HAC12_ARATH
ID HAC12_ARATH Reviewed; 1706 AA.
AC Q9FWQ5;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Histone acetyltransferase HAC12;
DE EC=2.3.1.48 {ECO:0000250|UniProtKB:Q9C5X9};
GN Name=HAC12; OrderedLocusNames=At1g16710; ORFNames=F17F16.8, F17F16_21;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP IDENTIFICATION, AND NOMENCLATURE.
RX PubMed=12466527; DOI=10.1093/nar/gkf660;
RA Pandey R., Mueller A., Napoli C.A., Selinger D.A., Pikaard C.S.,
RA Richards E.J., Bender J., Mount D.W., Jorgensen R.A.;
RT "Analysis of histone acetyltransferase and histone deacetylase families of
RT Arabidopsis thaliana suggests functional diversification of chromatin
RT modification among multicellular eukaryotes.";
RL Nucleic Acids Res. 30:5036-5055(2002).
CC -!- FUNCTION: Acetyltransferase enzyme. Acetylates histones, giving a
CC specific tag for transcriptional activation.
CC {ECO:0000250|UniProtKB:Q9C5X9}.
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:Q9C5X9};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q9FWQ5-1; Sequence=Displayed;
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG09087.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC026237; AAG09087.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE29487.1; -; Genomic_DNA.
DR PIR; E86302; E86302.
DR RefSeq; NP_173115.1; NM_101532.3. [Q9FWQ5-1]
DR AlphaFoldDB; Q9FWQ5; -.
DR SMR; Q9FWQ5; -.
DR STRING; 3702.AT1G16710.1; -.
DR iPTMnet; Q9FWQ5; -.
DR PaxDb; Q9FWQ5; -.
DR PRIDE; Q9FWQ5; -.
DR ProteomicsDB; 247213; -. [Q9FWQ5-1]
DR EnsemblPlants; AT1G16710.1; AT1G16710.1; AT1G16710. [Q9FWQ5-1]
DR GeneID; 838242; -.
DR Gramene; AT1G16710.1; AT1G16710.1; AT1G16710. [Q9FWQ5-1]
DR KEGG; ath:AT1G16710; -.
DR Araport; AT1G16710; -.
DR TAIR; locus:2015676; AT1G16710.
DR eggNOG; KOG1778; Eukaryota.
DR InParanoid; Q9FWQ5; -.
DR OrthoDB; 27931at2759; -.
DR PhylomeDB; Q9FWQ5; -.
DR PRO; PR:Q9FWQ5; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9FWQ5; baseline and differential.
DR Genevisible; Q9FWQ5; AT.
DR GO; GO:0000123; C:histone acetyltransferase complex; IBA:GO_Central.
DR GO; GO:0005667; C:transcription regulator complex; IBA:GO_Central.
DR GO; GO:0031490; F:chromatin DNA binding; IBA:GO_Central.
DR GO; GO:0004402; F:histone acetyltransferase activity; IDA:TAIR.
DR GO; GO:0003713; F:transcription coactivator activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0016573; P:histone acetylation; IBA:GO_Central.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006473; P:protein acetylation; IMP:TAIR.
DR Gene3D; 1.20.1020.10; -; 2.
DR Gene3D; 3.30.40.10; -; 1.
DR Gene3D; 3.30.60.90; -; 2.
DR InterPro; IPR031162; CBP_P300_HAT.
DR InterPro; IPR013178; Histone_AcTrfase_Rtt109/CBP.
DR InterPro; IPR035898; TAZ_dom_sf.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR000197; Znf_TAZ.
DR InterPro; IPR000433; Znf_ZZ.
DR InterPro; IPR043145; Znf_ZZ_sf.
DR PANTHER; PTHR13808; PTHR13808; 1.
DR Pfam; PF08214; HAT_KAT11; 1.
DR Pfam; PF02135; zf-TAZ; 2.
DR Pfam; PF00569; ZZ; 1.
DR SMART; SM01250; KAT11; 1.
DR SMART; SM00551; ZnF_TAZ; 2.
DR SMART; SM00291; ZnF_ZZ; 2.
DR SUPFAM; SSF57903; SSF57903; 1.
DR SUPFAM; SSF57933; SSF57933; 2.
DR PROSITE; PS51727; CBP_P300_HAT; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50134; ZF_TAZ; 2.
DR PROSITE; PS01357; ZF_ZZ_1; 2.
DR PROSITE; PS50135; ZF_ZZ_2; 2.
PE 3: Inferred from homology;
KW Activator; Acyltransferase; Alternative splicing; Chromatin regulator;
KW Metal-binding; Nucleus; Reference proteome; Repeat; Transcription;
KW Transcription regulation; Transferase; Zinc; Zinc-finger.
