Q9LG11 (HAC4_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Histone acetyltransferase HAC4
EC=2.3.1.48

Gene names

Name:	HAC4
Synonyms:	PCAT3
Ordered Locus Names:	At1g55970
ORF Names:	F14J16.27, T6H22.22

Organism

Arabidopsis thaliana (Mouse-ear cress) [Reference proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Viridiplantae › Streptophyta › Streptophytina › Embryophyta › Tracheophyta › Euphyllophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length	1470 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	Acetyltransferase enzyme. Acetylates histones, giving a specific tag for transcriptional activation By similarity.
Catalytic activity	Acetyl-CoA + [histone] = CoA + acetyl-[histone].
Subcellular location	Nucleus Probable.
Tissue specificity	Rosette leaves, stems and flowers. Ref.5
Developmental stage	Expressed in young seedlings. Ref.5
Sequence similarities	Contains 1 PHD-type zinc finger. Contains 2 TAZ-type zinc fingers. Contains 2 ZZ-type zinc fingers.
Sequence caution	The sequence AAF02849.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence AAF79331.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence AAK73519.1 differs from that shown. Reason: Frameshift at position 988. The sequence AEE33326.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Nucleus
Domain	Repeat Zinc-finger
Ligand	Metal-binding Zinc
Molecular function	Activator Acyltransferase Chromatin regulator Transferase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	histone acetylation Inferred from electronic annotation. Source: GOC regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	histone acetyltransferase activity Inferred from electronic annotation. Source: EC transcription cofactor activity Inferred from electronic annotation. Source: InterPro zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1470	1470	Histone acetyltransferase HAC4		PRO_0000269742
Regions
	Zinc finger	416 – 495	80	TAZ-type 1
	Zinc finger	764 – 841	78	PHD-type
	Zinc finger	1174 – 1221	48	ZZ-type 1
	Zinc finger	1294 – 1341	48	ZZ-type 2
	Zinc finger	1358 – 1436	79	TAZ-type 2
	Compositional bias	54 – 87	34	Gln-rich
	Compositional bias	323 – 395	73	Gln-rich

Sequences

	Sequence		Length	Mass (Da)
	Q9LG11 [UniParc]. Last modified January 9, 2007. Version 2. Checksum: C1583E17D19C06CD	FASTA	1,470	166,802
	10 20 30 40 50 60 MNNNKEVPQN SVAVSSSSSA PITVISPQQD ANNFIKKRRT ALRNRIYAIV RHKQKQHQIF 70 80 90 100 110 120 LDKKNQQQQQ RVDDATQRAL LEKQDQQCIA ATRMIEEELL KSSRSFEEYF DLRTFDARVR 130 140 150 160 170 180 TILQQLGTML SQRRAAAAAM NNGEAQCITS TRAVHTSISV SNSFQCGRSL VPINCTTATA 190 200 210 220 230 240 GAFSIGPDMQ THHSTGANHQ MVEVNRPNMN QITCGISSPL ITGFNGNCVP VSANIPMTSQ 250 260 270 280 290 300 DLFNATHFST LPQPFLQPPP DQSHMHRYSM SNVASFGQSN PYPCGVVMSS GSMAVAQNSI 310 320 330 340 350 360 PWNNPNPMQG LDPTVTSYHS NLQPMQQTPL PKRQLHHPLW NTNFQSAPNN RDNLPQVSQQ 370 380 390 400 410 420 LSNHGSRQHR GQHSQNLYPG QLQNQDRLLP NLTQQAMALA APVMHVPSKQ VNEDCGQTSS 430 440 450 460 470 480 NTVLRWIPFM FHARHCKAKK DKCASKFCFQ ARKIVKHIDC CKVPNCKYRY CLGTRMWLDH 490 500 510 520 530 540 FKQCKSISCR TCVAVREYME KNKYTIVPLR RAKCSSASSK CQPKKSSKSR QAYKKGGAEA 550 560 570 580 590 600 PSVDADLQRS IKRPKLHRPS QNITPETKSI SVTGCGVVCK PHSLMNMQEK DGLQSLKVEA 610 620 630 640 650 660 MPMDIDVPGA SEIPVTRELV KHVAEDTPKG NNCGGFAMVE KTSCLLAQGK SKCMNEMSAP 670 680 690 700 710 720 KEENVKQSVE VVDASKMEIS SLVELFTPEQ VKEHIRSLRQ WVGQSKTKAE KNKAMGCSMS 730 740 750 760 770 780 VNSCQLCAVE WLVFEPVPIY CSPCGIRIKK NALHYSIAVG ESRHYVCAPC YNEAREKLVF 790 800 810 820 830 840 LDGTSIPKTR LQKKKNDEQV PEGWVQCDKC EAWQHIICAL FNSRRNHGES TKYTCPSCYI 850 860 870 880 890 900 QEVEQRERRP LPLSAVPGAT SLPVTSLSKH LEERLFKKLK EERQERARLQ GKTYEEVPGA 910 920 930 940 950 960 ESLTVRVVAS VDKVLEVKER FLELFREENY PSEFPYKSKA IFLFQKIENV EVCLFGMFVQ 970 980 990 1000 1010 1020 EFGTDSGPPN ERRVYLSYLD SVKYFRPTFR TVSGEALRTF VYHEILIGYL DYCKKRGFTS 1030 1040 1050 1060 1070 1080 CYIWACPPLK GDDYILYCHP EIQKTPKTDK LREWYLAMLR KASKEDVVVE CTNLYNHFFV 1090 1100 1110 1120 1130 1140 QSGECRANVT AARLPYFDGD YWPSAAEDLL RQMNQEDDGE TKLHRKGLTK KVISKRALKA 1150 1160 1170 1180 1190 1200 VGQLDLSLNA SKDRLMMQKL GETICPMKED FIMVHLQHCC KHCTTLMVSG NRWVCNHCKN 1210 1220 1230 1240 1250 1260 FQICDKCYEV EQNRINIERH PINQKEKHAL FPVAIKDVPT KIEDKDNNLE SEFFHNRQAF 1270 1280 1290 1300 1310 1320 LNLCQGNNYQ YETLRRAKHS SMMILYHLHN PTAPAFATVC TICQQEVENS QGWHCEVCPG 1330 1340 1350 1360 1370 1380 YDVCSACYSK DSINHSHKLT SRSSSTDSTV VQQNGQASQS YQVKLEKLKK LLVHAATCRS 1390 1400 1410 1420 1430 1440 TQCQYQGCRK SKMLFRHCID CTTGDCPICK GLWSLLKLHA RNCRDSKCTV PKCSGLRAIS 1450 1460 1470 RRKQQQADKR RRAAVMEMMR ERAAEATRTG

