IntAct European Bioinformatics Institute IntAct intact http://www.ebi.ac.uk/ http://www.ebi.ac.uk/intact/query/${ac} EBI-[0-9]+|IA:[0-9]+ INTerAction database (IntAct) provides an open source database and toolkit for the storage, presentation and analysis of molecular interactions. http://www.ebi.ac.uk/intact European Bioinformatics Institute; Wellcome Trust Genome Campus; Hinxton, Cambridge; CB10 1SD; United Kingdom http://www.ebi.ac.uk/intact/ Lid2 is required for coordinating H3K4 and H3K9 methylation of heterochromatin and euchromatin. Lid2 is required for coordinating H3K4 and H3K9 methylation of heterochromatin and euchromatin. Cell (0092-8674) 2008 imex curation Li F., Huarte M., Zaratiegui M., Vaughn MW., Shi Y., Martienssen R., Cande WZ. Chromatin - Epigenetic interactions resulting in chromatin modulation Could not do CHIP assays as only vague regions of chromosomes identified as prey, not genes. Details of histone peptide supplied by author and from manufacturer's website. Peptide sequence has a 100% match to both S. pombe H3 proteins so both have been shown as binding to Lid3. feili@nature.berkeley.edu, zcande@berkeley.edu 16-Dec-2008: Contacted by JYOTI. davet Only protein-protein interactions 9 schpm Schizosaccharomyces pombe (fission yeast) Fission yeast tap tandem affinity purification TAP TAP tap ms participant Identification by mass spectrometry ms participant Li F., Huarte M., Zaratiegui M., Vaughn MW., Shi Y., Martienssen R., Cande WZ. Chromatin - Epigenetic interactions resulting in chromatin modulation Could not do CHIP assays as only vague regions of chromosomes identified as prey, not genes. Details of histone peptide supplied by author and from manufacturer's website. Peptide sequence has a 100% match to both S. pombe H3 proteins so both have been shown as binding to Lid3. feili@nature.berkeley.edu, zcande@berkeley.edu Accepted 2008-DEC-25 by DAVET. 16-Dec-2008: Contacted by JYOTI. Cell (0092-8674) 2008 davet Only protein-protein interactions 9 imex curation Lid2 is required for coordinating H3K4 and H3K9 methylation of heterochromatin and euchromatin. Lid2 is required for coordinating H3K4 and H3K9 methylation of heterochromatin and euchromatin. Cell (0092-8674) 2008 imex curation Li F., Huarte M., Zaratiegui M., Vaughn MW., Shi Y., Martienssen R., Cande WZ. Chromatin - Epigenetic interactions resulting in chromatin modulation Could not do CHIP assays as only vague regions of chromosomes identified as prey, not genes. Details of histone peptide supplied by author and from manufacturer's website. Peptide sequence has a 100% match to both S. pombe H3 proteins so both have been shown as binding to Lid3. feili@nature.berkeley.edu, zcande@berkeley.edu 16-Dec-2008: Contacted by JYOTI. davet Only protein-protein interactions 9 schpm Schizosaccharomyces pombe (fission yeast) Fission yeast