DIP Database of Interacting Proteins 611 Young Drive East; Los Angeles CA 90095; USA http://dip.doe-mbi.ucla.edu/ dip@mbi.ucla.edu Phosphorylation of histone H3T6 by PKCbeta(I) controls demethylation at histone H3K4. Phosphorylation of histone H3T6 by PKCbeta(I) controls demethylation at histone H3K4. Nature 2010 imex curation Metzger E., Imhof A., Patel D., Kahl P., Hoffmeyer K., Friedrichs N., Müller JM., Greschik H., Kirfel J., Ji S., Kunowska N., Beisenherz-Huss C., Günther T., Buettner R., Schüle R. Only protein-protein interactions in vitro In vitro pull down pull down autoradiography autoradiography Metzger E., Imhof A., Patel D., Kahl P., Hoffmeyer K., Friedrichs N., Müller JM., Greschik H., Kirfel J., Ji S., Kunowska N., Beisenherz-Huss C., Günther T., Buettner R., Schüle R. DIP original experiment: DIP-216240X Nature 2010 IMEx Phosphorylation of histone H3T6 by PKCbeta(I) controls demethylation at histone H3K4. Phosphorylation of histone H3T6 by PKCbeta(I) controls demethylation at histone H3K4. Phosphorylation of histone H3T6 by PKCbeta(I) controls demethylation at histone H3K4. Nature 2010 imex curation Metzger E., Imhof A., Patel D., Kahl P., Hoffmeyer K., Friedrichs N., Müller JM., Greschik H., Kirfel J., Ji S., Kunowska N., Beisenherz-Huss C., Günther T., Buettner R., Schüle R. Only protein-protein interactions in vitro In vitro protein kinase assay protein kinase assay predetermined predetermined participant predetermined Metzger E., Imhof A., Patel D., Kahl P., Hoffmeyer K., Friedrichs N., Müller JM., Greschik H., Kirfel J., Ji S., Kunowska N., Beisenherz-Huss C., Günther T., Buettner R., Schüle R. DIP original experiment: DIP-216234X Nature 2010 IMEx Phosphorylation of histone H3T6 by PKCbeta(I) controls demethylation at histone H3K4. Phosphorylation of histone H3T6 by PKCbeta(I) controls demethylation at histone H3K4. Phosphorylation of histone H3T6 by PKCbeta(I) controls demethylation at histone H3K4. Nature 2010 imex curation Metzger E., Imhof A., Patel D., Kahl P., Hoffmeyer K., Friedrichs N., Müller JM., Greschik H., Kirfel J., Ji S., Kunowska N., Beisenherz-Huss C., Günther T., Buettner R., Schüle R. Only protein-protein interactions human Homo sapiens Human anti tag coip anti tag coimmunoprecipitation anti tag coip predetermined predetermined participant predetermined Metzger E., Imhof A., Patel D., Kahl P., Hoffmeyer K., Friedrichs N., Müller JM., Greschik H., Kirfel J., Ji S., Kunowska N., Beisenherz-Huss C., Günther T., Buettner R., Schüle R. DIP original experiment: DIP-216237X Nature 2010 IMEx Phosphorylation of histone H3T6 by PKCbeta(I) controls demethylation at histone H3K4. Phosphorylation of histone H3T6 by PKCbeta(I) controls demethylation at histone H3K4. Phosphorylation of histone H3T6 by PKCbeta(I) controls demethylation at