DMAP1_HUMAN
ID DMAP1_HUMAN Reviewed; 467 AA.
AC Q9NPF5; A8K001; D3DPY8; Q0JSM4; Q5TG41; Q7Z3H7; Q9H0S8; Q9P2C2;
DT 21-FEB-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 203.
DE RecName: Full=DNA methyltransferase 1-associated protein 1;
DE Short=DNMAP1;
DE Short=DNMT1-associated protein 1;
GN Name=DMAP1; Synonyms=KIAA1425;
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], SUBCELLULAR LOCATION, AND INTERACTION WITH
RP DNMT1 AND TSG101.
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 [LARGE SCALE MRNA].
RA Rhodes S., Huckle E.;
RL Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=10718198; DOI=10.1093/dnares/7.1.65;
RA Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XVI. The
RT complete sequences of 150 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:65-73(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Fetal brain;
RX PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and analysis of
RT 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [7]
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 [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Placenta, and Skin;
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 [9]
RP PROTEIN SEQUENCE OF 9-27; 56-66; 117-128; 237-252; 271-282; 369-378;
RP 401-433 AND 434-449, IDENTIFICATION IN NUA4 COMPLEX, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=12963728; DOI=10.1074/jbc.c300389200;
RA Cai Y., Jin J., Tomomori-Sato C., Sato S., Sorokina I., Parmely T.J.,
RA Conaway R.C., Conaway J.W.;
RT "Identification of new subunits of the multiprotein mammalian TRRAP/TIP60-
RT containing histone acetyltransferase complex.";
RL J. Biol. Chem. 278:42733-42736(2003).
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 132-467.
RC TISSUE=Colon endothelium;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [11]
RP REVIEW ON NUA4 COMPLEX.
RX PubMed=15196461; DOI=10.1016/j.gde.2004.02.009;
RA Doyon Y., Cote J.;
RT "The highly conserved and multifunctional NuA4 HAT complex.";
RL Curr. Opin. Genet. Dev. 14:147-154(2004).
RN [12]
RP FUNCTION, AND INTERACTION WITH ING1.
RX PubMed=14665632; DOI=10.1074/jbc.m311587200;
RA Xin H., Yoon H.-G., Singh P.B., Wong J., Qin J.;
RT "Components of a pathway maintaining histone modification and
RT heterochromatin protein 1 binding at the pericentric heterochromatin in
RT mammalian cells.";
RL J. Biol. Chem. 279:9539-9546(2004).
RN [13]
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 [14]
RP FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN NUA4
RP COMPLEX, AND IDENTIFICATION IN NUA4-RELATED SRCAP-CONTAINING COMPLEX.
RX PubMed=14966270; DOI=10.1128/mcb.24.5.1884-1896.2004;
RA Doyon Y., Selleck W., Lane W.S., Tan S., Cote J.;
RT "Structural and functional conservation of the NuA4 histone
RT acetyltransferase complex from yeast to humans.";
RL Mol. Cell. Biol. 24:1884-1896(2004).
RN [15]
RP FUNCTION, INTERACTION WITH URI1, AND SUBCELLULAR LOCATION.
RX PubMed=15367675; DOI=10.1128/mcb.24.19.8556-8566.2004;
RA Delgermaa L., Hayashi N., Dorjsuren D., Nomura T., Thuy le T.T.,
RA Murakami S.;
RT "Subcellular localization of RPB5-mediating protein and its putative
RT functional partner.";
RL Mol. Cell. Biol. 24:8556-8566(2004).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-445, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-445, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-445, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [19]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-445 AND SER-448, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-445, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [22]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-445, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [23]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-445, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [24]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-445, 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 [25]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-27 AND LYS-214, AND
RP IDENTIFICATION BY MASS 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 [26]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 121-212.
RG Structural genomics consortium (SGC);
RT "SANT domain of human DNA methyltransferase 1 associated protein 1.";
RL Submitted (JUN-2009) to the PDB data bank.
