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Q8BZ21

- KAT6A_MOUSE

UniProt

Q8BZ21 - KAT6A_MOUSE

Protein

Histone acetyltransferase KAT6A

Gene

Kat6a

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 108 (01 Oct 2014)
      Sequence version 2 (05 Jul 2005)
      Previous versions | rss
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    Functioni

    Histone acetyltransferase that acetylates lysine residues in histone H3 and histone H4 (in vitro). Component of the MOZ/MORF complex which has a histone H3 acetyltransferase activity. May act as a transcriptional coactivator for RUNX1 and RUNX2 By similarity. Acetylates p53/TP53 at 'Lys-120' and 'Lys-382' and controls its transcriptional activity via association with PML By similarity.By similarity

    Catalytic activityi

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei603 – 6031By similarity
    Active sitei645 – 6451NucleophileBy similarity
    Binding sitei683 – 6831Acetyl-CoABy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri206 – 26560PHD-type 1PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri262 – 31352PHD-type 2PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri537 – 55923C2HC-typeAdd
    BLAST

    GO - Molecular functioni

    1. acetyltransferase activity Source: UniProtKB
    2. chromatin binding Source: MGI
    3. DNA binding Source: UniProtKB
    4. histone acetyltransferase activity Source: UniProtKB
    5. protein binding Source: MGI
    6. transcription factor binding Source: UniProtKB
    7. zinc ion binding Source: UniProtKB

    GO - Biological processi

    1. aorta morphogenesis Source: MGI
    2. cellular senescence Source: UniProtKB
    3. embryonic hemopoiesis Source: MGI
    4. face morphogenesis Source: MGI
    5. heart morphogenesis Source: MGI
    6. histone acetylation Source: UniProtKB
    7. histone H3 acetylation Source: UniProtKB
    8. myeloid cell differentiation Source: UniProtKB
    9. negative regulation of sequence-specific DNA binding transcription factor activity Source: MGI
    10. negative regulation of transcription, DNA-templated Source: UniProtKB
    11. nucleosome assembly Source: InterPro
    12. positive regulation of transcription, DNA-templated Source: UniProtKB
    13. protein acetylation Source: UniProtKB
    14. somatic stem cell maintenance Source: MGI
    15. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Activator, Acyltransferase, Chromatin regulator, Repressor, Transferase

    Keywords - Biological processi

    Transcription, Transcription regulation

    Keywords - Ligandi

    Metal-binding, Zinc

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Histone acetyltransferase KAT6A (EC:2.3.1.48)
    Alternative name(s):
    MOZ, YBF2/SAS3, SAS2 and TIP60 protein 3
    Short name:
    MYST-3
    Monocytic leukemia zinc finger homolog
    Monocytic leukemia zinc finger protein
    Gene namesi
    Name:Kat6a
    Synonyms:Moz, Myst3
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Unplaced

    Organism-specific databases

    MGIiMGI:2442415. Kat6a.

    Subcellular locationi

    Nucleus PROSITE-ProRule annotation. Nucleusnucleolus By similarity. Nucleusnucleoplasm By similarity. NucleusPML body By similarity
    Note: Recruited into PML body after DNA damage.By similarity

    GO - Cellular componenti

    1. MOZ/MORF histone acetyltransferase complex Source: UniProtKB
    2. nucleolus Source: UniProtKB-SubCell
    3. nucleosome Source: InterPro
    4. nucleus Source: UniProtKB
    5. PML body Source: UniProtKB

    Keywords - Cellular componenti

    Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 20032003Histone acetyltransferase KAT6APRO_0000051573Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei172 – 1721N6-acetyllysine1 Publication
    Modified residuei350 – 3501N6-acetyllysineBy similarity
    Modified residuei355 – 3551N6-acetyllysineBy similarity
    Modified residuei369 – 3691Phosphothreonine; by PKB/AKT1By similarity
    Modified residuei472 – 4721PhosphoserineBy similarity
    Modified residuei603 – 6031N6-acetyllysine; by autocatalysisBy similarity
    Modified residuei813 – 8131N6-acetyllysine1 Publication
    Modified residuei816 – 8161N6-acetyllysine1 Publication
    Modified residuei901 – 9011PhosphotyrosineBy similarity
    Modified residuei1007 – 10071N6-acetyllysineBy similarity
    Modified residuei1115 – 11151PhosphoserineBy similarity

    Post-translational modificationi

    Autoacetylated. Autoacetylation at Lys-603 is required for proper function By similarity.By similarity
    Phosphorylation at Thr-369 by PKB/AKT1 inhibits its interaction with PML and negatively regulates its acetylation activity towards p53/TP53.By similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    PRIDEiQ8BZ21.