histone H3K4. Nature 2010 imex curation Metzger E., Imhof A., Patel D., Kahl P., Hoffmeyer K., Friedrichs N., Müller JM., Greschik H., Kirfel J., Ji S., Kunowska N., Beisenherz-Huss C., Günther T., Buettner R., Schüle R. Only protein-protein interactions in vitro In vitro pull down pull down predetermined predetermined participant predetermined Metzger E., Imhof A., Patel D., Kahl P., Hoffmeyer K., Friedrichs N., Müller JM., Greschik H., Kirfel J., Ji S., Kunowska N., Beisenherz-Huss C., Günther T., Buettner R., Schüle R. DIP original experiment: DIP-216238X Nature 2010 IMEx Phosphorylation of histone H3T6 by PKCbeta(I) controls demethylation at histone H3K4. Phosphorylation of histone H3T6 by PKCbeta(I) controls demethylation at histone H3K4. Phosphorylation of histone H3T6 by PKCbeta(I) controls demethylation at histone H3K4. Nature 2010 imex curation Metzger E., Imhof A., Patel D., Kahl P., Hoffmeyer K., Friedrichs N., Müller JM., Greschik H., Kirfel J., Ji S., Kunowska N., Beisenherz-Huss C., Günther T., Buettner R., Schüle R. Only protein-protein interactions in vitro In vitro demethylase assay demethylase assay predetermined predetermined participant predetermined Metzger E., Imhof A., Patel D., Kahl P., Hoffmeyer K., Friedrichs N., Müller JM., Greschik H., Kirfel J., Ji S., Kunowska N., Beisenherz-Huss C., Günther T., Buettner R., Schüle R. DIP original experiment: DIP-216236X Nature 2010 IMEx Phosphorylation of histone H3T6 by PKCbeta(I) controls demethylation at histone H3K4. Phosphorylation of histone H3T6 by PKCbeta(I) controls demethylation at histone H3K4. Phosphorylation of histone H3T6 by PKCbeta(I) controls demethylation at histone H3K4. Nature 2010 imex curation Metzger E., Imhof A., Patel D., Kahl P., Hoffmeyer K., Friedrichs N., Müller JM., Greschik H., Kirfel J., Ji S., Kunowska N., Beisenherz-Huss C., Günther T., Buettner R., Schüle R. Only protein-protein interactions in vitro In vitro demethylase assay demethylase assay predetermined predetermined participant predetermined Metzger E., Imhof A., Patel D., Kahl P., Hoffmeyer K., Friedrichs N., Müller JM., Greschik H., Kirfel J., Ji S., Kunowska N., Beisenherz-Huss C., Günther T., Buettner R., Schüle R. DIP original experiment: DIP-216235X Nature 2010 IMEx Phosphorylation of histone H3T6 by PKCbeta(I) controls demethylation at histone H3K4. Phosphorylation of histone H3T6 by PKCbeta(I) controls demethylation at histone H3K4. Phosphorylation of histone H3T6 by PKCbeta(I) controls demethylation at histone H3K4. Nature 2010 imex curation Metzger E., Imhof A., Patel D., Kahl P., Hoffmeyer K., Friedrichs N., Müller JM., Greschik H., Kirfel J., Ji S., Kunowska N., Beisenherz-Huss C., Günther T., Buettner R., Schüle R. Only protein-protein interactions in vitro In vitro pull down pull down predetermined