anti tag coip anti tag coimmunoprecipitation anti tag coip anti tag western anti tag western blot anti tag western Li F., Huarte M., Zaratiegui M., Vaughn MW., Shi Y., Martienssen R., Cande WZ. Chromatin - Epigenetic interactions resulting in chromatin modulation Could not do CHIP assays as only vague regions of chromosomes identified as prey, not genes. Details of histone peptide supplied by author and from manufacturer's website. Peptide sequence has a 100% match to both S. pombe H3 proteins so both have been shown as binding to Lid3. feili@nature.berkeley.edu, zcande@berkeley.edu Accepted 2008-DEC-25 by DAVET. 16-Dec-2008: Contacted by JYOTI. Cell (0092-8674) 2008 davet Only protein-protein interactions 9 imex curation Lid2 is required for coordinating H3K4 and H3K9 methylation of heterochromatin and euchromatin. Lid2 is required for coordinating H3K4 and H3K9 methylation of heterochromatin and euchromatin. Cell (0092-8674) 2008 imex curation Li F., Huarte M., Zaratiegui M., Vaughn MW., Shi Y., Martienssen R., Cande WZ. Chromatin - Epigenetic interactions resulting in chromatin modulation Could not do CHIP assays as only vague regions of chromosomes identified as prey, not genes. Details of histone peptide supplied by author and from manufacturer's website. Peptide sequence has a 100% match to both S. pombe H3 proteins so both have been shown as binding to Lid3. feili@nature.berkeley.edu, zcande@berkeley.edu 16-Dec-2008: Contacted by JYOTI. davet Only protein-protein interactions 9 in vitro In vitro pull down pull down anti tag western anti tag western blot anti tag western Li F., Huarte M., Zaratiegui M., Vaughn MW., Shi Y., Martienssen R., Cande WZ. Chromatin - Epigenetic interactions resulting in chromatin modulation Could not do CHIP assays as only vague regions of chromosomes identified as prey, not genes. Details of histone peptide supplied by author and from manufacturer's website. Peptide sequence has a 100% match to both S. pombe H3 proteins so both have been shown as binding to Lid3. feili@nature.berkeley.edu, zcande@berkeley.edu Accepted 2008-DEC-25 by DAVET. 16-Dec-2008: Contacted by JYOTI. Cell (0092-8674) 2008 davet Only protein-protein interactions 9 imex curation set1_schpo Histone-lysine N-methyltransferase, H3 lysine-4 specific SPCC306.04c set1 kmt2 Set1 complex component set1 COMPASS component set1 SET domain-containing protein 1 Spset1 Lysine N-methyltransferase 2 protein protein schpo Schizosaccharomyces pombe (strain ATCC 38366 / 972) Fission yeast