ID   KAT6A_MOUSE             Reviewed;        2003 AA.
AC   Q8BZ21; Q8BW52; Q8BYH1; Q8C1F3;
DT   05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, sequence version 2.
DT   24-JAN-2024, entry version 162.
DE   RecName: Full=Histone acetyltransferase KAT6A;
DE            EC=2.3.1.48 {ECO:0000250|UniProtKB:Q92794};
DE   AltName: Full=MOZ, YBF2/SAS3, SAS2 and TIP60 protein 3;
DE            Short=MYST-3;
DE   AltName: Full=Monocytic leukemia zinc finger homolog;
DE   AltName: Full=Monocytic leukemia zinc finger protein;
GN   Name=Kat6a; Synonyms=Moz, Myst3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1010.
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum, Ovary, Spinal cord, and Vagina;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   INTERACTION WITH RUNX1, FUNCTION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=11742995; DOI=10.1093/emboj/20.24.7184;
RA   Kitabayashi I., Aikawa Y., Nguyen L.A., Yokoyama A., Ohki M.;
RT   "Activation of AML1-mediated transcription by MOZ and inhibition by the
RT   MOZ-CBP fusion protein.";
RL   EMBO J. 20:7184-7196(2001).
RN   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-786, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Kidney, and Spleen;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [6]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-172; LYS-813 AND LYS-816, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA   Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA   Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT   "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT   pathways.";
RL   Mol. Cell 50:919-930(2013).
CC   -!- FUNCTION: Histone acetyltransferase that acetylates lysine residues in
CC       histone H3 and histone H4 (in vitro). Component of the MOZ/MORF complex
CC       which has a histone H3 acetyltransferase activity. May act as a
CC       transcriptional coactivator for RUNX1 and RUNX2 (By similarity).
CC       Acetylates p53/TP53 at 'Lys-120' and 'Lys-382' and controls its
CC       transcriptional activity via association with PML (By similarity).
CC       {ECO:0000250|UniProtKB:Q92794, ECO:0000269|PubMed:11742995}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + L-lysyl-[protein] = CoA + H(+) + N(6)-acetyl-L-
CC         lysyl-[protein]; Xref=Rhea:RHEA:45948, Rhea:RHEA-COMP:9752,
CC         Rhea:RHEA-COMP:10731, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:61930; EC=2.3.1.48;
CC         Evidence={ECO:0000250|UniProtKB:Q92794};
CC   -!- SUBUNIT: Component of the MOZ/MORF complex composed at least of ING5,
CC       KAT6A, KAT6B, MEAF6 and one of BRPF1, BRD1/BRPF2 and BRPF3 (By
CC       similarity). Interacts with RUNX2 (By similarity). Interacts with
CC       RUNX1; phosphorylation of RUNX1 enhances the interaction. Interacts
CC       with p53/TP53 (By similarity). Interacts with PML and this interaction
CC       positively regulates its acetylation activity towards p53/TP53 (By
CC       similarity). {ECO:0000250|UniProtKB:Q92794}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00837}.
CC       Nucleus, nucleolus {ECO:0000250|UniProtKB:Q92794}. Nucleus, nucleoplasm
CC       {ECO:0000250|UniProtKB:Q92794}. Nucleus, PML body
CC       {ECO:0000250|UniProtKB:Q92794}. Note=Recruited into PML body after DNA
CC       damage. {ECO:0000250|UniProtKB:Q92794}.
CC   -!- DOMAIN: The N-terminus is involved in transcriptional activation while
CC       the C-terminus is involved in transcriptional repression.
CC       {ECO:0000250}.
CC   -!- PTM: Autoacetylated. Autoacetylation at Lys-603 is required for proper
CC       function. {ECO:0000250|UniProtKB:Q9H7Z6}.
CC   -!- PTM: Phosphorylation at Thr-369 by PKB/AKT1 inhibits its interaction
CC       with PML and negatively regulates its acetylation activity towards
CC       p53/TP53. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the MYST (SAS/MOZ) family. {ECO:0000305}.