predetermined participant predetermined Metzger E., Imhof A., Patel D., Kahl P., Hoffmeyer K., Friedrichs N., Müller JM., Greschik H., Kirfel J., Ji S., Kunowska N., Beisenherz-Huss C., Günther T., Buettner R., Schüle R. DIP original experiment: DIP-216239X Nature 2010 IMEx Phosphorylation of histone H3T6 by PKCbeta(I) controls demethylation at histone H3K4. h31_human Histone H3.1 H3FA H3FL H3FD H3FI H3FH H3FK H3FF H3FJ H3FB Histone H3/a Histone H3/b Histone H3/c Histone H3/d Histone H3/f Histone H3/h Histone H3/i Histone H3/j Histone H3/k Histone H3/l H3C1 HIST1H3A H3C2 HIST1H3B H3C3 H3FC HIST1H3C H3C4 HIST1H3D H3C6 HIST1H3E H3C7 HIST1H3F H3C8 HIST1H3G H3C10 HIST1H3H H3C11 HIST1H3I H3C12 HIST1H3J protein protein human Homo sapiens Human MARTKQTARKSTGGKAPRKQLATKAARKSAPATGGVKKPHRYRPGTVALREIRRYQKSTELLIRKLPFQRLVREIAQDFKTDLRFQSSAVMALQEACEAYLVGLFEDTNLCAIHAKRVTIMPKDIQLARRIRGERA DIP protein P68431 original sequence version: 78 DIP protein P68431 original sequence version: 79 DIP protein P68431 original sequence version: 76 DIP protein P68431 original sequence version: 92 DIP protein P68431 original sequence version: 87 DIP protein P68431 original sequence version: 101 DIP protein P68431 original sequence version: 130 DIP protein P68431 original sequence version: 115 9B89008EA50A0EF6 kdm5b_human Lysine-specific demethylase 5B KDM5B JARID1B PLU1 RBBP2H1 Histone demethylase JARID1B Jumonji/ARID domain-containing protein 1B PLU-1 Retinoblastoma-binding protein 2 homolog 1 Cancer/testis antigen 31 [histone H3]-trimethyl-L-lysine(4) demethylase 5B protein protein human Homo sapiens Human MEAATTLHPGPRPALPLGGPGPLGEFLPPPECPVFEPSWEEFADPFAFIHKIRPIAEQTGICKVRPPPDWQPPFACDVDKLHFTPRIQRLNELEAQTRVKLNFLDQIAKYWELQGSTLKIPHVERKILDLFQLNKLVAEEGGFAVVCKDRKWTKIATKMGFAPGKAVGSHIRGHYERILNPYNLFLSGDSLRCLQKPNLTTDTKDKEYKPHDIPQRQSVQPSETCPPARRAKRMRAEAMNIKIEPEETTEARTHNLRRRMGCPTPKCENEKEMKSSIKQEPIERKDYIVENEKEKPKSRSKKATNAVDLYVCLLCGSGNDEDRLLLCDGCDDSYHTFCLIPPLHDVPKGDWRCPKCLAQECSKPQEAFGFEQAARDYTLRTFGEMADAFKSDYFNMPVHMVPTELVEKEFWRLVSTIEEDVTVEYGADIASKEFGSGFPVRDGKIKLSPEEEEYLDSGWNLNNMPVMEQSVLAHITADICGMKLPWLYVGMCFSSFCWHIEDHWSYSINYLHWGEPKTWYGVPGYAAEQLENVMKKLAPELFVSQPDLLHQLVTIMNPNTLMTHEVPVYRTNQCAGEFVITFPRAYHSGFNQGFNFAEAVNFCTVDWLPLGRQCVEHYRLLHRYCVFSHDEMICKMASKADVLDVVVASTVQKDMAIMIEDEKALRETVRKLGVIDSERMDFELLPDDERQCVKCKTTCFMSAISCSCKPGLLVCLHHVKELCSCPPYKYKLRYRYTLDDLYPMMNALKLRAESYNEWALNVNEALEAKINKKKSLVSFKALIEESEMKKFPDNDLLRHLRLVTQDAEKCASVAQQLLNGKRQTRYRSGGGKSQNQLTVNELRQFVTQLYALPCVLSQTPLLKDLLNRVEDFQQHSQKLLSEETPSAAELQDLLDVSFEFDVELPQLAEMRIRLEQARWLEEVQQACLDPSSLTLDDMRRLIDLGVGLAPYSAVEKAMARLQELLTVSEHWDDKAKSLLKARPRHSLNSLATAVKEIEEIPAYLPNGAALKDSVQRARDWLQDVEGLQAGGRVPVLDTLIELVTRGRSIPVHLNSLPRLETLVAEVQAWKECAVNTFLTENSPYSLLEVLCPRCDIGLLGLKRKQRKLKEPLPNGKKKSTKLESLSDLERALTESKETASAMATLGEARLREMEALQSLRLANEGKLLSPLQDVDIKICLCQKAPAAPMIQCELCRDAFHTSCVAVPSISQGLRIWLCPHCRRSEKPPLEKILPLLASLQRIRVRLPEGDALRYMIERTVNWQHRAQQLLSSGNLKFVQDRVGSGLLYSRWQASAGQVSDTNKVSQPPGTTSFSLPDDWDNRTSYLHSPFSTGRSCIPLHGVSPEVNELLMEAQLLQVSLPEIQELYQTLLAKPSPAQQTDRSSPVRPSSEKNDCCRGKRDGINSLERKLKRRLEREGLSSERWERVKKMRTPKKKKIKLSHPKDMNNFKLERERSYELVRSAETHSLPSDTSYSEQEDSEDEDAICPAVSCLQPEGDEVDWVQCDGSCNQWFHQVCVGVSPEMAEKEDYICVRCTVKDAPSRK