SET1_DROME
ID SET1_DROME Reviewed; 1641 AA.
AC Q5LJZ2; M9WDY6; Q4V706; Q8SXR9;
DT 11-JUN-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Histone-lysine N-methyltransferase SETD1 {ECO:0000250|UniProtKB:Q9UPS6};
DE EC=2.1.1.354 {ECO:0000250|UniProtKB:Q9UPS6};
GN Name=Set1 {ECO:0000312|EMBL:EAL24598.1, ECO:0000312|FlyBase:FBgn0040022};
GN ORFNames=CG40351;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1] {ECO:0000312|EMBL:EAL24598.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2] {ECO:0000312|EMBL:EAL24598.1}
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [3] {ECO:0000312|EMBL:AAY51545.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RA Stapleton M., Booth B., Brokstein P., Hong L., Agbayani A., Carlson J.,
RA Champe M., Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E.,
RA George R., Gonzalez M., Guarin H., Kronmiller B., Li P., Liao G.,
RA Miranda A., Mungall C.J., Nunoo J., Pacleb J., Paragas V., Park S.,
RA Patel S., Phouanenavong S., Wan K., Yu C., Lewis S.E., Rubin G.M.,
RA Celniker S.;
RL Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000305}
RP FUNCTION, IDENTIFICATION IN THE SET1 COMPLEX, AND SUBCELLULAR LOCATION.
RX PubMed=21694722; DOI=10.1038/emboj.2011.194;
RA Ardehali M.B., Mei A., Zobeck K.L., Caron M., Lis J.T., Kusch T.;
RT "Drosophila Set1 is the major histone H3 lysine 4 trimethyltransferase with
RT role in transcription.";
RL EMBO J. 30:2817-2828(2011).
RN [5] {ECO:0000305}
RP FUNCTION, IDENTIFICATION IN THE SET1 COMPLEX, AND SUBCELLULAR LOCATION.
RX PubMed=21875999; DOI=10.1128/mcb.06092-11;
RA Mohan M., Herz H.M., Smith E.R., Zhang Y., Jackson J., Washburn M.P.,
RA Florens L., Eissenberg J.C., Shilatifard A.;
RT "The COMPASS family of H3K4 methylases in Drosophila.";
RL Mol. Cell. Biol. 31:4310-4318(2011).
RN [6] {ECO:0000305}
RP FUNCTION, INTERACTION WITH ASH2 AND WDS, AND MUTAGENESIS OF GLU-1613.
RX PubMed=22048023; DOI=10.1534/genetics.111.135863;
RA Hallson G., Hollebakken R.E., Li T., Syrzycka M., Kim I., Cotsworth S.,
RA Fitzpatrick K.A., Sinclair D.A., Honda B.M.;
RT "dSet1 is the main H3K4 di- and tri-methyltransferase throughout Drosophila
RT development.";
RL Genetics 190:91-100(2012).
CC -!- FUNCTION: Catalytic component of the SET1 complex that specifically
CC di- and trimethylates 'Lys-4' of histone H3 and is the main di- and
CC trimethyltransferase throughout development. Set1-dependent
CC trimethylation regulates chromatin changes at active promoters that
CC ensure optimal RNA polymerase II release into productive elongation,
CC thereby contributing to optimal transcription.
CC {ECO:0000269|PubMed:21694722, ECO:0000269|PubMed:21875999,
CC ECO:0000269|PubMed:22048023}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-lysyl(4)-[histone H3] + 3 S-adenosyl-L-methionine = 3 H(+) +
CC N(6),N(6),N(6)-trimethyl-L-lysyl(4)-[histone H3] + 3 S-adenosyl-L-
CC homocysteine; Xref=Rhea:RHEA:60260, Rhea:RHEA-COMP:15537, Rhea:RHEA-
CC COMP:15547, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:61961; EC=2.1.1.354;
CC Evidence={ECO:0000250|UniProtKB:Q9UPS6};
CC -!- SUBUNIT: Component of the SET1 complex, composed at least of the
CC catalytic subunit Set1, wds/WDR5, Wdr82, Rbbp5, ash2, Cfp1/CXXC1, hcf
CC and Dpy-30L1. Interacts with ash2 and wds.