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana." Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K. , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W. Nature 408:816-820(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[2]	The Arabidopsis Information Resource (TAIR) Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: cv. Columbia.
[3]	"Analysis of histone acetyltransferase and histone deacetylase families of Arabidopsis thaliana suggests functional diversification of chromatin modification among multicellular eukaryotes." Pandey R., Mueller A., Napoli C.A., Selinger D.A., Pikaard C.S., Richards E.J., Bender J., Mount D.W., Jorgensen R.A. Nucleic Acids Res. 30:5036-5055(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 10-760 AND 1086-1470, NOMENCLATURE.
[4]	Richards E.J. Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 772-1470.
[5]	"Plant orthologs of p300/CBP: conservation of a core domain in metazoan p300/CBP acetyltransferase-related proteins." Bordoli L., Netsch M., Luethi U., Lutz W., Eckner R. Nucleic Acids Res. 29:589-597(2001) [PubMed] [Europe PMC] [Abstract] Cited for: DEVELOPMENTAL STAGE, TISSUE SPECIFICITY.
+	Additional computationally mapped references.

Web resources

PlantsUBQ

A functional genomics database for the ubiquitin/26S proteasome proteolytic pathway in plants

Cross-references

Sequence databases
EMBL GenBank DDBJ	AC002304 Genomic DNA. Translation: AAF79331.1. Sequence problems. AC009894 Genomic DNA. Translation: AAF02849.1. Sequence problems. CP002684 Genomic DNA. Translation: AEE33326.1. Sequence problems. AF512559 mRNA. Translation: AAM34789.1. AF512560 mRNA. Translation: AAM34790.1. AF389513 mRNA. Translation: AAK73519.1. Frameshift.
IPI	IPI00516515. IPI01019494.
RefSeq	NP_564706.1. NM_104475.2.
UniGene	At.26162.
3D structure databases
HSSP	HSSP built from PDB template 1TOT based on UniProtKB P45481.
ProteinModelPortal	Q9LG11.
SMR	Q9LG11. Positions 859-1112, 1360-1433.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	842048.
KEGG	ath:AT1G55970.
Organism-specific databases
TAIR	At1g55970.
Phylogenomic databases
eggNOG	NOG257281.
InParanoid	Q9LG11.
KO	K04498.
PhylomeDB	Q9LG11.
Gene expression databases
Genevestigator	Q9LG11.
Family and domain databases
Gene3D	1.20.1020.10. 2 hits. 3.30.40.10. 1 hit.
InterPro	IPR013178. Histone_H3-K56_AcTrfase_RTT109. IPR019786. Zinc_finger_PHD-type_CS. IPR011011. Znf_FYVE_PHD. IPR001965. Znf_PHD. IPR019787. Znf_PHD-finger. IPR013083. Znf_RING/FYVE/PHD. IPR000197. Znf_TAZ. IPR000433. Znf_ZZ. [Graphical view]
Pfam	PF08214. KAT11. 1 hit. PF00628. PHD. 1 hit. PF02135. zf-TAZ. 2 hits. PF00569. ZZ. 1 hit. [Graphical view]
SMART	SM00249. PHD. 1 hit. SM00551. ZnF_TAZ. 2 hits. SM00291. ZnF_ZZ. 2 hits. [Graphical view]
SUPFAM	SSF57903. FYVE_PHD_ZnF. 1 hit. SSF57933. TAZ_finger. 2 hits.
PROSITE	PS01359. ZF_PHD_1. 1 hit. PS50016. ZF_PHD_2. False negative. PS50134. ZF_TAZ. 2 hits. PS01357. ZF_ZZ_1. 2 hits. PS50135. ZF_ZZ_2. 2 hits. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

HAC4_ARATH

Accession

Primary (citable) accession number: Q9LG11
Secondary accession number(s): F4I3I0 , Q8LRK3, Q8LRK4, Q94EW2, Q9SGS6

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 9, 2007
Last sequence update:	January 9, 2007
Last modified:	May 1, 2013
This is version 77 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program