KAT6B_MACFA
ID KAT6B_MACFA Reviewed; 1784 AA.
AC Q8WML3;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Histone acetyltransferase KAT6B;
DE EC=2.3.1.48 {ECO:0000250|UniProtKB:Q8WYB5};
DE AltName: Full=MOZ, YBF2/SAS3, SAS2 and TIP60 protein 4;
DE Short=MYST-4;
GN Name=KAT6B; Synonyms=MYST4; ORFNames=QflA-12408;
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Frontal cortex;
RA Osada N., Hida M., Kusuda J., Tanuma R., Hirata M., Terao K., Hirai M.,
RA Sugano S., Hashimoto K.;
RT "Isolation of full-length cDNA clones from macaque brain cDNA libraries.";
RL Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Histone acetyltransferase which may be involved in both
CC positive and negative regulation of transcription. Required for RUNX2-
CC dependent transcriptional activation. May be involved in cerebral
CC cortex development. Component of the MOZ/MORF complex which has a
CC histone H3 acetyltransferase activity. {ECO:0000250|UniProtKB:Q8WYB5}.
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:Q8WYB5};
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. Interacts
CC with RUNX1 and RUNX2. {ECO:0000250|UniProtKB:Q8WYB5}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
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: Autoacetylation at Lys-523 is required for proper function.
CC {ECO:0000250|UniProtKB:Q9H7Z6}.
CC -!- SIMILARITY: Belongs to the MYST (SAS/MOZ) family. {ECO:0000305}.
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DR EMBL; AB061870; BAB72094.1; -; mRNA.
DR AlphaFoldDB; Q8WML3; -.
DR SMR; Q8WML3; -.
DR eggNOG; KOG2747; Eukaryota.
DR Proteomes; UP000233100; Unplaced.
DR GO; GO:0070776; C:MOZ/MORF histone acetyltransferase complex; ISS:UniProtKB.
DR GO; GO:0000786; C:nucleosome; IEA:InterPro.
DR GO; GO:0016407; F:acetyltransferase activity; ISS:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0004402; F:histone acetyltransferase activity; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; ISS:UniProtKB.
DR GO; GO:0016573; P:histone acetylation; ISS:UniProtKB.
DR GO; GO:0043966; P:histone H3 acetylation; ISS:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0006334; P:nucleosome assembly; IEA:InterPro.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
DR Gene3D; 1.10.10.10; -; 2.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR002717; HAT_MYST-type.
DR InterPro; IPR005818; Histone_H1/H5_H15.
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 Pfam; PF01853; MOZ_SAS; 1.
DR Pfam; PF00628; PHD; 1.
DR Pfam; PF17772; zf-MYST; 1.
DR SMART; SM00526; H15; 1.
DR SMART; SM00249; PHD; 2.
DR SUPFAM; SSF46785; SSF46785; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR SUPFAM; SSF55729; SSF55729; 1.
DR SUPFAM; SSF57903; SSF57903; 1.
DR PROSITE; PS51504; H15; 1.
DR PROSITE; PS51726; MYST_HAT; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 2.
PE 2: Evidence at transcript 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..1784
FT /note="Histone acetyltransferase KAT6B"
FT /id="PRO_0000051576"
FT DOMAIN 103..176
FT /note="H15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00837"
FT DOMAIN 423..697
FT /note="MYST-type HAT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01063"
FT ZN_FING 213..272
FT /note="PHD-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT ZN_FING 269..320
FT /note="PHD-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT ZN_FING 456..481
FT /note="C2HC MYST-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01063"
FT REGION 72..98
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 361..425
FT /note="Negatively regulates HAT activity"
FT /evidence="ECO:0000250"
FT REGION 426..716
FT /note="Catalytic"
FT /evidence="ECO:0000250"
FT REGION 460..716
FT /note="Interaction with BRPF1"
FT /evidence="ECO:0000250"
FT REGION 730..884
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 904..1163
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1195..1273
