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Q9HAF1

- EAF6_HUMAN

UniProt

Q9HAF1 - EAF6_HUMAN

Protein

Chromatin modification-related protein MEAF6

Gene

MEAF6

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
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    • History
      Entry version 102 (01 Oct 2014)
      Sequence version 1 (01 Mar 2001)
      Previous versions | rss
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    Functioni

    Component of the NuA4 histone acetyltransferase 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. Component of the HBO1 complex which has a histone H4-specific acetyltransferase activity, a reduced activity toward histone H3 and is responsible for the bulk of histone H4 acetylation in vivo. Component of the MOZ/MORF complex which has a histone H3 acetyltransferase activity.3 Publications

    GO - Molecular functioni

    1. protein binding Source: IntAct

    GO - Biological processi

    1. chromatin organization Source: Reactome
    2. histone H2A acetylation Source: UniProtKB
    3. histone H3-K14 acetylation Source: UniProtKB
    4. histone H4-K12 acetylation Source: UniProtKB
    5. histone H4-K5 acetylation Source: UniProtKB
    6. histone H4-K8 acetylation Source: UniProtKB
    7. regulation of transcription, DNA-templated Source: UniProtKB-KW
    8. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Activator, Chromatin regulator

    Keywords - Biological processi

    Transcription, Transcription regulation

    Enzyme and pathway databases

    ReactomeiREACT_172610. HATs acetylate histones.
    REACT_197820. HATs acetylate histones.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Chromatin modification-related protein MEAF6
    Short name:
    MYST/Esa1-associated factor 6
    Alternative name(s):
    Esa1-associated factor 6 homolog
    Short name:
    Protein EAF6 homolog
    Short name:
    hEAF6
    Sarcoma antigen NY-SAR-91
    Gene namesi
    Name:MEAF6
    Synonyms:C1orf149, EAF6
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:25674. MEAF6.

    Subcellular locationi

    Nucleusnucleolus 1 Publication

    GO - Cellular componenti

    1. centrosome Source: HPA
    2. cytoplasm Source: HPA
    3. MOZ/MORF histone acetyltransferase complex Source: UniProtKB
    4. NuA4 histone acetyltransferase complex Source: UniProtKB
    5. nucleolus Source: UniProtKB
    6. nucleoplasm Source: Reactome
    7. nucleus Source: HPA

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    A chromosomal aberration involving MEAF6 may be a cause of endometrial stromal tumors. Translocation t(1;6)(p34;p21) with PHF1.1 Publication

    Organism-specific databases

    PharmGKBiPA165751536.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 191190Chromatin modification-related protein MEAF6PRO_0000272609Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanineBy similarity
    Modified residuei6 – 61N6-acetyllysineBy similarity
    Modified residuei69 – 691N6-acetyllysine1 Publication
    Modified residuei74 – 741N6-acetyllysine1 Publication
    Modified residuei118 – 1181Phosphoserine1 Publication
    Modified residuei120 – 1201Phosphothreonine1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ9HAF1.
    PaxDbiQ9HAF1.
    PRIDEiQ9HAF1.

    PTM databases

    PhosphoSiteiQ9HAF1.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9HAF1.
    BgeeiQ9HAF1.
    CleanExiHS_C1orf149.
    GenevestigatoriQ9HAF1.

    Organism-specific databases

    HPAiHPA029599.
    HPA029600.

    Interactioni

    Subunit structurei

    Component of the NuA4 histone acetyltransferase complex which contains the catalytic subunit KAT5 and the subunits EP400, TRRAP, BRD8, EPC1, DMAP1, RUVBL1, RUVBL2, ING3, actin, ACTL6A, MORF4L1, MORF4L2, MRGBP, YEATS4, VPS72 and MEAF6. Component of the HBO1 complex composed at least of ING4 or ING5, KAT7/HBO1, MEAF6, and one of JADE1, JADE2 and JADE3. Component of the MOZ/MORF complex composed at least of ING5, KAT6A, KAT6B, MEAF6 and one of BRPF1, BRD1/BRPF2 and BRPF3.5 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    FXR2P511163EBI-399266,EBI-740459

    Protein-protein interaction databases

    BioGridi122280. 20 interactions.
    IntActiQ9HAF1. 7 interactions.
    STRINGi9606.ENSP00000362166.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9HAF1.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili11 – 4737Sequence AnalysisAdd
    BLAST

    Sequence similaritiesi

    Belongs to the EAF6 family.Curated

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    eggNOGiNOG290756.
    HOGENOMiHOG000290166.
    KOiK11344.
    OMAiATAGKAN.
    OrthoDBiEOG79CZ1M.
    PhylomeDBiQ9HAF1.
    TreeFamiTF324130.

