DMAP1_MOUSE
ID DMAP1_MOUSE Reviewed; 468 AA.
AC Q9JI44; Q99LM0; Q9CSS9; Q9DB33;
DT 21-FEB-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=DNA methyltransferase 1-associated protein 1;
DE Short=DNMAP1;
DE Short=DNMT1-associated protein 1;
DE AltName: Full=MAT1-mediated transcriptional repressor;
GN Name=Dmap1; Synonyms=Mmtr;
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 [MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J;
RX PubMed=10888872; DOI=10.1038/77023;
RA Rountree M.R., Bachman K.E., Baylin S.B.;
RT "DNMT1 binds HDAC2 and a new co-repressor, DMAP1, to form a complex at
RT replication foci.";
RL Nat. Genet. 25:269-277(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC STRAIN=129/Sv;
RA Shin J.H., Kim C.G.;
RT "MMTR is a novel transcriptional regulator involved in MAT1-mediated
RT transcriptional repression.";
RL Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 1-257 (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Cerebellum, and Embryo;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J, and FVB/N; TISSUE=Mammary gland, and Olfactory epithelium;
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 [5]
RP FUNCTION, AND INTERACTION WITH DAXX.
RX PubMed=14978102; DOI=10.4049/jimmunol.172.5.2985;
RA Muromoto R., Sugiyama K., Takachi A., Imoto S., Sato N., Yamamoto T.,
RA Oritani K., Shimoda K., Matsuda T.;
RT "Physical and functional interactions between Daxx and DNA
RT methyltransferase 1-associated protein, DMAP1.";
RL J. Immunol. 172:2985-2993(2004).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-446, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic brain;
RX PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT "Phosphoproteomic analysis of the developing mouse brain.";
RL Mol. Cell. Proteomics 3:1093-1101(2004).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen;
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).
CC -!- FUNCTION: Involved in transcription repression and activation. Its
CC interaction with HDAC2 may provide a mechanism for histone
CC deacetylation in heterochromatin following replication of DNA at late
CC firing origins. Can also repress transcription independently of histone
CC deacetylase activity. May specifically potentiate DAXX-mediated
CC repression of glucocorticoid receptor-dependent transcription.
CC Component of the NuA4 histone acetyltransferase (HAT) complex which is
CC involved in transcriptional activation of select genes principally by
CC acetylation of nucleosomal histones H4 and H2A. This modification may
CC both alter nucleosome - DNA interactions and promote interaction of the
CC modified histones with other proteins which positively regulate
CC transcription. This complex may be required for the activation of
CC transcriptional programs associated with oncogene and proto-oncogene
CC mediated growth induction, tumor suppressor mediated growth arrest and
CC replicative senescence, apoptosis, and DNA repair. NuA4 may also play a
CC direct role in DNA repair when recruited to sites of DNA damage.
CC Participates in the nuclear localization of URI1 and increases its
CC transcriptional corepressor activity (By similarity). {ECO:0000250,
CC ECO:0000269|PubMed:14978102}.
CC -!- SUBUNIT: Component of the NuA4 histone acetyltransferase complex which
CC contains the catalytic subunit KAT5/TIP60 and the subunits EP400,
CC TRRAP/PAF400, BRD8/SMAP, EPC1, DMAP1/DNMAP1, RUVBL1/TIP49, RUVBL2,
CC ING3, actin, ACTL6A/BAF53A, MORF4L1/MRG15, MORF4L2/MRGX, MRGBP,
CC YEATS4/GAS41, VPS72/YL1 and MEAF6. Component of a NuA4-related complex
CC which contains EP400, TRRAP/PAF400, SRCAP, BRD8/SMAP, EPC1,
CC DMAP1/DNMAP1, RUVBL1/TIP49, RUVBL2, actin, ACTL6A/BAF53A, VPS72 and
CC YEATS4/GAS41. DMAP1 also forms a complex with DNMT1 and HDAC2.
CC Throughout S phase it interacts directly with the N-terminus of DNMT1,
CC which serves to recruit DMAP1 to replication foci. DMAP1 interacts with
CC ING1, a component of the mSIN3A transcription repressor complex,
CC although this interaction is not required for recruitment of ING1 to
CC heterochromatin. Interacts directly with the transcriptional
CC corepressor TSG101. Interacts with URI1 (By similarity). Interacts with
CC the pro-apoptotic protein DAXX. {ECO:0000250,
CC ECO:0000269|PubMed:14978102}.
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm {ECO:0000250}. Note=Targeted
CC to replication foci throughout S phase by DNMT1.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9JI44-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9JI44-2; Sequence=VSP_003850, VSP_003851;
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to intron retention.
CC {ECO:0000305}.
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DR EMBL; AF265229; AAF87080.1; -; mRNA.
DR EMBL; AF438610; AAL31640.1; -; mRNA.
DR EMBL; AK005270; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK012055; BAB27996.3; -; mRNA.
DR EMBL; BC002321; AAH02321.1; -; mRNA.
DR EMBL; BC045160; AAH45160.1; -; mRNA.
DR CCDS; CCDS18536.1; -. [Q9JI44-1]
DR RefSeq; NP_075667.1; NM_023178.2. [Q9JI44-1]
DR RefSeq; XP_006503329.1; XM_006503266.2. [Q9JI44-1]
DR RefSeq; XP_006503330.1; XM_006503267.3. [Q9JI44-1]
DR RefSeq; XP_006503331.1; XM_006503268.3. [Q9JI44-1]
DR AlphaFoldDB; Q9JI44; -.
DR SMR; Q9JI44; -.
DR BioGRID; 211314; 11.
DR ComplexPortal; CPX-976; SRCAP chromatin remodeling complex.
DR ComplexPortal; CPX-990; NuA4 histone acetyltransferase complex.
DR CORUM; Q9JI44; -.
DR IntAct; Q9JI44; 21.
DR MINT; Q9JI44; -.
DR STRING; 10090.ENSMUSP00000099748; -.
DR iPTMnet; Q9JI44; -.
DR PhosphoSitePlus; Q9JI44; -.
DR EPD; Q9JI44; -.
DR jPOST; Q9JI44; -.
DR MaxQB; Q9JI44; -.
DR PaxDb; Q9JI44; -.
DR PeptideAtlas; Q9JI44; -.
DR PRIDE; Q9JI44; -.
DR ProteomicsDB; 277337; -. [Q9JI44-1]
DR ProteomicsDB; 277338; -. [Q9JI44-2]
DR Antibodypedia; 18433; 295 antibodies from 35 providers.
DR DNASU; 66233; -.
DR Ensembl; ENSMUST00000102687; ENSMUSP00000099748; ENSMUSG00000009640. [Q9JI44-1]
DR GeneID; 66233; -.
DR KEGG; mmu:66233; -.
DR UCSC; uc008uiw.1; mouse. [Q9JI44-1]
DR CTD; 55929; -.
DR MGI; MGI:1913483; Dmap1.
DR VEuPathDB; HostDB:ENSMUSG00000009640; -.
DR eggNOG; KOG2656; Eukaryota.
DR GeneTree; ENSGT00390000016466; -.
DR HOGENOM; CLU_018539_1_1_1; -.
DR InParanoid; Q9JI44; -.
DR OMA; EKISWQW; -.
DR OrthoDB; 918816at2759; -.
DR PhylomeDB; Q9JI44; -.
DR TreeFam; TF354261; -.
DR BioGRID-ORCS; 66233; 28 hits in 116 CRISPR screens.
DR PRO; PR:Q9JI44; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q9JI44; protein.
DR Bgee; ENSMUSG00000009640; Expressed in skin of snout and 256 other tissues.
DR Genevisible; Q9JI44; MM.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0035267; C:NuA4 histone acetyltransferase complex; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0000786; C:nucleosome; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005657; C:replication fork; IDA:MGI.
DR GO; GO:0000812; C:Swr1 complex; IBA:GO_Central.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; ISS:UniProtKB.
