[1]	NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND INTERACTION WITH DNMT1 AND TSG101. DOI=10.1038/77023; PubMed=10888872 [NCBI, ExPASy, EBI, Israel, Japan] 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; DOI=10.1093/dnares/7.1.65; PubMed=10718198 [NCBI, ExPASy, EBI, Israel, Japan] 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; DOI=10.1101/gr.GR1547R; PubMed=11230166 [NCBI, ExPASy, EBI, Israel, Japan] 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; DOI=10.1038/ng1285; PubMed=14702039 [NCBI, ExPASy, EBI, Israel, Japan] 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]. DOI=10.1038/nature04727; PubMed=16710414 [NCBI, ExPASy, EBI, Israel, Japan] 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 MRNA]. TISSUE=Placenta, and Skin; DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[8]	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 MASS SPECTROMETRY. DOI=10.1074/jbc.C300389200; PubMed=12963728 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[9]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 132-467. TISSUE=Colon endothelium; The German cDNA consortium; Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
[10]	FUNCTION, AND INTERACTION WITH ING1. DOI=10.1074/jbc.M311587200; PubMed=14665632 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[11]	FUNCTION, AND INTERACTION WITH DAXX. PubMed=14978102 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[12]	IDENTIFICATION IN NUA4 COMPLEX, IDENTIFICATION IN NUA4-RELATED SRCAP-CONTAINING COMPLEX, AND MASS SPECTROMETRY. DOI=10.1128/MCB.24.5.1884-1896.2004; PubMed=14966270 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[13]	REVIEW ON NUA4 COMPLEX. DOI=10.1016/j.gde.2004.02.009; PubMed=15196461 [NCBI, ExPASy, EBI, Israel, Japan] Doyon Y., Cote J.; "The highly conserved and multifunctional NuA4 HAT complex."; Curr. Opin. Genet. Dev. 14:147-154(2004).
[14]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-445, AND MASS SPECTROMETRY. TISSUE=Epithelium; DOI=10.1016/j.cell.2006.09.026; PubMed=17081983 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[15]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-445, AND MASS SPECTROMETRY. TISSUE=Epithelium; DOI=10.1038/nbt1240; PubMed=16964243 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[16]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-456, AND MASS SPECTROMETRY. TISSUE=Epithelium; DOI=10.1021/pr070152u; PubMed=17924679 [NCBI, ExPASy, EBI, Israel, Japan] Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.; "Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."; J. Proteome Res. 6:4150-4162(2007).

Comments

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 histone 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.
SUBUNIT: Component of the NuA4 histone acetyltransferase complex which contains the catalytic subunit HTATIP/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 and VPS72/YL1. Component of a NuA4-related complex which contains EP400, TRRAP/PAF400, SRCAP, BRD8/SMAP, EPC1, DMAP1/DNMAP1, RUVBL1/TIP49, RUVBL2, actin, ACTL6A/BAF53A, TCFL1/YL1 and YEATS4/GAS41. DMAP1 slso 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.
INTERACTION:
Q99816:TSG101; NbExp=1; IntAct=EBI-399105, EBI-346882;
SUBCELLULAR LOCATION: Nucleus. Note=Targeted to replication foci throughout S phase by DNMT1.
SIMILARITY: Contains 1 SANT domain.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

AF265228; AAF87079.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AL137200; CAB69910.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AB037846; BAA92663.1; ALT_INIT; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AL136657; CAB66592.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AM393614; CAL38490.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AK021605; BAB13854.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AL035417; CAI23197.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC002855; AAH02855.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC008053; AAH08053.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BX537895; CAD97886.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_001029195.1; -.
NP_001029196.1; -.
NP_061973.1; -.

UniGene

Hs.8008

3D structure databases

ModBase

Q9NPF5.

Protein-protein interaction databases

IntAct

Q9NPF5; -.

PTM databases

PhosphoSite

Q9NPF5; -.

Organism-specific databases

HIX0020213; -.

HGNC:18291; DMAP1.

605077; gene. [NCBI / EBI]

PA134927315; -.

Gene expression databases

CleanEx

HS_DMAP1; -.

GermOnline

ENSG00000178028; Homo sapiens.