    Family and domain databases

    InterProiIPR015418. Hist_AcTrfase_NuA4_cplx.
    [Graphical view]
    PfamiPF09340. NuA4. 1 hit.
    [Graphical view]

    Sequences (4)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9HAF1-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MAMHNKAAPP QIPDTRRELA ELVKRKQELA ETLANLERQI YAFEGSYLED    50
    TQMYGNIIRG WDRYLTNQKN SNSKNDRRNR KFKEAERLFS KSSVTSAAAV 100
    SALAGVQDQL IEKREPGSGT ESDTSPDFHN QENEPSQEDP EDLDGSVQGV 150
    KPQKAASSTS SGSHHSSHKK RKNKNRHRID LKLNKKPRAD Y 191
    Length:191
    Mass (Da):21,635
    Last modified:March 1, 2001 - v1
    Checksum:iC0FBC7566BAAF1F7
    GO
    Isoform 2 (identifier: Q9HAF1-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         178-191: RIDLKLNKKPRADY → SPSGMFDYDFEYVY

    Note: No experimental confirmation available.

    Show »
    Length:191
    Mass (Da):21,625
    Checksum:i4A46263CF13F3C99
    GO
    Isoform 3 (identifier: Q9HAF1-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         178-178: R → SPSGMFDYDFE

    Note: No experimental confirmation available.

    Show »
    Length:201
    Mass (Da):22,755
    Checksum:iE30FC55A4AB5EBA0
    GO
    Isoform 4 (identifier: Q9HAF1-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         179-191: IDLKLNKKPRADY → MNVSPKTGWHQLHL

    Note: Gene prediction based on EST data.

    Show »
    Length:192
    Mass (Da):21,709
    Checksum:i3DC03438B928A5A3
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti2 – 32AM → RG in AAO65179. (PubMed:12601173)Curated
    Sequence conflicti4 – 41H → P in AAZ13760. 1 PublicationCurated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei178 – 19114RIDLK…PRADY → SPSGMFDYDFEYVY in isoform 2. 1 PublicationVSP_022450Add
    BLAST
    Alternative sequencei178 – 1781R → SPSGMFDYDFE in isoform 3. 1 PublicationVSP_022451
    Alternative sequencei179 – 19113IDLKL…PRADY → MNVSPKTGWHQLHL in isoform 4. CuratedVSP_047018Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BX538212 mRNA. Translation: CAD98071.1.
    BX640719 mRNA. Translation: CAE45838.1.
    AK021792 mRNA. Translation: BAB13898.1.
    DQ099384 mRNA. Translation: AAZ13760.1.
    AL034379 Genomic DNA. Translation: CAI20549.1.
    AL034379 Genomic DNA. Translation: CAI20550.1.
    BC056406 mRNA. Translation: AAH56406.1.
    BC016328 mRNA. Translation: AAH16328.1.
    AY211926 mRNA. Translation: AAO65179.1.
    CCDSiCCDS418.1. [Q9HAF1-3]
    CCDS59195.1. [Q9HAF1-4]
    CCDS59196.1. [Q9HAF1-1]
    RefSeqiNP_001257804.1. NM_001270875.1. [Q9HAF1-1]
    NP_001257805.1. NM_001270876.1. [Q9HAF1-4]
    NP_073593.2. NM_022756.5. [Q9HAF1-3]
    UniGeneiHs.17118.

    Genome annotation databases

    EnsembliENST00000296214; ENSP00000296214; ENSG00000163875. [Q9HAF1-1]
    ENST00000373073; ENSP00000362164; ENSG00000163875. [Q9HAF1-4]
    ENST00000373075; ENSP00000362166; ENSG00000163875. [Q9HAF1-3]
    ENST00000448519; ENSP00000394966; ENSG00000163875. [Q9HAF1-2]
    GeneIDi64769.
    KEGGihsa:64769.
    UCSCiuc001cbe.2. human. [Q9HAF1-3]
    uc001cbg.2. human. [Q9HAF1-1]

    Polymorphism databases

    DMDMi74752760.

    Keywords - Coding sequence diversityi

    Alternative splicing, Chromosomal rearrangement

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BX538212 mRNA. Translation: CAD98071.1 .
    BX640719 mRNA. Translation: CAE45838.1 .
    AK021792 mRNA. Translation: BAB13898.1 .
    DQ099384 mRNA. Translation: AAZ13760.1 .
    AL034379 Genomic DNA. Translation: CAI20549.1 .
    AL034379 Genomic DNA. Translation: CAI20550.1 .
    BC056406 mRNA. Translation: AAH56406.1 .
    BC016328 mRNA. Translation: AAH16328.1 .
    AY211926 mRNA. Translation: AAO65179.1 .
    CCDSi CCDS418.1. [Q9HAF1-3 ]
    CCDS59195.1. [Q9HAF1-4 ]
    CCDS59196.1. [Q9HAF1-1 ]
    RefSeqi NP_001257804.1. NM_001270875.1. [Q9HAF1-1 ]
    NP_001257805.1. NM_001270876.1. [Q9HAF1-4 ]
    NP_073593.2. NM_022756.5. [Q9HAF1-3 ]
    UniGenei Hs.17118.