FT CHAIN 1..1706
FT /note="Histone acetyltransferase HAC12"
FT /id="PRO_0000269744"
FT DOMAIN 1090..1526
FT /note="CBP/p300-type HAT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01065"
FT ZN_FING 637..716
FT /note="TAZ-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00203"
FT ZN_FING 998..1075
FT /note="PHD-type"
FT ZN_FING 1408..1471
FT /note="ZZ-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT ZN_FING 1528..1581
FT /note="ZZ-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT ZN_FING 1588..1671
FT /note="TAZ-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00203"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 251..284
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 397..456
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 524..543
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 791..909
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 791..805
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 806..826
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 872..909
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1213..1215
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q09472"
FT BINDING 1232..1233
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q09472"
FT BINDING 1288
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q09472"
FT BINDING 1413
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 1416
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 1428
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 1431
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 1437
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 1440
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 1453
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 1461
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 1533
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 1536
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 1548
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 1551
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 1557
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 1560
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 1569
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 1571
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
SQ SEQUENCE 1706 AA; 190272 MW; 71CDA5B8B6184518 CRC64;
MNVQAHMSGQ RSGQVPNQGT VPQNNGNSQM QNLVGSNGAA TAVTGAGAAT GSGTGVRPSR
NIVGAMDHDI MKLRQYMQTL VFNMLQQRQP SPADAASKAK YMDVARRLEE GLFKMAVTKE
DYMNRSTLES RITSLIKGRQ INNYNQRHAN SSSVGTMIPT PGLSQTAGNP NLMVTSSVDA
TIVGNTNITS TALNTGNPLI AGGMHGGNMS NGYQHSSRNF SLGSGGSMTS MGAQRSTAQM
IPTPGFVNSV TNNNSGGFSA EPTIVPQSQQ QQQRQHTGGQ NSHMLSNHMA AGVRPDMQSK
PSGAANSSVN GDVGANEKIV DSGSSYTNAS KKLQQGNFSL LSFCPDDLIS GQHIESTFHI
SGEGYSTTNP DPFDGAITSA GTGTKAHNIN TASFQPVSRV NSSLSHQQQF QQPPNRFQQQ
PNQIQQQQQQ FLNQRKLKQQ TPQQHRLISN DGLGKTQVDS DMVTKVKCEP GMENKSQAPQ
SQASERFQLS QLQNQYQNSG EDCQADAQLL PVESQSDICT SLPQNSQQIQ QMMHPQNIGS
DSSNSFSNLA VGVKSESSPQ GQWPSKSQEN TLMSNAISSG KHIQEDFRQR ITGMDEAQPN
NLTEGSVIGQ NHTSTISESH NLQNSIGTTC RYGNVSHDPK FKNQQRWLLF LRHARSCKPP
GGRCQDQNCV TVQKLWSHMD NCADPQCLYP RCRHTKALIG HYKNCKDPRC PVCVPVKTYQ
QQANVRALAR LKNESSAVGS VNRSVVSNDS LSANAGAVSG TPRCADTLDN LQPSLKRLKV
EQSFQPVVPK TESCKSSIVS TTEADLSQDA ERKDHRPLKS ETMEVKVEIP DNSVQAGFGI
KETKSEPFEN VPKPKPVSEP GKHGLSGDSP KQENIKMKKE PGWPKKEPGC PKKEELVESP
ELTSKSRKPK IKGVSLTELF TPEQVREHIR GLRQWVGQSK AKAEKNQAME NSMSENSCQL
CAVEKLTFEP PPIYCTPCGA RIKRNAMYYT VGGGETRHYF CIPCYNESRG DTILAEGTSM
PKAKLEKKKN DEEIEESWVQ CDKCQAWQHQ ICALFNGRRN DGGQAEYTCP YCYVIDVEQN
ERKPLLQSAV LGAKDLPRTI LSDHIEQRLF KRLKQERTER ARVQGTSYDE IPTVESLVVR
VVSSVDKKLE VKSRFLEIFR EDNFPTEFPY KSKVVLLFQK IEGVEVCLFG MYVQEFGSEC
SNPNQRRVYL SYLDSVKYFR PDIKSANGEA LRTFVYHEIL IGYLEYCKLR GFTSCYIWAC
PPLKGEDYIL YCHPEIQKTP KSDKLREWYL AMLRKAAKEG IVAETTNLYD HFFLQTGECR
AKVTAARLPY FDGDYWPGAA EDIISQMSQE DDGRKGNKKG ILKKPITKRA LKASGQSDFS
GNASKDLLLM HKLGETIHPM KEDFIMVHLQ HSCTHCCTLM VTGNRWVCSQ CKDFQLCDGC
YEAEQKREDR ERHPVNQKDK HNIFPVEIAD IPTDTKDRDE ILESEFFDTR QAFLSLCQGN
HYQYDTLRRA KHSSMMVLYH LHNPTAPAFV TTCNVCHLDI ESGLGWRCEV CPDYDVCNAC
YKKEGCINHP HKLTTHPSLA DQNAQNKEAR QLRVLQLRKM LDLLVHASQC RSPVCLYPNC
RKVKGLFRHG LRCKVRASGG CVLCKKMWYL LQLHARACKE SECDVPRCGD LKEHLRRLQQ
QSDSRRRAAV MEMMRQRAAE VAGTSG
