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DNA methyltransferase 1-associated protein 1 (DNMAP1) (DNMT1-associated protein 1)

 DMAP1_HUMAN             Reviewed;         467 AA.
Q9NPF5; A8K001; D3DPY8; Q0JSM4; Q5TG41; Q7Z3H7; Q9H0S8; Q9P2C2;
21-FEB-2002, integrated into UniProtKB/Swiss-Prot.
01-OCT-2000, sequence version 1.
02-JUN-2021, entry version 199.
RecName: Full=DNA methyltransferase 1-associated protein 1;
Short=DNMAP1;
Short=DNMT1-associated protein 1;
Name=DMAP1; Synonyms=KIAA1425;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND INTERACTION WITH
DNMT1 AND TSG101.
PubMed=10888872; DOI=10.1038/77023;
Rountree M.R., Bachman K.E., Baylin S.B.;
"DNMT1 binds HDAC2 and a new co-repressor, DMAP1, to form a complex at
replication foci.";
Nat. Genet. 25:269-277(2000).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Rhodes S., Huckle E.;
Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
PubMed=10718198; DOI=10.1093/dnares/7.1.65;
Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.;
"Prediction of the coding sequences of unidentified human genes. XVI. The
complete sequences of 150 new cDNA clones from brain which code for large
proteins in vitro.";
DNA Res. 7:65-73(2000).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Fetal brain;
PubMed=11230166; DOI=10.1101/gr.gr1547r;
Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
Klein M., Poustka A.;
"Towards a catalog of human genes and proteins: sequencing and analysis of
500 novel complete protein coding human cDNAs.";
Genome Res. 11:422-435(2001).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Embryo;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
Hunkapiller M.W., Myers E.W., Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Placenta, and Skin;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project:
the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[9]
PROTEIN SEQUENCE OF 9-27; 56-66; 117-128; 237-252; 271-282; 369-378;
401-433 AND 434-449, IDENTIFICATION IN NUA4 COMPLEX, AND IDENTIFICATION BY
MASS SPECTROMETRY.
PubMed=12963728; DOI=10.1074/jbc.c300389200;
Cai Y., Jin J., Tomomori-Sato C., Sato S., Sorokina I., Parmely T.J.,
Conaway R.C., Conaway J.W.;
"Identification of new subunits of the multiprotein mammalian TRRAP/TIP60-
containing histone acetyltransferase complex.";
J. Biol. Chem. 278:42733-42736(2003).
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 132-467.
TISSUE=Colon endothelium;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[11]
REVIEW ON NUA4 COMPLEX.
PubMed=15196461; DOI=10.1016/j.gde.2004.02.009;
Doyon Y., Cote J.;
"The highly conserved and multifunctional NuA4 HAT complex.";
Curr. Opin. Genet. Dev. 14:147-154(2004).
[12]
FUNCTION, AND INTERACTION WITH ING1.
PubMed=14665632; DOI=10.1074/jbc.m311587200;
Xin H., Yoon H.-G., Singh P.B., Wong J., Qin J.;
"Components of a pathway maintaining histone modification and
heterochromatin protein 1 binding at the pericentric heterochromatin in
mammalian cells.";
J. Biol. Chem. 279:9539-9546(2004).
[13]
FUNCTION, AND INTERACTION WITH DAXX.
PubMed=14978102; DOI=10.4049/jimmunol.172.5.2985;
Muromoto R., Sugiyama K., Takachi A., Imoto S., Sato N., Yamamoto T.,
Oritani K., Shimoda K., Matsuda T.;
"Physical and functional interactions between Daxx and DNA
methyltransferase 1-associated protein, DMAP1.";
J. Immunol. 172:2985-2993(2004).
[14]
FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN NUA4
COMPLEX, AND IDENTIFICATION IN NUA4-RELATED SRCAP-CONTAINING COMPLEX.
PubMed=14966270; DOI=10.1128/mcb.24.5.1884-1896.2004;
Doyon Y., Selleck W., Lane W.S., Tan S., Cote J.;
"Structural and functional conservation of the NuA4 histone
acetyltransferase complex from yeast to humans.";
Mol. Cell. Biol. 24:1884-1896(2004).
[15]
FUNCTION, INTERACTION WITH URI1, AND SUBCELLULAR LOCATION.