    3D structure databases

    ProteinModelPortali Q9HAF1.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 122280. 20 interactions.
    IntActi Q9HAF1. 7 interactions.
    STRINGi 9606.ENSP00000362166.

    PTM databases

    PhosphoSitei Q9HAF1.

    Polymorphism databases

    DMDMi 74752760.

    Proteomic databases

    MaxQBi Q9HAF1.
    PaxDbi Q9HAF1.
    PRIDEi Q9HAF1.

    Protocols and materials databases

    DNASUi 64769.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000296214 ; ENSP00000296214 ; ENSG00000163875 . [Q9HAF1-1 ]
    ENST00000373073 ; ENSP00000362164 ; ENSG00000163875 . [Q9HAF1-4 ]
    ENST00000373075 ; ENSP00000362166 ; ENSG00000163875 . [Q9HAF1-3 ]
    ENST00000448519 ; ENSP00000394966 ; ENSG00000163875 . [Q9HAF1-2 ]
    GeneIDi 64769.
    KEGGi hsa:64769.
    UCSCi uc001cbe.2. human. [Q9HAF1-3 ]
    uc001cbg.2. human. [Q9HAF1-1 ]

    Organism-specific databases

    CTDi 64769.
    GeneCardsi GC01M037951.
    HGNCi HGNC:25674. MEAF6.
    HPAi HPA029599.
    HPA029600.
    MIMi 611001. gene.
    neXtProti NX_Q9HAF1.
    PharmGKBi PA165751536.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG290756.
    HOGENOMi HOG000290166.
    KOi K11344.
    OMAi ATAGKAN.
    OrthoDBi EOG79CZ1M.
    PhylomeDBi Q9HAF1.
    TreeFami TF324130.

    Enzyme and pathway databases

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

    Miscellaneous databases

    GeneWikii C1orf149.
    GenomeRNAii 64769.
    NextBioi 35466510.
    PROi Q9HAF1.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9HAF1.
    Bgeei Q9HAF1.
    CleanExi HS_C1orf149.
    Genevestigatori Q9HAF1.

    Family and domain databases

    InterProi IPR015418. Hist_AcTrfase_NuA4_cplx.
    [Graphical view ]
    Pfami PF09340. NuA4. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
      Tissue: Cerebellum and Fetal brain.
    2. "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] (ISOFORM 1).
      Tissue: Embryo.
    3. Lin L., Nong W., Zhou G., Ke R., Shen C., Zhong G., Zheng Z., Liang M., Li M., Li H., Yang S.
      Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    4. "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].
    5. "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] (ISOFORM 1).
      Tissue: Brain and Uterus.
    6. Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 2-191 (ISOFORM 1).
    7. "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: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE NUA4 HISTONE ACETYLTRANSFERASE COMPLEX.
    8. "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 THE NUA4 HISTONE ACETYLTRANSFERASE COMPLEX.
    9. "The mammalian YL1 protein is a shared subunit of the TRRAP/TIP60 histone acetyltransferase and SRCAP complexes."
      Cai Y., Jin J., Florens L., Swanson S.K., Kusch T., Li B., Workman J.L., Washburn M.P., Conaway R.C., Conaway J.W.
      J. Biol. Chem. 280:13665-13670(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE NUA4 HISTONE ACETYLTRANSFERASE COMPLEX.
    10. "ING tumor suppressor proteins are critical regulators of chromatin acetylation required for genome expression and perpetuation."
      Doyon Y., Cayrou C., Ullah M., Landry A.-J., Cote V., Selleck W., Lane W.S., Tan S., Yang X.-J., Cote J.
      Mol. Cell 21:51-64(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE NUA4 HISTONE ACETYLTRANSFERASE COMPLEX, IDENTIFICATION IN THE HBO1 COMPLEX, IDENTIFICATION IN THE MOZ/MORF COMPLEX.
    11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic kidney.
    12. Cited for: FUNCTION, IDENTIFICATION IN THE MOZ/MORF COMPLEX, INTERACTION WITH BRPF1, SUBCELLULAR LOCATION.
    13. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-118 AND THR-120, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    14. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-69 AND LYS-74, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    16. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. "Novel fusion of MYST/Esa1-associated factor 6 and PHF1 in endometrial stromal sarcoma."
      Panagopoulos I., Micci F., Thorsen J., Gorunova L., Eibak A.M., Bjerkehagen B., Davidson B., Heim S.
      PLoS ONE 7:E39354-E39354(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISEASE, CHROMOSOMAL TRANSLOCATION WITH PHF1.

    Entry informationi

    Entry nameiEAF6_HUMAN
    AccessioniPrimary (citable) accession number: Q9HAF1
    Secondary accession number(s): B1AK64
    , Q4F967, Q7Z311, Q86WE3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 23, 2007
    Last sequence update: March 1, 2001
    Last modified: October 1, 2014
    This is version 102 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

    Complete proteome, 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3