DIP protein Q9UGL1 original sequence version: 62 70A0738D9A709F61 p05771-1 Protein kinase C beta type PKCB PRKCB1 PRKCB1 PRKCB protein protein human Homo sapiens Human MADPAAGPPPSEGEESTVRFARKGALRQKNVHEVKNHKFTARFFKQPTFCSHCTDFIWGFGKQGFQCQVCCFVVHKRCHEFVTFSCPGADKGPASDDPRSKHKFKIHTYSSPTFCDHCGSLLYGLIHQGMKCDTCMMNVHKRCVMNVPSLCGTDHTERRGRIYIQAHIDRDVLIVLVRDAKNLVPMDPNGLSDPYVKLKLIPDPKSESKQKTKTIKCSLNPEWNETFRFQLKESDKDRRLSVEIWDWDLTSRNDFMGSLSFGISELQKASVDGWFKLLSQEEGEYFNVPVPPEGSEANEELRQKFERAKISQGTKVPEEKTTNTVSKFDNNGNRDRMKLTDFNFLMVLGKGSFGKVMLSERKGTDELYAVKILKKDVVIQDDDVECTMVEKRVLALPGKPPFLTQLHSCFQTMDRLYFVMEYVNGGDLMYHIQQVGRFKEPHAVFYAAEIAIGLFFLQSKGIIYRDLKLDNVMLDSEGHIKIADFGMCKENIWDGVTTKTFCGTPDYIAPEIIAYQPYGKSVDWWAFGVLLYEMLAGQAPFEGEDEDELFQSIMEHNVAYPKSMSKEAVAICKGLMTKHPGKRLGCGPEGERDIKEHAFFRYIDWEKLERKEIQPPYKPKARDKRDTSNFDKEFTRQPVELTPTDKLFIMNLDQNEFAGFSYTNPEFVINV DIP protein P05771-1 original sequence version: 141 DIP protein P05771 original sequence version: 196 3937E7B667108C68 o60341-1 Lysine-specific histone demethylase 1A KDM1A AOF2 KDM1 KIAA0601 LSD1 BRAF35-HDAC complex protein BHC110 Flavin-containing amine oxidase domain-containing protein 2 [histone H3]-dimethyl-L-lysine(4) FAD-dependent demethylase 1A protein protein human Homo sapiens Human MLSGKKAAAAAAAAAAAATGTEAGPGTAGGSENGSEVAAQPAGLSGPAEVGPGAVGERTPRKKEPPRASPPGGLAEPPGSAGPQAGPTVVPGSATPMETGIAETPEGRRTSRRKRAKVEYREMDESLANLSEDEYYSEEERNAKAEKEKKLPPPPPQAPPEEENESEPEEPSGVEGAAFQSRLPHDRMTSQEAACFPDIISGPQQTQKVFLFIRNRTLQLWLDNPKIQLTFEATLQQLEAPYNSDTVLVHRVHSYLERHGLINFGIYKRIKPLPTKKTGKVIIIGSGVSGLAAARQLQSFGMDVTLLEARDRVGGRVATFRKGNYVADLGAMVVTGLGGNPMAVVSKQVNMELAKIKQKCPLYEANGQAVPKEKDEMVEQEFNRLLEATSYLSHQLDFNVLNNKPVSLGQALEVVIQLQEKHVKDEQIEHWKKIVKTQEELKELLNKMVNLKEKIKELHQQYKEASEVKPPRDITAEFLVKSKHRDLTALCKEYDELAETQGKLEEKLQELEANPPSDVYLSSRDRQILDWHFANLEFANATPLSTLSLKHWDQDDDFEFTGSHLTVRNGYSCVPVALAEGLDIKLNTAVRQVRYTASGCEVIAVNTRSTSQTFIYKCDAVLCTLPLGVLKQQPPAVQFVPPLPEWKTSAVQRMGFGNLNKVVLCFDRVFWDPSVNLFGHVGSTTASRGELFLFWNLYKAPILLALVAGEAAGIMENISDDVIVGRCLAILKGIFGSSAVPQPKETVVSRWRADPWARGSYSYVAAGSSGNDYDLMAQPITPGPSIPGAPQPIPRLFFAGEHTIRNYPATVHGALLSGLREAGRIADQFLGAMYTLPRQATPGVPAQQSPSM DIP protein O60341-1 original sequence version: 151 DIP protein O60341 original sequence version: 99 DIP protein O60341 original sequence version: 123 DIP protein O60341 original sequence version: 134 DIP protein O60341 original sequence version: 137 DIP protein O60341-1 original sequence version: 137 DIP protein O60341-1 original sequence version: 109 DIP protein O60341 original sequence