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DR   EMBL; AC115361; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AK028058; BAC25728.1; -; mRNA.
DR   EMBL; AK036885; BAC29621.1; -; mRNA.
DR   EMBL; AK039615; BAC30401.1; -; mRNA.
DR   EMBL; AK054322; BAC35729.1; -; mRNA.
DR   CCDS; CCDS40294.1; -.
DR   AlphaFoldDB; Q8BZ21; -.
DR   BMRB; Q8BZ21; -.
DR   SMR; Q8BZ21; -.
DR   ComplexPortal; CPX-800; MOZ1 histone acetyltransferase complex.
DR   ComplexPortal; CPX-801; MOZ2 histone acetyltransferase complex.
DR   ComplexPortal; CPX-802; MOZ3 histone acetyltransferase complex.
DR   IntAct; Q8BZ21; 1.
DR   STRING; 10090.ENSMUSP00000038181; -.
DR   BindingDB; Q8BZ21; -.
DR   ChEMBL; CHEMBL4523382; -.
DR   GlyGen; Q8BZ21; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q8BZ21; -.
DR   PhosphoSitePlus; Q8BZ21; -.
DR   EPD; Q8BZ21; -.
DR   jPOST; Q8BZ21; -.
DR   MaxQB; Q8BZ21; -.
DR   PaxDb; 10090-ENSMUSP00000038181; -.
DR   ProteomicsDB; 263574; -.
DR   AGR; MGI:2442415; -.
DR   MGI; MGI:2442415; Kat6a.
DR   eggNOG; KOG2747; Eukaryota.
DR   InParanoid; Q8BZ21; -.
DR   PhylomeDB; Q8BZ21; -.
DR   BRENDA; 2.3.1.48; 3474.
DR   Reactome; R-MMU-3214847; HATs acetylate histones.
DR   Reactome; R-MMU-6804758; Regulation of TP53 Activity through Acetylation.
DR   ChiTaRS; Kat6a; mouse.
DR   PRO; PR:Q8BZ21; -.
DR   Proteomes; UP000000589; Unplaced.
DR   RNAct; Q8BZ21; Protein.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0070776; C:MOZ/MORF histone acetyltransferase complex; ISS:UniProtKB.
DR   GO; GO:0016607; C:nuclear speck; ISO:MGI.
DR   GO; GO:0005730; C:nucleolus; ISO:MGI.
DR   GO; GO:0000786; C:nucleosome; IEA:InterPro.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0016605; C:PML body; ISS:UniProtKB.
DR   GO; GO:0003682; F:chromatin binding; IGI:MGI.
DR   GO; GO:0003677; F:DNA binding; ISS:UniProtKB.
DR   GO; GO:0140297; F:DNA-binding transcription factor binding; ISO:MGI.
DR   GO; GO:0004402; F:histone acetyltransferase activity; ISO:MGI.
DR   GO; GO:0036408; F:histone H3K14 acetyltransferase activity; ISS:UniProtKB.
DR   GO; GO:0043992; F:histone H3K9 acetyltransferase activity; IMP:MGI.
DR   GO; GO:0043997; F:histone H4K12 acetyltransferase activity; ISO:MGI.
DR   GO; GO:0046972; F:histone H4K16 acetyltransferase activity; ISO:MGI.
DR   GO; GO:0043995; F:histone H4K5 acetyltransferase activity; ISS:UniProtKB.
DR   GO; GO:0043996; F:histone H4K8 acetyltransferase activity; ISO:MGI.
DR   GO; GO:0003713; F:transcription coactivator activity; ISO:MGI.
DR   GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central.
DR   GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR   GO; GO:0035909; P:aorta morphogenesis; IMP:MGI.
DR   GO; GO:0090398; P:cellular senescence; ISS:UniProtKB.
DR   GO; GO:0035162; P:embryonic hemopoiesis; IMP:MGI.