PubMed=15367675; DOI=10.1128/mcb.24.19.8556-8566.2004;
Delgermaa L., Hayashi N., Dorjsuren D., Nomura T., Thuy le T.T.,
Murakami S.;
"Subcellular localization of RPB5-mediating protein and its putative
functional partner.";
Mol. Cell. Biol. 24:8556-8566(2004).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-445, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in signaling
networks.";
Cell 127:635-648(2006).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-445, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=16964243; DOI=10.1038/nbt1240;
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
"A probability-based approach for high-throughput protein phosphorylation
analysis and site localization.";
Nat. Biotechnol. 24:1285-1292(2006).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-445, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of the
kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[19]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-445 AND SER-448, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-445, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
"Quantitative phosphoproteomics reveals widespread full phosphorylation
site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[22]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-445, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
"System-wide temporal characterization of the proteome and phosphoproteome
of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[23]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-445, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[24]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-445, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
phosphoproteome.";
J. Proteomics 96:253-262(2014).
[25]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-27 AND LYS-214, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-modification
with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[26]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 121-212.
Structural genomics consortium (SGC);
"SANT domain of human DNA methyltransferase 1 associated protein 1.";
Submitted (JUN-2009) to the PDB data bank.
-!- FUNCTION: Involved in transcription repression and activation. Its
interaction with HDAC2 may provide a mechanism for histone
deacetylation in heterochromatin following replication of DNA at late
firing origins. Can also repress transcription independently of histone
deacetylase activity. May specifically potentiate DAXX-mediated
repression of glucocorticoid receptor-dependent transcription.
Component of the NuA4 histone acetyltransferase (HAT) complex which is
involved in transcriptional activation of select genes principally by
acetylation of nucleosomal histones H4 and H2A. This modification may
both alter nucleosome - DNA interactions and promote interaction of the
modified histones with other proteins which positively regulate
transcription. This complex may be required for the activation of
transcriptional programs associated with oncogene and proto-oncogene
mediated growth induction, tumor suppressor mediated growth arrest and
replicative senescence, apoptosis, and DNA repair. NuA4 may also play a
direct role in DNA repair when recruited to sites of DNA damage.
Participates in the nuclear localization of URI1 and increases its
transcriptional corepressor activity. {ECO:0000269|PubMed:14665632,
ECO:0000269|PubMed:14966270, ECO:0000269|PubMed:14978102,
ECO:0000269|PubMed:15367675}.
-!- SUBUNIT: Component of the NuA4 histone acetyltransferase complex which
contains the catalytic subunit KAT5/TIP60 and the subunits EP400,
TRRAP/PAF400, BRD8/SMAP, EPC1, DMAP1/DNMAP1, RUVBL1/TIP49, RUVBL2,
ING3, actin, ACTL6A/BAF53A, MORF4L1/MRG15, MORF4L2/MRGX, MRGBP,
YEATS4/GAS41, VPS72/YL1 and MEAF6. Component of a NuA4-related complex
which contains EP400, TRRAP/PAF400, SRCAP, BRD8/SMAP, EPC1,
DMAP1/DNMAP1, RUVBL1/TIP49, RUVBL2, actin, ACTL6A/BAF53A, VPS72 and
YEATS4/GAS41. DMAP1 also forms a complex with DNMT1 and HDAC2.
Throughout S phase it interacts directly with the N-terminus of DNMT1,
which serves to recruit DMAP1 to replication foci. DMAP1 interacts with
ING1, a component of the mSin3A transcription repressor complex,
although this interaction is not required for recruitment of ING1 to
heterochromatin. Interacts directly with the transcriptional
corepressor TSG101. Interacts with the pro-apoptotic protein DAXX.
Interacts with URI1. {ECO:0000269|PubMed:10888872,
ECO:0000269|PubMed:12963728, ECO:0000269|PubMed:14665632,
ECO:0000269|PubMed:14966270, ECO:0000269|PubMed:14978102,
ECO:0000269|PubMed:15367675}.
