DPY30_HUMAN
ID DPY30_HUMAN Reviewed; 99 AA.
AC Q9C005; D6W578;
DT 11-JUL-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Protein dpy-30 homolog;
DE AltName: Full=Dpy-30-like protein;
DE Short=Dpy-30L;
GN Name=DPY30;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Roberts R.G., Sheng M.;
RT "Dystrophin-related protein 2 (DRP2) is located in the postsynaptic density
RT of the CNS.";
RL Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Urinary bladder;
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 [4]
RP IDENTIFICATION IN THE MEN1-ASSOCIATED HISTONE METHYLTRANSFERASE COMPLEX.
RX PubMed=14992727; DOI=10.1016/s1097-2765(04)00081-4;
RA Hughes C.M., Rozenblatt-Rosen O., Milne T.A., Copeland T.D., Levine S.S.,
RA Lee J.C., Hayes D.N., Shanmugam K.S., Bhattacharjee A., Biondi C.A.,
RA Kay G.F., Hayward N.K., Hess J.L., Meyerson M.;
RT "Menin associates with a trithorax family histone methyltransferase complex
RT and with the hoxc8 locus.";
RL Mol. Cell 13:587-597(2004).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE MLL2/3
RP COMPLEX.
RX PubMed=17500065; DOI=10.1074/jbc.m701574200;
RA Cho Y.-W., Hong T., Hong S., Guo H., Yu H., Kim D., Guszczynski T.,
RA Dressler G.R., Copeland T.D., Kalkum M., Ge K.;
RT "PTIP associates with MLL3- and MLL4-containing histone H3 lysine 4
RT methyltransferase complex.";
RL J. Biol. Chem. 282:20395-20406(2007).
RN [6]
RP IDENTIFICATION IN SET1 COMPLEX.
RX PubMed=18838538; DOI=10.1128/mcb.00976-08;
RA Wu M., Wang P.F., Lee J.S., Martin-Brown S., Florens L., Washburn M.,
RA Shilatifard A.;
RT "Molecular regulation of H3K4 trimethylation by Wdr82, a component of human
RT Set1/COMPASS.";
RL Mol. Cell. Biol. 28:7337-7344(2008).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [8]
RP FUNCTION, DIMERIZATION, CHARACTERIZATION OF THE MLL1/MLL COMPLEX, AND
RP INTERACTION WITH ASH2L.
RX PubMed=19556245; DOI=10.1074/jbc.m109.014498;
RA Patel A., Dharmarajan V., Vought V.E., Cosgrove M.S.;
RT "On the mechanism of multiple lysine methylation by the human mixed lineage
RT leukemia protein-1 (MLL1) core complex.";
RL J. Biol. Chem. 284:24242-24256(2009).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH ARFGEF1.
RX PubMed=19651892; DOI=10.1083/jcb.200902146;
RA Xu Z., Gong Q., Xia B., Groves B., Zimmermann M., Mugler C., Mu D.,
RA Matsumoto B., Seaman M., Ma D.;
RT "A role of histone H3 lysine 4 methyltransferase components in endosomal
RT trafficking.";
RL J. Cell Biol. 186:343-353(2009).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-35, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [12]
RP FUNCTION.
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).
RN [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [15]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-35, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (1.20 ANGSTROMS) OF 45-99, AND DIMERIZATION.
RX PubMed=19481096; DOI=10.1016/j.jmb.2009.05.061;
RA Wang X., Lou Z., Dong X., Yang W., Peng Y., Yin B., Gong Y., Yuan J.,
RA Zhou W., Bartlam M., Peng X., Rao Z.;
RT "Crystal structure of the C-terminal domain of human DPY-30-like protein: A
RT component of the histone methyltransferase complex.";
RL J. Mol. Biol. 390:530-537(2009).
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 a
CC teratocarcinoma cell, plays a crucial role in retinoic acid-induced
CC differentiation along the neural lineage, regulating gene induction and
CC H3 'Lys-4' methylation at key developmental loci. May also play an
CC indirect or direct role in endosomal transport.
CC {ECO:0000269|PubMed:19556245, ECO:0000269|PubMed:19651892,
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 (By similarity). Interacts with
CC ASH2L; the interaction is direct. Interacts with ARFGEF1. Component of
CC the SET1 complex, at least composed of the catalytic subunit (SETD1A or
CC SETD1B), WDR5, WDR82, RBBP5, ASH2L/ASH2, CXXC1/CFP1, HCFC1 and DPY30.
CC {ECO:0000250, ECO:0000269|PubMed:14992727, ECO:0000269|PubMed:17500065,
CC ECO:0000269|PubMed:18838538, ECO:0000269|PubMed:19556245,
CC ECO:0000269|PubMed:19651892}.
