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Protein

DNA methyltransferase 1-associated protein 1

Gene

DMAP1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.4 Publications

GO - Molecular functioni

  1. chromatin binding Source: InterPro
  2. RNA polymerase II repressing transcription factor binding Source: UniProtKB
  3. transcription corepressor activity Source: Ensembl

GO - Biological processi

  1. chromatin organization Source: Reactome
  2. chromatin remodeling Source: InterPro
  3. DNA methylation Source: UniProtKB
  4. DNA repair Source: InterPro
  5. histone H2A acetylation Source: UniProtKB
  6. histone H4 acetylation Source: UniProtKB
  7. negative regulation of transcription, DNA-templated Source: UniProtKB
  8. negative regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  9. positive regulation of transcription factor import into nucleus Source: UniProtKB
  10. regulation of growth Source: UniProtKB-KW
  11. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Activator, Chromatin regulator, Repressor

Keywords - Biological processi

Growth regulation, Transcription, Transcription regulation

Enzyme and pathway databases

ReactomeiREACT_264245. HATs acetylate histones.

Names & Taxonomyi

Protein namesi
Recommended name:
DNA methyltransferase 1-associated protein 1
Short name:
DNMAP1
Short name:
DNMT1-associated protein 1
Gene namesi
Name:DMAP1
Synonyms:KIAA1425
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:18291. DMAP1.

Subcellular locationi

Nucleus. Cytoplasm
Note: Targeted to replication foci throughout S phase by DNMT1.

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. NuA4 histone acetyltransferase complex Source: UniProtKB
  3. nucleoplasm Source: Reactome
  4. nucleus Source: UniProtKB
  5. replication fork Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134927315.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 467467DNA methyltransferase 1-associated protein 1PRO_0000079935Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei445 – 4451Phosphothreonine7 Publications
Modified residuei448 – 4481Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9NPF5.
PaxDbiQ9NPF5.
PRIDEiQ9NPF5.

PTM databases

PhosphoSiteiQ9NPF5.

Expressioni

Gene expression databases

BgeeiQ9NPF5.
CleanExiHS_DMAP1.
ExpressionAtlasiQ9NPF5. baseline and differential.
GenevestigatoriQ9NPF5.

Organism-specific databases

HPAiCAB033018.

Interactioni

Subunit structurei

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 URI1.6 Publications

Protein-protein interaction databases

BioGridi121004. 51 interactions.
IntActiQ9NPF5. 13 interactions.
MINTiMINT-4719752.
STRINGi9606.ENSP00000312697.

Structurei

Secondary structure

1
467
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi140 – 1467Combined sources
Helixi154 – 16613Combined sources
Turni167 – 1693Combined sources
Helixi171 – 1777Combined sources
Turni180 – 1823Combined sources
Helixi188 – 20518Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3HM5X-ray1.80A121-212[»]
4IEJX-ray1.45A121-212[»]
ProteinModelPortaliQ9NPF5.
SMRiQ9NPF5. Positions 133-207.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9NPF5.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini149 – 19951SANTAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili225 – 27551Sequence AnalysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi454 – 4607Poly-Ser

Sequence similaritiesi

Contains 1 SANT domain.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiNOG298520.
GeneTreeiENSGT00390000016466.
HOVERGENiHBG051364.
InParanoidiQ9NPF5.
KOiK11324.
OMAiSNPARND.
PhylomeDBiQ9NPF5.
TreeFamiTF354261.

Family and domain databases

InterProiIPR008468. DMAP1.
IPR001005. SANT/Myb.
IPR027109. Swc4/Dmap1.
[Graphical view]
PANTHERiPTHR12855. PTHR12855. 1 hit.
PfamiPF05499. DMAP1. 1 hit.
[Graphical view]
ProDomiPD492828. DMAP1. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM00717. SANT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9NPF5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MATGADVRDI LELGGPEGDA ASGTISKKDI INPDKKKSKK SSETLTFKRP
60 70 80 90 100
EGMHREVYAL LYSDKKDAPP LLPSDTGQGY RTVKAKLGSK KVRPWKWMPF
110 120 130 140 150
TNPARKDGAM FFHWRRAAEE GKDYPFARFN KTVQVPVYSE QEYQLYLHDD
160 170 180 190 200
AWTKAETDHL FDLSRRFDLR FVVIHDRYDH QQFKKRSVED LKERYYHICA
210 220 230 240 250
KLANVRAVPG TDLKIPVFDA GHERRRKEQL ERLYNRTPEQ VAEEEYLLQE
260 270 280 290 300
LRKIEARKKE REKRSQDLQK LITAADTTAE QRRTERKAPK KKLPQKKEAE
310 320 330 340 350
KPAVPETAGI KFPDFKSAGV TLRSQRMKLP SSVGQKKIKA LEQMLLELGV
360 370 380 390 400
ELSPTPTEEL VHMFNELRSD LVLLYELKQA CANCEYELQM LRHRHEALAR
410 420 430 440 450
AGVLGGPATP ASGPGPASAE PAVTEPGLGP DPKDTIIDVV GAPLTPNSRK
460
RRESASSSSS VKKAKKP
Length:467
Mass (Da):52,993
Last modified:September 30, 2000 - v1
Checksum:i54500B252E076A29
GO