-!- INTERACTION:
Q9NPF5; P53365: ARFIP2; NbExp=3; IntAct=EBI-399105, EBI-638194;
Q9NPF5; Q13515: BFSP2; NbExp=5; IntAct=EBI-399105, EBI-10229433;
Q9NPF5; Q8TAB5: C1orf216; NbExp=5; IntAct=EBI-399105, EBI-747505;
Q9NPF5; Q8TD31-3: CCHCR1; NbExp=3; IntAct=EBI-399105, EBI-10175300;
Q9NPF5; Q96GN5: CDCA7L; NbExp=3; IntAct=EBI-399105, EBI-5278764;
Q9NPF5; Q9UER7: DAXX; NbExp=3; IntAct=EBI-399105, EBI-77321;
Q9NPF5; Q8IYI6: EXOC8; NbExp=3; IntAct=EBI-399105, EBI-742102;
Q9NPF5; O95995: GAS8; NbExp=3; IntAct=EBI-399105, EBI-1052570;
Q9NPF5; Q9BRT9: GINS4; NbExp=3; IntAct=EBI-399105, EBI-747500;
Q9NPF5; O75031: HSF2BP; NbExp=3; IntAct=EBI-399105, EBI-7116203;
Q9NPF5; O95678: KRT75; NbExp=3; IntAct=EBI-399105, EBI-2949715;
Q9NPF5; P20700: LMNB1; NbExp=3; IntAct=EBI-399105, EBI-968218;
Q9NPF5; Q6UWE0: LRSAM1; NbExp=3; IntAct=EBI-399105, EBI-720984;
Q9NPF5; Q9NYP9: MIS18A; NbExp=3; IntAct=EBI-399105, EBI-1104552;
Q9NPF5; Q9UBU8-2: MORF4L1; NbExp=4; IntAct=EBI-399105, EBI-10288852;
Q9NPF5; Q9ULW6: NAP1L2; NbExp=3; IntAct=EBI-399105, EBI-3911716;
Q9NPF5; O60925: PFDN1; NbExp=3; IntAct=EBI-399105, EBI-356919;
Q9NPF5; Q4G0R1: PIBF1; NbExp=3; IntAct=EBI-399105, EBI-14066006;
Q9NPF5; P0C264: SBK3; NbExp=3; IntAct=EBI-399105, EBI-17181801;
Q9NPF5; P51687: SUOX; NbExp=3; IntAct=EBI-399105, EBI-3921347;
Q9NPF5; Q8N8B7-2: TCEANC; NbExp=3; IntAct=EBI-399105, EBI-11955057;
Q9NPF5; Q9BT92: TCHP; NbExp=5; IntAct=EBI-399105, EBI-740781;
Q9NPF5; Q86UE8: TLK2; NbExp=3; IntAct=EBI-399105, EBI-1047967;
Q9NPF5; P19474: TRIM21; NbExp=3; IntAct=EBI-399105, EBI-81290;
Q9NPF5; Q3SY00: TSGA10IP; NbExp=3; IntAct=EBI-399105, EBI-10241197;
Q9NPF5; P40222: TXLNA; NbExp=3; IntAct=EBI-399105, EBI-359793;
Q9NPF5; Q8N3L3: TXLNB; NbExp=3; IntAct=EBI-399105, EBI-6116822;
-!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=Targeted to replication
foci throughout S phase by DNMT1.
-!- SEQUENCE CAUTION:
Sequence=BAA92663.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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EMBL; AF265228; AAF87079.1; -; mRNA.
EMBL; AL137200; CAB69910.1; -; mRNA.
EMBL; AB037846; BAA92663.1; ALT_INIT; mRNA.
EMBL; AL136657; CAB66592.1; -; mRNA.
EMBL; AM393614; CAL38490.1; -; mRNA.
EMBL; AK021605; BAB13854.1; -; mRNA.
EMBL; AK289366; BAF82055.1; -; mRNA.
EMBL; AL035417; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471059; EAX07046.1; -; Genomic_DNA.
EMBL; CH471059; EAX07047.1; -; Genomic_DNA.
EMBL; CH471059; EAX07048.1; -; Genomic_DNA.
EMBL; CH471059; EAX07051.1; -; Genomic_DNA.
EMBL; BC002855; AAH02855.1; -; mRNA.
EMBL; BC008053; AAH08053.1; -; mRNA.
EMBL; BX537895; CAD97886.1; -; mRNA.
CCDS; CCDS509.1; -.
RefSeq; NP_001029195.1; NM_001034023.1.
RefSeq; NP_001029196.1; NM_001034024.1.
RefSeq; NP_061973.1; NM_019100.4.
RefSeq; XP_016857297.1; XM_017001808.1.
PDB; 3HM5; X-ray; 1.80 A; A=121-212.
PDB; 4IEJ; X-ray; 1.45 A; A=121-212.
PDBsum; 3HM5; -.
PDBsum; 4IEJ; -.
SMR; Q9NPF5; -.
BioGRID; 121004; 113.