MDFNTSTRSKSQPVQRNNYKVLYDPELGIKENLGRKIIYRFNGVSKPPLVVRDPRLKNPIYARGIPKSGRPFLKSLQTINYDYNENSLGPEPPTQVFVSNISPLVTSEQLRYHFKSFGEVFDLDLKLNPYTGTSLGLCCISFDKRSSISVAAHSAKIAVQQANGLRFSGKPLSVVLDRDGSLCEEAFKKALNAVEKQFQEETLQKQRFEREDESSRQKLSAAMNEDIPPWRQPSKNSQTLSNGDLQHSKVQNVDQKSGFLTSSETDVPKNINDYIYLLIDDRFVPPDRVYYTDIKHHFRKFLYEKIYMNKDGFYITFNNYREASNCYRALDRTYVQNCRIKLKFHDIPSRTKEDGKKSAVRRVVLPPEEAYAEATSVVLRDLEAALLRDVKSKIIGPAIFKYLHSMPKPSVKEELQENLLVSSTSVPDVPLKIESTVGKLPSLPKFKKRVDSSKMNLSAGSKTKSKLQRRRRRRHEARPLHYQLNQMYNSSASEAESDQELLLSSGDERVERGKIGSIKSVKSDEATPVFSDTSDENDKFHRFRTKSKISKKKYEKMEVDYTSSSETESDASILSPSAAIPKSGSAIKDELISPKKEIDEVLALAPKWRINEFDETGSVYYGALPYNYPEDDVLLDLDGLQYLVKNDEDYSYLQEALKDEPLMDINDPNFWAYERKSCKFKNGDVKYGDTAILPEPKGYFRSNTSGSAKSEGYYIIPTTEKSLYLPLRNRSTIDTISHSTSRITSRMNRVNNRRLAAGVEKSQLPAEADLLRFNALKARKKQLHFGPSRIHTLGLFAMENIDKNDMVIEYIGEIIRQRVADNREKNYVREGIGDSYLFRIDEDVIVDATKKGNIARFINHSCAPNCIARIIRVEGKRKIVIYADRDIMHGEELTYDYKFPEEADKIPCLCGAPTCRGYLN C4AD7E6C3ECFF8BC h31_schpo Histone H3.1/H3.2 hht1 hht2 SPAC1834.04 SPBC8D2.04 pi060 protein protein schpo Schizosaccharomyces pombe (strain ATCC 38366 / 972) Fission yeast MARTKQTARKSTGGKAPRKQLASKAARKAAPATGGVKKPHRYRPGTVALREIRRYQKSTELLIRKLPFQRLVREIAQDFKTDLRFQSSAIGALQEAVEAYLVSLFEDTNLCAIHGKRVTIQPKDMQLARRLRGERS 346976EDD06C2284 fas2_schpo Fatty acid synthase subunit alpha fas2 lsd1 p190/210 SPAC4A8.11c protein protein schpo Schizosaccharomyces pombe (strain ATCC 38366 / 972) Fission yeast MRPEVEQELAHTLLLELLAYQFASPVRWIETQDVILSPPVSAERIVEIGPSPTLAGMAKRTLKLKYENMDAALSINREVLCYSKDAREIYYNFEDEVADEPAEAPASTSSTPKVETAAAAAPAATPAPAPAQTSAPAAALPDEPPKALEVLHTLVAQKLKKSIEEVSPQKSIKDLVGGKSTLQNEILGDLQKEFGATPEKPEEVPLDELGAIMQSSFNGSLGKQSSSLISRMISSKMPGGFNNSAVRGYLGNRYGLGPGRLESVLLLALTMEPASRLGSEADAKAWLDSVAQKYAARNGVTLSSPTAEGGSSSGSAAVIDEETFKKLTKNNTMLVTQQLELFARYLNKDLRAGQKAQVAEKVISDTLRAQLDLWNEEHGEFYASGIAPIFSPLKARVYDSDWNWARQDALKMFFDIIFGRLKHVDTEIVARCISVMNRSNPTLLEFMQYHIDHCPAEKGETYQLAKTLGQQLIDNCKSVIDAPPVFKNVNHPTAPSTTIDERGNLNYEEIPRPGVRKLTHYVTEMAKGGKLPTESKNKAKVQNDLARIYRIIKSQNKMSRSSKLQIKQLYGQVLHALSLPLPSSNDEQTPVKETIPFLHIRKKSVDGNWEFNKSLTGTYLDVLESGAKNGITYQDKYALVTGAGAGSIGAQIVEGLLAGGAKVVVTTSRFSRKVTEFYQSLYTRHGSRGSCLIVVPFNQGSKTDVEALIDYIYDEKKGLGWNLDYIVPFAAIPENGREIDGIDSRSEFAHRIMLTNILRLLGAVKSQKASRGMDTRPAQVILPLSPNHGTFGNDGLYSESKLGLETLFNRWYSESWANYLTICGAVIGWTRGTGLMAPNNIVSQGIEKYGVRTFSQSEMAFNILGLMSQKVVDLCQSEPIYANLNGGLELLPDLKDLSTRLRTELLETAEIRRAVAAETAFDHSITNGPDSEAVFQKTAIQPRANLKFNFPKLKPYEALSHLSDLRGMVDLEKVPVVTGFSEVGPWGNSRTRWDMECYGEFSLEGCVEIAWIMGLIKNFNGKGKDGKPYSGWVDTKTGEPVDDKDVKAKYEKYILEHCGIRIIEAELFHGYNPEKKELLQEVVIDHDLEPFEASKEAAHEFKLRHGDQVEIFEIPDSTEWSVRFKRGTSMLIPKALRFDRFVAGQIPLGWDPKRYGIPDDIISQVDPTTLYVLVSTVEALVASGITDPYECYKYIHVSELGNTVGSGIGGMSALRGMYKDRWTDKPVQKDILQESFINTANAWINMLLLSASGPIKTPVGACATAVESVDAAVDLITSGKARICISGGYDDFSEEGSYEFANMGATSNAAKETERGRTPQEMSRPATSTRDGFMESQGAGVQIIMQAKLAIEMGVPIHGIVGYVSTAMDKQGRSVPAPGQGILTGAREIATKTPLPIVDLKFRSRQLQRRRSQIGEWAEREYLYLEEELDAMKVQNPDLDLEAYRIERINVIKEEVVRQEKEALNTFGNEFWKRDPTIAPIRGALAVWGLTIDDLGVASFHGTSTKANEKNECDVIDSQLTHLGRSKGNAVYGVFQKYLTGHSKGGAGAWMLNGALQILRSGFVPGNRNADNIDEYLARFDRVMFPSEGIQTDGIKAASVTAFGFGQVGGQVIVIHPDYIYGVIDEATYNAYKAKTAARYKASYRYTHDALVYNNLVRAKDSPPYTKEQEKAVYLNPLARASKSKAGTWTFPATLPAESDISKTNETTRTLQSLTTSLTNSNENVGVDVELVSAISIDNETFIERNFTDTERKYCFAAPNPQASFAGRWSAKEAVFKSLGISGKGAAAPLKDIEIISSESGAPEVVLHGEAAKAATTAGVKSVSVSISHDDNQSVSVALAHK