KAT8_RAT
ID KAT8_RAT Reviewed; 458 AA.
AC Q5XI06;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Histone acetyltransferase KAT8;
DE EC=2.3.1.48 {ECO:0000250|UniProtKB:Q9H7Z6};
DE AltName: Full=Lysine acetyltransferase 8;
DE AltName: Full=MOZ, YBF2/SAS3, SAS2 and TIP60 protein 1;
DE Short=MYST-1;
GN Name=Kat8; Synonyms=Myst1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-37 AND SER-42, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Histone acetyltransferase which may be involved in
CC transcriptional activation. May influence the function of ATM. As part
CC of the MSL complex it is involved in acetylation of nucleosomal histone
CC H4 producing specifically H4K16ac. As part of the NSL complex it may be
CC involved in acetylation of nucleosomal histone H4 on several lysine
CC residues. That activity is less specific than the one of the MSL
CC complex. Can also acetylate TP53/p53 at 'Lys-120'.
CC {ECO:0000250|UniProtKB:Q9H7Z6}.
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:Q9H7Z6};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45949;
CC Evidence={ECO:0000250|UniProtKB:Q9H7Z6};
CC -!- SUBUNIT: Component of a multisubunit histone acetyltransferase complex
CC (MSL) at least composed of the MOF/KAT8, MSL1/hampin, MSL2L1 and MSL3L1
CC (By similarity). Component of the NSL complex at least composed of
CC MOF/KAT8, KANSL1, KANSL2, KANSL3, MCRS1, PHF20, OGT1/OGT, WDR5 and
CC HCFC1 (By similarity). Interacts with KANSL1; the interaction is direct
CC (By similarity). Component of some MLL1/MLL complex, at least composed
CC of the core components KMT2A/MLL1, ASH2L, HCFC1, WDR5 and RBBP5, as
CC well as the facultative components BAP18, CHD8, E2F6, HSP70, INO80C,
CC KANSL1, LAS1L, MAX, MCRS1, MGA, MOF/KAT8, PELP1, PHF20, PRP31, RING2,
CC RUVB1/TIP49A, RUVB2/TIP49B, SENP3, TAF1, TAF4, TAF6, TAF7, TAF9 and
CC TEX10 (By similarity). Interacts with the chromodomain of MORF4L1/MRG15
CC (By similarity). Interacts with ATM (via its Tudor-knot domain) (By
CC similarity). Interacts with MSL1; the interaction is direct (By
CC similarity). Interacts with MSL3 (By similarity). Interacts with NELFD
CC (By similarity). {ECO:0000250|UniProtKB:Q9D1P2,
CC ECO:0000250|UniProtKB:Q9H7Z6}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9H7Z6}.
CC Chromosome {ECO:0000250|UniProtKB:Q9H7Z6}.
CC -!- PTM: Autoacetylation at Lys-274 is required for binding histone H4 with
CC high affinity and for proper function. {ECO:0000250|UniProtKB:Q9H7Z6}.
CC -!- SIMILARITY: Belongs to the MYST (SAS/MOZ) family. {ECO:0000305}.
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DR EMBL; BC083891; AAH83891.1; -; mRNA.
DR RefSeq; NP_001017378.1; NM_001017378.1.
DR AlphaFoldDB; Q5XI06; -.
DR BMRB; Q5XI06; -.
DR SMR; Q5XI06; -.
DR STRING; 10116.ENSRNOP00000026527; -.
DR iPTMnet; Q5XI06; -.
DR PhosphoSitePlus; Q5XI06; -.
DR PaxDb; Q5XI06; -.
DR GeneID; 310194; -.
DR KEGG; rno:310194; -.
DR UCSC; RGD:1311512; rat.
DR CTD; 84148; -.
DR RGD; 1311512; Kat8.
DR VEuPathDB; HostDB:ENSRNOG00000019485; -.
DR eggNOG; KOG2747; Eukaryota.
DR HOGENOM; CLU_011815_2_1_1; -.
DR InParanoid; Q5XI06; -.
DR OMA; MNMVKYW; -.
DR OrthoDB; 629545at2759; -.
DR PhylomeDB; Q5XI06; -.
DR TreeFam; TF317619; -.
DR Reactome; R-RNO-3214847; HATs acetylate histones.
DR PRO; PR:Q5XI06; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000019585; Expressed in testis and 19 other tissues.
DR GO; GO:0000123; C:histone acetyltransferase complex; ISS:UniProtKB.
DR GO; GO:0000776; C:kinetochore; ISO:RGD.
DR GO; GO:0071339; C:MLL1 complex; ISS:UniProtKB.
DR GO; GO:0072487; C:MSL complex; ISS:UniProtKB.
DR GO; GO:0044545; C:NSL complex; ISO:RGD.
DR GO; GO:0016363; C:nuclear matrix; ISO:RGD.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0016407; F:acetyltransferase activity; ISO:RGD.