    PTM databases

    PhosphoSiteiQ8BZ21.

    Expressioni

    Gene expression databases

    GenevestigatoriQ8BZ21.

    Interactioni

    Subunit structurei

    Component of the MOZ/MORF complex composed at least of ING5, KAT6A, KAT6B, MEAF6 and one of BRPF1, BRD1/BRPF2 and BRPF3 By similarity. Interacts with RUNX2 By similarity. Interacts with RUNX1; phosphorylation of RUNX1 enhances the interaction. Interacts with p53/TP53 By similarity. Interacts with PML and this interaction positively regulates its acetylation activity towards p53/TP53 By similarity.By similarity

    Structurei

    3D structure databases

    ProteinModelPortaliQ8BZ21.
    SMRiQ8BZ21. Positions 194-315, 506-778.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini95 – 17177H15PROSITE-ProRule annotationAdd
    BLAST
    Domaini503 – 777275MYST-type HATAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 144144Required for activation of RUNX1-1By similarityAdd
    BLAST
    Regioni52 – 166115Required for nuclear localizationBy similarityAdd
    BLAST
    Regioni144 – 663520Interaction with PMLBy similarityAdd
    BLAST
    Regioni312 – 663352Interaction with RUNX1-1By similarityAdd
    BLAST
    Regioni487 – 777291CatalyticBy similarityAdd
    BLAST
    Regioni506 – 809304Mediates interaction with BRPF1, required for histone H3 acetyltransferase activityBy similarityAdd
    BLAST
    Regioni644 – 6485Acetyl-CoA bindingBy similarity
    Regioni653 – 6597Acetyl-CoA bindingBy similarity
    Regioni1511 – 1740230Interaction with PMLBy similarityAdd
    BLAST
    Regioni1511 – 1636126Interaction with RUNX1-2By similarityAdd
    BLAST
    Regioni1912 – 194736Required for activation of RUNX1-2By similarityAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi989 – 9957Poly-Glu
    Compositional biasi1019 – 10268Poly-Arg
    Compositional biasi1066 – 107914Poly-GluAdd
    BLAST
    Compositional biasi1107 – 11148Poly-Glu
    Compositional biasi1149 – 117628Lys-richAdd
    BLAST
    Compositional biasi1232 – 12387Poly-Glu
    Compositional biasi1405 – 14084Poly-Glu
    Compositional biasi1471 – 1591121Ser-richAdd
    BLAST
    Compositional biasi1601 – 1703103Gln-richAdd
    BLAST
    Compositional biasi1896 – 197681Met-richAdd
    BLAST

    Domaini

    The N-terminus is involved in transcriptional activation while the C-terminus is involved in transcriptional repression.By similarity

    Sequence similaritiesi

    Belongs to the MYST (SAS/MOZ) family.Curated
    Contains 1 C2HC-type zinc finger.Curated
    Contains 1 H15 (linker histone H1/H5 globular) domain.PROSITE-ProRule annotation
    Contains 2 PHD-type zinc fingers.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri206 – 26560PHD-type 1PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri262 – 31352PHD-type 2PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri537 – 55923C2HC-typeAdd
    BLAST

    Keywords - Domaini

    Repeat, Zinc-finger

    Phylogenomic databases

    eggNOGiCOG5027.
    HOGENOMiHOG000234365.
    HOVERGENiHBG052563.
    InParanoidiQ8BZ21.
    PhylomeDBiQ8BZ21.

    Family and domain databases

    Gene3Di3.30.40.10. 2 hits.
    3.40.630.30. 1 hit.
    InterProiIPR016181. Acyl_CoA_acyltransferase.
    IPR005818. Histone_H1/H5_H15.
    IPR002717. MOZ_SAS.
    IPR011011. Znf_FYVE_PHD.
    IPR001965. Znf_PHD.
    IPR019787. Znf_PHD-finger.
    IPR001841. Znf_RING.
    IPR013083. Znf_RING/FYVE/PHD.
    [Graphical view]
    PfamiPF01853. MOZ_SAS. 1 hit.
    PF00628. PHD. 1 hit.
    [Graphical view]
    SMARTiSM00526. H15. 1 hit.
    SM00249. PHD. 2 hits.
    SM00184. RING. 2 hits.
    [Graphical view]
    SUPFAMiSSF55729. SSF55729. 1 hit.
    SSF57903. SSF57903. 2 hits.
    PROSITEiPS51504. H15. 1 hit.
    PS51726. MYST_HAT. 1 hit.
    PS01359. ZF_PHD_1. 1 hit.
    PS50016. ZF_PHD_2. 2 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q8BZ21-1 [UniParc]FASTAAdd to Basket

