GenomeNet

Database: UniProt
Entry: Q5LJZ2
LinkDB: Q5LJZ2
Original site: Q5LJZ2 
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   16-JAN-2019, entry version 132.
DE   RecName: Full=Histone-lysine N-methyltransferase SETD1 {ECO:0000250|UniProtKB:Q9UPS6};
DE            EC=2.1.1.43 {ECO:0000250|UniProtKB:Q9UPS6};
GN   Name=Set1 {ECO:0000312|EMBL:EAL24598.1,
GN   ECO:0000312|FlyBase:FBgn0040022}; ORFNames=CG40351;
OS   Drosophila melanogaster (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
OC   Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
OC   Ephydroidea; 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.,
RA   Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D.,
RA   Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G.,
RA   Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D.,
RA   Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
RA   Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
RA   Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
RA   Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
RA   Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
RA   de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
RA   Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
RA   Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
RA   Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
RA   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.,
RA   Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C.,
RA   Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
RA   Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z.,
RA   Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X.,
RA   Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
RA   Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
RA   Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
RA   Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
RA   Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
RA   Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H.,
RA   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.,
RA   Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
RA   Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
RA   Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A.,
RA   Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
RA   Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X.,
RA   Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., 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.,
RA   Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
RA   Lewis S.E.;
RT   "Annotation of the Drosophila melanogaster euchromatic genome: a
RT   systematic 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.,
RA   Carlson J., Champe M., Chavez C., Dorsett V., Dresnek D., Farfan D.,
RA   Frise E., George R., Gonzalez M., Guarin H., Kronmiller B., Li P.,
RA   Liao G., Miranda A., Mungall C.J., Nunoo J., Pacleb J., Paragas V.,
RA   Park S., Patel S., Phouanenavong S., Wan K., Yu C., Lewis S.E.,
RA   Rubin G.M., 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
RP   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
RT   with role in transcription.";
RL   EMBO J. 30:2817-2828(2011).
RN   [5] {ECO:0000305}
RP   FUNCTION, IDENTIFICATION IN THE SET1 COMPLEX, AND SUBCELLULAR
RP   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.,
RA   Cotsworth S., Fitzpatrick K.A., Sinclair D.A., Honda B.M.;
RT   "dSet1 is the main H3K4 di- and tri-methyltransferase throughout
RT   Drosophila development.";
RL   Genetics 190:91-100(2012).
CC   -!- FUNCTION: Catalytic component of the SET1 complex that
CC       specifically di- and trimethylates 'Lys-4' of histone H3 and is
CC       the main di- and trimethyltransferase throughout development.
CC       Set1-dependent trimethylation regulates chromatin changes at
CC       active promoters that ensure optimal RNA polymerase II release
CC       into productive elongation, thereby contributing to optimal
CC       transcription. {ECO:0000269|PubMed:21694722,
CC       ECO:0000269|PubMed:21875999, ECO:0000269|PubMed:22048023}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-lysyl-[histone] + S-adenosyl-L-methionine = H(+) +
CC         N(6)-methyl-L-lysyl-[histone] + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:10024, Rhea:RHEA-COMP:9845, Rhea:RHEA-COMP:9846,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC         ChEBI:CHEBI:59789, ChEBI:CHEBI:61929; EC=2.1.1.43;
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,
CC       hcf 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       Q9V4C8:Hcf; NbExp=3; IntAct=EBI-3405171, EBI-2912878;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21694722,
CC       ECO:0000269|PubMed:21875999}. Chromosome
CC       {ECO:0000269|PubMed:21694722, ECO:0000269|PubMed:21875999}.
CC       Note=Colocalizes with di- and trimethylated H3 'Lys-4' and with
CC       phosphorylated RNA polymerase II at transcriptional puffs on
CC       polytene chromosomes. {ECO:0000269|PubMed:21694722,
CC       ECO:0000269|PubMed:21875999}.
CC   -!- SIMILARITY: Belongs to the class V-like SAM-binding
CC       methyltransferase superfamily. {ECO:0000255|PROSITE-
CC       ProRule:PRU00190}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAL89913.1; Type=Frameshift; Positions=661; 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};
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   UniGene; Dm.5195; -.
DR   ProteinModelPortal; 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   eggNOG; KOG1080; Eukaryota.
DR   eggNOG; COG2940; LUCA.
DR   GeneTree; ENSGT00940000169211; -.
DR   InParanoid; Q5LJZ2; -.
DR   KO; K11422; -.
DR   OMA; DAEDINF; -.
DR   OrthoDB; 1234689at2759; -.
DR   PhylomeDB; Q5LJZ2; -.
DR   GenomeRNAi; 3354971; -.
DR   PRO; PR:Q5LJZ2; -.
DR   Proteomes; UP000000803; Chromosome 3L.
DR   Bgee; FBgn0040022; Expressed in 4 organ(s), highest expression level in head.
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:0035327; C:transcriptionally active chromatin; 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: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; 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; IPR001214; SET_dom.
DR   InterPro; IPR037861; SETD1-like.
DR   PANTHER; PTHR22884:SF464; PTHR22884:SF464; 3.
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   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;
KW   Complete proteome; Methyltransferase; Nucleus; Reference proteome;
KW   RNA-binding; S-adenosyl-L-methionine; Transcription;
KW   Transcription regulation; Transferase.
FT   CHAIN         1   1641       Histone-lysine N-methyltransferase SETD1.
FT                                /FTId=PRO_0000429378.
FT   DOMAIN      101    179       RRM. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00176}.
FT   DOMAIN     1502   1619       SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00190}.
FT   DOMAIN     1625   1641       Post-SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00155}.
FT   COILED     1091   1132       {ECO:0000255}.
FT   COMPBIAS    247    386       Arg-rich. {ECO:0000255}.
FT   COMPBIAS    460    465       Poly-Pro. {ECO:0000255}.
FT   COMPBIAS    888    918       Ser-rich. {ECO:0000255}.
FT   MUTAGEN    1613   1613       E->K: In G5; predominantly lethal at the
FT                                pupal stage with low levels of late L3
FT                                larval lethality.
FT                                {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
//
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