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Q9H7Z6

- KAT8_HUMAN

UniProt

Q9H7Z6 - KAT8_HUMAN

Protein

Histone acetyltransferase KAT8

Gene

KAT8

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 124 (01 Oct 2014)
      Sequence version 2 (05 Jul 2005)
      Previous versions | rss
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    Functioni

    Histone acetyltransferase which may be involved in transcriptional activation. May influence the function of ATM. As part of the MSL complex it is involved in acetylation of nucleosomal histone H4 producing specifically H4K16ac. As part of the NSL complex it may be involved in acetylation of nucleosomal histone H4 on several lysine residues. That activity is less specific than the one of the MSL complex.5 Publications

    Catalytic activityi

    Acetyl-CoA + [histone] = CoA + acetyl-[histone].3 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei274 – 2741
    Binding sitei319 – 3191Acetyl-CoA1 Publication
    Active sitei350 – 3501Proton donor/acceptorCurated
    Binding sitei354 – 3541Acetyl-CoA1 Publication
    Binding sitei363 – 3631Acetyl-CoA1 Publication
    Binding sitei432 – 4321Acetyl-CoA1 Publication

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri208 – 23023C2HC-typeAdd
    BLAST

    GO - Molecular functioni

    1. acetyltransferase activity Source: UniProtKB
    2. histone acetyltransferase activity Source: UniProtKB
    3. metal ion binding Source: UniProtKB-KW
    4. methylated histone binding Source: UniProtKB
    5. protein binding Source: UniProtKB
    6. transcription factor binding Source: UniProtKB

    GO - Biological processi

    1. chromatin organization Source: Reactome
    2. histone acetylation Source: UniProtKB
    3. histone H4-K16 acetylation Source: UniProtKB
    4. histone H4-K5 acetylation Source: UniProtKB
    5. histone H4-K8 acetylation Source: UniProtKB
    6. myeloid cell differentiation Source: UniProtKB
    7. negative regulation of transcription, DNA-templated Source: UniProtKB
    8. positive regulation of transcription, DNA-templated Source: UniProtKB
    9. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Activator, Acyltransferase, Chromatin regulator, Transferase

    Keywords - Biological processi

    Transcription, Transcription regulation

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_172610. HATs acetylate histones.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Histone acetyltransferase KAT8 (EC:2.3.1.48)
    Alternative name(s):
    Lysine acetyltransferase 8
    MOZ, YBF2/SAS3, SAS2 and TIP60 protein 1
    Short name:
    MYST-1
    Short name:
    hMOF
    Gene namesi
    Name:KAT8
    Synonyms:MOF, MYST1
    ORF Names:PP7073
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 16

    Organism-specific databases

    HGNCiHGNC:17933. KAT8.

    Subcellular locationi

    Nucleus 2 Publications. Chromosome By similarity

    GO - Cellular componenti

    1. histone acetyltransferase complex Source: UniProtKB
    2. kinetochore Source: Ensembl
    3. MLL1 complex Source: UniProtKB
    4. MSL complex Source: UniProtKB
    5. nuclear membrane Source: HPA
    6. nucleoplasm Source: Reactome
    7. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Chromosome, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi274 – 2741K → A: Abolishes histone acetyltransferase activity. 1 Publication
    Mutagenesisi316 – 3161C → S: Strongly reduces histone acetyltransferase activity. 1 Publication
    Mutagenesisi350 – 3501E → Q: Abolishes histone acetyltransferase activity. 1 Publication

    Organism-specific databases

    PharmGKBiPA38476.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 458457Histone acetyltransferase KAT8PRO_0000051566Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine2 Publications
    Modified residuei113 – 1131N6-acetyllysine1 Publication
    Modified residuei274 – 2741N6-acetyllysine; by autocatalysis4 Publications

    Post-translational modificationi

    Autoacetylation at Lys-274 is required for proper function.