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. {ECO:0000269|PubMed:14665632,
CC ECO:0000269|PubMed:14966270, ECO:0000269|PubMed:14978102,
CC ECO:0000269|PubMed:15367675}.
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 the pro-apoptotic protein DAXX.
CC Interacts with URI1. {ECO:0000269|PubMed:10888872,
CC ECO:0000269|PubMed:12963728, ECO:0000269|PubMed:14665632,
CC ECO:0000269|PubMed:14966270, ECO:0000269|PubMed:14978102,
CC ECO:0000269|PubMed:15367675}.
CC -!- INTERACTION:
CC Q9NPF5; P53365: ARFIP2; NbExp=3; IntAct=EBI-399105, EBI-638194;
CC Q9NPF5; Q13515: BFSP2; NbExp=5; IntAct=EBI-399105, EBI-10229433;
CC Q9NPF5; Q8TAB5: C1orf216; NbExp=5; IntAct=EBI-399105, EBI-747505;
CC Q9NPF5; Q8TD31-3: CCHCR1; NbExp=3; IntAct=EBI-399105, EBI-10175300;
CC Q9NPF5; Q96GN5: CDCA7L; NbExp=3; IntAct=EBI-399105, EBI-5278764;
CC Q9NPF5; Q9UER7: DAXX; NbExp=3; IntAct=EBI-399105, EBI-77321;
CC Q9NPF5; Q8IYI6: EXOC8; NbExp=3; IntAct=EBI-399105, EBI-742102;
CC Q9NPF5; O95995: GAS8; NbExp=3; IntAct=EBI-399105, EBI-1052570;
CC Q9NPF5; Q9BRT9: GINS4; NbExp=3; IntAct=EBI-399105, EBI-747500;
CC Q9NPF5; O75031: HSF2BP; NbExp=3; IntAct=EBI-399105, EBI-7116203;
CC Q9NPF5; O95678: KRT75; NbExp=3; IntAct=EBI-399105, EBI-2949715;
CC Q9NPF5; P20700: LMNB1; NbExp=3; IntAct=EBI-399105, EBI-968218;
CC Q9NPF5; Q6UWE0: LRSAM1; NbExp=3; IntAct=EBI-399105, EBI-720984;
CC Q9NPF5; Q9NYP9: MIS18A; NbExp=3; IntAct=EBI-399105, EBI-1104552;
CC Q9NPF5; Q9UBU8-2: MORF4L1; NbExp=4; IntAct=EBI-399105, EBI-10288852;
CC Q9NPF5; Q9ULW6: NAP1L2; NbExp=3; IntAct=EBI-399105, EBI-3911716;
CC Q9NPF5; O60925: PFDN1; NbExp=3; IntAct=EBI-399105, EBI-356919;
CC Q9NPF5; Q4G0R1: PIBF1; NbExp=3; IntAct=EBI-399105, EBI-14066006;
CC Q9NPF5; P0C264: SBK3; NbExp=3; IntAct=EBI-399105, EBI-17181801;
CC Q9NPF5; P51687: SUOX; NbExp=3; IntAct=EBI-399105, EBI-3921347;
CC Q9NPF5; Q8N8B7-2: TCEANC; NbExp=3; IntAct=EBI-399105, EBI-11955057;
CC Q9NPF5; Q9BT92: TCHP; NbExp=5; IntAct=EBI-399105, EBI-740781;
CC Q9NPF5; Q86UE8: TLK2; NbExp=3; IntAct=EBI-399105, EBI-1047967;
CC Q9NPF5; P19474: TRIM21; NbExp=3; IntAct=EBI-399105, EBI-81290;
CC Q9NPF5; Q3SY00: TSGA10IP; NbExp=3; IntAct=EBI-399105, EBI-10241197;
CC Q9NPF5; P40222: TXLNA; NbExp=3; IntAct=EBI-399105, EBI-359793;
CC Q9NPF5; Q8N3L3: TXLNB; NbExp=3; IntAct=EBI-399105, EBI-6116822;
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Targeted to replication
CC foci throughout S phase by DNMT1.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA92663.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF265228; AAF87079.1; -; mRNA.
