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Q9D1P2

- KAT8_MOUSE

UniProt

Q9D1P2 - KAT8_MOUSE

Protein

Histone acetyltransferase KAT8

Gene

Kat8

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 116 (01 Oct 2014)
      Sequence version 1 (01 Jun 2001)
      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 By similarity.By similarity

    Catalytic activityi

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

    Sites

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

    Regions

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

    GO - Molecular functioni

    1. acetyltransferase activity Source: UniProtKB
    2. enzyme binding Source: UniProtKB
    3. histone acetyltransferase activity (H4-K16 specific) Source: Ensembl
    4. histone acetyltransferase activity (H4-K5 specific) Source: Ensembl
    5. histone acetyltransferase activity (H4-K8 specific) Source: Ensembl
    6. metal ion binding Source: UniProtKB-KW

    GO - Biological processi

    1. histone H4-K16 acetylation Source: UniProtKB
    2. histone H4-K5 acetylation Source: UniProtKB
    3. histone H4-K8 acetylation Source: UniProtKB
    4. myeloid cell differentiation Source: Ensembl
    5. negative regulation of transcription, DNA-templated Source: Ensembl
    6. positive regulation of transcription, DNA-templated Source: UniProtKB
    7. 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_226917. 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
    Gene namesi
    Name:Kat8
    Synonyms:Mof, Myst1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 7

    Organism-specific databases

    MGIiMGI:1915023. Kat8.

    Subcellular locationi

    Nucleus. Chromosome By similarity

    GO - Cellular componenti

    1. histone acetyltransferase complex Source: UniProtKB
    2. kinetochore Source: MGI
    3. MLL1 complex Source: UniProtKB
    4. MSL complex Source: UniProtKB

    Keywords - Cellular componenti

    Chromosome, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 458457Histone acetyltransferase KAT8PRO_0000051567Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanineBy similarity
    Modified residuei113 – 1131N6-acetyllysineBy similarity
    Modified residuei274 – 2741N6-acetyllysine; by autocatalysisBy similarity

    Post-translational modificationi

    Autoacetylation at Lys-274 is required for proper function.By similarity

    Keywords - PTMi

    Acetylation

    Proteomic databases

    PaxDbiQ9D1P2.
    PRIDEiQ9D1P2.

    PTM databases

    PhosphoSiteiQ9D1P2.

    Expressioni

    Gene expression databases

    BgeeiQ9D1P2.
    CleanExiMM_MYST1.
    GenevestigatoriQ9D1P2.

    Interactioni

    Subunit structurei

    Component of a multisubunit histone acetyltransferase complex (MSL) at least composed of the MOF/KAT8, MSL1/hampin, MSL2L1 and MSL3L1. 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 By similarity. Interacts with MSL1; the interaction is direct.By similarity1 Publication

    Protein-protein interaction databases

    BioGridi212433. 21 interactions.
    IntActiQ9D1P2. 16 interactions.

    Structurei

    Secondary structure

    1
    458
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi59 – 657
    Turni66 – 683
    Beta strandi69 – 8113
    Turni82 – 854
    Beta strandi86 – 927
    Turni94 – 963
    Beta strandi102 – 1043
    Turni106 – 1083
    Turni112 – 1143
    Beta strandi115 – 1173

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1WGSNMR-A50-169[»]
    ProteinModelPortaliQ9D1P2.
    SMRiQ9D1P2. Positions 47-169, 178-448.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9D1P2.

    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 KANSL1By similarityAdd
    BLAST
    Regioni324 – 3307Acetyl-CoA bindingBy similarity

    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.
    GeneTreeiENSGT00550000074503.
    HOGENOMiHOG000182457.
    HOVERGENiHBG053268.
    InParanoidiQ9D1P2.
    KOiK11308.
    OMAiDGRDHKI.
    OrthoDBiEOG7WHH8N.
    PhylomeDBiQ9D1P2.
    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: Q9D1P2-1) [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

    MAAQGATAAV AATTSGTVGE GEPGPGENAA VEGPARSPGR VSPPTPARGE    50
    PEVTVEIGET YLCRRPDSTW HSAEVIQSRV NDQEGREEFY VHYVGFNRRL 100
    DEWVDKNRLA LTKTVKDAVQ KNSEKYLSEL AEQPERKITR NQKRKHDEIN 150
    HVQKTYAEMD PTTAALEKEH EAITKVKYVD KIHIGNYEID AWYFSPFPED 200
    YGKQPKLWLC EYCLKYMKFE 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):52,574
    Last modified:June 1, 2001 - v1
    Checksum:iFA25E0C8D7E46CEC
    GO
    Isoform 2 (identifier: Q9D1P2-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         155-194: TYAEMDPTTA...GNYEIDAWYF → VLAPPFSGPS...LFTYEKILSL
         195-458: Missing.

