GenomeNet

Database: UniProt/SWISS-PROT
Entry: DOT1L_DROME
LinkDB: DOT1L_DROME
Original site: DOT1L_DROME 
ID   DOT1L_DROME             Reviewed;        1848 AA.
AC   Q8INR6; A4V2H8; Q1RKY0; Q9VI22;
DT   21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 2.
DT   23-MAY-2018, entry version 131.
DE   RecName: Full=Histone-lysine N-methyltransferase, H3 lysine-79 specific;
DE            EC=2.1.1.43;
DE   AltName: Full=DOT1-like protein;
DE            Short=dDOT1L;
DE   AltName: Full=Histone H3-K79 methyltransferase;
DE            Short=H3-K79-HMTase;
DE   AltName: Full=Protein grappa;
GN   Name=gpp; ORFNames=CG10272;
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]
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]
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]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM C).
RC   STRAIN=Berkeley;
RA   Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A.,
RA   Pacleb J.M., Park S., Wan K.H., Yu C., Celniker S.E.;
RL   Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   FUNCTION, SUBCELLULAR LOCATION, CATALYTIC ACTIVITY, AND DEVELOPMENTAL
RP   STAGE.
RX   PubMed=15371351; DOI=10.1534/genetics.104.033191;
RA   Shanower G.A., Mueller M., Blanton J.L., Honti V., Gyurkovics H.,
RA   Schedl P.;
RT   "Characterization of the grappa gene, the Drosophila histone H3 lysine
RT   79 methyltransferase.";
RL   Genetics 169:173-184(2005).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-491; SER-492; SER-494;
RP   SER-1318; SER-1324 AND SER-1325, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryo;
RX   PubMed=18327897; DOI=10.1021/pr700696a;
RA   Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT   "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL   J. Proteome Res. 7:1675-1682(2008).
CC   -!- FUNCTION: Histone methyltransferase. Methylates 'Lys-79' of
CC       histone H3. Required for Polycomb Group (PcG) and trithorax Group
CC       (trxG) maintenance of expression. Also involved in telomeric
CC       silencing but do not in centric heterochromatin. Probably
CC       participates in pairing sensitivity.
CC       {ECO:0000269|PubMed:15371351}.
CC   -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + L-lysine-[histone] =
CC       S-adenosyl-L-homocysteine + N(6)-methyl-L-lysine-[histone].
CC       {ECO:0000255|PROSITE-ProRule:PRU00902,
CC       ECO:0000269|PubMed:15371351}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15371351}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=A; Synonyms=B;
CC         IsoId=Q8INR6-1; Sequence=Displayed;
CC         Note=No experimental confirmation available.;
CC       Name=C;
CC         IsoId=Q8INR6-2; Sequence=VSP_027492, VSP_012312, VSP_012313;
CC         Note=No experimental confirmation available.;
CC   -!- DEVELOPMENTAL STAGE: Expressed in embryos, larvae and adults.
CC       {ECO:0000269|PubMed:15371351}.
CC   -!- MISCELLANEOUS: In contrast to other lysine histone
CC       methyltransferases, it does not contain a SET domain, suggesting
CC       the existence of another mechanism for methylation of lysine
CC       residues of histones.
CC   -!- MISCELLANEOUS: Was named 'grappa' because the eyes of mutant flies
CC       are of a color similar to that of the Italian spirit.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding
CC       methyltransferase superfamily. DOT1 family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00902}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABE73251.1; Type=Frameshift; Positions=127; Evidence={ECO:0000305};
DR   EMBL; AE014297; AAF54122.2; -; Genomic_DNA.
DR   EMBL; AE014297; AAN13378.1; -; Genomic_DNA.
DR   EMBL; BT025080; ABE73251.1; ALT_FRAME; mRNA.
DR   RefSeq; NP_649655.1; NM_141398.4. [Q8INR6-1]
DR   RefSeq; NP_731083.1; NM_169142.2. [Q8INR6-1]
DR   RefSeq; NP_731084.1; NM_169143.2. [Q8INR6-1]
DR   UniGene; Dm.20383; -.
DR   ProteinModelPortal; Q8INR6; -.
DR   SMR; Q8INR6; -.
DR   BioGrid; 65994; 11.
DR   IntAct; Q8INR6; 3.
DR   STRING; 7227.FBpp0292801; -.
DR   iPTMnet; Q8INR6; -.
DR   PaxDb; Q8INR6; -.
DR   PRIDE; Q8INR6; -.
DR   EnsemblMetazoa; FBtr0303787; FBpp0292799; FBgn0264495. [Q8INR6-1]
DR   EnsemblMetazoa; FBtr0303788; FBpp0292800; FBgn0264495. [Q8INR6-1]
DR   EnsemblMetazoa; FBtr0303790; FBpp0292802; FBgn0264495. [Q8INR6-1]
DR   GeneID; 40793; -.
DR   KEGG; dme:Dmel_CG42803; -.
DR   UCSC; CG10272-RA; d. melanogaster. [Q8INR6-1]
DR   CTD; 40793; -.
DR   FlyBase; FBgn0264495; gpp.