DR EMBL; AL137200; CAB69910.1; -; mRNA.
DR EMBL; AB037846; BAA92663.1; ALT_INIT; mRNA.
DR EMBL; AL136657; CAB66592.1; -; mRNA.
DR EMBL; AM393614; CAL38490.1; -; mRNA.
DR EMBL; AK021605; BAB13854.1; -; mRNA.
DR EMBL; AK289366; BAF82055.1; -; mRNA.
DR EMBL; AL035417; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471059; EAX07046.1; -; Genomic_DNA.
DR EMBL; CH471059; EAX07047.1; -; Genomic_DNA.
DR EMBL; CH471059; EAX07048.1; -; Genomic_DNA.
DR EMBL; CH471059; EAX07051.1; -; Genomic_DNA.
DR EMBL; BC002855; AAH02855.1; -; mRNA.
DR EMBL; BC008053; AAH08053.1; -; mRNA.
DR EMBL; BX537895; CAD97886.1; -; mRNA.
DR CCDS; CCDS509.1; -.
DR RefSeq; NP_001029195.1; NM_001034023.1.
DR RefSeq; NP_001029196.1; NM_001034024.1.
DR RefSeq; NP_061973.1; NM_019100.4.
DR RefSeq; XP_016857297.1; XM_017001808.1.
DR PDB; 3HM5; X-ray; 1.80 A; A=121-212.
DR PDB; 4IEJ; X-ray; 1.45 A; A=121-212.
DR PDBsum; 3HM5; -.
DR PDBsum; 4IEJ; -.
DR AlphaFoldDB; Q9NPF5; -.
DR SMR; Q9NPF5; -.
DR BioGRID; 121004; 173.
DR ComplexPortal; CPX-974; SRCAP chromatin remodeling complex.
DR ComplexPortal; CPX-978; NuA4 histone acetyltransferase complex.
DR CORUM; Q9NPF5; -.
DR IntAct; Q9NPF5; 86.
DR MINT; Q9NPF5; -.
DR STRING; 9606.ENSP00000361363; -.
DR GlyGen; Q9NPF5; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9NPF5; -.
DR PhosphoSitePlus; Q9NPF5; -.
DR BioMuta; DMAP1; -.
DR DMDM; 20138031; -.
DR EPD; Q9NPF5; -.
DR jPOST; Q9NPF5; -.
DR MassIVE; Q9NPF5; -.
DR MaxQB; Q9NPF5; -.
DR PaxDb; Q9NPF5; -.
DR PeptideAtlas; Q9NPF5; -.
DR PRIDE; Q9NPF5; -.
DR ProteomicsDB; 81985; -.
DR Antibodypedia; 18433; 295 antibodies from 35 providers.
DR DNASU; 55929; -.
DR Ensembl; ENST00000315913.9; ENSP00000312697.5; ENSG00000178028.14.
DR Ensembl; ENST00000361745.10; ENSP00000354697.6; ENSG00000178028.14.
DR Ensembl; ENST00000372289.7; ENSP00000361363.2; ENSG00000178028.14.
DR GeneID; 55929; -.
DR KEGG; hsa:55929; -.
DR MANE-Select; ENST00000372289.7; ENSP00000361363.2; NM_019100.5; NP_061973.1.
DR UCSC; uc001clq.2; human.
DR CTD; 55929; -.
DR DisGeNET; 55929; -.
DR GeneCards; DMAP1; -.
DR HGNC; HGNC:18291; DMAP1.
DR HPA; ENSG00000178028; Low tissue specificity.
DR MIM; 605077; gene.
DR neXtProt; NX_Q9NPF5; -.
DR OpenTargets; ENSG00000178028; -.
DR PharmGKB; PA134927315; -.
DR VEuPathDB; HostDB:ENSG00000178028; -.
DR eggNOG; KOG2656; Eukaryota.
DR GeneTree; ENSGT00390000016466; -.
DR HOGENOM; CLU_018539_1_1_1; -.
DR InParanoid; Q9NPF5; -.
DR OMA; EKISWQW; -.
DR OrthoDB; 918816at2759; -.
DR PhylomeDB; Q9NPF5; -.
DR TreeFam; TF354261; -.
DR PathwayCommons; Q9NPF5; -.
DR Reactome; R-HSA-3214847; HATs acetylate histones.
DR SignaLink; Q9NPF5; -.
DR SIGNOR; Q9NPF5; -.
DR BioGRID-ORCS; 55929; 749 hits in 1105 CRISPR screens.
DR ChiTaRS; DMAP1; human.
DR EvolutionaryTrace; Q9NPF5; -.
DR GeneWiki; DMAP1; -.
DR GenomeRNAi; 55929; -.
DR Pharos; Q9NPF5; Tbio.
DR PRO; PR:Q9NPF5; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q9NPF5; protein.
DR Bgee; ENSG00000178028; Expressed in right adrenal gland cortex and 143 other tissues.
DR ExpressionAtlas; Q9NPF5; baseline and differential.
DR Genevisible; Q9NPF5; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0035267; C:NuA4 histone acetyltransferase complex; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0000786; C:nucleosome; IDA:ComplexPortal.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005657; C:replication fork; IEA:Ensembl.
DR GO; GO:0000812; C:Swr1 complex; IBA:GO_Central.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IDA:UniProtKB.
DR GO; GO:0003714; F:transcription corepressor activity; IBA:GO_Central.
DR GO; GO:0006306; P:DNA methylation; TAS:UniProtKB.
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; IDA:UniProtKB.
DR GO; GO:0043967; P:histone H4 acetylation; IDA:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; NAS:UniProtKB.
DR GO; GO:1905168; P:positive regulation of double-strand break repair via homologous recombination; IDA:ComplexPortal.
DR GO; GO:0042307; P:positive regulation of protein import into nucleus; IDA: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; IMP:ComplexPortal.
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 3D-structure; Activator; Chromatin regulator; Coiled coil; Cytoplasm;
KW Direct protein sequencing; Growth regulation; Isopeptide bond; Nucleus;
KW Phosphoprotein; Reference proteome; Repressor; Transcription;
KW Transcription regulation; Ubl conjugation.
FT CHAIN 1..467
FT /note="DNA methyltransferase 1-associated protein 1"
FT /id="PRO_0000079935"
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 404..467
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 445
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 448
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT CROSSLNK 27
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 214
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CONFLICT 135
FT /note="V -> E (in Ref. 4; CAB66592/CAL38490)"
FT /evidence="ECO:0000305"
FT CONFLICT 150
FT /note="D -> N (in Ref. 4; CAB66592/CAL38490)"
FT /evidence="ECO:0000305"
FT CONFLICT 171
FT /note="F -> L (in Ref. 10; CAD97886)"
FT /evidence="ECO:0000305"
FT CONFLICT 424
FT /note="T -> S (in Ref. 4; CAB66592/CAL38490)"
FT /evidence="ECO:0000305"
FT HELIX 140..146
FT /evidence="ECO:0007829|PDB:4IEJ"
FT HELIX 154..166
FT /evidence="ECO:0007829|PDB:4IEJ"
FT TURN 167..169
FT /evidence="ECO:0007829|PDB:4IEJ"
FT HELIX 171..177
FT /evidence="ECO:0007829|PDB:4IEJ"
FT TURN 180..182
FT /evidence="ECO:0007829|PDB:4IEJ"
FT HELIX 188..205
FT /evidence="ECO:0007829|PDB:4IEJ"
SQ SEQUENCE 467 AA; 52993 MW; 54500B252E076A29 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 AGVLGGPATP ASGPGPASAE
PAVTEPGLGP DPKDTIIDVV GAPLTPNSRK RRESASSSSS VKKAKKP