E4019F2D133EE571 raf1_schpo Rik1-associated factor 1 SPCC613.12c Cryptic loci regulator 8 De-localization of swi6 protein 1 raf1 clr8 cmc1 dos1 protein protein schpo Schizosaccharomyces pombe (strain ATCC 38366 / 972) Fission yeast MTNSSPRVKRRTDTQYLHSVSSKLPKVDFDTNNEEFFEEEFEIYDPFYRAELPCPKPSLSISKHSIAKVPSNVNKRLELQLLLTSGTFLPNSRPYLSERVRKHTHLLSNSITGDDKPSLIHVDFTPEECFILQEAKLKFGPVNSVQFNDAYSTHISPKLPGRAYEDCQKFEIDNPSLSPVDKHGAIILRTYKKNKKLLPDYLKSFYNAGSSYFQREQVHQLMDGESVFFLKPWKHFNETSGDTVCVAYNPLCEKFALGSTAQDGAYNRLGNLWIGDFHSETIQSLESHYKLNQVGEKEYSTISDLCFSKGNLFLYTGAFDNAVKVWDMEGNLCGIFNAPTDYIHKLALSDDDLLAVACKNGYGYLLSTDNSTGEILTSANLIYPEALEKGYSASLIEFSNFLGRSSDKVIIGYDSFHTSNNRGCLALFDASTASFVQKFNTADEAFTSLYMHPSQVGFVASSNTLSNGRVYYLDTRMYKVCLNFTTTQKDINHATISNSGILVTSSGTDNQTFVWDSRKPDKPLSLLKHGKTKMIHFDGANEEEVDAGINMAQWQPKGNLFVTGGSDGIVKVWDLRLNNPFIQNFTEMNSAITYGGFSEDASKLTVCCVGGDVNMYSLGNDNGNKFGEFRIIENRLLT 6CD360D8748AAF98 6CD360D8748AAF98 h33_schpo Histone H3.3 hht3 SPBC1105.11c protein protein schpo Schizosaccharomyces pombe (strain ATCC 38366 / 972) Fission yeast MARTKQTARKSTGGKAPRKQLASKAARKAAPATGGVKKPHRYRPPTVALREIRRYQKSTELLIRKLPFQRLVREIAQDFKTDLRFQSSAIGALQEAVEAYLVSLFEDTNLCAIHGKRVTIQPKDMQLARRLRGERS 2A9766FBB77A53E3 lid2_schpo Lid2 complex component lid2 lid2 SPBP19A11.06 SPBP4H10.01 protein protein schpo Schizosaccharomyces pombe (strain ATCC 38366 / 972) Fission yeast MICQLLWHEHNSMGSGREKKIRKLGDNFSLPYLKFDCDHNDKNYRASNRPFGLSTGLSVQLNASNMTDPFKFLLDNWHTIFKNGAIKLLPPEGWQIPVVLDQGAFEFQSKRQCLNKGCLNYEKNYDYFKKLKAFHESRGLYFYHPPIIGNRPVDFLRLRNAISKFTNSGSSLNNEILHKVIIYLRLEDTKEVRQVLTRCYDRYIKPFERDSSPSFKSKRSESSTRKIRNTRSSAQQESPIPETSAQSPVQTIQVNGSTSLKRPLIERGEQCEYCGLDKNPETILLCDGCEAAYHTSCLDPPLTSIPKEDWYCDACKFNISDYDPRKGFKWKLSSLKERSAEIFNTLGERNSSSKLTNLTEDDIELFYWSSLAESNSGFAPLELEGLSQAYTSTIQSSLPSKEVFPLEKYSSEPWNLHNLPFENPCLFNYSFSDLSSLTITRLSIGMVFYTHGWTKSSLSTGLLHHHRFGDTVTWYVLPPDESDAFERYLISSYPQYTMEDLNRSNGLPVIVSPSSLIENGFHPIAIDLRPNEFLVVSPNSYHMGFHQGFSSFESVNFATVNWIKDGLLNSSISVLKSMRIPSSVSYEAVIISMVLSKNPCFSSEWLIKCFEDMIANESASKNEIMKLVPNIQALKLESSVPLEIRCSNCKQPCFLSFMQCHEPKKFICLGDCVKEVSLNATSWMLFYRWDVHELSNLAERFVSLIRGPEEWTNRLRSVLSTSPKPQLKVLKSLLVDAEKAMLTTPETVNLRDFVQNANSWIDSVNECLKVASLKRKKDKKPPLFKAHDHWNNTSNLKDSAVLFKVLQTSRSMAFTCQEIENMKQKAFDLLEFRNRLINSFSGPLDKNTCQRLLTEAELLGFTIPELGIIQKYLIQFEWLDMFYSFETTRTTDSDLERLITYGVSAGIPEDNDYMIFAKAMKGRAEIWENQVYDTLSKSNISYDKLSLLRDEAMNLCVNKELFSKVVGILNNAEEIKNKIATLCERSQEKDFALRPSIDEVKEALASAEKLPILSESTVTLQKMYDVVLEWIRRGKRLFGKANAPLEILGQHLDYVEKRNSASLSLNDRPGPPMEPASRETSPDSEGRLTIRKKKGCIFCFCRLPESGVMIECEICHEWYHAKCLKMSKKKLRQDEKFTCPICDYRVEIPRLSNRPKLEDLQSLYKDVKLLPFQPKETETLRKVVDLASKFRQEMQALAHNPFGLTMAEVPLARFYLRKMEGAEILLVDETNLFRQKLHECVPIAPNPPPIIGESKSTRKPRPTKRQRQIMKQVAEGLLPASAIAPPKSSNEKKSSNNVKAVEAETKSKSEKSPKKNGTNISDANNKNESHVSLMKNWKLGSPAFVTLVKEKNSSCLCGEEFSPRDSFIDCTICERRFHYDCVGLNNEIADSVSKFTCPICMEQSGGIYPWQLRPRNGMHPDHISGFSKEVETDPKLGSSGYTLNNSKFDKAAVSKTLSAQDVSRLQKVSCGEHLYFGTDVFTPLGDMATSASMFSLDDSSEKTDAFTENFLNV