DR   eggNOG; KOG3924; Eukaryota.
DR   eggNOG; ENOG410XSYC; LUCA.
DR   GeneTree; ENSGT00390000013515; -.
DR   InParanoid; Q8INR6; -.
DR   KO; K11427; -.
DR   OrthoDB; EOG091G00FV; -.
DR   Reactome; R-DME-3214841; PKMTs methylate histone lysines.
DR   ChiTaRS; gpp; fly.
DR   GenomeRNAi; 40793; -.
DR   PRO; PR:Q8INR6; -.
DR   Proteomes; UP000000803; Chromosome 3R.
DR   Bgee; FBgn0264495; -.
DR   ExpressionAtlas; Q8INR6; baseline and differential.
DR   Genevisible; Q8INR6; DM.
DR   GO; GO:0000781; C:chromosome, telomeric region; IEA:GOC.
DR   GO; GO:0035097; C:histone methyltransferase complex; IC:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IMP:FlyBase.
DR   GO; GO:0031151; F:histone methyltransferase activity (H3-K79 specific); IMP:UniProtKB.
DR   GO; GO:0006342; P:chromatin silencing; IMP:UniProtKB.
DR   GO; GO:0006348; P:chromatin silencing at telomere; IMP:UniProtKB.
DR   GO; GO:0048096; P:chromatin-mediated maintenance of transcription; IMP:UniProtKB.
DR   GO; GO:0000077; P:DNA damage checkpoint; IBA:GO_Central.
DR   GO; GO:0006281; P:DNA repair; IBA:GO_Central.
DR   GO; GO:0034729; P:histone H3-K79 methylation; IMP:FlyBase.
DR   GO; GO:0016571; P:histone methylation; IMP:UniProtKB.
DR   GO; GO:2000637; P:positive regulation of gene silencing by miRNA; IMP:FlyBase.
DR   GO; GO:2000677; P:regulation of transcription regulatory region DNA binding; IBA:GO_Central.
DR   InterPro; IPR025789; DOT1_dom.
DR   InterPro; IPR021169; DOT1L/grappa.
DR   InterPro; IPR029063; SAM-dependent_MTases.
DR   Pfam; PF08123; DOT1; 1.
DR   PIRSF; PIRSF037123; Histone_H3-K79_MeTrfase_met; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   PROSITE; PS51569; DOT1; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Chromatin regulator; Complete proteome;
KW   Methyltransferase; Nucleus; Phosphoprotein; Reference proteome;
KW   S-adenosyl-L-methionine; Transferase.
FT   CHAIN         1   1848       Histone-lysine N-methyltransferase, H3
FT                                lysine-79 specific.
FT                                /FTId=PRO_0000186090.
FT   DOMAIN       19    336       DOT1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00902}.
FT   REGION      142    145       S-adenosyl-L-methionine binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00902}.
FT   REGION      165    174       S-adenosyl-L-methionine binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00902}.
FT   REGION      228    229       S-adenosyl-L-methionine binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00902}.
FT   COMPBIAS    544    547       Poly-Ala.
FT   COMPBIAS    551    558       Poly-Ala.
FT   COMPBIAS    866    871       Poly-Ser.
FT   COMPBIAS    959    962       Poly-Pro.
FT   COMPBIAS    988    993       Poly-Gln.
FT   COMPBIAS   1119   1122       Poly-Pro.
FT   COMPBIAS   1158   1163       Poly-Pro.
FT   COMPBIAS   1201   1210       Poly-Gln.
FT   COMPBIAS   1214   1220       Poly-Ala.
FT   COMPBIAS   1230   1235       Poly-Gln.
FT   COMPBIAS   1236   1246       Poly-His.
FT   COMPBIAS   1585   1589       Poly-Ala.
FT   COMPBIAS   1676   1679       Poly-Pro.
FT   COMPBIAS   1691   1696       Poly-Ser.
FT   COMPBIAS   1736   1741       Poly-Gln.
FT   COMPBIAS   1747   1752       Poly-Gln.
FT   COMPBIAS   1839   1842       Poly-Ser.
FT   BINDING     192    192       S-adenosyl-L-methionine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00902}.
FT   MOD_RES     491    491       Phosphoserine.
FT                                {ECO:0000269|PubMed:18327897}.
FT   MOD_RES     492    492       Phosphoserine.
FT                                {ECO:0000269|PubMed:18327897}.
FT   MOD_RES     494    494       Phosphoserine.
FT                                {ECO:0000269|PubMed:18327897}.
FT   MOD_RES    1318   1318       Phosphoserine.
FT                                {ECO:0000269|PubMed:18327897}.
FT   MOD_RES    1324   1324       Phosphoserine.
FT                                {ECO:0000269|PubMed:18327897}.
FT   MOD_RES    1325   1325       Phosphoserine.
FT                                {ECO:0000269|PubMed:18327897}.
FT   VAR_SEQ     430   1253       Missing (in isoform C).
FT                                {ECO:0000303|Ref.3}.
FT                                /FTId=VSP_027492.
FT   VAR_SEQ    1561   1573       LAASLQDHVRARK -> KLPLVFVRRAWTF (in
FT                                isoform C). {ECO:0000303|Ref.3}.
FT                                /FTId=VSP_012312.
FT   VAR_SEQ    1574   1848       Missing (in isoform C).
FT                                {ECO:0000303|Ref.3}.
FT                                /FTId=VSP_012313.
SQ   SEQUENCE   1848 AA;  201284 MW;  7F391ABB35C3C96D CRC64;
     MATPQVKDLV LRSPAGSSDV ISFAWPLQIG HGQDKHDNGI DIIDTIKFVC DELPSMSSAF
     EETNLHQIDT ACYKTMTGLV DRFNKAVDSI VALEKGTSLP AERLNKFAHP SLLRHILQLV
     YNAAVLDPDK LNQYEPFSPE VYGETSYELV QQMLKHVTVS KEDTFIDLGS GVGQVVLQMA
     GSFPLKTCIG IEKADTPARY AERMDVIFRQ YMGWFGKRFC EYKLIKGDFL VDEHRENITS
     STLVFVNNFA FGPTVDHQLK ERFADLRDGA RVVSSKSFCP LNFRITDRNL SDIGTIMHVS
     EIPPLKGSVS WTCKPVSYYL HVIDRTILER YFQRLKTKGG NDHESVGTVR TTRDRAKREA
     NVGQHHHNNH HSNNHANSNN HQRDREQSNG ATATAAHQQR HQSQSPANVS GAGIVLAASG
     QQAASKTRQQ LQHQHNQQQR SLDMESSTES DGDATNGNGG NTTTATNTTS ASNGPMTRKV
     WSDWCSSKGK SSQSDDEENN NSNSNGGSNG GSIGGGSVGR QARATTQKKR KKLTRKAAIA
     SKSAAAAQRE AEAAAAAAVS VPSKESSSKE DPPRAASAGP GRKGRMKKGA RGRKSLKIVG
     LEALHKQTVL STSLDTMTKK LPAAPGTVDQ QLTALLTENM SHAELDIPTA PQDTPYALQI
     LLDVFRSQYT SMIEHMKSSA YVPQVQKQIA QEQERMARLK NRASQLDKQI KVLIDDSVAL
     LKVRMNELGI HVNSPNDLIA QAKEIVGRHK DLQHTASRMR NEVTFYEGEQ KLLLNKQLKN
     LPEYQKLCGT VNGKVKLEVP PELSETTAQE LVLKEIANTL SQRKKLYAQV STIEQETSVL
     QKTAEERSTA ATLLAQGTNM IVSTGSSSSS STTVCASAVT AQSNKLNSVK NSRRNREHRA
     RSQEWPEVPE VGKIQESNPE VLAQKIVETC RQIEAGKFQG AGAPSSQVNG KNKAIIEVPP
     PPATAPVSIK SSPGHHYKDT TLMPAPKQQQ QQQMTLSQLP KCELPGLSTS RKQESPKVAN
     FEDRLKSIIT TALNEDQEQR SKAVESSPSP SPLHSPAPKR SKQHPAGAIN PAQSLPNNLH
     NIITVSTQGL MHLNANTTIS PITPPLPGPG AGATASTAPP PPANLPYGAY GGAVAKTTIS
     GKYQAAKEPK YSPVRQAPLP PPPSHMASLY PAGQQTTPAD LGYQRRRSSV SATSYEHYMV
     QQQQQLQQQQ LMLAAAAHAA QRQQMRVEEQ QQQQQHQHHH HHHHHHPQHR LPQHVQHQHP
     HQHHPNEFKA PPADSHLQRS SSREQLIVEP PQTQPLELLP RASSANSDYS GYRIRPPSRP
     SSNSSQPDYT QVSPAKMALR RHLSQEKLSQ HVTPQATPPL PGHGGAPTSG KTIGDLVNGE
     IERTLEISHQ SIINAAVNMS TSGASFMERA FLNERSNDRL LINLNAQRPE RVHVRPLSEE
     SQDPQPTSYA QERGPGLGAG GAAAGGNSNL ATLAHVAYAQ KAQGGARANA GTAPPATHSS
     SARSGRDYQP VALPRAELKG SIEAYFHEEQ QQKQSKGAGS AGSSSLRGPR LNGANPPLEG
     LAASLQDHVR ARKYKEETEE RQRRAAAAAS SSAGPPAGME LPTHYAHQAP PAHSYHHHGA
     SINGTPHKVE LGIKRSSPLA PHQQPPRPSK LAHYEPPTTQ QQHAHAHLYA NGQVLPPPPA
     HDATTPSPTP SSSSSSCGRR SNSNNGKLLV DPPLLMSPEI NSLLGDERPL QLSHHQQQQQ
     QMLHHHQSQQ QQHLQLTQQQ LRVAHLGHGL SHGHSTMPTL GGQRNGNGNA ADDVNDLATQ
     RTITNYDPRR RLRTTLSGPT KLSAAHSNQN LNGYVMADSS SSCPTIPQ
//
DBGET integrated database retrieval system