version: 163 DIP protein O60341 original sequence version: 97 pkn1_human Serine/threonine-protein kinase N1 PKN1 PKN PRK1 PRKCL1 PAK1 Protease-activated kinase 1 Protein kinase C-like 1 Protein kinase C-like PKN Protein kinase PKN-alpha Protein-kinase C-related kinase 1 Serine-threonine protein kinase N protein protein human Homo sapiens Human MASDAVQSEPRSWSLLEQLGLAGADLAAPGVQQQLELERERLRREIRKELKLKEGAENLRRATTDLGRSLGPVELLLRGSSRRLDLLHQQLQELHAHVVLPDPAATHDGPQSPGAGGPTCSATNLSRVAGLEKQLAIELKVKQGAENMIQTYSNGSTKDRKLLLTAQQMLQDSKTKIDIIRMQLRRALQAGQLENQAAPDDTQGSPDLGAVELRIEELRHHFRVEHAVAEGAKNVLRLLSAAKAPDRKAVSEAQEKLTESNQKLGLLREALERRLGELPADHPKGRLLREELAAASSAAFSTRLAGPFPATHYSTLCKPAPLTGTLEVRVVGCRDLPETIPWNPTPSMGGPGTPDSRPPFLSRPARGLYSRSGSLSGRSSLKAEAENTSEVSTVLKLDNTVVGQTSWKPCGPNAWDQSFTLELERARELELAVFWRDQRGLCALKFLKLEDFLDNERHEVQLDMEPQGCLVAEVTFRNPVIERIPRLRRQKKIFSKQQGKAFQRARQMNIDVATWVRLLRRLIPNATGTGTFSPGASPGSEARTTGDISVEKLNLGTDSDSSPQKSSRDPPSSPSSLSSPIQESTAPELPSETQETPGPALCSPLRKSPLTLEDFKFLAVLGRGHFGKVLLSEFRPSGELFAIKALKKGDIVARDEVESLMCEKRILAAVTSAGHPFLVNLFGCFQTPEHVCFVMEYSAGGDLMLHIHSDVFSEPRAIFYSACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKEGMGYGDRTSTFCGTPEFLAPEVLTDTSYTRAVDWWGLGVLLYEMLVGESPFPGDDEEEVFDSIVNDEVRYPRFLSAEAIGIMRRLLRRNPERRLGSSERDAEDVKKQPFFRTLGWEALLARRLPPPFVPTLSGRTDVSNFDEEFTGEAPTLSPPRDARPLTAAEQAAFLDFDFVAGGC DIP protein Q16512 original sequence version: 126 DIP protein Q16512 original sequence version: 153 61360295EC70BB8E andr_human Androgen receptor Dihydrotestosterone receptor Nuclear receptor subfamily 3 group C member 4 AR DHTR NR3C4 protein protein human Homo sapiens Human MEVQLGLGRVYPRPPSKTYRGAFQNLFQSVREVIQNPGPRHPEAASAAPPGASLLLLQQQQQQQQQQQQQQQQQQQQQQQETSPRQQQQQQGEDGSPQAHRRGPTGYLVLDEEQQPSQPQSALECHPERGCVPEPGAAVAASKGLPQQLPAPPDEDDSAAPSTLSLLGPTFPGLSSCSADLKDILSEASTMQLLQQQQQEAVSEGSSSGRAREASGAPTSSKDNYLGGTSTISDNAKELCKAVSVSMGLGVEALEHLSPGEQLRGDCMYAPLLGVPPAVRPTPCAPLAECKGSLLDDSAGKSTEDTAEYSPFKGGYTKGLEGESLGCSGSAAAGSSGTLELPSTLSLYKSGALDEAAAYQSRDYYNFPLALAGPPPPPPPPHPHARIKLENPLDYGSAWAAAAAQCRYGDLASLHGAGAAGPGSGSPSAAASSSWHTLFTAEEGQLYGPCGGGGGGGGGGGGGGGGGGGGGGGEAGAVAPYGYTRPPQGLAGQESDFTAPDVWYPGGMVSRVPYPSPTCVKSEMGPWMDSYSGPYGDMRLETARDHVLPIDYYFPPQKTCLICGDEASGCHYGALTCGSCKVFFKRAAEGKQKYLCASRNDCTIDKFRRKNCPSCRLRKCYEAGMTLGARKLKKLGNLKLQEEGEASSTTSPTEETTQKLTVSHIEGYECQPIFLNVLEAIEPGVVCAGHDNNQPDSFAALLSSLNELGERQLVHVVKWAKALPGFRNLHVDDQMAVIQYSWMGLMVFAMGWRSFTNVNSRMLYFAPDLVFNEYRMHKSRMYSQCVRMRHLSQEFGWLQITPQEFLCMKALLLFSIIPVDGLKNQKFFDELRMNYIKELDRIIACKRKNPTSCSRRFYQLTKLLDSVQPIARELHQFTFDLLIKSHMVSVDFPEMMAEIISVQVPKILSGKVKPIYFHTQ DIP protein P10275 original sequence version: 220 DIP protein P10275-1 original sequence version: 213 DIP protein P10275 original sequence version: 216 DIP protein P10275 original sequence version: 143 DIP protein P10275 original sequence version: 174 DIP protein P10275 original sequence version: 169 DIP protein