B8787624F9E7DFAD cul4_schpo Cullin-4 pcu4 cul4 SPAC3A11.08 protein protein schpo Schizosaccharomyces pombe (strain ATCC 38366 / 972) Fission yeast MPPEAKRIVVKGFDPRKSRQRQETYYVTMIDRLNMALQVVMAGLGLKTGYQELYSGVENLTRADQASRCFNILQHHMSSGIQLLKDSAESFIQLEGTETDTNACTVVVGCWNKWLERVEIVQNIFYYMDKTFLSHHPDYPTIEELSLSLFREKLMAVKNIQIPFLNSLLQSFENLHSSKSTDHAYLQDAMLMLHRTEMYSSVFVPMYLVMLSRFYDTESSQKIQELPLEEYLEYAMSSLEREDAYVEKFDIVRDKKSIRETVQRCLITSHLDTLTKGISQFIEKRDAHSCKLLYALLQFNHETEYLIQPWSDCLVDVGFKLVNDESKDDTLVQELLSFHKFLQVVVDESFLHDETLSYAMRKAFETFINGAKGSQREAPARLIAKYIDYLLRVGEQASGGKPLKEVFSEILDLFRYIASKDIFEAYYKLDIAKRLLLNKSASAQNELMLLDMLKKTCGSQFTHSLEGMFRDVNISKEFTSSFRHSKAAHNLHRDLYVNVLSQAYWPSYPESHIRLPDDMQQDLDCFEKFYLSKQVGKKISWYASLGHCIVKARFPLGNKELSISLFQACVLLQFNNCLGGEGISYQDLKKSTELSDIDLTRTLQSLSCARIRPLVMVPKSKKPSPDTMFYVNEKFTDKLYRVKINQIYLKEERQENSDVQEQVVRDRQFELQASIVRVMKQKEKMKHDDLVQYVINNVKDRGIPLVSDVKTAIEKLLEKEYLEREDNDIYTYVT E90FFFE06D071C3E rik1_schpo Chromatin modification-related protein rik1 rik1 SPCC11E10.08 Silencing protein rik1 protein protein schpo Schizosaccharomyces pombe (strain ATCC 38366 / 972) Fission yeast MALCVHSFWATAVDTATSCHFISSENCLVLLQALKINIYLCSEVHGLQFFTSIPLFSTVKHIRPYRPPGLDRDYLFVVLNDDTYFSIYWDEDYQKVIVDHPPVRYRVTFPWNRNAKSYCLVDLRMRAIFLSIDEISMICIRILSAEERLKTGRSIDSGFPFSFPVHLIYDMCILNDSSTPTLVVLHSDGLDCYVTAFLLDLSSKSLGKGIRLFERVKPSMIMPFGKRGLLVFESLFIHCMYRGNFVTINGPCTTYMHWTPLKGQKMHYIVCDTNGYLFGVYSSILGKNKWSLVMERLPIPPFDFITSLNSIHEGLLFIGSKNSESKLINLSTLKDVDSIPNLGPIHDLLVLKNDIEKSFLVCAGTPRNASLIYFQHALKLDILGQTKISGILRAMVLPSYPEHKLFLGFPSETVAFNIKEDFQLELDPSLSTKERTIALSGTNGEFVQVTSTFLCIYDSAKRSRLVYIEKITNAACYQEYSAIVINGTALAIFKKDTEVARKVFESEISCLDFSAQFQIGVGFWSKQVMILTFSDNSSISCAFQTNVPSLPRNIILEGVGVDRNLLLVSSGSGEFKSYVLFKNNLVFSETKHFGTTPVSFRRFTMNIGTYIICNNDCPHMVYGFNGALCYMPLSMPQSYDVCQFRDNSGKDFLISVSLGGLKFLQLNPLPELTPRKVLLEHVPLQAIIFQNKLLLRTLENRYEDYESYKENYHLELVDSYDDNSFRVFSFTENERCEKVLKINESSLLVGTSIIEQDKLVPVNGRLILLEFEKELQSLKVVSSMVLSAAVIDLGVYNDRYIVAFGQQVAIVKLTEERLMIDSRISLGSIVLQLIVEGNEIAIADSIGRFTIMYFDGQKFIVVARYLFGENIVKAALYEGTVYIIATNSGLLKLLRYNKDAKNFNDRFICESVYHLHDKVSKFQNFPITNTNSFLEPKMLFATEIGAIGSIVSLKDKELELEELTRKIRKLKFSYLSSMDYESIEADLISPVPFIDGDLVIDVKRWASSELFRLCRSVEHRESLNSYQKVQALLEEIQSLC 0C76BB59E1215BF1 0C76BB59E1215BF1 raf1-5 1 9 unspecified role unspecified role prey prey 7 unspecified role unspecified role bait bait n-terminal tap tagged calmodulin binding peptide plus protein a tag CBP-ProtA tagged CBP-ProtA tagged tap tagged n-term range n-terminal range n-term range n-term range n-terminal range n-term range 10 unspecified role unspecified role prey prey association association Fig. 1C Mass spectrometry analysis revealed that the purified fraction included Clr8 and Cul4, consistent with previous findings ([Hong et al., 2005] and [Thon et al., 2005]), as well as a 170 kDa JmjC-domain protein, Lid2 (Figure 1B). raf1-lid2-1 2 7 unspecified role unspecified