CC -!- INTERACTION:
CC Q9C005; Q96MA6: AK8; NbExp=3; IntAct=EBI-744973, EBI-8466265;
CC Q9C005; Q86UN6: AKAP14; NbExp=3; IntAct=EBI-744973, EBI-2119626;
CC Q9C005; O43823: AKAP8; NbExp=7; IntAct=EBI-744973, EBI-1237481;
CC Q9C005; Q9UBL3: ASH2L; NbExp=22; IntAct=EBI-744973, EBI-540797;
CC Q9C005; Q9UBL3-3: ASH2L; NbExp=7; IntAct=EBI-744973, EBI-16130425;
CC Q9C005; Q8IXM2: BAP18; NbExp=3; IntAct=EBI-744973, EBI-4280811;
CC Q9C005; Q8TDM0-3: BCAS4; NbExp=3; IntAct=EBI-744973, EBI-13025473;
CC Q9C005; Q5T5X7: BEND3; NbExp=3; IntAct=EBI-744973, EBI-1211496;
CC Q9C005; Q00537: CDK17; NbExp=3; IntAct=EBI-744973, EBI-624648;
CC Q9C005; Q7Z4T9: CFAP91; NbExp=3; IntAct=EBI-744973, EBI-2119657;
CC Q9C005; Q68CJ9: CREB3L3; NbExp=3; IntAct=EBI-744973, EBI-852194;
CC Q9C005; Q9C005: DPY30; NbExp=9; IntAct=EBI-744973, EBI-744973;
CC Q9C005; Q8WWB3: DYDC1; NbExp=4; IntAct=EBI-744973, EBI-740680;
CC Q9C005; Q96IM9: DYDC2; NbExp=3; IntAct=EBI-744973, EBI-749277;
CC Q9C005; Q96C01: FAM136A; NbExp=3; IntAct=EBI-744973, EBI-373319;
CC Q9C005; Q9NW75-2: GPATCH2; NbExp=3; IntAct=EBI-744973, EBI-12068108;
CC Q9C005; P78347-2: GTF2I; NbExp=7; IntAct=EBI-744973, EBI-12033200;
CC Q9C005; Q8NDH6-2: ICA1L; NbExp=3; IntAct=EBI-744973, EBI-12141931;
CC Q9C005; Q9Y605: MRFAP1; NbExp=3; IntAct=EBI-744973, EBI-995714;
CC Q9C005; P17980: PSMC3; NbExp=3; IntAct=EBI-744973, EBI-359720;
CC Q9C005; O00487: PSMD14; NbExp=6; IntAct=EBI-744973, EBI-722193;
CC Q9C005; P49023-2: PXN; NbExp=3; IntAct=EBI-744973, EBI-11954250;
CC Q9C005; Q86UC2: RSPH3; NbExp=3; IntAct=EBI-744973, EBI-6873025;
CC Q9C005; P0CW01: TSPY10; NbExp=4; IntAct=EBI-744973, EBI-19697726;
CC Q9C005; A6NKD2: TSPY2; NbExp=3; IntAct=EBI-744973, EBI-12817075;
CC Q9C005; Q96K21: ZFYVE19; NbExp=3; IntAct=EBI-744973, EBI-6448240;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19651892}. Golgi
CC apparatus, trans-Golgi network {ECO:0000269|PubMed:19651892}.
CC Note=Associated with chromatin at regions enriched in histone H3
CC trimethylated at 'Lys-4. Highly enriched in gene promoter regions and
CC 5' UTRs, but not in downstream regions of genes or 3' UTRs (By
CC similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the dpy-30 family. {ECO:0000305}.
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DR EMBL; AF226998; AAK00640.1; -; mRNA.
DR EMBL; CH471053; EAX00463.1; -; Genomic_DNA.
DR EMBL; CH471053; EAX00466.1; -; Genomic_DNA.
DR EMBL; BC015970; AAH15970.1; -; mRNA.
DR CCDS; CCDS1777.1; -.
DR RefSeq; NP_001308138.1; NM_001321209.1.
DR RefSeq; NP_115963.1; NM_032574.3.
DR PDB; 3G36; X-ray; 1.20 A; A/B/C/D=45-99.
DR PDB; 4RIQ; X-ray; 2.23 A; A/B/D/E/G/H/J/K/M/N/P/Q/S/T/V/Z=45-99.
DR PDB; 4RT4; X-ray; 2.00 A; A/B/C/D=41-99.
DR PDB; 4RTA; X-ray; 2.12 A; A/B=1-99.
DR PDB; 6E2H; X-ray; 2.24 A; E/F=1-99.
DR PDB; 6PWV; EM; 6.20 A; E/F=1-99.
DR PDBsum; 3G36; -.
DR PDBsum; 4RIQ; -.
DR PDBsum; 4RT4; -.
DR PDBsum; 4RTA; -.
DR PDBsum; 6E2H; -.
DR PDBsum; 6PWV; -.
DR AlphaFoldDB; Q9C005; -.
DR SMR; Q9C005; -.
DR BioGRID; 124181; 171.
DR ComplexPortal; CPX-5850; Histone-lysine N-methyltransferase complex, KMT2A variant.
DR ComplexPortal; CPX-7062; Histone-lysine N-methyltransferase complex, KMT2B variant.
DR ComplexPortal; CPX-7091; Histone-lysine N-methyltransferase complex, KMT2C variant.
DR ComplexPortal; CPX-7104; Histone-lysine N-methyltransferase complex, KMT2D variant.