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiQ9H7Z6.
    PaxDbiQ9H7Z6.
    PRIDEiQ9H7Z6.

    PTM databases

    PhosphoSiteiQ9H7Z6.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9H7Z6.
    BgeeiQ9H7Z6.
    CleanExiHS_MYST1.
    GenevestigatoriQ9H7Z6.

    Organism-specific databases

    HPAiHPA057106.

    Interactioni

    Subunit structurei

    Component of a multisubunit histone acetyltransferase complex (MSL) at least composed of the MOF/KAT8, MSL1/hampin, MSL2L1 and MSL3L1. Interacts with MSL1; the interaction is direct. Component of the NSL complex at least composed of MOF/KAT8, KANSL1, KANSL2, KANSL3, MCRS1, PHF20, OGT1/OGT, WDR5 and HCFC1. Interacts with KANSL1; the interaction is direct. Component of some MLL1/MLL complex, at least composed of the core components KMT2A/MLL1, ASH2L, HCFC1, WDR5 and RBBP5, as well as the facultative components BAP18, CHD8, E2F6, HSP70, INO80C, KANSL1, LAS1L, MAX, MCRS1, MGA, MOF/KAT8, PELP1, PHF20, PRP31, RING2, RUVB1/TIP49A, RUVB2/TIP49B, SENP3, TAF1, TAF4, TAF6, TAF7, TAF9 and TEX10. Interacts with the chromodomain of MORF4L1/MRG15. Interacts with ATM through the chromodomain. Interacts with KANSL1; the interaction is direct.9 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    HHF2P023092EBI-896414,EBI-8113From a different organism.
    KMT2AQ031643EBI-896414,EBI-591370
    RNF2Q994962EBI-896414,EBI-722416
    TP53P046372EBI-896414,EBI-366083

    Protein-protein interaction databases

    BioGridi123914. 44 interactions.
    IntActiQ9H7Z6. 12 interactions.
    MINTiMINT-1897597.

    Structurei

    Secondary structure

    1
    458
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi181 – 1844
    Beta strandi187 – 1904
    Helixi199 – 2035
    Beta strandi207 – 2093
    Turni211 – 2133
    Beta strandi216 – 2183
    Helixi220 – 22910
    Beta strandi236 – 2438
    Beta strandi246 – 2527
    Turni253 – 2553
    Helixi257 – 26812
    Helixi274 – 2774
    Beta strandi283 – 29210
    Beta strandi295 – 30511
    Beta strandi312 – 3154
    Beta strandi317 – 3193
    Helixi321 – 3233
    Beta strandi325 – 3273
    Helixi328 – 34215
    Beta strandi347 – 3493
    Helixi355 – 37218
    Helixi383 – 3897
    Helixi393 – 40210
    Beta strandi406 – 4094
    Beta strandi412 – 4154
    Helixi419 – 4279
    Turni429 – 4313
    Helixi440 – 4423

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2GIVX-ray1.94A174-449[»]
    2PQ8X-ray1.45A174-449[»]
    2Y0MX-ray2.70A174-458[»]
    3QAHX-ray2.10A174-449[»]
    3TOAX-ray3.00A177-458[»]
    3TOBX-ray2.70A177-458[»]
    4DNCX-ray2.05A/B170-458[»]
    ProteinModelPortaliQ9H7Z6.
    SMRiQ9H7Z6. Positions 47-169, 178-448.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9H7Z6.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini69 – 12355ChromoAdd
    BLAST
    Domaini174 – 447274MYST-type HATAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni174 – 458285Sufficient for interaction with KANSL1Add
    BLAST
    Regioni324 – 3307Acetyl-CoA binding

    Sequence similaritiesi

    Belongs to the MYST (SAS/MOZ) family.Curated
    Contains 1 C2HC-type zinc finger.Curated
    Contains 1 chromo domain.Curated

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri208 – 23023C2HC-typeAdd
    BLAST

    Keywords - Domaini

    Zinc-finger

    Phylogenomic databases

    eggNOGiCOG5027.
    HOVERGENiHBG053268.
    InParanoidiQ9H7Z6.
    KOiK11308.
    OMAiDGRDHKI.
    PhylomeDBiQ9H7Z6.
    TreeFamiTF317619.

    Family and domain databases

    Gene3Di3.40.630.30. 1 hit.
    InterProiIPR016181. Acyl_CoA_acyltransferase.
    IPR000953. Chromo_domain/shadow.
    IPR016197. Chromodomain-like.
    IPR002717. MOZ_SAS.
    IPR025995. Tudor-knot.
    [Graphical view]
    PfamiPF01853. MOZ_SAS. 1 hit.
    PF11717. Tudor-knot. 1 hit.
    [Graphical view]
    SMARTiSM00298. CHROMO. 1 hit.
    [Graphical view]
    SUPFAMiSSF54160. SSF54160. 1 hit.
    SSF55729. SSF55729. 1 hit.
    PROSITEiPS51726. MYST_HAT. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9H7Z6-1) [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

    MAAQGAAAAV AAGTSGVAGE GEPGPGENAA AEGTAPSPGR VSPPTPARGE    50
    PEVTVEIGET YLCRRPDSTW HSAEVIQSRV NDQEGREEFY VHYVGFNRRL 100
    DEWVDKNRLA LTKTVKDAVQ KNSEKYLSEL AEQPERKITR NQKRKHDEIN 150
    HVQKTYAEMD PTTAALEKEH EAITKVKYVD KIHIGNYEID AWYFSPFPED 200
    YGKQPKLWLC EYCLKYMKYE KSYRFHLGQC QWRQPPGKEI YRKSNISVYE 250
    VDGKDHKIYC QNLCLLAKLF LDHKTLYFDV EPFVFYILTE VDRQGAHIVG 300
    YFSKEKESPD GNNVACILTL PPYQRRGYGK FLIAFSYELS KLESTVGSPE 350
    KPLSDLGKLS YRSYWSWVLL EILRDFRGTL SIKDLSQMTS ITQNDIISTL 400
    QSLNMVKYWK GQHVICVTPK LVEEHLKSAQ YKKPPITVDS VCLKWAPPKH 450
    KQVKLSKK 458
    Length:458
    Mass (Da):52,403
    Last modified:July 5, 2005 - v2
    Checksum:i66C474BE5B90E8E3
    GO
    Isoform 2 (identifier: Q9H7Z6-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         438-458: VDSVCLKWAPPKHKQVKLSKK → GGWGAAVCRGRWGSVSIWTGRSQGLLIAVT

    Show »
    Length:467
    Mass (Da):53,085
    Checksum:i69AA4F8800E687E0
    GO

    Sequence cautioni

    The sequence AAL55762.1 differs from that shown. Reason: Probable cloning artifact.
    The sequence AAL56648.1 differs from that shown. Reason: Frameshift at positions 23, 26 and 52.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti222 – 2221S → T in AAL55762. (PubMed:15498874)Curated
    Sequence conflicti249 – 2491Y → H in BAB14827. (PubMed:14702039)Curated
    Sequence conflicti372 – 3721I → N in BAB14827. (PubMed:14702039)Curated
    Isoform 2 (identifier: Q9H7Z6-2)
    Sequence conflicti454 – 4541I → M in AAH37773. (PubMed:15489334)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei438 – 45821VDSVC…KLSKK → GGWGAAVCRGRWGSVSIWTG RSQGLLIAVT in isoform 2. 2 PublicationsVSP_014579Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK021872 mRNA. Translation: BAB13924.1.
    AK024102 mRNA. Translation: BAB14827.1.
    AK291106 mRNA. Translation: BAF83795.1.
    AC009088 Genomic DNA. No translation available.
    AC135050 Genomic DNA. No translation available.
    CH471192 Genomic DNA. Translation: EAW52157.1.
    CH471192 Genomic DNA. Translation: EAW52158.1.
    BC037773 mRNA. Translation: AAH37773.1.
    AF217501 mRNA. Translation: AAL56648.1. Frameshift.
    AF260665 mRNA. Translation: AAF72665.2.
    AF289578 mRNA. Translation: AAL55762.1. Sequence problems.
    AL050395 mRNA. Translation: CAH56416.1.
    CCDSiCCDS10706.1. [Q9H7Z6-1]
    CCDS45468.1. [Q9H7Z6-2]
    RefSeqiNP_115564.2. NM_032188.2. [Q9H7Z6-1]
    NP_892003.2. NM_182958.2. [Q9H7Z6-2]
    UniGeneiHs.533803.

