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Q9NPF5

- DMAP1_HUMAN

UniProt

Q9NPF5 - DMAP1_HUMAN

Protein

DNA methyltransferase 1-associated protein 1

Gene

DMAP1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 139 (01 Oct 2014)
      Sequence version 1 (01 Oct 2000)
      Previous versions | rss
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    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. protein binding Source: UniProtKB
    3. RNA polymerase II repressing transcription factor binding Source: UniProtKB
    4. 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

    Keywords - Molecular functioni

    Activator, Chromatin regulator, Repressor

    Keywords - Biological processi

    Growth regulation, Transcription, Transcription regulation

    Enzyme and pathway databases

    ReactomeiREACT_172610. HATs acetylate histones.
    REACT_197820. 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: 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

    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 – 4451Phosphothreonine6 Publications
    Modified residuei448 – 4481Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ9NPF5.
    PaxDbiQ9NPF5.
    PRIDEiQ9NPF5.

    PTM databases

    PhosphoSiteiQ9NPF5.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9NPF5.
    BgeeiQ9NPF5.
    CleanExiHS_DMAP1.
    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. 43 interactions.
    IntActiQ9NPF5. 12 interactions.
    MINTiMINT-4719752.
    STRINGi9606.ENSP00000312697.

    Structurei

    Secondary structure

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

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    HOVERGENiHBG051364.
    InParanoidiQ9NPF5.
    KOiK11324.
    OMAiPTEDICT.
    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

    MATGADVRDI LELGGPEGDA ASGTISKKDI INPDKKKSKK SSETLTFKRP    50
    EGMHREVYAL LYSDKKDAPP LLPSDTGQGY RTVKAKLGSK KVRPWKWMPF 100
    TNPARKDGAM FFHWRRAAEE GKDYPFARFN KTVQVPVYSE QEYQLYLHDD 150
    AWTKAETDHL FDLSRRFDLR FVVIHDRYDH QQFKKRSVED LKERYYHICA 200
    KLANVRAVPG TDLKIPVFDA GHERRRKEQL ERLYNRTPEQ VAEEEYLLQE 250
    LRKIEARKKE REKRSQDLQK LITAADTTAE QRRTERKAPK KKLPQKKEAE 300
    KPAVPETAGI KFPDFKSAGV TLRSQRMKLP SSVGQKKIKA LEQMLLELGV 350
    ELSPTPTEEL VHMFNELRSD LVLLYELKQA CANCEYELQM LRHRHEALAR 400
    AGVLGGPATP ASGPGPASAE PAVTEPGLGP DPKDTIIDVV GAPLTPNSRK 450
    RRESASSSSS VKKAKKP 467
    Length:467
    Mass (Da):52,993
    Last modified:October 1, 2000 - v1
    Checksum:i54500B252E076A29
    GO

    Sequence cautioni

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

    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS509.1.
    RefSeqi NP_001029195.1. NM_001034023.1.
    NP_001029196.1. NM_001034024.1.
    NP_061973.1. NM_019100.4.
    UniGenei Hs.8008.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3HM5 X-ray 1.80 A 121-212 [» ]
    4IEJ X-ray 1.45 A 121-212 [» ]
    ProteinModelPortali Q9NPF5.
    SMRi Q9NPF5. Positions 133-207.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 121004. 43 interactions.
    IntActi Q9NPF5. 12 interactions.
    MINTi MINT-4719752.
    STRINGi 9606.ENSP00000312697.

    PTM databases

    PhosphoSitei Q9NPF5.

    Polymorphism databases

    DMDMi 20138031.

    Proteomic databases

    MaxQBi Q9NPF5.
    PaxDbi Q9NPF5.
    PRIDEi Q9NPF5.

    Protocols and materials databases

    DNASUi 55929.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000315913 ; ENSP00000312697 ; ENSG00000178028 .
    ENST00000361745 ; ENSP00000354697 ; ENSG00000178028 .
    ENST00000372289 ; ENSP00000361363 ; ENSG00000178028 .
    GeneIDi 55929.
    KEGGi hsa:55929.
    UCSCi uc001clq.1. human.

    Organism-specific databases

    CTDi 55929.
    GeneCardsi GC01P044680.
    HGNCi HGNC:18291. DMAP1.
    HPAi CAB033018.
    MIMi 605077. gene.
    neXtProti NX_Q9NPF5.
    PharmGKBi PA134927315.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG298520.
    HOVERGENi HBG051364.
    InParanoidi Q9NPF5.
    KOi K11324.
    OMAi PTEDICT.
    PhylomeDBi Q9NPF5.
    TreeFami TF354261.

    Enzyme and pathway databases

    Reactomei REACT_172610. HATs acetylate histones.
    REACT_197820. HATs acetylate histones.

    Miscellaneous databases

    EvolutionaryTracei Q9NPF5.
    GeneWikii DMAP1.
    GenomeRNAii 55929.
    NextBioi 61337.
    PROi Q9NPF5.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9NPF5.
    Bgeei Q9NPF5.
    CleanExi HS_DMAP1.
    Genevestigatori Q9NPF5.

    Family and domain databases

    InterProi IPR008468. DMAP1.
    IPR001005. SANT/Myb.
    IPR027109. Swc4/Dmap1.
    [Graphical view ]
    PANTHERi PTHR12855. PTHR12855. 1 hit.
    Pfami PF05499. DMAP1. 1 hit.
    [Graphical view ]
    ProDomi PD492828. DMAP1. 1 hit.
    [Graphical view ] [Entries sharing at least one domain ]
    SMARTi SM00717. SANT. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, INTERACTION WITH DNMT1 AND TSG101.
    2. Rhodes S., Huckle E.
      Submitted (JAN-2000) 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(2000) [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(2004) [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(2006) [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(2004) [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(2003) [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(2004) [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(2004) [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(2004) [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(2004) [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(2004) [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(2006) [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(2006) [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(2008) [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(2009) [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(2010) [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(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-445, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    23. "SANT domain of human DNA methyltransferase 1 associated protein 1."
      Structural genomics consortium (SGC)
      Submitted (JUN-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 21, 2002
    Last sequence update: October 1, 2000
    Last modified: October 1, 2014
    This is version 139 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