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1271..1784
FT /note="Interaction with RUNX1 and RUNX2"
FT /evidence="ECO:0000250"
FT REGION 1291..1330
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 736..756
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 775..819
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 838..853
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 857..871
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 911..930
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 939..954
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1023..1037
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1061..1089
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1090..1115
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1116..1147
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1148..1163
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1218..1244
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1247..1267
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 599
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q9H7Z6"
FT BINDING 564..568
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q92794"
FT BINDING 573..579
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q92794"
FT BINDING 603
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q92794"
FT MOD_RES 355
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WYB5"
FT MOD_RES 523
FT /note="N6-acetyllysine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:Q92794"
FT MOD_RES 746
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8WYB5"
FT MOD_RES 750
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8WYB5"
FT MOD_RES 752
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8WYB5"
FT MOD_RES 756
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WYB5"
FT CROSSLNK 381
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8WYB5"
SQ SEQUENCE 1784 AA; 200154 MW; F5A93EB283D3AE17 CRC64;
MVKLANPLYT EWILEAIQKI KKQKQRPSEE RICHAVSTSH GLDKKTVSEQ LELSVQDGSV
LKVTNKGLAS YKDPDNPGRF SSVKPGTFPK STKESRGSCN DLRNVDWNKL LRRAIEGLEE
PNGSSLKNIE KYLRSQSDLT STTNNPAFQQ RLRLGAKRAV NNGRLLKDGP QYRVNYGSLD
GKGAPQYPSA FPSSLPPVSL LPHEKDQPRA DPIPICSFCL GTKESNREKK PEELLSCADC
GSSGHPSCLK FCPELTTNVK ALRWQCIECK TCSACRVQGR NADNMLFCDS CDRGFHMECC
DPPLSRMPKG MWICQVCRPK KKGRKLLHEK AAQIKRRYAK PIGRPKNKLK QRLLSVTSDE
GSMNAFTGRG SPDTEIKINI KQESADVNVI GNKDVVTEED LDVFKQAQEL SWEKIECESG
VEDCGRYPSV IEFGKYEIQT WYSSPYPQEY ARLPKLYLCE FCLKYMKSKN ILLRHSKKCG
WFHPPANEIY RRKDLSVFEV DGNMSKIYCQ NLCLLAKLFL DHKTLYYDVE PFLFYVLTKN
DEKGCHLVGY FSKEKLCQQK YNVSCIMIMP QHQRQGFGRF LIDFSYLLSR REGQAGSPEK
PLSDLGRLSY LAYWKSVILE YLYHHHERHI SIKAISRATG MCPHDIATTL QHLHMIDKRD
GGFVIIRREK LILSHMEKLK TCSRANELDP DSLRWTPILI SNAAVSEEER EAEKEAERLM
EQASCWEKEE QEVLSTRANS RQSPAKVQSK NKYLHSPESR PVTGERGQLL ELSKESSEEE
EEEEEDEEEE DEEEEEEEEE DEEEEEEEEE EEEEEEEENI QSSPPRLTKP QSVAIKRKRP
FVLKKKRGRK RRRINSSVTT ETISETTEVL NEPFDNSDEE RPMPQLEPTC EIEVEEDGRK
PVLRKAFQHQ PGKKRQTEEE EGKDNHCFKN ADPCRNNMND DSRNLKEGSK DNPEPLKCKQ
AWPKGTKRGL SKWRQNKERK TGFKLNLYTP PETPLEPDEQ VTVEEQKETS EGKTSPTPIS
IEEEAKEAGE ALLPQEENRR QETCAPVSPN TSPGEKPEDD LIKPEEEEEE EEEEEEEEGE
EEEEEGGNVE KDPDGAKSQE KEEPEISPEK EDSARLDDHE EEEEEDEEPS HNEDHDADDE
DDSHMESAEV EKEELPRESF KEVLENEEAF LDLNVQPSHS NPEVLMDCGV DLTASCNSEP
KELAGDPEAV PESDEEPPPG EQAQKQDQKN SKEVDTEFKE GNPATMEIDS ETVQAVQSLT
QESSEQDDTF QDCAETQEAC RSLQNYTRAD QSPQIATTLD DCQQSDHSSP VSSVHSHPGQ
SVRSVNSPSV PALENSYAQI SPDQSAISVP SLQNMETSPM MDVPSVSDHS QQVVDSGFSD
LGSIESTTEN YENPSSYDST MGGSICGNGS SQNSCSYSNL TSSSLTQSSC AVTQQMSNIS
GSCSMLQQTS ISSPPTCSVK SPQGCVVERP PSSSQQLAQC SMAANFTPPM QLAEIPETGN
ANIGLYERMG QSDFGAGHYP QPSATFSLAK LQQLTNTLID HSLPYSHSAA VTSYANSASL
STPLSNTGLV QLSQSPHSVP GGPQAQATMT PPPNLTPPPM NLPPPLLQRN MAASNIGISH
SQRLQTQIAS KGHVSMRTKS ASLSPAAATH QSQIYGRSQT VAMQGPARTL TMQRGMNMSV
NLMPAPAYNV NSVNMNMNTL NAMNGYSMSQ PMMNSGYHSN HGYMNQTPQY PMQMQMGMMG
TQPYAQQPMQ TPPHGNMMYT APGHHGYMNT GMSKQSLNGS YMRR