role bait bait region myc tag myc tag EUKLISEED epitope tag EUKLISEED epitope tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined 9 unspecified role unspecified role prey prey c-terminal tap tagged calmodulin binding peptide plus protein a tag CBP-ProtA tagged CBP-ProtA tagged tap tagged c-term range C-terminal range c-term range c-term range C-terminal range c-term range physical association physical association Fig. 1D Coimmunoprecipitation (Co-IP) showed that Myc-Clr8 coprecipitated with Lid2 (Figure 1D). rik1-lid2-1 2 11 unspecified role unspecified role bait bait region myc tag myc tag EUKLISEED epitope tag EUKLISEED epitope tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined 9 unspecified role unspecified role prey prey c-terminal tap tagged calmodulin binding peptide plus protein a tag CBP-ProtA tagged CBP-ProtA tagged tap tagged c-term range C-terminal range c-term range c-term range C-terminal range c-term range physical association physical association Supp. Fig. 1 Lid2 interacts with Rik1 as shown by a Co-IP lsd1-lid2-1 2 9 unspecified role unspecified role prey prey c-terminal tap tagged calmodulin binding peptide plus protein a tag CBP-ProtA tagged CBP-ProtA tagged tap tagged c-term range C-terminal range c-term range c-term range C-terminal range c-term range 6 unspecified role unspecified role bait bait region myc tag myc tag EUKLISEED epitope tag EUKLISEED epitope tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined physical association physical association Fig. 6E Lid2-TAP and Lsd1-Myc coprecipitated (Figure 6E), set1-lid2-1 2 9 unspecified role unspecified role prey prey c-terminal tap tagged calmodulin binding peptide plus protein a tag CBP-ProtA tagged CBP-ProtA tagged tap tagged c-term range C-terminal range c-term range c-term range C-terminal range c-term range jmjc region required to bind necessary binding region required to bind deletion analysis deletion analysis range range range range 4 unspecified role unspecified role bait bait region myc tag myc tag EUKLISEED epitope tag EUKLISEED epitope tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined physical association physical association Fig. 6G Lid2-TAP and Lsd1-Myc coprecipitated (Figure 6E), The boundaries of the JmjC domain are not given in the paper so these have been inferred from the UniProt record cul4-lid2-1 2 9 unspecified role unspecified role bait bait c-terminal tap tagged calmodulin binding peptide plus protein a tag CBP-ProtA tagged CBP-ProtA tagged tap tagged c-term range C-terminal range c-term range c-term range C-terminal range c-term range 10 unspecified role unspecified role prey prey region myc tag myc tag EUKLISEED epitope tag EUKLISEED epitope tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined physical association physical association Supp. Fig. 6 Co-IP showed that point mutation