DR   GO; GO:0060325; P:face morphogenesis; IMP:MGI.
DR   GO; GO:0003007; P:heart morphogenesis; IMP:MGI.
DR   GO; GO:0030099; P:myeloid cell differentiation; ISS:UniProtKB.
DR   GO; GO:0045892; P:negative regulation of DNA-templated transcription; ISS:UniProtKB.
DR   GO; GO:0006334; P:nucleosome assembly; IEA:InterPro.
DR   GO; GO:0045893; P:positive regulation of DNA-templated transcription; ISS:UniProtKB.
DR   GO; GO:0010628; P:positive regulation of gene expression; ISO:MGI.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0006473; P:protein acetylation; ISS:UniProtKB.
DR   GO; GO:0050793; P:regulation of developmental process; NAS:ComplexPortal.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; ISO:MGI.
DR   GO; GO:1903706; P:regulation of hemopoiesis; NAS:ComplexPortal.
DR   GO; GO:0035019; P:somatic stem cell population maintenance; IMP:MGI.
DR   CDD; cd04301; NAT_SF; 1.
DR   CDD; cd15618; PHD1_MOZ_MORF; 1.
DR   CDD; cd15527; PHD2_KAT6A_6B; 1.
DR   Gene3D; 3.40.630.30; -; 1.
DR   Gene3D; 3.30.60.60; N-acetyl transferase-like; 1.
DR   Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 2.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR   InterPro; IPR002717; HAT_MYST-type.
DR   InterPro; IPR005818; Histone_H1/H5_H15.
DR   InterPro; IPR048589; SAMD1-like_WH.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   InterPro; IPR040706; Zf-MYST.
DR   InterPro; IPR011011; Znf_FYVE_PHD.
DR   InterPro; IPR001965; Znf_PHD.
DR   InterPro; IPR019787; Znf_PHD-finger.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR10615; HISTONE ACETYLTRANSFERASE; 1.
DR   PANTHER; PTHR10615:SF26; HISTONE ACETYLTRANSFERASE KAT6A; 1.
DR   Pfam; PF01853; MOZ_SAS; 1.
DR   Pfam; PF00628; PHD; 2.
DR   Pfam; PF21524; SAMD1_WH; 1.
DR   Pfam; PF17772; zf-MYST; 1.
DR   SMART; SM00526; H15; 1.
DR   SMART; SM00249; PHD; 2.
DR   SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 1.
DR   SUPFAM; SSF57903; FYVE/PHD zinc finger; 2.
DR   SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR   PROSITE; PS51504; H15; 1.
DR   PROSITE; PS51726; MYST_HAT; 1.
DR   PROSITE; PS52014; SAMD1_WH; 1.
DR   PROSITE; PS01359; ZF_PHD_1; 1.
DR   PROSITE; PS50016; ZF_PHD_2; 2.
PE   1: Evidence at protein level;
KW   Acetylation; Activator; Acyltransferase; Chromatin regulator;
KW   Isopeptide bond; Metal-binding; Nucleus; Phosphoprotein;
KW   Reference proteome; Repeat; Repressor; Transcription;
KW   Transcription regulation; Transferase; Ubl conjugation; Zinc; Zinc-finger.