Sequence cautioni

The sequence BAA92663.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti135 – 1351V → E in CAB66592 (PubMed:11230166).Curated
Sequence conflicti135 – 1351V → E in CAL38490 (PubMed:11230166).Curated
Sequence conflicti150 – 1501D → N in CAB66592 (PubMed:11230166).Curated
Sequence conflicti150 – 1501D → N in CAL38490 (PubMed:11230166).Curated
Sequence conflicti171 – 1711F → L in CAD97886 (PubMed:17974005).Curated
Sequence conflicti424 – 4241T → S in CAB66592 (PubMed:11230166).Curated
Sequence conflicti424 – 4241T → S in CAL38490 (PubMed:11230166).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF265228 mRNA. Translation: AAF87079.1.
AL137200 mRNA. Translation: CAB69910.1.
AB037846 mRNA. Translation: BAA92663.1. Different initiation.
AL136657 mRNA. Translation: CAB66592.1.
AM393614 mRNA. Translation: CAL38490.1.
AK021605 mRNA. Translation: BAB13854.1.
AK289366 mRNA. Translation: BAF82055.1.
AL035417 Genomic DNA. Translation: CAI23197.1.
CH471059 Genomic DNA. Translation: EAX07046.1.
CH471059 Genomic DNA. Translation: EAX07047.1.
CH471059 Genomic DNA. Translation: EAX07048.1.
CH471059 Genomic DNA. Translation: EAX07051.1.
BC002855 mRNA. Translation: AAH02855.1.
BC008053 mRNA. Translation: AAH08053.1.
BX537895 mRNA. Translation: CAD97886.1.
CCDSiCCDS509.1.
RefSeqiNP_001029195.1. NM_001034023.1.
NP_001029196.1. NM_001034024.1.
NP_061973.1. NM_019100.4.
UniGeneiHs.8008.

Genome annotation databases

EnsembliENST00000315913; ENSP00000312697; ENSG00000178028.
ENST00000361745; ENSP00000354697; ENSG00000178028.
ENST00000372289; ENSP00000361363; ENSG00000178028.
GeneIDi55929.
KEGGihsa:55929.
UCSCiuc001clq.1. human.

Polymorphism databases

DMDMi20138031.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF265228 mRNA. Translation: AAF87079.1.
AL137200 mRNA. Translation: CAB69910.1.
AB037846 mRNA. Translation: BAA92663.1. Different initiation.
AL136657 mRNA. Translation: CAB66592.1.
AM393614 mRNA. Translation: CAL38490.1.
AK021605 mRNA. Translation: BAB13854.1.
AK289366 mRNA. Translation: BAF82055.1.
AL035417 Genomic DNA. Translation: CAI23197.1.
CH471059 Genomic DNA. Translation: EAX07046.1.
CH471059 Genomic DNA. Translation: EAX07047.1.
CH471059 Genomic DNA. Translation: EAX07048.1.
CH471059 Genomic DNA. Translation: EAX07051.1.
BC002855 mRNA. Translation: AAH02855.1.
BC008053 mRNA. Translation: AAH08053.1.
BX537895 mRNA. Translation: CAD97886.1.
CCDSiCCDS509.1.
RefSeqiNP_001029195.1. NM_001034023.1.
NP_001029196.1. NM_001034024.1.
NP_061973.1. NM_019100.4.
UniGeneiHs.8008.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3HM5X-ray1.80A121-212[»]
4IEJX-ray1.45A121-212[»]
ProteinModelPortaliQ9NPF5.
SMRiQ9NPF5. Positions 133-207.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi121004. 51 interactions.
IntActiQ9NPF5. 13 interactions.
MINTiMINT-4719752.
STRINGi9606.ENSP00000312697.

PTM databases

PhosphoSiteiQ9NPF5.

Polymorphism databases

DMDMi20138031.

Proteomic databases

MaxQBiQ9NPF5.
PaxDbiQ9NPF5.
PRIDEiQ9NPF5.

Protocols and materials databases

DNASUi55929.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000315913; ENSP00000312697; ENSG00000178028.
ENST00000361745; ENSP00000354697; ENSG00000178028.
ENST00000372289; ENSP00000361363; ENSG00000178028.
GeneIDi55929.
KEGGihsa:55929.
UCSCiuc001clq.1. human.