ComplexPortal; CPX-974; SRCAP histone exchanging complex.
ComplexPortal; CPX-978; NuA4 histone acetyltransferase complex.
CORUM; Q9NPF5; -.
IntAct; Q9NPF5; 76.
MINT; Q9NPF5; -.
STRING; 9606.ENSP00000361363; -.
iPTMnet; Q9NPF5; -.
PhosphoSitePlus; Q9NPF5; -.
BioMuta; DMAP1; -.
DMDM; 20138031; -.
EPD; Q9NPF5; -.
jPOST; Q9NPF5; -.
MassIVE; Q9NPF5; -.
MaxQB; Q9NPF5; -.
PaxDb; Q9NPF5; -.
PeptideAtlas; Q9NPF5; -.
PRIDE; Q9NPF5; -.
ProteomicsDB; 81985; -.
Antibodypedia; 18433; 277 antibodies.
DNASU; 55929; -.
Ensembl; ENST00000315913; ENSP00000312697; ENSG00000178028.
Ensembl; ENST00000361745; ENSP00000354697; ENSG00000178028.
Ensembl; ENST00000372289; ENSP00000361363; ENSG00000178028.
GeneID; 55929; -.
KEGG; hsa:55929; -.
UCSC; uc001clq.2; human.
CTD; 55929; -.
DisGeNET; 55929; -.
GeneCards; DMAP1; -.
HGNC; HGNC:18291; DMAP1.
HPA; ENSG00000178028; Low tissue specificity.
MIM; 605077; gene.
neXtProt; NX_Q9NPF5; -.
OpenTargets; ENSG00000178028; -.
PharmGKB; PA134927315; -.
VEuPathDB; HostDB:ENSG00000178028.13; -.
eggNOG; KOG2656; Eukaryota.
GeneTree; ENSGT00390000016466; -.
HOGENOM; CLU_018539_1_1_1; -.
InParanoid; Q9NPF5; -.
OMA; PTEDICT; -.
OrthoDB; 918816at2759; -.
PhylomeDB; Q9NPF5; -.
TreeFam; TF354261; -.
PathwayCommons; Q9NPF5; -.
Reactome; R-HSA-3214847; HATs acetylate histones.
BioGRID-ORCS; 55929; 734 hits in 1016 CRISPR screens.
ChiTaRS; DMAP1; human.
EvolutionaryTrace; Q9NPF5; -.
GeneWiki; DMAP1; -.
GenomeRNAi; 55929; -.
Pharos; Q9NPF5; Tbio.
PRO; PR:Q9NPF5; -.
Proteomes; UP000005640; Chromosome 1.
RNAct; Q9NPF5; protein.
Bgee; ENSG00000178028; Expressed in right adrenal gland cortex and 184 other tissues.
ExpressionAtlas; Q9NPF5; baseline and differential.
Genevisible; Q9NPF5; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0035267; C:NuA4 histone acetyltransferase complex; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0005657; C:replication fork; IEA:Ensembl.
GO; GO:0000812; C:Swr1 complex; IBA:GO_Central.
GO; GO:0001103; F:RNA polymerase II repressing transcription factor binding; IDA:UniProtKB.
GO; GO:0003714; F:transcription corepressor activity; IBA:GO_Central.
GO; GO:0006306; P:DNA methylation; TAS:UniProtKB.
GO; GO:0006281; P:DNA repair; IEA:InterPro.
GO; GO:0043486; P:histone exchange; IBA:GO_Central.
GO; GO:0043968; P:histone H2A acetylation; IDA:UniProtKB.
GO; GO:0043967; P:histone H4 acetylation; IDA:UniProtKB.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:UniProtKB.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; NAS:UniProtKB.
GO; GO:0042307; P:positive regulation of protein import into nucleus; IDA:UniProtKB.
GO; GO:0040008; P:regulation of growth; IEA:UniProtKB-KW.
GO; GO:0045471; P:response to ethanol; IEA:Ensembl.
InterPro; IPR032563; DAMP1_SANT-like.
InterPro; IPR008468; DMAP1.
InterPro; IPR027109; Swc4/Dmap1.
PANTHER; PTHR12855; PTHR12855; 1.
Pfam; PF05499; DMAP1; 1.
Pfam; PF16282; SANT_DAMP1_like; 1.
1: Evidence at protein level;
3D-structure; Activator; Chromatin regulator; Coiled coil; Cytoplasm;
Direct protein sequencing; Growth regulation; Isopeptide bond; Nucleus;
Phosphoprotein; Reference proteome; Repressor; Transcription;
Transcription regulation; Ubl conjugation.
CHAIN 1..467
/note="DNA methyltransferase 1-associated protein 1"
/id="PRO_0000079935"
DOMAIN 149..199
/note="SANT"
REGION 1..48
/note="Disordered"
/evidence="ECO:0000256|SAM:MobiDB-lite"
REGION 258..305
/note="Disordered"
/evidence="ECO:0000256|SAM:MobiDB-lite"
REGION 404..467
/note="Disordered"
/evidence="ECO:0000256|SAM:MobiDB-lite"
COILED 225..275
/evidence="ECO:0000255"
COMPBIAS 29..48
/note="Basic and acidic residues"
/evidence="ECO:0000256|SAM:MobiDB-lite"
COMPBIAS 279..304
/note="Basic and acidic residues"
/evidence="ECO:0000256|SAM:MobiDB-lite"
MOD_RES 445
/note="Phosphothreonine"
/evidence="ECO:0007744|PubMed:16964243,
ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18691976,
ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
ECO:0007744|PubMed:24275569"
MOD_RES 448
/note="Phosphoserine"
/evidence="ECO:0007744|PubMed:19690332"
CROSSLNK 27
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO2)"
/evidence="ECO:0007744|PubMed:28112733"
CROSSLNK 214
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO2)"
/evidence="ECO:0007744|PubMed:28112733"
CONFLICT 135
/note="V -> E (in Ref. 4; CAB66592/CAL38490)"
/evidence="ECO:0000305"
CONFLICT 150
/note="D -> N (in Ref. 4; CAB66592/CAL38490)"
/evidence="ECO:0000305"
CONFLICT 171
/note="F -> L (in Ref. 10; CAD97886)"
/evidence="ECO:0000305"
CONFLICT 424
/note="T -> S (in Ref. 4; CAB66592/CAL38490)"
/evidence="ECO:0000305"
HELIX 140..146
/evidence="ECO:0007829|PDB:4IEJ"
HELIX 154..166
/evidence="ECO:0007829|PDB:4IEJ"
TURN 167..169
/evidence="ECO:0007829|PDB:4IEJ"
HELIX 171..177
/evidence="ECO:0007829|PDB:4IEJ"
TURN 180..182
/evidence="ECO:0007829|PDB:4IEJ"
HELIX 188..205
/evidence="ECO:0007829|PDB:4IEJ"
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


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WP210: Cytoplasmic Ribosomal Proteins
WP813: G Protein Signaling Pathways
WP1624: Bacterial secretion system
WP2203: TSLP Signaling Pathway
WP1689: Porphyrin and chlorophyll metabolism
WP1693: Purine metabolism
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Related Genes :
[DNMT1 AIM CXXC9 DNMT] DNA (cytosine-5)-methyltransferase 1 (Dnmt1) (EC 2.1.1.37) (CXXC-type zinc finger protein 9) (DNA methyltransferase HsaI) (DNA MTase HsaI) (M.HsaI) (MCMT)
[Dnmt1 Dnmt Met1 Uim] DNA (cytosine-5)-methyltransferase 1 (Dnmt1) (Met-1) (EC 2.1.1.37) (DNA methyltransferase MmuI) (DNA MTase MmuI) (M.MmuI) (MCMT)
[Dnmt1] DNA (cytosine-5)-methyltransferase 1 (Dnmt1) (EC 2.1.1.37) (DNA MTase RnoIP) (M.RnoIP) (DNA methyltransferase I) (MCMT)
[DNMT1 AIM DNMT] DNA (cytosine-5)-methyltransferase 1 (Dnmt1) (EC 2.1.1.37) (DNA methyltransferase GgaI) (DNA MTase GgaI) (M.GgaI) (MCMT)
[DNMT1] DNA (cytosine-5)-methyltransferase 1 (Dnmt1) (EC 2.1.1.37)
[Setdb1 Eset Kiaa0067] Histone-lysine N-methyltransferase SETDB1 (EC 2.1.1.366) (ERG-associated protein with SET domain) (ESET) (SET domain bifurcated 1)
[DNMT3A] DNA (cytosine-5)-methyltransferase 3A (Dnmt3a) (EC 2.1.1.37) (Cysteine methyltransferase DNMT3A) (EC 2.1.1.-) (DNA methyltransferase HsaIIIA) (DNA MTase HsaIIIA) (M.HsaIIIA)
[DNMT3B] DNA (cytosine-5)-methyltransferase 3B (Dnmt3b) (EC 2.1.1.37) (DNA methyltransferase HsaIIIB) (DNA MTase HsaIIIB) (M.HsaIIIB)
[dim-5 29E8.110 NCU04402] Histone-lysine N-methyltransferase, H3 lysine-9 specific dim-5 (EC 2.1.1.355) (Histone H3-K9 methyltransferase dim-5) (H3-K9-HMTase dim-5) (HKMT)
[ORF1ab orf1ab] 2'-O-methyltransferase (EC 2.7.7.48) (EC 3.4.19.12) (EC 3.4.22.69) (EC 3.6.4.12) (EC 3.6.4.13) (3C-like proteinase) (Growth factor-like peptide) (Guanine-N7 methyltransferase) (Helicase) (Host translation inhibitor nsp1) (Leader protein) (NendoU) (Non-structural protein 10) (Non-structural protein 2) (Non-structural protein 3) (Non-structural protein 4) (Non-structural protein 6) (Non-structural protein 7) (Non-structural protein 8) (Non-structural protein 9) (ORF1ab polyprotein) (Papain-like proteinase) (RNA-directed RNA polymerase) (Replicase polyprotein 1ab) (Uridylate-specific endoribonuclease) (p65 homolog)
[SETDB1 ESET KIAA0067 KMT1E] Histone-lysine N-methyltransferase SETDB1 (EC 2.1.1.366) (ERG-associated protein with SET domain) (ESET) (Histone H3-K9 methyltransferase 4) (H3-K9-HMTase 4) (Lysine N-methyltransferase 1E) (SET domain bifurcated 1)
[EHMT2 BAT8 C6orf30 G9A KMT1C NG36] Histone-lysine N-methyltransferase EHMT2 (EC 2.1.1.-) (Euchromatic histone-lysine N-methyltransferase 2) (HLA-B-associated transcript 8) (Histone H3-K9 methyltransferase 3) (H3-K9-HMTase 3) (Lysine N-methyltransferase 1C) (Protein G9a)
[RUVBL1 INO80H NMP238 TIP49 TIP49A] RuvB-like 1 (EC 3.6.4.12) (49 kDa TATA box-binding protein-interacting protein) (49 kDa TBP-interacting protein) (54 kDa erythrocyte cytosolic protein) (ECP-54) (INO80 complex subunit H) (Nuclear matrix protein 238) (NMP 238) (Pontin 52) (TIP49a) (TIP60-associated protein 54-alpha) (TAP54-alpha)
[orf1ab ORF1ab] 2'-O-methyltransferase (EC 2.7.7.48) (EC 3.4.19.12) (EC 3.4.22.69) (EC 3.6.4.12) (EC 3.6.4.13) (3C-like proteinase) (Growth factor-like peptide) (Guanine-N7 methyltransferase) (Helicase) (Host translation inhibitor nsp1) (Leader protein) (NendoU) (Non-structural protein 10) (Non-structural protein 2) (Non-structural protein 3) (Non-structural protein 4) (Non-structural protein 6) (Non-structural protein 7) (Non-structural protein 8) (Non-structural protein 9) (ORF1ab polyprotein) (Papain-like proteinase) (RNA-directed RNA polymerase) (Replicase polyprotein 1ab) (Uridylate-specific endoribonuclease) (p65 homolog)
[EZH2 KMT6] Histone-lysine N-methyltransferase EZH2 (EC 2.1.1.356) (ENX-1) (Enhancer of zeste homolog 2) (Lysine N-methyltransferase 6)
[Ehmt2 Bat8 G9a Ng36] Histone-lysine N-methyltransferase EHMT2 (EC 2.1.1.-) (Euchromatic histone-lysine N-methyltransferase 2) (HLA-B-associated transcript 8) (Histone H3-K9 methyltransferase 3) (H3-K9-HMTase 3) (Protein G9a)
[SETD7 KIAA1717 KMT7 SET7 SET9] Histone-lysine N-methyltransferase SETD7 (EC 2.1.1.364) (Histone H3-K4 methyltransferase SETD7) (H3-K4-HMTase SETD7) (Lysine N-methyltransferase 7) (SET domain-containing protein 7) (SET7/9)
