQPSLH KMSMMAHRVKVMPYSTFRLNLSVTSPYNADFDGDEMNLHV PQSEETRAELSQLCAVPLQIVSPQSNKPVMGIVQDTLCGV RKMTLRDTFIEYEQVMNMLFWVPSWDGVVPQPAILKPKPL WTGKQLLSIAIPSGIHLQRTDGGNSLLSPKDNGMLIVDGK VMFGVVDKKTVGSGGGGLIHTVMREKGPKICAELFGNIQK VVNYWLLHNGFSIGIGDAIADASTMKEITHAISSAKEQVQ EIIYKAQHNELELKPGMTLRESFEGEVSRTLNDARDSAGR SAEMNLKDLNNVKQMVSAGSKGSFINIAQMSACVGQQMVE GKRIAFGFADRSLPHFTKDDFSPESKGFVENSYLRGLTPQ EFFFHAMAGREGLIDTAVKTAETGYIQRRLVKALEDIMVH YDGTTRNSLGDIIQFLYGEDGLDGTQVERQTIDTIPGSDK AFHKRYYVDLMDEKNSIKPDVIEYAADILGDVELQKELNS EYEQLVSDRKFLREIVFVNGDHNWPLPVNLRRIIQNAQQI FHLDRAKASDLTIPEIIHGVRDLCKKLFVLRGENELIKEA QQNATSLFQCLVRARLATRRILEEFRLNRDAFEWVLGTIE AQFQRSLVHPGEMVGVIAAQSIGEPATQMNVTLGVPRLKE ILNVAKNIKTPALTVYLDREIALDIEKAKVIQSSIEYTTL KNVTSATEIYYDPDPTSTVIEEDFDTVEAYFSQSPWLLRL ELDRARMLDKQLTMNQVADKISEVFSDDLFVMWSEDNADK LIIRCRVIEEDQMLKRIEAHMLDLIALRGIPGISKVYMVK HKVSVPDESGEYKNEELWALETDGINLAEVMAVPGVDSSR TYSNSFVEILSVLGIEATRSSLYKEILNVIAFDGSYVNYR HMALLVDVMTSRGYLMAITRHGINRADTGALMRCSFEETV EILFEAGAAAELDDCRGVSENVMLGQLAPMGTGAFDVMID EKLLTSLP B:  DDTITTEDCWTVISAFFEEKGLVSQQLDSFDEFMETSIQD LVWEEPRLILDQPAQHTNEKDNINKRYEIRFGKIYLSRPT MTEADGTTHAMFPQEARLRNLTYSSPVYLDMEKSMFTSID GNKVHIGKVPIMLRSKFCSLRTLDEVDLYKMKECPYDMGG YFVINGSEKVLIAQERSAANIVQVFKKAAPSPISHVAEIR SALEKGSRLISTMQIKLYGREDKGTGRTIKATLPYVKQDI PIVIVFRALGVVPDGEILQHICYDENDWQMLEMLKPCIEE GFVIQDKEVALDFIGRRGSAALGIRREKRIQYAKDILQKE LLPHITQEEGFETRKTFFLGYMVNRLLLCALERKDQDDRD HFGKKRLDLAGPLLANLFRILFRKLTREIYRYMQRCIETD RDFNLNLAVKSTTITSGLKYSLATGNWGEQKKAMSSRAGV SQVLNRYTYSSTLSHLRRTNTPIGRDGKLAKPRQLHNTHW GLVCPAETPEGQACGLVKNLSLLSGISIGSPSEPIINFLE EWGMEPLEDYDPAQHTKSTRIFVNGVWTGIHRDPSMLVST MRDLRRSGAISPEVSIIRDIREREFKIFTDVGRVYRPLFI VEDDESKDNKGELRITKEHIRKIQQGYDDDVYGWSSLVTS GVIEYVDGEEEETIMIAMTPEDLQTRSLNDTAKRIKPEMS TSSHHTFTHCEIHPSMILGVAASIIPFPDHNQSPRNTYQS AMGKQAMGVFLTNYNVRMDTMANILYYPQKPLAKTQAMEY LKFRELPAGQNAIVAIACYSGYNQEDSMIMNQSSIDRGLF RSLFFRSYMDQEKRFGISIVEEFEKPTRATTLRLKHGTYE KLDEDGLIAPGVRVSGDDIIIGKTTPIPPYHTKRDASTPL RSTENGIVDQVLLTTNQEGLKFVKVRMRTTKVPQIGDKFA SRHGQKGTIGVTYRHEDMPFSAEGIVPDLIINPHAIPSRM TVAHLIECLLSKVGSIRGYEGDATPFTDLTVDAVSNLLRD NGYQSRGFEVMYNGHTGKKLMAQVFFGPTYYQRLRHMVDD KIHARARGPVQVLTRQPVEGRSRDGGLRFGEMERDCMIAH GAAGFLKERLMEASDAFRVHVCGICGLMSVIANLKKNQFE CRSCKNKTNIYQLHIPYAAKLLFQELMAMNIAPRLYTERS G C:  EPKVNIINAQDDEVELMLSDVNLSLANSLRRTMLAEVPTL AIDLVEIKMNTSVLADEFISHRLGLIPLVSEDVEEMKYSR DCTCEDYCDECSVVLELSARHEGEEGTTDVYSSSLIKVSG PGNLNVGEPVRRDDYDQGILLCKLRNHQELNIRCIAKKGI AKEHAKWSPCSAIAFEYDPHNKLKHTDFWFEVDAKKEWPD SKYATWEEPPKPGEVFDYKAKPNRFYMTVETTGSLKANQV FSRGIKTLQEKLANVLFELENSR D:  VSTSTVGEENATLLRLGPEFALKQYDHDGNEHDLIALSLS ESRLLIREALKARSRARNGGVIDDDELAKVTSGAVANGVV KKTLDYLNTFARFKDEETCTAVDQLLHLHPFEIAQLSSLG CEDVDEAITLIPSLAAKKEVNLQRILDELNRLEDPY E:  EDNNRIISRLWRSFRTVKEMAADRGYFISQEEMDQSLEEF RSKICDSMGNPQRKLMSFLANPTPEALEKYSDLGTLWVEF CDEPSVGIKTMRNFCLRIQEKNFSTGIFIYQNNITPSANK MIPTVSPAIIETFQESDLVVNITHHELVPKHIRLSDGEKS QLLQRYKLKESQLPRIQREDPVARYLGLKRGQVVKIIRRS ETSGRYASYRICL F:  ELAILKEERTTTPYLTKYERARILGTRALQISMNAPVLVD IEGETDPLQIAMKELSQRKIPLVIRRYLPDGSYEDWGCDE LIVD G:  MFFLKDLSLILTLHPSYFGPQMNQYLREKLLTDVEGTCTG QFGYIVTVLDGMNIDVGKGRIIPGSGSAEFEVKYRAVVWK PFKGEVVDAIVSNVSPIGFFADVGPLNVFVSTRLIPDNLV YNPSNSPPAYMSNDELITKGSKVRLKVVGTRTDVNEIYAI GSIKEDFLGAI H:  SALFDDIFTVQTVDNGRYNKVSRIIGISTTNSAIKLTLDI NNEMFPVSQDDSLTVTLANSLSLKSWRPPKPTDKSLADDY