DR ComplexPortal; CPX-7110; Histone-lysine N-methyltransferase complex, SET1A variant.
DR ComplexPortal; CPX-7111; Histone-lysine N-methyltransferase complex, SET1B variant.
DR CORUM; Q9C005; -.
DR DIP; DIP-34476N; -.
DR IntAct; Q9C005; 107.
DR MINT; Q9C005; -.
DR STRING; 9606.ENSP00000345837; -.
DR iPTMnet; Q9C005; -.
DR PhosphoSitePlus; Q9C005; -.
DR BioMuta; DPY30; -.
DR DMDM; 14916555; -.
DR EPD; Q9C005; -.
DR jPOST; Q9C005; -.
DR MassIVE; Q9C005; -.
DR MaxQB; Q9C005; -.
DR PaxDb; Q9C005; -.
DR PeptideAtlas; Q9C005; -.
DR PRIDE; Q9C005; -.
DR ProteomicsDB; 79938; -.
DR TopDownProteomics; Q9C005; -.
DR Antibodypedia; 51686; 71 antibodies from 17 providers.
DR DNASU; 84661; -.
DR Ensembl; ENST00000295066.3; ENSP00000295066.3; ENSG00000162961.14.
DR Ensembl; ENST00000342166.10; ENSP00000345837.5; ENSG00000162961.14.
DR GeneID; 84661; -.
DR KEGG; hsa:84661; -.
DR MANE-Select; ENST00000342166.10; ENSP00000345837.5; NM_001321209.2; NP_001308138.1.
DR UCSC; uc002roa.2; human.
DR CTD; 84661; -.
DR DisGeNET; 84661; -.
DR GeneCards; DPY30; -.
DR HGNC; HGNC:24590; DPY30.
DR HPA; ENSG00000162961; Low tissue specificity.
DR MIM; 612032; gene.
DR neXtProt; NX_Q9C005; -.
DR OpenTargets; ENSG00000162961; -.
DR PharmGKB; PA162384063; -.
DR VEuPathDB; HostDB:ENSG00000162961; -.
DR eggNOG; KOG4109; Eukaryota.
DR GeneTree; ENSGT00390000008808; -.
DR HOGENOM; CLU_135823_3_1_1; -.
DR InParanoid; Q9C005; -.
DR OMA; METPHEK; -.
DR PhylomeDB; Q9C005; -.
DR PathwayCommons; Q9C005; -.
DR Reactome; R-HSA-3214841; PKMTs methylate histone lysines.
DR Reactome; R-HSA-8936459; RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function.
DR SignaLink; Q9C005; -.
DR SIGNOR; Q9C005; -.
DR BioGRID-ORCS; 84661; 299 hits in 1052 CRISPR screens.
DR ChiTaRS; DPY30; human.
DR EvolutionaryTrace; Q9C005; -.
DR GenomeRNAi; 84661; -.
DR Pharos; Q9C005; Tbio.
DR PRO; PR:Q9C005; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q9C005; protein.
DR Bgee; ENSG00000162961; Expressed in bronchial epithelial cell and 181 other tissues.
DR Genevisible; Q9C005; HS.
DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR GO; GO:0035097; C:histone methyltransferase complex; IDA:UniProtKB.
DR GO; GO:0071339; C:MLL1 complex; IPI:ComplexPortal.
DR GO; GO:0044665; C:MLL1/2 complex; IPI:ComplexPortal.
DR GO; GO:0044666; C:MLL3/4 complex; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0048188; C:Set1C/COMPASS complex; IDA:UniProtKB.
DR GO; GO:0005802; C:trans-Golgi network; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0016197; P:endosomal transport; IMP:UniProtKB.
DR GO; GO:0051568; P:histone H3-K4 methylation; IDA: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 3D-structure; Acetylation; Chromatin regulator; Golgi apparatus;
KW Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome;
KW Transcription; Transcription regulation; Ubl conjugation.
FT CHAIN 1..99
FT /note="Protein dpy-30 homolog"
FT /id="PRO_0000114683"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22814378"
FT MOD_RES 19
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 35
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:19608861"
FT CROSSLNK 35
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:28112733"
FT HELIX 31..34
FT /evidence="ECO:0007829|PDB:4RTA"
FT HELIX 48..50
FT /evidence="ECO:0007829|PDB:3G36"
FT HELIX 53..58
FT /evidence="ECO:0007829|PDB:3G36"
FT TURN 59..61
FT /evidence="ECO:0007829|PDB:3G36"
FT HELIX 62..75
FT /evidence="ECO:0007829|PDB:3G36"
FT HELIX 80..91
FT /evidence="ECO:0007829|PDB:3G36"
FT HELIX 92..95
FT /evidence="ECO:0007829|PDB:3G36"
SQ SEQUENCE 99 AA; 11250 MW; 5356AC515B9C2ADB CRC64;
MEPEQMLEGQ TQVAENPHSE YGLTDNVERI VENEKINAEK SSKQKVDLQS LPTRAYLDQT
VVPILLQGLA VLAKERPPNP IEFLASYLLK NKAQFEDRN