CC {ECO:0000269|PubMed:21694722, ECO:0000269|PubMed:21875999,
CC ECO:0000269|PubMed:22048023}.
CC -!- INTERACTION:
CC Q5LJZ2; Q9V4C8: Hcf; NbExp=3; IntAct=EBI-3405171, EBI-2912878;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21694722,
CC ECO:0000269|PubMed:21875999}. Chromosome {ECO:0000269|PubMed:21694722,
CC ECO:0000269|PubMed:21875999}. Note=Colocalizes with di- and
CC trimethylated H3 'Lys-4' and with phosphorylated RNA polymerase II at
CC transcriptional puffs on polytene chromosomes.
CC {ECO:0000269|PubMed:21694722, ECO:0000269|PubMed:21875999}.
CC -!- SIMILARITY: Belongs to the class V-like SAM-binding methyltransferase
CC superfamily. {ECO:0000255|PROSITE-ProRule:PRU00190}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL89913.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAL89913.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=AAY51545.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
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DR EMBL; AE014296; EAL24598.1; -; Genomic_DNA.
DR EMBL; AE014296; EAL24599.1; -; Genomic_DNA.
DR EMBL; AE014296; EDP28071.1; -; Genomic_DNA.
DR EMBL; AE014296; EFA98694.1; -; Genomic_DNA.
DR EMBL; AE014296; EFA98695.1; -; Genomic_DNA.
DR EMBL; AE014296; EFA98696.1; -; Genomic_DNA.
DR EMBL; AE014296; EFA98697.1; -; Genomic_DNA.
DR EMBL; AE014296; EFA98698.1; -; Genomic_DNA.
DR EMBL; AE014296; EFA98699.1; -; Genomic_DNA.
DR EMBL; AY084175; AAL89913.1; ALT_SEQ; mRNA.
DR EMBL; BT022150; AAY51545.1; ALT_SEQ; mRNA.
DR EMBL; BT150052; AGJ89714.1; -; mRNA.
DR RefSeq; NP_001015221.1; NM_001015221.3.
DR RefSeq; NP_001015222.1; NM_001015222.3.
DR RefSeq; NP_001104406.1; NM_001110936.3.
DR RefSeq; NP_001163846.1; NM_001170375.2.
DR RefSeq; NP_001163847.1; NM_001170376.2.
DR RefSeq; NP_001163848.1; NM_001170377.1.
DR RefSeq; NP_001163849.1; NM_001170378.1.
DR RefSeq; NP_001163850.1; NM_001170379.1.
DR RefSeq; NP_001163851.1; NM_001170380.2.
DR AlphaFoldDB; Q5LJZ2; -.
DR SMR; Q5LJZ2; -.
DR BioGRID; 78096; 6.
DR IntAct; Q5LJZ2; 27.
DR MINT; Q5LJZ2; -.
DR STRING; 7227.FBpp0291454; -.
DR PaxDb; Q5LJZ2; -.
DR PRIDE; Q5LJZ2; -.
DR EnsemblMetazoa; FBtr0113869; FBpp0112592; FBgn0040022.
DR EnsemblMetazoa; FBtr0113870; FBpp0112593; FBgn0040022.
DR EnsemblMetazoa; FBtr0113871; FBpp0112594; FBgn0040022.
DR EnsemblMetazoa; FBtr0302243; FBpp0291452; FBgn0040022.
DR EnsemblMetazoa; FBtr0302244; FBpp0291453; FBgn0040022.
DR EnsemblMetazoa; FBtr0302245; FBpp0291454; FBgn0040022.
DR EnsemblMetazoa; FBtr0302246; FBpp0291455; FBgn0040022.
DR EnsemblMetazoa; FBtr0302247; FBpp0291456; FBgn0040022.
DR EnsemblMetazoa; FBtr0302248; FBpp0291457; FBgn0040022.
DR GeneID; 3354971; -.
DR KEGG; dme:Dmel_CG40351; -.
DR UCSC; CG40351-RA; d. melanogaster.
DR CTD; 3354971; -.
DR FlyBase; FBgn0040022; Set1.
DR VEuPathDB; VectorBase:FBgn0040022; -.
DR eggNOG; KOG1080; Eukaryota.
DR GeneTree; ENSGT00940000169211; -.
DR HOGENOM; CLU_001226_3_0_1; -.
DR InParanoid; Q5LJZ2; -.
DR OMA; RMIEMTA; -.
DR OrthoDB; 1234689at2759; -.
DR PhylomeDB; Q5LJZ2; -.
DR Reactome; R-DME-8936459; RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function.
DR BioGRID-ORCS; 3354971; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 3354971; -.
DR PRO; PR:Q5LJZ2; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0040022; Expressed in saliva-secreting gland and 24 other tissues.
DR Genevisible; Q5LJZ2; DM.
DR GO; GO:0000791; C:euchromatin; IDA:FlyBase.
DR GO; GO:0005700; C:polytene chromosome; IDA:FlyBase.
DR GO; GO:0048188; C:Set1C/COMPASS complex; IDA:FlyBase.
DR GO; GO:0042800; F:histone methyltransferase activity (H3-K4 specific); IDA:FlyBase.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0044648; P:histone H3-K4 dimethylation; IDA:FlyBase.
DR GO; GO:0051568; P:histone H3-K4 methylation; IMP:FlyBase.
DR GO; GO:0080182; P:histone H3-K4 trimethylation; IDA:FlyBase.
DR Gene3D; 2.170.270.10; -; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR024657; COMPASS_Set1_N-SET.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR003616; Post-SET_dom.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR044570; Set1-like.
DR InterPro; IPR001214; SET_dom.
DR InterPro; IPR046341; SET_dom_sf.
DR PANTHER; PTHR45814; PTHR45814; 1.
DR Pfam; PF11764; N-SET; 1.
DR Pfam; PF00076; RRM_1; 1.
DR Pfam; PF00856; SET; 1.
DR SMART; SM01291; N-SET; 1.
DR SMART; SM00508; PostSET; 1.
DR SMART; SM00360; RRM; 1.
DR SMART; SM00317; SET; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR SUPFAM; SSF82199; SSF82199; 1.
DR PROSITE; PS50868; POST_SET; 1.
DR PROSITE; PS50102; RRM; 1.
DR PROSITE; PS50280; SET; 1.
PE 1: Evidence at protein level;
KW Activator; Chromatin regulator; Chromosome; Coiled coil; Methyltransferase;
KW Nucleus; Reference proteome; RNA-binding; S-adenosyl-L-methionine;
KW Transcription; Transcription regulation; Transferase.
FT CHAIN 1..1641
FT /note="Histone-lysine N-methyltransferase SETD1"
FT /id="PRO_0000429378"
FT DOMAIN 101..179
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 1502..1619
FT /note="SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT DOMAIN 1625..1641
FT /note="Post-SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00155"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 236..384
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 537..596
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 831..915
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 930..949
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1119..1155
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1205..1226
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1091..1132
FT /evidence="ECO:0000255"
FT COMPBIAS 244..292
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 300..384
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 566..580
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 840..873
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 887..915
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1129..1144
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 1613
FT /note="E->K: In G5; predominantly lethal at the pupal stage
FT with low levels of late L3 larval lethality."