Organism-specific databases

CTDi55929.
GeneCardsiGC01P044680.
HGNCiHGNC:18291. DMAP1.
HPAiCAB033018.
MIMi605077. gene.
neXtProtiNX_Q9NPF5.
PharmGKBiPA134927315.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG298520.
GeneTreeiENSGT00390000016466.
HOVERGENiHBG051364.
InParanoidiQ9NPF5.
KOiK11324.
OMAiSNPARND.
PhylomeDBiQ9NPF5.
TreeFamiTF354261.

Enzyme and pathway databases

ReactomeiREACT_264245. HATs acetylate histones.

Miscellaneous databases

EvolutionaryTraceiQ9NPF5.
GeneWikiiDMAP1.
GenomeRNAii55929.
NextBioi61337.
PROiQ9NPF5.
SOURCEiSearch...

Gene expression databases

BgeeiQ9NPF5.
CleanExiHS_DMAP1.
ExpressionAtlasiQ9NPF5. baseline and differential.
GenevestigatoriQ9NPF5.

Family and domain databases

InterProiIPR008468. DMAP1.
IPR001005. SANT/Myb.
IPR027109. Swc4/Dmap1.
[Graphical view]
PANTHERiPTHR12855. PTHR12855. 1 hit.
PfamiPF05499. DMAP1. 1 hit.
[Graphical view]
ProDomiPD492828. DMAP1. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM00717. SANT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "DNMT1 binds HDAC2 and a new co-repressor, DMAP1, to form a complex at replication foci."
    Rountree M.R., Bachman K.E., Baylin S.B.
    Nat. Genet. 25:269-277(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, INTERACTION WITH DNMT1 AND TSG101.
  2. Rhodes S., Huckle E.
    Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  3. "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."
    Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.
    DNA Res. 7:65-73(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Fetal brain.
  5. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    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.
    Nat. Genet. 36:40-45(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Embryo.
  6. "The DNA sequence and biological annotation of human chromosome 1."
    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.
    Nature 441:315-321(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Placenta and Skin.
  9. "Identification of new subunits of the multiprotein mammalian TRRAP/TIP60-containing histone acetyltransferase complex."
    Cai Y., Jin J., Tomomori-Sato C., Sato S., Sorokina I., Parmely T.J., Conaway R.C., Conaway J.W.
    J. Biol. Chem. 278:42733-42736(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 9-27; 56-66; 117-128; 237-252; 271-282; 369-378; 401-433 AND 434-449, IDENTIFICATION IN NUA4 COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
  10. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 132-467.
    Tissue: Colon endothelium.
  11. "The highly conserved and multifunctional NuA4 HAT complex."
    Doyon Y., Cote J.
    Curr. Opin. Genet. Dev. 14:147-154(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON NUA4 COMPLEX.
  12. "Components of a pathway maintaining histone modification and heterochromatin protein 1 binding at the pericentric heterochromatin in mammalian cells."
    Xin H., Yoon H.-G., Singh P.B., Wong J., Qin J.
    J. Biol. Chem. 279:9539-9546(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH ING1.
  13. "Physical and functional interactions between Daxx and DNA methyltransferase 1-associated protein, DMAP1."
    Muromoto R., Sugiyama K., Takachi A., Imoto S., Sato N., Yamamoto T., Oritani K., Shimoda K., Matsuda T.
    J. Immunol. 172:2985-2993(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH DAXX.
  14. "Structural and functional conservation of the NuA4 histone acetyltransferase complex from yeast to humans."
    Doyon Y., Selleck W., Lane W.S., Tan S., Cote J.
    Mol. Cell. Biol. 24:1884-1896(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN NUA4 COMPLEX, IDENTIFICATION IN NUA4-RELATED SRCAP-CONTAINING COMPLEX.
  15. "Subcellular localization of RPB5-mediating protein and its putative functional partner."
    Delgermaa L., Hayashi N., Dorjsuren D., Nomura T., Thuy le T.T., Murakami S.
    Mol. Cell. Biol. 24:8556-8566(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH URI1, SUBCELLULAR LOCATION.
  16. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-445, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  17. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
    Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
    Nat. Biotechnol. 24:1285-1292(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-445, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  18. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-445, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  19. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  20. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-445 AND SER-448, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  21. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    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.
    Sci. Signal. 3:RA3-RA3(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-445, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  22. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-445, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  23. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-445, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  24. "SANT domain of human DNA methyltransferase 1 associated protein 1."
    Structural genomics consortium (SGC)
    Submitted (MAY-2009) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 121-212.

Entry informationi

Entry nameiDMAP1_HUMAN
AccessioniPrimary (citable) accession number: Q9NPF5
Secondary accession number(s): A8K001
, D3DPY8, Q0JSM4, Q5TG41, Q7Z3H7, Q9H0S8, Q9P2C2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 20, 2002
Last sequence update: September 30, 2000
Last modified: March 31, 2015
This is version 145 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.