DPY30_MOUSE
ID DPY30_MOUSE Reviewed; 99 AA.
AC Q99LT0;
DT 11-JUL-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Protein dpy-30 homolog;
DE AltName: Full=Dpy-30-like protein;
DE Short=Dpy-30L;
GN Name=Dpy30;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [4]
RP FUNCTION, IDENTIFICATION IN THE MLL COMPLEX, INTERACTION WITH ASH2L; KMT2A;
RP KMT2D; RRBP5 AND WDR5, AND SUBCELLULAR LOCATION.
RX PubMed=21335234; DOI=10.1016/j.cell.2011.01.020;
RA Jiang H., Shukla A., Wang X., Chen W.Y., Bernstein B.E., Roeder R.G.;
RT "Role for Dpy-30 in ES cell-fate specification by regulation of H3K4
RT methylation within bivalent domains.";
RL Cell 144:513-525(2011).
CC -!- FUNCTION: As part of the MLL1/MLL complex, involved in the methylation
CC of histone H3 at 'Lys-4', particularly trimethylation. Histone H3 'Lys-
CC 4' methylation represents a specific tag for epigenetic transcriptional
CC activation. May play some role in histone H3 acetylation. In embryonic
CC stem (ES) cells, plays a crucial role in the differentiation potential,
CC particularly along the neural lineage, regulating gene induction and
CC histone H3 'Lys-4' methylation at key developmental loci, including
CC that mediated by retinoic acid. Does not affect ES cell self-renewal.
CC May also play an indirect or direct role in endosomal transport.
CC {ECO:0000269|PubMed:21335234}.
CC -!- SUBUNIT: Homodimer. Core component of several methyltransferase-
CC containing complexes including MLL1/MLL, MLL2/3 (also named ASCOM
CC complex) and MLL4/WBP7. Each complex is at least composed of ASH2L,
CC RBBP5, WDR5, DPY30, one or more specific histone methyltransferases
CC (KMT2A/MLL1, KMT2D/MLL2, KMT2C/MLL3 and KMT2B/MLL4), and the
CC facultative components MEN1, HCFC1, HCFC2, NCOA6, KDM6A, PAXIP1/PTIP,
CC PAGR1 and alpha- and beta-tubulin PAXIP1/PTIP, PAGR1 and alpha- and
CC beta-tubulin. Interacts with ASH2L. The interaction with ASH2L is
CC direct (By similarity). Interacts with ARFGEF1 (By similarity).
CC Component of the SET1 complex, at least composed of the catalytic
CC subunit (SETD1A or SETD1B), WDR5, WDR82, RBBP5, ASH2L/ASH2, CXXC1/CFP1,
CC HCFC1 and DPY30 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21335234}. Golgi
CC apparatus, trans-Golgi network {ECO:0000250}. Note=Associated with
CC chromatin at regions enriched in histone H3 trimethylated at 'Lys-4'.
CC Highly enriched in gene promoter regions and 5' UTRs, but not in
CC downstream regions of genes or 3' UTRs.
CC -!- SIMILARITY: Belongs to the dpy-30 family. {ECO:0000305}.
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DR EMBL; AK003688; BAC25047.1; -; mRNA.
DR EMBL; AK011643; BAC25341.1; -; mRNA.
DR EMBL; AK013073; BAC25389.1; -; mRNA.
DR EMBL; AK077902; BAC37054.1; -; mRNA.
DR EMBL; BC002240; AAH02240.1; -; mRNA.
DR CCDS; CCDS28970.1; -.
DR RefSeq; NP_001139694.1; NM_001146222.1.
DR RefSeq; NP_001139695.1; NM_001146223.1.
DR RefSeq; NP_001139696.1; NM_001146224.1.
DR RefSeq; NP_077746.3; NM_024428.4.
DR AlphaFoldDB; Q99LT0; -.
DR SMR; Q99LT0; -.
DR BioGRID; 211374; 22.
DR DIP; DIP-61810N; -.
DR IntAct; Q99LT0; 4.
DR STRING; 10090.ENSMUSP00000126702; -.
DR iPTMnet; Q99LT0; -.
DR PhosphoSitePlus; Q99LT0; -.
DR EPD; Q99LT0; -.
DR jPOST; Q99LT0; -.
DR MaxQB; Q99LT0; -.
DR PaxDb; Q99LT0; -.
DR PeptideAtlas; Q99LT0; -.
DR PRIDE; Q99LT0; -.
DR ProteomicsDB; 277391; -.
DR TopDownProteomics; Q99LT0; -.
DR Antibodypedia; 51686; 71 antibodies from 17 providers.
DR DNASU; 66310; -.
DR Ensembl; ENSMUST00000112571; ENSMUSP00000108190; ENSMUSG00000024067.
DR Ensembl; ENSMUST00000164832; ENSMUSP00000126702; ENSMUSG00000024067.
DR Ensembl; ENSMUST00000232687; ENSMUSP00000156830; ENSMUSG00000024067.
DR Ensembl; ENSMUST00000233581; ENSMUSP00000156795; ENSMUSG00000024067.
DR GeneID; 66310; -.
DR KEGG; mmu:66310; -.
DR UCSC; uc008dnw.2; mouse.
DR CTD; 84661; -.
DR MGI; MGI:1913560; Dpy30.
DR VEuPathDB; HostDB:ENSMUSG00000024067; -.
DR eggNOG; KOG4109; Eukaryota.
DR GeneTree; ENSGT00390000008808; -.
DR HOGENOM; CLU_135823_3_1_1; -.
DR InParanoid; Q99LT0; -.
DR OMA; METPHEK; -.
DR OrthoDB; 1596051at2759; -.
DR PhylomeDB; Q99LT0; -.
DR Reactome; R-MMU-3214841; PKMTs methylate histone lysines.
DR Reactome; R-MMU-8936459; RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function.
DR BioGRID-ORCS; 66310; 15 hits in 73 CRISPR screens.
DR ChiTaRS; Dpy30; mouse.
DR PRO; PR:Q99LT0; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q99LT0; protein.
DR Bgee; ENSMUSG00000024067; Expressed in urogenital fold and 276 other tissues.
DR ExpressionAtlas; Q99LT0; baseline and differential.
DR Genevisible; Q99LT0; MM.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0035097; C:histone methyltransferase complex; ISS:UniProtKB.
DR GO; GO:0071339; C:MLL1 complex; ISO:MGI.
DR GO; GO:0044665; C:MLL1/2 complex; ISO:MGI.
DR GO; GO:0044666; C:MLL3/4 complex; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0048188; C:Set1C/COMPASS complex; ISS:UniProtKB.
DR GO; GO:0005802; C:trans-Golgi network; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0016197; P:endosomal transport; ISS:UniProtKB.
DR GO; GO:0051568; P:histone H3-K4 methylation; ISS:UniProtKB.
DR InterPro; IPR007858; Dpy-30_motif.
DR InterPro; IPR037856; Sdc1/DPY30.
DR PANTHER; PTHR23356; PTHR23356; 1.
DR Pfam; PF05186; Dpy-30; 1.
PE 1: Evidence at protein level;
KW Acetylation; Chromatin regulator; Golgi apparatus; Isopeptide bond;
KW Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation; Ubl conjugation.
FT CHAIN 1..99
FT /note="Protein dpy-30 homolog"
FT /id="PRO_0000114684"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..19
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q9C005"
FT MOD_RES 19
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9C005"
FT MOD_RES 35
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9C005"
FT CROSSLNK 35
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9C005"
SQ SEQUENCE 99 AA; 11213 MW; 51B34D856E7DFC0B CRC64;
MESEQMLEGQ TQVAENPHSE YGLTDSVERI VENEKINAEK SSKQKVDLQS LPTRAYLDQT
VVPILLQGLA VLAKERPPNP IEFLASYLLK NKAQFEDRN