    Genome annotation databases

    EnsembliENST00000219797; ENSP00000219797; ENSG00000103510. [Q9H7Z6-1]
    ENST00000448516; ENSP00000406037; ENSG00000103510. [Q9H7Z6-2]
    ENST00000543774; ENSP00000456933; ENSG00000103510. [Q9H7Z6-1]
    GeneIDi84148.
    KEGGihsa:84148.
    UCSCiuc002eax.3. human. [Q9H7Z6-2]
    uc002eay.3. human. [Q9H7Z6-1]

    Polymorphism databases

    DMDMi68565938.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK021872 mRNA. Translation: BAB13924.1 .
    AK024102 mRNA. Translation: BAB14827.1 .
    AK291106 mRNA. Translation: BAF83795.1 .
    AC009088 Genomic DNA. No translation available.
    AC135050 Genomic DNA. No translation available.
    CH471192 Genomic DNA. Translation: EAW52157.1 .
    CH471192 Genomic DNA. Translation: EAW52158.1 .
    BC037773 mRNA. Translation: AAH37773.1 .
    AF217501 mRNA. Translation: AAL56648.1 . Frameshift.
    AF260665 mRNA. Translation: AAF72665.2 .
    AF289578 mRNA. Translation: AAL55762.1 . Sequence problems.
    AL050395 mRNA. Translation: CAH56416.1 .
    CCDSi CCDS10706.1. [Q9H7Z6-1 ]
    CCDS45468.1. [Q9H7Z6-2 ]
    RefSeqi NP_115564.2. NM_032188.2. [Q9H7Z6-1 ]
    NP_892003.2. NM_182958.2. [Q9H7Z6-2 ]
    UniGenei Hs.533803.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2GIV X-ray 1.94 A 174-449 [» ]
    2PQ8 X-ray 1.45 A 174-449 [» ]
    2Y0M X-ray 2.70 A 174-458 [» ]
    3QAH X-ray 2.10 A 174-449 [» ]
    3TOA X-ray 3.00 A 177-458 [» ]
    3TOB X-ray 2.70 A 177-458 [» ]
    4DNC X-ray 2.05 A/B 170-458 [» ]
    ProteinModelPortali Q9H7Z6.
    SMRi Q9H7Z6. Positions 47-169, 178-448.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 123914. 44 interactions.
    IntActi Q9H7Z6. 12 interactions.
    MINTi MINT-1897597.

    Chemistry

    BindingDBi Q9H7Z6.
    ChEMBLi CHEMBL1932912.
    GuidetoPHARMACOLOGYi 2668.

    PTM databases

    PhosphoSitei Q9H7Z6.

    Polymorphism databases

    DMDMi 68565938.