DYVMFGTVYKFEEGDEDKIKVYVSFGGLLMCLEGGYKSLA SLKQDNLYILIRR I:  SFRFCLECNNMLYPKEDKENQRLLYSCRNCDYTELAEDPK VYRHELITNIGETAGIVDDIGQDPTLPRSDKECPECHSRD CVFFQSQQRRKDTNMTLFYVCLNCKKTFRDE J:  MIIPVRCFSCGKVVGDKWDAYLRLLEEGKQEGDALDELKL KRYCCRRMVLTHVDLIEKFLRYNPLE K:  MNAPDRFELFILPDDVPKLKITPDSRVPNCIIIKFEREDH TLANLLREELALYPDVTFVAYKVEHPLFANFVMRLQTEEG TRPKQALERACASIINKLKTLDHKFNEEWNIKN L:  GVKYTCGACAHNFSLNKSDPVRCKECGHRVIYKARTKRMI QFDAR N:  GGTGTGTTTGGGTTTTCGTTGTTTTTTTCTGTCTCGTGCC TGGTGTCTTGGGTGTAATCCCCTTGGCGGTTAAAACGCGG GGGACAGCGCGTACGTGCGTTTAAGCGGTGCTAGAGCTGT CTACGACCAATTGAGCGGCCTCGGCACCGGGATTCTGAT P:  UGGGUGGUGGC T:  ATCAGAATCCCGGTGCCGAGGCCGCTCAATTGGTCGTAGA CAGCTCTAGCACCGCTTAAACGCACGTACGCGCTGTCCCC CGCGTTTTAACCGCCAAGGGGATTACACCCAAGACACCAG GCACGAGACAGAAAAAAACAACGAAAACGGCCACCACCCA AACACACC a:  PHRYRPGTVALREIRRYQKSTELLIRKLPFQRLVREIAQD FKTDLRFQSAAIGALQEASEAYLVGLFEDTNLCAIHAKRV TIMPKDIQLARRIRGER b:  RDNIQGITKPAIRRLARRGGVKRISGLIYEETRGVLKVFL ENVIRDAVTYTEHAKRKTVTAMDVVYALKRQGRTLYGFGG c:  TRSSRAGLQFPVGRVHRLLRKGNYSERVGAGAPVYLAAVL EYLTAEILELAGNAARDNKKTRIIPRHLQLAIRNDEELNK LLGRVTIAQGGVLPNIQAVLLPK d:  RSRKESYSIYVYKVLKQVHPDTGISSKAMGIMNSFVNDIF ERIAGEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHA VSEGTKAVTKYTSAK e:  HRYRPGTVALREIRRYQKSTELLIRKLPFQRLVREIAQDF KTDLRFQSAAIGALQEASEAYLVGLFEDTNLCAIHAKRVT IMPKDIQLARRIRGERA f:  NIQGITKPAIRRLARRGGVKRISGLIYEETRGVLKVFLEN VIRDAVTYTEHAKRKTVTAMDVVYALKRQGRTLYGFGG g:  AKTRSSRAGLQFPVGRVHRLLRKGNYSERVGAGAPVYLAA VLEYLTAEILELAGNAARDNKKTRIIPRHLQLAIRNDEEL NKLLGRVTIAQGGVLPNIQAVLLPK h:  SRKESYSIYVYKVLKQVHPDTGISSKAMGIMNSFVNDIFE RIAGEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHAV SEGTKAVTKYTSA Description Functional site 1) chain A residue 67 type sequence C description binding site for residue ZN A 1801 source : AC1 2) chain A residue 70 type sequence C description binding site for residue ZN A 1801 source : AC1 3) chain A residue 77 type sequence C description binding site for residue ZN A 1801 source : AC1 4) chain A residue 80 type sequence H description binding site for residue ZN A 1801 source : AC1 5) chain A residue 107 type sequence C description binding site for residue ZN A 1802 source : AC2 6) chain A residue 148 type sequence C description binding site for residue ZN A 1802 source : AC2 7) chain A residue 167 type sequence G description binding site for residue ZN A 1802 source : AC2 8) chain A residue 168 type sequence C description binding site for residue ZN A 1802 source : AC2 9) chain A residue 482 type sequence D description binding site for residue MG A 1803 source : AC3 10) chain A residue 484 type sequence D description binding site for residue MG A 1803 source : AC3 11) chain P residue 10 type sequence C description binding site for residue MG A 1803 source : AC3 12) chain B residue 1163 type sequence C description binding site for residue ZN B 1301 source : AC4 13) chain B residue 1166 type sequence C description binding site for residue ZN B 1301 source : AC4 14) chain B residue 1182 type sequence C description binding site for residue ZN B 1301 source : AC4 15) chain B residue 1185 type sequence C description binding site for residue ZN B 1301 source : AC4 16) chain C residue 85 type sequence C description binding site for residue ZN C 401 source : AC5 