    « Hide

    MVKLANPLYT EWILEAIKKV KKQKQRPSEE RICNAVSSSH GLDRRTVLEQ     50
    LELSVKDGTI LKVSNKGLNS YKDPDNPGRI ALPKPRNHGK LDTKQSVDWN 100
    KLLKRAFEGL AETGGSTLKS IERFLKSQKD VSAACGGSAA PGFHQQLRLA 150
    IKRAVGHGRL LKDGPLYRLN TKAASAEGKE GCESLSCLPP VSLLPHEKDK 200
    PVAEPIPICS FCLGTKEQNR EKQPEELVSC ADCGNSGHPS CLKFSPELTV 250
    RVKALRWQCI ECKTCSSCRD QGKNADNMLF CDSCDRGFHM ECCDPPLTRM 300
    PKGMWICQIC RPRKKGRKLL QKKAAQIKRR YANPIGRPKN RLKKQNTVSK 350
    GPFSKVRTGP GRGRKRKITV SSQSASSSEE GYLERIDGLD FCRDSNAPLK 400
    FNKKTKGLID GLTKFFTPSP DGRKARGEVV DYSEQYRIRK KGNRKSSTSD 450
    WPTDNQDGWE SKQENEERLF GSQEIMTERD MELFRDIQEQ ALQKVGVTGP 500
    PDPQVRCPSV IEFGKYEIHT WYSSPYPQEY SRLPKLYLCE FCLKYMKSRT 550
    ILQQHMKKCG WFHPPANEIY RKNNISVFEV DGNVSTIYCQ NLCLLAKLFL 600
    DHKTLYYDVE PFLFYVLTQN DVKGCHLVGY FSKEKHCQQK YNVSCIMILP 650
    QYQRKGYGRF LIDFSYLLSK REGQAGSPEK PLSDLGRLSY MAYWKSVILE 700
    CLYHQNDKQI SIKKLSKLTG VCPQDITSTL HHLRMLDFRS DQFVIIRREK 750
    LIQDHMAKLQ LNLRPVDVDP ECLRWTPVIV SNSVVSEDED EEADEGEKEE 800
    PQGQERELET RVKVGKSVSR EKKDQESSSL IETDKKPEVK ELASSSRLSK 850
    QALPRDSLPA NSQPPRRGRC GRKNRKTQER FGDKDSKMLV DETLSASQEQ 900
    YGDCEEKSET SQERFTEMEE QLAAPQVQAD GKPDIPKGRF SESVELWRGQ 950
    LKKSPETLKC RLPEGNDRLP CCYTDGDRAF FRGFSESSEE EEEPESPRSN 1000
    SPPILTKPTL KRKKPILHRR RRVRKRKHHN SSVVTETISE TTEVLDEPFE 1050
    DSDSERPMPR LEPTFEMEEE EEEEEEESEL FPRGYFHCLS SQDILRCQSS 1100
    SKRPSKEEEE EEEESDDADD TPVLKPVSLL RKCDVNSASL EPDTSTPMKK 1150
    KKGWPKGKSR KPIHWKKRPG RKPGFKLNQE IIAASAQECI VEPVVPIKPG 1200
    RKPRTQENEE IVEVKEDLLE ERKEEMHTEP DEEAEEEEDT TSSDIRAMSP 1250
    LDSSNSPEAE PKEPEPEEED EKPSDDQRQS EEEPQELEEQ EQEEEDEVTT 1300
    EANQNEDHDA DDEDEGHLDS LKTKEPEEQP AREDDKEEPG IQGSFLAANM 1350
    QDSRENTKDK DEAEPDSEED QPSHEASVVS ETMPGSEEDH EEDSNTKEEL 1400
    IELKEEEEIP HSELDLETVQ AVQSLTQEES SEHEGAYQDC EETLAACQTL 1450
    QSYTHTDEDP QMSMVEDCHA SEHNSPISSI PSHPSQSVRS VNSPSMPALE 1500
    SGYTQISPEQ GSLSAPSMQN METSPMMDVP SVSDHSQQVV DSGFSDLGSI 1550
    ESTTENYENP SSYDSTMGSS ICGNNSSQSS CSYGGLSSSS SLTQNSCVVT 1600
    QQMANMGNSC SMLQQNTVQP AANCNIKSPQ TCVVERPPSN QQPPPPPPPP 1650
    PPPQQPQPPP QQQAAPQPPP PQPQQQQQQQ QQPPPPQQQP QPPPPQQQPP 1700
    LSQCSMNNSF TAAPMIMEIP ESGSTGNISI YERIPGDFGA GSYSQPSATF 1750
    SLAKLQQLTN TIMDPHAMPY SHSPAVTSYA TSVSLSNTGL AQLAPSHPLA 1800
    GTPQAQATMT PPPNLASTTM NLTSPLLQCN MSATNIGIPH TQRLQGQMPV 1850
    KGHISIRSKS APLPSATAHQ QQLYGRSPPA VAMQAGPRAL AVQRGMNMGV 1900
    NLMPTPAYNV NSMNMNTLNA MNSYRMTQPM MNSSYHSNPA YMNQTAQYPM 1950
    QMQMGMMGSQ AYTQQPMQPN PHGNMMYTGP SHHSYMNAAG VPKQSLNGPY 2000
    MRR 2003
    Length:2,003
    Mass (Da):224,919
    Last modified:July 5, 2005 - v2
    Checksum:i93D0D687A1621B31
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AC115361 Genomic DNA. No translation available.
    AK028058 mRNA. Translation: BAC25728.1.
    AK036885 mRNA. Translation: BAC29621.1.
    AK039615 mRNA. Translation: BAC30401.1.
    AK054322 mRNA. Translation: BAC35729.1.
    CCDSiCCDS40294.1.
    UniGeneiMm.182776.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AC115361 Genomic DNA. No translation available.
    AK028058 mRNA. Translation: BAC25728.1 .
    AK036885 mRNA. Translation: BAC29621.1 .
    AK039615 mRNA. Translation: BAC30401.1 .
    AK054322 mRNA. Translation: BAC35729.1 .
    CCDSi CCDS40294.1.
    UniGenei Mm.182776.