    Show »
    Length:194
    Mass (Da):21,398
    Checksum:i36334369729A61C2
    GO

    Sequence cautioni

    The sequence BAC25539.1 differs from that shown. Reason: Frameshift at position 236.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti385 – 3851L → F in AAH36284. (PubMed:15489334)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei155 – 19440TYAEM…DAWYF → VLAPPFSGPSQQSHSNSHVK AGSMPGFFSRLFTYEKILSL in isoform 2. 1 PublicationVSP_014580Add
    BLAST
    Alternative sequencei195 – 458264Missing in isoform 2. 1 PublicationVSP_014581Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK003264 mRNA. Translation: BAB22680.1.
    AK018002 mRNA. Translation: BAC25539.1. Frameshift.
    AK029350 mRNA. Translation: BAC26411.1.
    AK146710 mRNA. Translation: BAE27376.1.
    BC036284 mRNA. Translation: AAH36284.1.
    CCDSiCCDS21885.1. [Q9D1P2-1]
    RefSeqiNP_080646.1. NM_026370.1. [Q9D1P2-1]
    UniGeneiMm.425492.

    Genome annotation databases

    EnsembliENSMUST00000033070; ENSMUSP00000033070; ENSMUSG00000030801. [Q9D1P2-1]
    GeneIDi67773.
    KEGGimmu:67773.
    UCSCiuc009jxg.1. mouse. [Q9D1P2-2]
    uc009jxh.1. mouse. [Q9D1P2-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK003264 mRNA. Translation: BAB22680.1 .
    AK018002 mRNA. Translation: BAC25539.1 . Frameshift.
    AK029350 mRNA. Translation: BAC26411.1 .
    AK146710 mRNA. Translation: BAE27376.1 .
    BC036284 mRNA. Translation: AAH36284.1 .
    CCDSi CCDS21885.1. [Q9D1P2-1 ]
    RefSeqi NP_080646.1. NM_026370.1. [Q9D1P2-1 ]
    UniGenei Mm.425492.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1WGS NMR - A 50-169 [» ]
    ProteinModelPortali Q9D1P2.
    SMRi Q9D1P2. Positions 47-169, 178-448.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 212433. 21 interactions.
    IntActi Q9D1P2. 16 interactions.

    PTM databases

    PhosphoSitei Q9D1P2.

    Proteomic databases

    PaxDbi Q9D1P2.
    PRIDEi Q9D1P2.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000033070 ; ENSMUSP00000033070 ; ENSMUSG00000030801 . [Q9D1P2-1 ]
    GeneIDi 67773.
    KEGGi mmu:67773.
    UCSCi uc009jxg.1. mouse. [Q9D1P2-2 ]
    uc009jxh.1. mouse. [Q9D1P2-1 ]

    Organism-specific databases

    CTDi 84148.
    MGIi MGI:1915023. Kat8.

    Phylogenomic databases

    eggNOGi COG5027.
    GeneTreei ENSGT00550000074503.
    HOGENOMi HOG000182457.
    HOVERGENi HBG053268.
    InParanoidi Q9D1P2.
    KOi K11308.
    OMAi DGRDHKI.
    OrthoDBi EOG7WHH8N.
    PhylomeDBi Q9D1P2.
    TreeFami TF317619.

    Enzyme and pathway databases

    Reactomei REACT_226917. HATs acetylate histones.

    Miscellaneous databases

    EvolutionaryTracei Q9D1P2.
    NextBioi 325529.
    PROi Q9D1P2.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q9D1P2.
    CleanExi MM_MYST1.
    Genevestigatori Q9D1P2.

    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. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
      Strain: C57BL/6J.
      Tissue: Amnion, Embryo, Head and Thymus.
    2. "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).
      Strain: FVB/N.
      Tissue: Liver.
    3. "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: INTERACTION WITH MSL1.
    4. "Solution structure of the Tudor domain from mouse hypothetical protein homologous to histone acetyltransferase."
      RIKEN structural genomics initiative (RSGI)
      Submitted (MAY-2004) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 50-169 (ISOFORM 1).

    Entry informationi

    Entry nameiKAT8_MOUSE
    AccessioniPrimary (citable) accession number: Q9D1P2
    Secondary accession number(s): Q3UIY0
    , Q8BJ69, Q8BJ76, Q8CI73
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 5, 2005
    Last sequence update: June 1, 2001
    Last modified: October 1, 2014
    This is version 116 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3