17) chain C residue 87 type sequence C description binding site for residue ZN C 401 source : AC5 18) chain C residue 91 type sequence C description binding site for residue ZN C 401 source : AC5 19) chain C residue 93 type sequence E description binding site for residue ZN C 401 source : AC5 20) chain I residue 75 type sequence C description binding site for residue ZN I 201 source : AC6 21) chain I residue 77 type sequence E description binding site for residue ZN I 201 source : AC6 22) chain I residue 78 type sequence C description binding site for residue ZN I 201 source : AC6 23) chain I residue 103 type sequence C description binding site for residue ZN I 201 source : AC6 24) chain I residue 105 type sequence N description binding site for residue ZN I 201 source : AC6 25) chain I residue 106 type sequence C description binding site for residue ZN I 201 source : AC6 26) chain I residue 9 type sequence E description binding site for residue ZN I 202 source : AC7 27) chain I residue 10 type sequence C description binding site for residue ZN I 202 source : AC7 28) chain I residue 32 type sequence C description binding site for residue ZN I 202 source : AC7 29) chain J residue 7 type sequence C description binding site for residue ZN J 101 source : AC8 30) chain J residue 10 type sequence C description binding site for residue ZN J 101 source : AC8 31) chain J residue 44 type sequence C description binding site for residue ZN J 101 source : AC8 32) chain J residue 45 type sequence C description binding site for residue ZN J 101 source : AC8 33) chain L residue 33 type sequence C description binding site for residue ZN L 101 source : AC9 34) chain L residue 35 type sequence A description binding site for residue ZN L 101 source : AC9 35) chain L residue 36 type sequence C description binding site for residue ZN L 101 source : AC9 36) chain L residue 50 type sequence C description binding site for residue ZN L 101 source : AC9 37) chain c residue 21-27 type prosite sequence AGLQFPV description HISTONE_H2A Histone H2A signature. AGLqFPV source prosite : PS00046 38) chain d residue 89-111 type prosite sequence REIQTAVRLLLPGELAKHAVSEG description HISTONE_H2B Histone H2B signature. REIQTavRlLLpGELaKHAVSEG source prosite : PS00357 39) chain C residue 30-70 type prosite sequence NSLRRTMLAEVPTLAIDLVEIKMNTSVLADEFISHRLGLI P description RNA_POL_D_30KD RNA polymerases D / 30 to 40 Kd subunits signature. NSLRRtmlaevptlAidlVeikmNtSvlaDEfIShRLGLIP source prosite : PS00446 40) chain a residue 66-74 type prosite sequence PFQRLVREI description HISTONE_H3_2 Histone H3 signature 2. PFqRLVREI source prosite : PS00959 41) chain I residue 6-32 type prosite sequence FCLECNNMLYPKEDKENQRLLYSCRNC description RNA_POL_M_15KD RNA polymerases M / 15 Kd subunits signature. FCLECNNMLypkedkenqrllysCrnC source prosite : PS01030 42) chain E residue 146-159 type prosite sequence HELVPKHIRLSDGE description RNA_POL_H_23KD RNA polymerases H / 23 Kd subunits signature. HELVPKHirLsdGE source prosite : PS01110 43) chain F residue 86-100 type prosite sequence TKYERARILGTRALQ description RNA_POL_K_14KD RNA polymerases K / 14 to 18 Kd subunits signature. TkYErARiLGtRAlQ source prosite : PS01111 44) chain J residue 