at the iron-binding site (H512A) of Lid2 did not disrupt its interaction with Set1 (upper panel) or Cul4 (lower panel). set1-lid2-2 2 4 unspecified role unspecified role prey prey region myc tag myc tag EUKLISEED epitope tag EUKLISEED epitope tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined 9 unspecified role unspecified role bait bait c-terminal tap tagged calmodulin binding peptide plus protein a tag CBP-ProtA tagged CBP-ProtA tagged tap tagged c-term range C-terminal range c-term range c-term range C-terminal range c-term range physical association physical association Supp. Fig. 6 Co-IP showed that point mutation at the iron-binding site (H512A) of Lid2 did not disrupt its interaction with Set1 (upper panel) or Cul4 (lower panel). hht3-lid3-1 3 8 unspecified role unspecified role bait bait region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain lys-10 xlnk-n6lys-1gly N6-glycyl-L-lysine (2S)-2-amino-6-[(aminoacetyl)amino]hexanoic acid N6-(glycyl)-L-lysine N6-glycyllysine XLNK-N6Lys-1Gly CROSSLNK Glycyl lysine isopeptide (Gly-Lys) (interchain with K-...) CROSSLNK Glycyl lysine isopeptide (Lys-Gly) (interchain with G-...) certain certain sequence position certain certain certain sequence position certain c-terminal biotin tag biotin tag c-term range C-terminal range c-term range c-term range C-terminal range c-term range chemical synthesis Chemical synthesis (Chemical synthesis) 9 unspecified role unspecified role prey prey phd2 region sufficient to bind sufficient binding region sufficient to bind deletion analysis deletion analysis range range range range direct interaction direct interaction Histone numbering does not take account of the N-terminal cleaved methionine Coordinates of the PHD2 domain are not supplied in the paper and have been inferred from the UniProtKB entry. The PHD2 domain preferentially binds to H3K9me3, indicated by the peptide pull-down assay. Fig. 7D hht3-lid3-2 3 9 unspecified role unspecified role prey prey phd2 region sufficient to bind sufficient binding region sufficient to bind deletion analysis deletion analysis range range range range 5 unspecified role unspecified role bait bait c-terminal biotin tag biotin tag c-term range C-terminal range c-term range c-term range C-terminal range c-term range lys-10 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 region sufficient to bind sufficient binding region sufficient to bind deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain chemical synthesis Chemical synthesis (Chemical synthesis) direct interaction direct interaction Histone numbering does not take account of the N-terminal cleaved methionine Coordinates of the PHD2 domain are not supplied in the paper and have been inferred from the UniProtKB entry. The PHD2 domain preferentially binds to H3K9me3, indicated by the peptide pull-down assay. Fig. 7D