    Proteomic databases

    MaxQBi Q9H7Z6.
    PaxDbi Q9H7Z6.
    PRIDEi Q9H7Z6.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000219797 ; ENSP00000219797 ; ENSG00000103510 . [Q9H7Z6-1 ]
    ENST00000448516 ; ENSP00000406037 ; ENSG00000103510 . [Q9H7Z6-2 ]
    ENST00000543774 ; ENSP00000456933 ; ENSG00000103510 . [Q9H7Z6-1 ]
    GeneIDi 84148.
    KEGGi hsa:84148.
    UCSCi uc002eax.3. human. [Q9H7Z6-2 ]
    uc002eay.3. human. [Q9H7Z6-1 ]

    Organism-specific databases

    CTDi 84148.
    GeneCardsi GC16P031130.
    HGNCi HGNC:17933. KAT8.
    HPAi HPA057106.
    MIMi 609912. gene.
    neXtProti NX_Q9H7Z6.
    PharmGKBi PA38476.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5027.
    HOVERGENi HBG053268.
    InParanoidi Q9H7Z6.
    KOi K11308.
    OMAi DGRDHKI.
    PhylomeDBi Q9H7Z6.
    TreeFami TF317619.

    Enzyme and pathway databases

    Reactomei REACT_172610. HATs acetylate histones.

    Miscellaneous databases

    ChiTaRSi KAT8. human.
    EvolutionaryTracei Q9H7Z6.
    GeneWikii MYST1.
    GenomeRNAii 84148.
    NextBioi 73476.
    PROi Q9H7Z6.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9H7Z6.
    Bgeei Q9H7Z6.
    CleanExi HS_MYST1.
    Genevestigatori Q9H7Z6.