2-11 type prosite sequence IIPVRCFSCG description RNA_POL_N_8KD RNA polymerases N / 8 Kd subunits signature. IIPVrCFSCG source prosite : PS01112 45) chain K residue 35-66 type prosite sequence FEREDHTLANLLREELALYPDVTFVAYKVEHP description RNA_POL_L_13KD RNA polymerases L / 13 to 16 Kd subunits signature. FerEdHTLaNlLreeLalypdVtfvaYkveHP source prosite : PS01154 46) chain B residue 977-989 type prosite sequence GDKFASRHGQKGT description RNA_POL_BETA RNA polymerases beta chain signature. GdKFASrHGQKGT source prosite : PS01166 47) chain d residue 33 type MOD_RES sequence S description Phosphoserine; by AMPK => ECO:0000250|UniProtKB:Q64475 source Swiss-Prot : SWS_FT_FI10 48) chain h residue 33 type MOD_RES sequence S description Phosphoserine; by AMPK => ECO:0000250|UniProtKB:Q64475 source Swiss-Prot : SWS_FT_FI10 49) chain d residue 43 type MOD_RES sequence K description N6-methyllysine; alternate => ECO:0000269|PubMed:16627869 source Swiss-Prot : SWS_FT_FI11 50) chain d residue 105 type MOD_RES sequence K description N6-methyllysine; alternate => ECO:0000269|PubMed:16627869 source Swiss-Prot : SWS_FT_FI11 51) chain h residue 43 type MOD_RES sequence K description N6-methyllysine; alternate => ECO:0000269|PubMed:16627869 source Swiss-Prot : SWS_FT_FI11 52) chain h residue 105 type MOD_RES sequence K description N6-methyllysine; alternate => ECO:0000269|PubMed:16627869 source Swiss-Prot : SWS_FT_FI11 53) chain d residue 54 type MOD_RES sequence K description N6-(2-hydroxyisobutyryl)lysine; alternate => ECO:0000269|PubMed:24681537 source Swiss-Prot : SWS_FT_FI12 54) chain h residue 54 type MOD_RES sequence K description N6-(2-hydroxyisobutyryl)lysine; alternate => ECO:0000269|PubMed:24681537 source Swiss-Prot : SWS_FT_FI12 55) chain d residue 76 type MOD_RES sequence R description Dimethylated arginine => ECO:0000250|UniProtKB:Q96A08 source Swiss-Prot : SWS_FT_FI13 56) chain h residue 76 type MOD_RES sequence R description Dimethylated arginine => ECO:0000250|UniProtKB:Q96A08 source Swiss-Prot : SWS_FT_FI13 57) chain e residue 64 type MOD_RES sequence K description Dimethylated arginine => ECO:0000250|UniProtKB:Q96A08 source Swiss-Prot : SWS_FT_FI13 58) chain d residue 83 type MOD_RES sequence R description Omega-N-methylarginine => ECO:0000250|UniProtKB:Q96A08 source Swiss-Prot : SWS_FT_FI14 59) chain d residue 89 type MOD_RES sequence R description Omega-N-methylarginine => ECO:0000250|UniProtKB:Q96A08 source Swiss-Prot : SWS_FT_FI14 60) chain h residue 83 type MOD_RES sequence R description Omega-N-methylarginine => ECO:0000250|UniProtKB:Q96A08 source Swiss-Prot : SWS_FT_FI14 61) chain h residue 89 type MOD_RES sequence R description Omega-N-methylarginine => ECO:0000250|UniProtKB:Q96A08 source Swiss-Prot : SWS_FT_FI14 62) chain d residue 112 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:Q00729 source Swiss-Prot : SWS_FT_FI15 63) chain h residue 112 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:Q00729 source Swiss-Prot : SWS_FT_FI15 64) chain f residue 91 type MOD_RES sequence K description Phosphothreonine => ECO:0000250|UniProtKB:Q00729 source Swiss-Prot : SWS_FT_FI15 65) chain d residue 109 type CARBOHYD sequence S description O-linked (GlcNAc) serine => ECO:0000250|UniProtKB:P62807 source Swiss-Prot : SWS_FT_FI16 66) chain h residue 109 type CARBOHYD sequence S description O-linked (GlcNAc) serine => ECO:0000250|UniProtKB:P62807 source Swiss-Prot : SWS_FT_FI16 67) chain b residue 79 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250|UniProtKB:P62807 source Swiss-Prot : SWS_FT_FI16 68) chain f residue 59 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250|UniProtKB:P62807 source Swiss-Prot : SWS_FT_FI16 69) chain f residue 79 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250|UniProtKB:P62807 source Swiss-Prot : SWS_FT_FI16 70) chain d residue 117 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000269|PubMed:16307923, ECO:0000269|PubMed:16627869, ECO:0000269|PubMed:16713563 source Swiss-Prot : SWS_FT_FI18 71) chain h residue 117 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000269|PubMed:16307923, ECO:0000269|PubMed:16627869, ECO:0000269|PubMed:16713563 source Swiss-Prot : SWS_FT_FI18 72) chain d residue 31 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000269|PubMed:21726816 source Swiss-Prot : SWS_FT_FI20 73) chain h residue 31 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000269|PubMed:21726816 source Swiss-Prot : SWS_FT_FI20 74) chain a residue 57 type MOD_RES sequence S description Phosphoserine => ECO:0000269|PubMed:20850016 source Swiss-Prot : SWS_FT_FI21 75) chain e residue 57 type MOD_RES sequence S description Phosphoserine => ECO:0000269|PubMed:20850016 source Swiss-Prot : SWS_FT_FI21 76) chain a residue 79 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000269|PubMed:22389435, ECO:0000269|PubMed:29211711 source Swiss-Prot : SWS_FT_FI22 77) chain e residue 79 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000269|PubMed:22389435, ECO:0000269|PubMed:29211711 source Swiss-Prot : SWS_FT_FI22 78) chain a residue 80 type MOD_RES sequence T description Phosphothreonine => ECO:0000269|PubMed:20850016 source Swiss-Prot : SWS_FT_FI23 79) chain e residue 80 type MOD_RES sequence T description Phosphothreonine => ECO:0000269|PubMed:20850016 source Swiss-Prot : SWS_FT_FI23 80) chain a residue 86 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI24 81) chain e residue 86 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI24 82) chain a residue 107 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI25 83) chain e residue 107 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI25 84) chain a residue 115 type MOD_RES sequence K description N6-glutaryllysine; alternate => ECO:0000269|PubMed:31542297 source Swiss-Prot : SWS_FT_FI26 85) chain e residue 115 type MOD_RES sequence K description N6-glutaryllysine; alternate => ECO:0000269|PubMed:31542297 source Swiss-Prot : SWS_FT_FI26 86) chain a residue 122 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000269|PubMed:22389435, ECO:0000269|PubMed:27436229 source Swiss-Prot : SWS_FT_FI27 87) chain e residue 122 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000269|PubMed:22389435, ECO:0000269|PubMed:27436229 source Swiss-Prot : SWS_FT_FI27 88) chain h residue 40 type MOD_RES sequence K description N6-lactoyllysine; alternate => ECO:0000269|PubMed:31645732 source Swiss-Prot : SWS_FT_FI3 89) chain h