FT   CHAIN           1..2003
FT                   /note="Histone acetyltransferase KAT6A"
FT                   /id="PRO_0000051573"
FT   DOMAIN          1..77
FT                   /note="SAMD1-like winged helix (WH)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01358"
FT   DOMAIN          95..171
FT                   /note="H15"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00837"
FT   DOMAIN          503..777
FT                   /note="MYST-type HAT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01063"
FT   ZN_FING         206..265
FT                   /note="PHD-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT   ZN_FING         262..313
FT                   /note="PHD-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT   ZN_FING         536..561
FT                   /note="C2HC MYST-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01063"
FT   REGION          1..144
FT                   /note="Required for activation of RUNX1-1"
FT                   /evidence="ECO:0000250|UniProtKB:Q92794"
FT   REGION          52..166
FT                   /note="Required for nuclear localization"
FT                   /evidence="ECO:0000250"
FT   REGION          144..663
FT                   /note="Interaction with PML"
FT                   /evidence="ECO:0000250"
FT   REGION          312..663
FT                   /note="Interaction with RUNX1-1"
FT                   /evidence="ECO:0000250"
FT   REGION          336..377
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          439..466
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          487..777
FT                   /note="Catalytic"
FT                   /evidence="ECO:0000250"
FT   REGION          506..809
FT                   /note="Mediates interaction with BRPF1, required for
FT                   histone H3 acetyltransferase activity"
FT                   /evidence="ECO:0000250"
FT   REGION          784..939
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          983..1083
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1096..1174
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1197..1438
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1455..1533
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1511..1740
FT                   /note="Interaction with PML"
FT                   /evidence="ECO:0000250"
FT   REGION          1511..1636
FT                   /note="Interaction with RUNX1-2"
FT                   /evidence="ECO:0000250"
FT   REGION          1546..1568
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1631..1707
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1912..1947
FT                   /note="Required for activation of RUNX1-2"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        799..843
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        844..858
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        875..890
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        902..916
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1011..1029
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1065..1079
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1151..1172
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1202..1229
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1262..1314
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1315..1340
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1396..1414
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1417..1431
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1472..1533
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1638..1700
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        679
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H7Z6"
FT   BINDING         644..648
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000250|UniProtKB:Q92794"
FT   BINDING         653..659
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000250|UniProtKB:Q92794"
FT   BINDING         683
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000250|UniProtKB:Q92794"
FT   MOD_RES         172
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:23806337"