Ontologies

GO:0005634;	Cellular component: nucleus (non-traceable author statement from UniProtKB).
GO:0003677;	Molecular function: DNA binding (inferred from electronic annotation from InterPro).
GO:0005515;	Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0016564;	Molecular function: transcription repressor activity (non-traceable author statement from UniProtKB).
GO:0016568;	Biological process: chromatin modification (inferred from electronic annotation from UniProtKB-KW).
GO:0006306;	Biological process: DNA methylation (traceable author statement from UniProtKB).
GO:0016481;	Biological process: negative regulation of transcription (non-traceable author statement from UniProtKB).
GO:0001558;	Biological process: regulation of cell growth (inferred from electronic annotation from UniProtKB-KW).
GO:0006355;	Biological process: regulation of transcription, DNA-dependent (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR008468; DMAP1.
IPR001005; SANT_DNA-bd.
Graphical view of domain structure.

Pfam

PF05499; DMAP1; 1.
Pfam graphical view of domain structure.

SMART

SM00717; SANT; 1.
SMART graphical view of domain structure.

PROSITE

PS51293; SANT; FALSE_NEG.
PROSITE graphical view of domain structure (profiles).

ProtoNet

Q9NPF5.

Genome annotation databases

Ensembl

ENSG00000178028; Homo sapiens. [Contig view]

GeneID

55929; -.

KEGG

hsa:55929; -.

Phylogenomic databases

HOVERGEN

Q9NPF5; -.

Other

NextBio

61337; -.

SOURCE

DMAP1; Homo sapiens.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Activator; Chromatin regulator; Coiled coil; Direct protein sequencing; Growth regulation; Nucleus; Phosphoprotein; Repressor; Transcription; Transcription regulation.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 467`	`467`	`DNA methyltransferase 1-associated protein 1.`	`PRO_0000079935`
`DOMAIN`	`149 199`	`51`	`SANT.`
`COILED`	`225 275`	`51`	`Potential.`
`COMPBIAS`	`454 460`	`7`	`Poly-Ser.`
`MOD_RES`	`445 445`		`Phosphothreonine.`
`MOD_RES`	`456 456`		`Phosphoserine.`
`CONFLICT`	`135 135`		`V -> E (in Ref. 4; CAB66592/CAL38490).`
`CONFLICT`	`150 150`		`D -> N (in Ref. 4; CAB66592/CAL38490).`
`CONFLICT`	`171 171`		`F -> L (in Ref. 9; CAD97886).`
`CONFLICT`	`424 424`		`T -> S (in Ref. 4; CAB66592/CAL38490).`

Sequence information

Length: 467 AA [This is the length of the unprocessed precursor]

Molecular weight: 52993 Da [This is the MW of the unprocessed precursor]

CRC64: 54500B252E076A29 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MATGADVRDI LELGGPEGDA ASGTISKKDI INPDKKKSKK SSETLTFKRP EGMHREVYAL 

        70         80         90        100        110        120 
LYSDKKDAPP LLPSDTGQGY RTVKAKLGSK KVRPWKWMPF TNPARKDGAM FFHWRRAAEE 

       130        140        150        160        170        180 
GKDYPFARFN KTVQVPVYSE QEYQLYLHDD AWTKAETDHL FDLSRRFDLR FVVIHDRYDH 

       190        200        210        220        230        240 
QQFKKRSVED LKERYYHICA KLANVRAVPG TDLKIPVFDA GHERRRKEQL ERLYNRTPEQ 

       250        260        270        280        290        300 
VAEEEYLLQE LRKIEARKKE REKRSQDLQK LITAADTTAE QRRTERKAPK KKLPQKKEAE 

       310        320        330        340        350        360 
KPAVPETAGI KFPDFKSAGV TLRSQRMKLP SSVGQKKIKA LEQMLLELGV ELSPTPTEEL 

       370        380        390        400        410        420 
VHMFNELRSD LVLLYELKQA CANCEYELQM LRHRHEALAR AGVLGGPATP ASGPGPASAE 

       430        440        450        460 
PAVTEPGLGP DPKDTIIDVV GAPLTPNSRK RRESASSSSS VKKAKKP

Q9NPF5 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools