DPY30_RAT
ID DPY30_RAT Reviewed; 99 AA.
AC Q8K3E7;
DT 19-JAN-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 25-MAY-2022, entry version 101.
DE RecName: Full=Protein dpy-30 homolog;
DE AltName: Full=Dpy-30-like protein;
DE Short=Dpy-30L;
DE AltName: Full=Protein rAIP1;
GN Name=Dpy30; Synonyms=Aip1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Testis;
RA Kankare K.A., Janne O.A.;
RT "Novel rat gene coding for a rAIP1 protein.";
RL Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP 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).
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 cells, may play 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 (By similarity).
CC {ECO:0000250}.
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 (By similarity). Interacts with
CC ARFGEF1. Component of the SET1 complex, at least composed of the
CC catalytic subunit (SETD1A or SETD1B), WDR5, WDR82, RBBP5, ASH2L/ASH2,
CC CXXC1/CFP1, HCFC1 and DPY30 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Golgi apparatus, trans-
CC Golgi network {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the dpy-30 family. {ECO:0000305}.
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DR EMBL; AY129401; AAN02167.1; -; mRNA.
DR RefSeq; NP_775140.2; NM_173117.2.
DR AlphaFoldDB; Q8K3E7; -.
DR SMR; Q8K3E7; -.
DR IntAct; Q8K3E7; 1.
DR STRING; 10116.ENSRNOP00000035649; -.
DR iPTMnet; Q8K3E7; -.
DR PhosphoSitePlus; Q8K3E7; -.
DR jPOST; Q8K3E7; -.
DR PaxDb; Q8K3E7; -.
DR PRIDE; Q8K3E7; -.
DR GeneID; 286897; -.
DR KEGG; rno:286897; -.
DR UCSC; RGD:708575; rat.
DR CTD; 84661; -.
DR RGD; 708575; Dpy30.
DR eggNOG; KOG4109; Eukaryota.
DR InParanoid; Q8K3E7; -.
DR OrthoDB; 1596051at2759; -.
DR PhylomeDB; Q8K3E7; -.
DR Reactome; R-RNO-3214841; PKMTs methylate histone lysines.
DR Reactome; R-RNO-8936459; RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function.
DR PRO; PR:Q8K3E7; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0035097; C:histone methyltransferase complex; ISS:UniProtKB.
DR GO; GO:0071339; C:MLL1 complex; ISO:RGD.
DR GO; GO:0044665; C:MLL1/2 complex; ISO:RGD.
DR GO; GO:0044666; C:MLL3/4 complex; ISO:RGD.
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:RGD.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:RGD.
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_0000390660"
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; 11201 MW; 51B3585F5E7DFC0B CRC64;
MESEQMLEGQ TQVAENPHSE YGLTDSVERI VENEKINAEK SSKQKVDLQS LPTRAYLDQT
VVPILLQGLA VLAKERPPNP TEFLASYLLK NKAQFEDRN