P10275 original sequence version: 188 DIP protein P10275-1 original sequence version: 188 DIP protein P10275 original sequence version: 196 DIP protein P10275 original sequence version: 217 DIP protein P10275-1 original sequence version: 217 DIP protein P10275-1 original sequence version: 207 A73432C55D39AE06 hist1h3a-prkcb-1 2 10 enzyme enzyme unspecified role unspecified role spofr Spodoptera frugiperda (Fall armyworm) Fall armyworm 8 enzyme target enzyme target substrate substrate unspecified role unspecified role Region 2-16 Region 2-16 sufficient to bind sufficient binding region sufficient to bind deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain P68431:p.Thr7Ala T7A mutation disrupting mutation disrupting interaction mutation disrupting mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain T A This feature has been corrected as a result of our quality control procedures. The original label was 'T7A'. Wed May 02 17:01:54 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'thr7ala' Tue Jun 30 15:57:01 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Thr7Ala' ecolx Escherichia coli phosphorylation phosphorylation reaction phosphorylation hist1h3a-kdm5b-1 5 9 enzyme enzyme unspecified role unspecified role ecolx Escherichia coli 8 enzyme target enzyme target substrate substrate unspecified role unspecified role Region 2-21 Region 2-21 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain K5me3 K5me3 n6me3+lys N6,N6,N6-trimethyl-L-lysine (5S)-5-amino-5-carboxy-N,N,N-trimethylpentan-1-aminium 2-amino-6-(trimethylammonio)hexanoic acid 5-azanyl-5-carboxy-N,N,N-trimethylpentanazanium MOD_RES N6,N6,N6-trimethyllysine N(zeta)-trimethyllysine N6,N6,N6-trimethyl-L-lysine N6,N6,N6-trimethylated L-lysine N6,N6,N6-trimethyllysin-N6-ium N6,N6,N6-trimethyllysine cation epsilon-trimethyllysine N-trimethylation (of lysine) N6Me3+Lys Trimethyl tri-Methylation certain certain sequence position certain certain certain sequence position certain K5me2 K5me2 n6me2lys N6,N6-dimethyl-L-lysine (2S)-2-amino-6-(dimethylamino)hexanoic acid MOD_RES N6,N6-dimethyllysine N(zeta)-dimethyllysine N6,N6-dimethyl-L-lysine N6,N6-dimethylated L-lysine epsilon-dimethyllysine lysine derivative Lys(y) Dimethyl N6Me2Lys di-Methylation dimethylk certain certain sequence position certain certain certain sequence position certain in vitro In vitro demethylation demethylation reaction demethylation kdm1a-prkcb-1 4 10 unspecified role unspecified role prey prey 35S-label 35S-label 35s radiolabel 35s radiolabel 35S s35 radiolabelled S35 s35 radiolabelled 35S S35 undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined in vitro In vitro 11 unspecified role unspecified role bait bait GST-tag GST-tag gst tag glutathione s tranferase tag glutathione S-tranferase tag glutathione S-tranferase