[Ezh2 Enx1h] Histone-lysine N-methyltransferase EZH2 (EC 2.1.1.356) (ENX-1) (Enhancer of zeste homolog 2)
[ACTL6A BAF53 BAF53A INO80K] Actin-like protein 6A (53 kDa BRG1-associated factor A) (Actin-related protein Baf53a) (ArpNbeta) (BRG1-associated factor 53A) (BAF53A) (INO80 complex subunit K)
[Actl6a Actl6 Baf53a] Actin-like protein 6A (53 kDa BRG1-associated factor A) (Actin-related protein Baf53a) (BRG1-associated factor 53A) (BAF53A)
[YEATS4 GAS41] YEATS domain-containing protein 4 (Glioma-amplified sequence 41) (Gas41) (NuMA-binding protein 1) (NuBI-1) (NuBI1)
[SUV39H1 KMT1A SUV39H] Histone-lysine N-methyltransferase SUV39H1 (EC 2.1.1.355) (Histone H3-K9 methyltransferase 1) (H3-K9-HMTase 1) (Lysine N-methyltransferase 1A) (Position-effect variegation 3-9 homolog) (Suppressor of variegation 3-9 homolog 1) (Su(var)3-9 homolog 1)
[ORF1ab orf1ab] 2'-O-methyltransferase (EC 2.7.7.48) (EC 3.4.19.12) (EC 3.4.22.69) (EC 3.6.4.12) (EC 3.6.4.13) (3C-like proteinase) (Growth factor-like peptide) (Guanine-N7 methyltransferase) (Helicase) (Host translation inhibitor nsp1) (Leader protein) (NendoU) (Non-structural protein 10) (Non-structural protein 2) (Non-structural protein 3) (Non-structural protein 4) (Non-structural protein 6) (Non-structural protein 7) (Non-structural protein 8) (Non-structural protein 9) (ORF1ab polyprotein) (Papain-like proteinase) (RNA-directed RNA polymerase) (Replicase polyprotein 1ab) (Uridylate-specific endoribonuclease) (p65 homolog)
[SIRT1 SIR2L1] NAD-dependent protein deacetylase sirtuin-1 (hSIRT1) (EC 2.3.1.286) (NAD-dependent protein deacylase sirtuin-1) (EC 2.3.1.-) (Regulatory protein SIR2 homolog 1) (SIR2-like protein 1) (hSIR2) [Cleaved into: SirtT1 75 kDa fragment (75SirT1)]
[MORF4L1 MRG15 FWP006 HSPC008 HSPC061 PP368] Mortality factor 4-like protein 1 (MORF-related gene 15 protein) (Protein MSL3-1) (Transcription factor-like protein MRG15)
[KAT5 HTATIP TIP60] Histone acetyltransferase KAT5 (EC 2.3.1.48) (60 kDa Tat-interactive protein) (Tip60) (Histone acetyltransferase HTATIP) (HIV-1 Tat interactive protein) (Lysine acetyltransferase 5) (cPLA(2)-interacting protein)
[pep NCU02549] Mitochondrial-processing peptidase subunit beta (EC 3.4.24.64) (Beta-MPP) (Complex III subunit I) (Core protein I) (Cytochrome b-c1 complex subunit 1, mitochondrial) (Processing enhancing protein) (Ubiquinol-cytochrome c oxidoreductase core protein 1) (Ubiquinol-cytochrome c reductase complex 50 kDa protein)
[Uhrf1 Np95] E3 ubiquitin-protein ligase UHRF1 (EC 2.3.2.27) (Nuclear protein 95) (Nuclear zinc finger protein Np95) (RING-type E3 ubiquitin transferase UHRF1) (Ubiquitin-like PHD and RING finger domain-containing protein 1) (mUhrf1) (Ubiquitin-like-containing PHD and RING finger domains protein 1)
[stk-1 bur1 B20D17.070 NCU01435] Serine/threonine-protein kinase bur1 (EC 2.7.11.22) (EC 2.7.11.23) (Serine-threonine kinase 1)
[Sirt1 Sir2l1] NAD-dependent protein deacetylase sirtuin-1 (EC 2.3.1.286) (NAD-dependent protein deacylase sirtuin-1) (EC 2.3.1.-) (Regulatory protein SIR2 homolog 1) (SIR2-like protein 1) (SIR2alpha) (Sir2) (mSIR2a) [Cleaved into: SirtT1 75 kDa fragment (75SirT1)]

Bibliography :