    3D structure databases

    ProteinModelPortali Q8BZ21.
    SMRi Q8BZ21. Positions 194-315, 506-778.
    ModBasei Search...
    MobiDBi Search...

    PTM databases

    PhosphoSitei Q8BZ21.

    Proteomic databases

    PRIDEi Q8BZ21.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Organism-specific databases

    MGIi MGI:2442415. Kat6a.

    Phylogenomic databases

    eggNOGi COG5027.
    HOGENOMi HOG000234365.
    HOVERGENi HBG052563.
    InParanoidi Q8BZ21.
    PhylomeDBi Q8BZ21.

    Miscellaneous databases

    ChiTaRSi KAT6A. mouse.
    PROi Q8BZ21.
    SOURCEi Search...

    Gene expression databases

    Genevestigatori Q8BZ21.

    Family and domain databases

    Gene3Di 3.30.40.10. 2 hits.
    3.40.630.30. 1 hit.
    InterProi IPR016181. Acyl_CoA_acyltransferase.
    IPR005818. Histone_H1/H5_H15.
    IPR002717. MOZ_SAS.
    IPR011011. Znf_FYVE_PHD.
    IPR001965. Znf_PHD.
    IPR019787. Znf_PHD-finger.
    IPR001841. Znf_RING.
    IPR013083. Znf_RING/FYVE/PHD.
    [Graphical view ]
    Pfami PF01853. MOZ_SAS. 1 hit.
    PF00628. PHD. 1 hit.
    [Graphical view ]
    SMARTi SM00526. H15. 1 hit.
    SM00249. PHD. 2 hits.
    SM00184. RING. 2 hits.
    [Graphical view ]
    SUPFAMi SSF55729. SSF55729. 1 hit.
    SSF57903. SSF57903. 2 hits.
    PROSITEi PS51504. H15. 1 hit.
    PS51726. MYST_HAT. 1 hit.
    PS01359. ZF_PHD_1. 1 hit.
    PS50016. ZF_PHD_2. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    2. "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] OF 1-1010.
      Strain: C57BL/6J.
      Tissue: Cerebellum, Ovary, Spinal cord and Vagina.
    3. "Activation of AML1-mediated transcription by MOZ and inhibition by the MOZ-CBP fusion protein."
      Kitabayashi I., Aikawa Y., Nguyen L.A., Yokoyama A., Ohki M.
      EMBO J. 20:7184-7196(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RUNX1, FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY.
    4. "The phagosomal proteome in interferon-gamma-activated macrophages."
      Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
      Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    5. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
      Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
      Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-172; LYS-813 AND LYS-816, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic fibroblast.

    Entry informationi

    Entry nameiKAT6A_MOUSE
    AccessioniPrimary (citable) accession number: Q8BZ21
    Secondary accession number(s): Q8BW52, Q8BYH1, Q8C1F3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 5, 2005
    Last sequence update: July 5, 2005
    Last modified: October 1, 2014
    This is version 108 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

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

    External Data

    Dasty 3