DR GO; GO:0019899; F:enzyme binding; ISO:RGD.
DR GO; GO:0010484; F:H3 histone acetyltransferase activity; ISO:RGD.
DR GO; GO:0010485; F:H4 histone acetyltransferase activity; ISO:RGD.
DR GO; GO:0046972; F:histone acetyltransferase activity (H4-K16 specific); ISS:UniProtKB.
DR GO; GO:0043995; F:histone acetyltransferase activity (H4-K5 specific); ISS:UniProtKB.
DR GO; GO:0043996; F:histone acetyltransferase activity (H4-K8 specific); ISS:UniProtKB.
DR GO; GO:0042393; F:histone binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0035064; F:methylated histone binding; ISO:RGD.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; ISO:RGD.
DR GO; GO:0003713; F:transcription coactivator activity; ISO:RGD.
DR GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0016573; P:histone acetylation; ISO:RGD.
DR GO; GO:0043984; P:histone H4-K16 acetylation; ISS:UniProtKB.
DR GO; GO:0043981; P:histone H4-K5 acetylation; ISS:UniProtKB.
DR GO; GO:0043982; P:histone H4-K8 acetylation; ISS:UniProtKB.
DR GO; GO:0030099; P:myeloid cell differentiation; ISO:RGD.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISO:RGD.
DR GO; GO:0051571; P:positive regulation of histone H3-K4 methylation; ISO:RGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0010506; P:regulation of autophagy; ISO:RGD.
DR GO; GO:1900095; P:regulation of dosage compensation by inactivation of X chromosome; ISO:RGD.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR016197; Chromo-like_dom_sf.
DR InterPro; IPR000953; Chromo/chromo_shadow_dom.
DR InterPro; IPR002717; HAT_MYST-type.
DR InterPro; IPR037906; KAT8.
DR InterPro; IPR025995; Tudor-knot.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR040706; Zf-MYST.
DR PANTHER; PTHR10615:SF82; PTHR10615:SF82; 1.
DR Pfam; PF01853; MOZ_SAS; 1.
DR Pfam; PF11717; Tudor-knot; 1.
DR Pfam; PF17772; zf-MYST; 1.
DR SMART; SM00298; CHROMO; 1.
DR SUPFAM; SSF54160; SSF54160; 1.
DR SUPFAM; SSF55729; SSF55729; 1.
DR PROSITE; PS51726; MYST_HAT; 1.
PE 1: Evidence at protein level;
KW Acetylation; Activator; Acyltransferase; Chromatin regulator; Chromosome;
KW Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation; Transferase; Zinc; Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9H7Z6"
FT CHAIN 2..458
FT /note="Histone acetyltransferase KAT8"
FT /id="PRO_0000051568"
FT DOMAIN 55..110
FT /note="Tudor-knot"
FT /evidence="ECO:0000255"
FT DOMAIN 174..447
FT /note="MYST-type HAT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01063"
FT ZN_FING 207..232
FT /note="C2HC MYST-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01063"
FT REGION 1..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 174..458
FT /note="Sufficient for interaction with KANSL1"
FT /evidence="ECO:0000250|UniProtKB:Q9H7Z6"
FT ACT_SITE 350
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q9H7Z6"
FT BINDING 317..319
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q9H7Z6"
FT BINDING 324..330
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q9H7Z6"
FT BINDING 354
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q9H7Z6"
FT BINDING 363
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q9H7Z6"
FT BINDING 432
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q9H7Z6"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q9H7Z6"
FT MOD_RES 37
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 42
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 113
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9H7Z6"
FT MOD_RES 274
FT /note="N6-acetyllysine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:Q9H7Z6"
FT MOD_RES 348
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H7Z6"
SQ SEQUENCE 458 AA; 52632 MW; 0D3AFF8A5EDB1459 CRC64;
MAAQGATAAV AATTSGIVGE GEPGPGENTS VEGPARSPGR VSPPTPARGE PEVTVEIGET
YLCRRPDSTW HSAEVIQSRV NDQEGREEFY VHYVGFNRRL DEWVDKNRLA LTKTVKDAVQ
KNSEKYLSEL AEQPERKITR NQKRKHDEIN HVQKTYAEMD PTTAALEKEH EAITKVKYVD
KIHIGNYEID AWYFSPFPED YGKQPKLWLC EYCLKYMKFE KSYRFHLGQC QWRQPPGKEI
YRKSNISVYE VDGKDHKIYC QNLCLLAKLF LDHKTLYFDV EPFVFYILTE VDRQGAHIVG
YFSKEKESPD GNNVACILTL PPYQRRGYGK FLIAFSYELS KLESTVGSPE KPLSDLGKLS
YRSYWSWVLL EILRDFRGTL SIKDLSQMTS ITQNDIISTL QSLNMVKYWK GQHVICVTPK
LVEEHLKSAQ YKKPPITVDS VCLKWAPPKH KQVKLSKK