FT /evidence="ECO:0000269|PubMed:22048023"
SQ SEQUENCE 1641 AA; 188383 MW; 89877A04B630D954 CRC64;
MQDVRNINLV NNSSNSHDSS LANSKMPRNF KLLSDPQLVK CGTRLYRYDG LMPGDPSYPT
ITPRDPRNPL IRIRARAVEP LMLLIPRFVI DSDYVGQPPA VEVTIVNLND NIDKQFLASM
LDKCGTSDEI NIYHHPITNK HLGIARIVFD STKGARQFVE KYNQKSVMGK ILDVFCDPFG
ATLKKSLESL TNSVAGKQLI GPKVTPQWTF QQAALEDTEF IHGYPEKNGE HIKDIYTTQT
NHEIPNRSRD RNWNRDKERE RDRHFKERSR HSSERSYDRD RGMRENVGTS IRRRRTFYRR
RSSDISPEDS RDILIMTRER SRDSDSRPRD YCRSRERESF RDRKRSHEKG RDQPREKREH
YYNSSKDREY RGRDRDRSAE IDQRDRGSLK YCSRYSLHEY IETDVRRSSN TISSYYSASS
LPIASHGFNS CSFPSIENIK TWSDRRAWTA FQPDFHPVQP PPPPPEEIDN WDEEEHDKNS
IVPTHYGCMA KLQPPVPSNV NFATKLQSVT QPNSDPGTVD LDTRIALIFK GKTFGNAPPF
LQMDSSDSET DQGKPEVFSD VNSDSNNSEN KKRSCEKNNK VLHQPNEASD ISSDEELIGK
KDKSKLSLIC EKEVNDDNMS LSSLSSQEDP IQTKEGAEYK SIMSSYMYSH SNQNPFYYHA
SGYGHYLSGI PSESASRLFS NGAYVHSEYL KAVASFNFDS FSKPYDYNKG ALSDQNDGIR
QKVKQVIGYI VEELKQILKR DVNKRMIEIT AFKHFETWWD EHTSKARSKP LFEKADSTVN
TPLNCIKDTS YNEKNPDINL LINAHREVAD FQSYSSIGLR AAMPKLPSFR RIRKHPSPIP
TKRNFLERDL SDQEEMVQRS DSDKEDSNVE ISDTARSKIK GPVPIQESDS KSHTSGLNSK
RKGSASSFFS SSSSSTSSEA EYEAIDCVEK ARTSEEDSPR GYGQRNLNQR TTTIRNRNLV
GTMDVINVRN LCSGSNEFKK ENVTKRTKKN IYSDTDEDND RTLFPALKEK NISTILSDLE
EISKDSCIGL DENGIEPTIL RKIPNTPKLN EECRRSLTPV PPPGYNEEEI KKKVDCKQKP
SFEYDRIYSD SEEEKEYQER RKRNTEYMAQ MEREFLEEQE KRIEKSLDKN LQSPNNIVKN
NNSPRNKNDE TRKTAISQTR SCFESASKVD TTLVNIISVE NDINEFGPHE EGDVLTNGCN
KMYTNSKGKT KRTQSPVYSE GGSSQASQAS QVALEHCYSL PPHSVSLGDY PSGKVNETKN
ILKREAENIA IVSQMTRTGP GRPRKDPICI QKKKRDLAPR MSNVKSKMTP NGDEWPDLAH
KNVHFVPCDM YKTRDQNEEM VILYTFLTKG IDAEDINFIK MSYLDHLHKE PYAMFLNNTH
WVDHCTTDRA FWPPPSKKRR KDDELIRHKT GCARTEGFYK LDVREKAKHK YHYAKANTED
SFNEDRSDEP TALTNHHHNK LISKMQGISR EARSNQRRLL TAFGSMGESE LLKFNQLKFR
KKQLKFAKSA IHDWGLFAME PIAADEMVIE YVGQMIRPVV ADLRETKYEA IGIGSSYLFR
IDMETIIDAT KCGNLARFIN HSCNPNCYAK VITIESEKKI VIYSKQPIGI NEEITYDYKF
PLEDEKIPCL CGAQGCRGTL N