    Family and domain databases

    Gene3Di 3.40.630.30. 1 hit.
    InterProi IPR016181. Acyl_CoA_acyltransferase.
    IPR000953. Chromo_domain/shadow.
    IPR016197. Chromodomain-like.
    IPR002717. MOZ_SAS.
    IPR025995. Tudor-knot.
    [Graphical view ]
    Pfami PF01853. MOZ_SAS. 1 hit.
    PF11717. Tudor-knot. 1 hit.
    [Graphical view ]
    SMARTi SM00298. CHROMO. 1 hit.
    [Graphical view ]
    SUPFAMi SSF54160. SSF54160. 1 hit.
    SSF55729. SSF55729. 1 hit.
    PROSITEi PS51726. MYST_HAT. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "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.
    2. "The sequence and analysis of duplication-rich human chromosome 16."
      Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.
      , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
      Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "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 2).
      Tissue: Brain.
    5. "Structure and function of the human MYST family: MOZ2, MYST1 and MYST2."
      Borrow J., Housman D.E.
      Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 6-458 (ISOFORM 1).
    6. "A new human member of the MYST family of histone acetyl transferases with high sequence similarity to Drosophila MOF."
      Neal K.C., Pannuti A., Smith E.R., Lucchesi J.C.
      Biochim. Biophys. Acta 1490:170-174(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 29-458 (ISOFORM 1), CATALYTIC ACTIVITY, SUBCELLULAR LOCATION.
      Tissue: Heart.
    7. "Large-scale cDNA transfection screening for genes related to cancer development and progression."
      Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X., Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X.
      , Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J.
      Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 153-458 (ISOFORM 1).
    8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 201-458 (ISOFORM 2).
      Tissue: Uterus.
    9. "MRG15, a novel chromodomain protein, is present in two distinct multiprotein complexes involved in transcriptional activation."
      Pardo P.S., Leung J.K., Lucchesi J.C., Pereira-Smith O.M.
      J. Biol. Chem. 277:50860-50866(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MORF4L1, FUNCTION.
    10. "Physical association and coordinate function of the H3 K4 methyltransferase MLL1 and the H4 K16 acetyltransferase MOF."
      Dou Y., Milne T.A., Tackett A.J., Smith E.R., Fukuda A., Wysocka J., Allis C.D., Chait B.T., Hess J.L., Roeder R.G.
      Cell 121:873-885(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE MLL1/MLL COMPLEX.
    11. Cited for: INTERACTION WITH ATM, FUNCTION.
    12. "A human protein complex homologous to the Drosophila MSL complex is responsible for the majority of histone H4 acetylation at lysine 16."
      Smith E.R., Cayrou C., Huang R., Lane W.S., Cote J., Lucchesi J.C.
      Mol. Cell. Biol. 25:9175-9188(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION OF MSL COMPLEX COMPONENTS, IDENTIFICATION BY MASS SPECTROMETRY.
    13. Erratum
      Smith E.R., Cayrou C., Huang R., Lane W.S., Cote J., Lucchesi J.C.
      Mol. Cell. Biol. 26:387-387(2006)
    14. "Nuclear pore components are involved in the transcriptional regulation of dosage compensation in Drosophila."
      Mendjan S., Taipale M., Kind J., Holz H., Gebhardt P., Schelder M., Vermeulen M., Buscaino A., Duncan K., Mueller J., Wilm M., Stunnenberg H.G., Saumweber H., Akhtar A.
      Mol. Cell 21:811-823(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH KANSL1.
    15. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    16. "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-113, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. "Subunit composition and substrate specificity of a MOF-containing histone acetyltransferase distinct from the male-specific lethal (MSL) complex."
      Cai Y., Jin J., Swanson S.K., Cole M.D., Choi S.H., Florens L., Washburn M.P., Conaway J.W., Conaway R.C.
      J. Biol. Chem. 285:4268-4272(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN HISTONE H4 ACETYLATION, IDENTIFICATION IN NSL COMPLEX, SUBCELLULAR LOCATION.
    18. "The nonspecific lethal complex is a transcriptional regulator in Drosophila."
      Raja S.J., Charapitsa I., Conrad T., Vaquerizas J.M., Gebhardt P., Holz H., Kadlec J., Fraterman S., Luscombe N.M., Akhtar A.
      Mol. Cell 38:827-841(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH KANSL1.
    19. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    20. "Structural insight into the regulation of MOF in the male-specific lethal complex and the non-specific lethal complex."
      Huang J., Wan B., Wu L., Yang Y., Dou Y., Lei M.
      Cell Res. 22:1078-1081(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 170-458 IN COMPLEX WITH MSL1, ACETYLATION AT LYS-274, FUNCTION IN MSL AND NSL COMPLEX, FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH KANSL1; MSL1 AND MSL3.
    21. "Regulation of the histone acetyltransferase activity of hMOF via autoacetylation of Lys274."
      Sun B., Guo S., Tang Q., Li C., Zeng R., Xiong Z., Zhong C., Ding J.
      Cell Res. 21:1262-1266(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) OF 174-449 IN COMPLEX WITH ACETYL COENZYME A, ACETYLATION AT LYS-274.
    22. "Structural basis for MOF and MSL3 recruitment into the dosage compensation complex by MSL1."
      Kadlec J., Hallacli E., Lipp M., Holz H., Sanchez-Weatherby J., Cusack S., Akhtar A.
      Nat. Struct. Mol. Biol. 18:142-149(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 174-458 IN COMPLEX WITH MSL1; ZINC ION AND ACETYL-COA, FUNCTION, CATALYTIC ACTIVITY, ACTIVE SITE, IDENTIFICATION BY MASS SPECTROMETRY, ACETYLATION AT LYS-274, INTERACTION WITH KANSL1; MSL1 AND MSL3, MUTAGENESIS OF LYS-274; CYS-316 AND GLU-350.
    23. Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 177-458, ACTIVE SITE, ACETYLATION AT LYS-274.

    Entry informationi

    Entry nameiKAT8_HUMAN
    AccessioniPrimary (citable) accession number: Q9H7Z6
    Secondary accession number(s): A8K4Z1
    , G5E9P2, Q659G0, Q7LC17, Q8IY59, Q8WYB4, Q8WZ14, Q9HAC5, Q9NR35
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 5, 2005
    Last sequence update: July 5, 2005
    Last modified: October 1, 2014
    This is version 124 of the entry and version 2 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, Reference proteome

    Documents

    1. Human chromosome 16
      Human chromosome 16: 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