DR GO; GO:0003714; F:transcription corepressor activity; IDA:MGI.
DR GO; GO:0006281; P:DNA repair; IEA:InterPro.
DR GO; GO:0016573; P:histone acetylation; IC:ComplexPortal.
DR GO; GO:0043486; P:histone exchange; IBA:GO_Central.
DR GO; GO:0043968; P:histone H2A acetylation; ISS:UniProtKB.
DR GO; GO:0043967; P:histone H4 acetylation; ISS:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:1905168; P:positive regulation of double-strand break repair via homologous recombination; ISO:MGI.
DR GO; GO:0042307; P:positive regulation of protein import into nucleus; ISS:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IC:ComplexPortal.
DR GO; GO:0042981; P:regulation of apoptotic process; IC:ComplexPortal.
DR GO; GO:0051726; P:regulation of cell cycle; ISO:MGI.
DR GO; GO:2000779; P:regulation of double-strand break repair; IC:ComplexPortal.
DR GO; GO:0040008; P:regulation of growth; IEA:UniProtKB-KW.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IC:ComplexPortal.
DR GO; GO:0045471; P:response to ethanol; IEA:Ensembl.
DR InterPro; IPR032563; DAMP1_SANT-like.
DR InterPro; IPR008468; DMAP1.
DR InterPro; IPR027109; Swc4/Dmap1.
DR PANTHER; PTHR12855; PTHR12855; 1.
DR Pfam; PF05499; DMAP1; 1.
DR Pfam; PF16282; SANT_DAMP1_like; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Chromatin regulator; Coiled coil; Cytoplasm;
KW Growth regulation; Isopeptide bond; Nucleus; Phosphoprotein;
KW Reference proteome; Repressor; Transcription; Transcription regulation;
KW Ubl conjugation.
FT CHAIN 1..468
FT /note="DNA methyltransferase 1-associated protein 1"
FT /id="PRO_0000079936"
FT DOMAIN 149..199
FT /note="SANT"
FT REGION 1..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 258..305
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 411..468
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 225..275
FT /evidence="ECO:0000255"
FT COMPBIAS 29..48
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 279..304
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 446
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:15345747"
FT MOD_RES 449
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NPF5"
FT CROSSLNK 27
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9NPF5"
FT CROSSLNK 214
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9NPF5"
FT VAR_SEQ 242..323
FT /note="AEEEYLLQELRKIEARKKEREKRSQDLQKLITAADTTAEQRRTERKAPKKKL
FT PQKKEAEKPAVPETAGIKFPDFKSAGVTLR -> ITSSTPPSTAQLSLPPGPFTSSPFL
FT WSLFLPSLQESPYLWSLIDNLVSRQLPSHLLPHSPHTHGSISCFAGGRGGVPPTGAA
FT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_003850"
FT VAR_SEQ 324..468
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_003851"
SQ SEQUENCE 468 AA; 53130 MW; CDDADF2165801C9B CRC64;
MATGADVRDI LELGGPEGDA ASGTISKKDI INPDKKKSKK SSETLTFKRP EGMHREVYAL
LYSDKKDAPP LLPSDTGQGY RTVKAKLGSK KVRPWKWMPF TNPARKDGAM FFHWRRAAEE
GKDYPFARFN KTVQVPVYSE QEYQLYLHDD AWTKAETDHL FDLSRRFDLR FVVIHDRYDH
QQFKKRSVED LKERYYHICA KLANVRAVPG TDLKIPVFDA GHERRRKEQL ERLYNRTPEQ
VAEEEYLLQE LRKIEARKKE REKRSQDLQK LITAADTTAE QRRTERKAPK KKLPQKKEAE
KPAVPETAGI KFPDFKSAGV TLRSQRMKLP SSVGQKKIKA LEQMLLELGV ELSPTPTEEL
VHMFNELRSD LVLLYELKQA CANCEYELQM LRHRHEALAR AGVLGAPAAA AVGPTPASAE
PTVSESGLGL DPTKDTIIDV VGAPLTPNSR KRRESASSSS SVKKAKKP