tag gst tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range ecolx Escherichia coli physical association physical association prkcb-pkn1-1 1 10 unspecified role unspecified role bait bait GST-tag GST-tag gst tag glutathione s tranferase tag glutathione S-tranferase tag glutathione S-tranferase tag gst tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range ecolx Escherichia coli 12 unspecified role unspecified role prey prey 35S-label 35S-label 35s radiolabel 35s radiolabel 35S s35 radiolabelled S35 s35 radiolabelled 35S S35 undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined in vitro In vitro physical association physical association hist1h3a-kdm1a-1 6 11 enzyme enzyme unspecified role unspecified role ecolx Escherichia coli 8 enzyme target enzyme target substrate substrate unspecified role unspecified role Region 2-21 Region 2-21 binding region binding-associated region binding region certain certain sequence position certain certain certain sequence position certain K5me1 K5me1 n6me1lys N6-methyl-L-lysine (2S)-2-amino-6-methylaminohexanoic acid MOD_RES N6-methyllysine N(zeta)-methyllysine N6-methyl-L-lysine N6-methylated L-lysine epsilon-methyllysine Methyl Methylation N-methyl Lysyl N6Me1Lys certain certain sequence position certain certain certain sequence position certain K5me2 K5me2 n6me2lys N6,N6-dimethyl-L-lysine (2S)-2-amino-6-(dimethylamino)hexanoic acid MOD_RES N6,N6-dimethyllysine N(zeta)-dimethyllysine N6,N6-dimethyl-L-lysine N6,N6-dimethylated L-lysine epsilon-dimethyllysine lysine derivative Lys(y) Dimethyl N6Me2Lys di-Methylation dimethylk certain certain sequence position certain certain certain sequence position certain in vitro In vitro demethylation demethylation reaction demethylation kdm1a-ar-1 3 10 unspecified role unspecified role prey prey human Homo sapiens Human 12 unspecified role unspecified role prey prey human Homo sapiens Human 13 unspecified role unspecified role prey prey human Homo sapiens Human 11 unspecified role unspecified role bait bait Flag-tag Flag-tag flag tag flag tag FLAG-tagged FLAG DYKDDDDKV epitope tag DYKDDDDKV epitope tag FLAG FLAG-tagged n-term range n-terminal range n-term range n-term range n-terminal range n-term range human Homo sapiens Human association association ar-prkcb-1 7 10 unspecified role unspecified role prey prey 35S-label 35S-label 35s radiolabel 35s radiolabel 35S s35 radiolabelled S35 s35 radiolabelled 35S S35 undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined in vitro In vitro 13 unspecified role unspecified role bait bait GST-tag GST-tag gst tag glutathione s tranferase tag glutathione S-tranferase tag glutathione S-tranferase tag gst tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range ecolx Escherichia coli physical association physical association