residue 82 type MOD_RES sequence K description N6-lactoyllysine; alternate => ECO:0000269|PubMed:31645732 source Swiss-Prot : SWS_FT_FI3 90) chain d residue 40 type MOD_RES sequence K description N6-lactoyllysine; alternate => ECO:0000269|PubMed:31645732 source Swiss-Prot : SWS_FT_FI3 91) chain d residue 82 type MOD_RES sequence K description N6-lactoyllysine; alternate => ECO:0000269|PubMed:31645732 source Swiss-Prot : SWS_FT_FI3 92) chain g residue 95 type MOD_RES sequence K description ADP-ribosylserine => ECO:0000269|PubMed:34874266 source Swiss-Prot : SWS_FT_FI4 93) chain b residue 44 type MOD_RES sequence K description N6-crotonyllysine; alternate => ECO:0000269|PubMed:21925322 source Swiss-Prot : SWS_FT_FI5 94) chain f residue 44 type MOD_RES sequence K description N6-crotonyllysine; alternate => ECO:0000269|PubMed:21925322 source Swiss-Prot : SWS_FT_FI5 95) chain b residue 77 type MOD_RES sequence K description Phosphoserine; by STK4/MST1 => ECO:0000269|PubMed:12757711 source Swiss-Prot : SWS_FT_FI6 96) chain b residue 91 type MOD_RES sequence K description Phosphoserine; by STK4/MST1 => ECO:0000269|PubMed:12757711 source Swiss-Prot : SWS_FT_FI6 97) chain f residue 31 type MOD_RES sequence K description Phosphoserine; by STK4/MST1 => ECO:0000269|PubMed:12757711 source Swiss-Prot : SWS_FT_FI6 98) chain f residue 77 type MOD_RES sequence K description Phosphoserine; by STK4/MST1 => ECO:0000269|PubMed:12757711 source Swiss-Prot : SWS_FT_FI6 99) chain f residue 91 type MOD_RES sequence K description Phosphoserine; by STK4/MST1 => ECO:0000269|PubMed:12757711 source Swiss-Prot : SWS_FT_FI6 100) chain g residue 74 type MOD_RES sequence K description N6-(2-hydroxyisobutyryl)lysine => ECO:0000269|PubMed:24681537 source Swiss-Prot : SWS_FT_FI7 101) chain g residue 75 type MOD_RES sequence K description N6-(2-hydroxyisobutyryl)lysine => ECO:0000269|PubMed:24681537 source Swiss-Prot : SWS_FT_FI7 102) chain d residue 31 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000269|PubMed:22389435 source Swiss-Prot : SWS_FT_FI8 103) chain d residue 113 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000269|PubMed:22389435 source Swiss-Prot : SWS_FT_FI8 104) chain d residue 117 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000269|PubMed:22389435 source Swiss-Prot : SWS_FT_FI8 105) chain h residue 31 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000269|PubMed:22389435 source Swiss-Prot : SWS_FT_FI8 106) chain h residue 113 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000269|PubMed:22389435 source Swiss-Prot : SWS_FT_FI8 107) chain h residue 117 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000269|PubMed:22389435 source Swiss-Prot : SWS_FT_FI8 108) chain d residue 32 type MOD_RES sequence E description PolyADP-ribosyl glutamic acid => ECO:0000250|UniProtKB:Q64475 source Swiss-Prot : SWS_FT_FI9 109) chain h residue 32 type MOD_RES sequence E description PolyADP-ribosyl glutamic acid => ECO:0000250|UniProtKB:Q64475 source Swiss-Prot : SWS_FT_FI9 110) chain g residue 118 type MOD_RES sequence K description PolyADP-ribosyl glutamic acid => ECO:0000250|UniProtKB:Q64475 source Swiss-Prot : SWS_FT_FI9

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