Q8LPU4 (HAT1_MAIZE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Histone acetyltransferase type B catalytic subunit
EC=2.3.1.48

Alternative name(s):
Histone acetyltransferase HAT B
Histone acetyltransferase HAT-B-p50

Gene names

Name:	HAT1
Synonyms:	HAC106, HATB1

Organism

Zea mays (Maize)

Taxonomic identifier

4577 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Viridiplantae › Streptophyta › Streptophytina › Embryophyta › Tracheophyta › Euphyllophyta › Spermatophyta › Magnoliophyta › Liliopsida › commelinids › Poales › Poaceae › PACMAD clade › Panicoideae › Andropogoneae › Zea

Protein attributes

Sequence length	468 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Acetylates newly synthesized histones during DNA replication. Highly specific in vitro for the non-acetylated H4 which is acetylated sequentially at 'Lys-12' and 'Lys-5' into a di-acetylated form.
Catalytic activity	Acetyl-CoA + [histone] = CoA + acetyl-[histone].
Enzyme regulation	Inhibited by 5 mM of zinc, copper and iron. Unaffected by low concentrations of detergents and irreversibly inactivated by 2% ethanol, isopropanol or dimethyl sulfoxide.
Subunit structure	Heteromer of HAT1/p50 and p45 subunits.
Subcellular location	Nucleus. Cytoplasm Ref.1.
Developmental stage	Found in the dry embryo (at protein level). Maximum level of expression 22 hours after start of seed imbibition. Ref.1
Sequence similarities	Belongs to the HAT1 family.
Biophysicochemical properties	Kinetic parameters: KM=25 µM for core histones Ref.3 KM=9 µM for acetyl-CoA pH dependence: Optimum pH is 8.2-8.5. Temperature dependence: Optimum temperature is 37 degrees Celsius.

Ontologies

Keywords
Cellular component	Cytoplasm Nucleus
Molecular function	Acyltransferase Transferase
Gene Ontology (GO)
Biological_process	chromatin silencing at telomere Inferred from electronic annotation. Source: InterPro histone H4 acetylation Inferred from electronic annotation. Source: GOC
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	H4 histone acetyltransferase activity Inferred from electronic annotation. Source: EnsemblPlants/Gramene
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 468	468	Histone acetyltransferase type B catalytic subunit		PRO_0000232126
Experimental info
	Sequence conflict	354	1	V → I in AAM28228. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q8LPU4 [UniParc]. Last modified April 4, 2006. Version 2. Checksum: 049F68157ED8443C	FASTA	468	52,721
	10 20 30 40 50 60 MALKQKDTDA AATATGTKKR RRVFFSDTDA GVEANECMKV FLVWNPGEVS SVDCTAIQPF 70 80 90 100 110 120 DLNHFFGEDG KIYGYKNLKI NVWISAKSFH GYADVSFDET SDGGKGITDL KPVLQNIFGE 130 140 150 160 170 180 NLVEKEEFLH TFSKECEYIR TAVTNGSAIK HDGSYESDPA VEIVRVELQG AAAFLYSRLV 190 200 210 220 230 240 PLVLLLVEGS TPIDIGEHGW EMLLVVKKAT QEAGSKFELL GFAAVHNFYH YPESIRLRIS 250 260 270 280 290 300 QILVLPPYQG EGHGLGLLEA INYIAQSENI YDVTIESPSD YLQYVRSSID CLRLLMFDPI 310 320 330 340 350 360 KPALGAIVLS LKETNLSKRA QSLRMVPPAD LMETVRQKLK INKKQFLRCW EILVFLSLDS 370 380 390 400 410 420 QDHKSMDNFR ACIYDRMKGE ILGSASGTNR KRLLQMPTSF NKEASFAVYW TQEIEDEDEQ 430 440 450 460 TVEQQPEDLK TQEQQLNELV DIQIEEIAGV AKNVTSRCKD KMTELVVQ

References

[1]	"Analysis of the histone acetyltransferase B complex of maize embryos." Lusser A., Eberharter A., Loidl A., Goralik-Schramel M., Horngacher M., Hass H., Loidl P. Nucleic Acids Res. 27:4427-4435(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], INTERACTION WITH P45, DEVELOPMENTAL STAGE, SUBCELLULAR LOCATION. Strain: cv. Cuzco 251.
[2]	"Sequences from the plant chromatin consortium." Chandler V.L., Kaeppler S.M., Kaeppler H.F., Cone K.C. Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: cv. B73.
[3]	"Purification and characterization of the cytoplasmic histone acetyltransferase B of maize embryos." Eberharter A., Lechner T., Goralik-Schramel M., Loidl P. FEBS Lett. 386:75-81(1996) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION, BIOPHYSICOCHEMICAL PROPERTIES.
[4]	"Substrate and sequential site specificity of cytoplasmic histone acetyltransferases of maize and rat liver." Koelle D., Sarg B., Lindner H., Loidl P. FEBS Lett. 421:109-114(1998) [PubMed] [Europe PMC] [Abstract] Cited for: SUBSTRATE SPECIFICITY.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U90274 mRNA. Translation: AAC03423.2. AF171927 Genomic DNA. Translation: AAF06742.1. AY093417 mRNA. Translation: AAM28228.1.
PIR	T02064.
RefSeq	NP_001105187.1. NM_001111717.1.
UniGene	Zm.94647.
3D structure databases
ProteinModelPortal	Q8LPU4.
ModBase	Search...
Proteomic databases
PRIDE	Q8LPU4.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	542083.
KEGG	zma:542083.
Organism-specific databases
Gramene	Q8LPU4.
MaizeGDB	273678.
Phylogenomic databases
HOGENOM	HOG000084749.
KO	K11303.
Family and domain databases
Gene3D	3.40.630.30. 1 hit. 3.90.360.10. 1 hit.
InterPro	IPR016181. Acyl_CoA_acyltransferase. IPR019467. Hat1_N. IPR017380. Hist_AcTrfase_B-typ_cat-su. [Graphical view]
PANTHER	PTHR12046. PTHR12046. 1 hit.
Pfam	PF10394. Hat1_N. 1 hit. [Graphical view]
PIRSF	PIRSF038084. HAT-B_cat. 1 hit.
SUPFAM	SSF55729. Acyl_CoA_acyltransferase. 1 hit.
ProtoNet	Search...

Entry information

Entry name

HAT1_MAIZE

Accession

Primary (citable) accession number: Q8LPU4
Secondary accession number(s): O49994

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 4, 2006
Last sequence update:	April 4, 2006
Last modified:	April 3, 2013
This is version 53 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program