FT   MOD_RES         350
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q92794"
FT   MOD_RES         355
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q92794"
FT   MOD_RES         369
FT                   /note="Phosphothreonine; by PKB/AKT1"
FT                   /evidence="ECO:0000250|UniProtKB:Q92794"
FT   MOD_RES         419
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q92794"
FT   MOD_RES         472
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q92794"
FT   MOD_RES         603
FT                   /note="N6-acetyllysine; by autocatalysis"
FT                   /evidence="ECO:0000250|UniProtKB:Q92794"
FT   MOD_RES         786
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         813
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:23806337"
FT   MOD_RES         816
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:23806337"
FT   MOD_RES         901
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:Q5TKR9"
FT   MOD_RES         941
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q92794"
FT   MOD_RES         954
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q92794"
FT   MOD_RES         1007
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q92794"
FT   MOD_RES         1090
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q92794"
FT   MOD_RES         1091
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q92794"
FT   MOD_RES         1115
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q92794"
FT   CROSSLNK        836
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q92794"
FT   CROSSLNK        1336
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q92794"
SQ   SEQUENCE   2003 AA;  224919 MW;  93D0D687A1621B31 CRC64;
     MVKLANPLYT EWILEAIKKV KKQKQRPSEE RICNAVSSSH GLDRRTVLEQ LELSVKDGTI
     LKVSNKGLNS YKDPDNPGRI ALPKPRNHGK LDTKQSVDWN KLLKRAFEGL AETGGSTLKS
     IERFLKSQKD VSAACGGSAA PGFHQQLRLA IKRAVGHGRL LKDGPLYRLN TKAASAEGKE
     GCESLSCLPP VSLLPHEKDK PVAEPIPICS FCLGTKEQNR EKQPEELVSC ADCGNSGHPS
     CLKFSPELTV RVKALRWQCI ECKTCSSCRD QGKNADNMLF CDSCDRGFHM ECCDPPLTRM
     PKGMWICQIC RPRKKGRKLL QKKAAQIKRR YANPIGRPKN RLKKQNTVSK GPFSKVRTGP
     GRGRKRKITV SSQSASSSEE GYLERIDGLD FCRDSNAPLK FNKKTKGLID GLTKFFTPSP
     DGRKARGEVV DYSEQYRIRK KGNRKSSTSD WPTDNQDGWE SKQENEERLF GSQEIMTERD
     MELFRDIQEQ ALQKVGVTGP PDPQVRCPSV IEFGKYEIHT WYSSPYPQEY SRLPKLYLCE
     FCLKYMKSRT ILQQHMKKCG WFHPPANEIY RKNNISVFEV DGNVSTIYCQ NLCLLAKLFL
     DHKTLYYDVE PFLFYVLTQN DVKGCHLVGY FSKEKHCQQK YNVSCIMILP QYQRKGYGRF
     LIDFSYLLSK REGQAGSPEK PLSDLGRLSY MAYWKSVILE CLYHQNDKQI SIKKLSKLTG
     VCPQDITSTL HHLRMLDFRS DQFVIIRREK LIQDHMAKLQ LNLRPVDVDP ECLRWTPVIV
     SNSVVSEDED EEADEGEKEE PQGQERELET RVKVGKSVSR EKKDQESSSL IETDKKPEVK
     ELASSSRLSK QALPRDSLPA NSQPPRRGRC GRKNRKTQER FGDKDSKMLV DETLSASQEQ
     YGDCEEKSET SQERFTEMEE QLAAPQVQAD GKPDIPKGRF SESVELWRGQ LKKSPETLKC
     RLPEGNDRLP CCYTDGDRAF FRGFSESSEE EEEPESPRSN SPPILTKPTL KRKKPILHRR
     RRVRKRKHHN SSVVTETISE TTEVLDEPFE DSDSERPMPR LEPTFEMEEE EEEEEEESEL
     FPRGYFHCLS SQDILRCQSS SKRPSKEEEE EEEESDDADD TPVLKPVSLL RKCDVNSASL
     EPDTSTPMKK KKGWPKGKSR KPIHWKKRPG RKPGFKLNQE IIAASAQECI VEPVVPIKPG
     RKPRTQENEE IVEVKEDLLE ERKEEMHTEP DEEAEEEEDT TSSDIRAMSP LDSSNSPEAE
     PKEPEPEEED EKPSDDQRQS EEEPQELEEQ EQEEEDEVTT EANQNEDHDA DDEDEGHLDS
     LKTKEPEEQP AREDDKEEPG IQGSFLAANM QDSRENTKDK DEAEPDSEED QPSHEASVVS
     ETMPGSEEDH EEDSNTKEEL IELKEEEEIP HSELDLETVQ AVQSLTQEES SEHEGAYQDC
     EETLAACQTL QSYTHTDEDP QMSMVEDCHA SEHNSPISSI PSHPSQSVRS VNSPSMPALE
     SGYTQISPEQ GSLSAPSMQN METSPMMDVP SVSDHSQQVV DSGFSDLGSI ESTTENYENP
     SSYDSTMGSS ICGNNSSQSS CSYGGLSSSS SLTQNSCVVT QQMANMGNSC SMLQQNTVQP
     AANCNIKSPQ TCVVERPPSN QQPPPPPPPP PPPQQPQPPP QQQAAPQPPP PQPQQQQQQQ
     QQPPPPQQQP QPPPPQQQPP LSQCSMNNSF TAAPMIMEIP ESGSTGNISI YERIPGDFGA
     GSYSQPSATF SLAKLQQLTN TIMDPHAMPY SHSPAVTSYA TSVSLSNTGL AQLAPSHPLA
     GTPQAQATMT PPPNLASTTM NLTSPLLQCN MSATNIGIPH TQRLQGQMPV KGHISIRSKS
     APLPSATAHQ QQLYGRSPPA VAMQAGPRAL AVQRGMNMGV NLMPTPAYNV NSMNMNTLNA
     MNSYRMTQPM MNSSYHSNPA YMNQTAQYPM QMQMGMMGSQ AYTQQPMQPN PHGNMMYTGP
     SHHSYMNAAG VPKQSLNGPY MRR
//