[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], INTERACTION WITH P45, DEVELOPMENTAL STAGE, AND SUBCELLULAR LOCATION. STRAIN=cv. Cuzco 251; DOI=10.1093/nar/27.22.4427; PubMed=10536152 [NCBI, ExPASy, EBI, Israel, Japan] Lusser A., Eberharter A., Loidl A., Goralik-Schramel M., Horngacher M., Hass H., Loidl P.; "Analysis of the histone acetyltransferase B complex of maize embryos."; Nucleic Acids Res. 27:4427-4435(1999).
[2]	NUCLEOTIDE SEQUENCE [MRNA]. STRAIN=cv. B73; Chandler V.L., Kaeppler S.M., Kaeppler H.F., Cone K.C.; "Sequences from the plant chromatin consortium."; Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases.
[3]	CHARACTERIZATION, AND BIOPHYSICOCHEMICAL PROPERTIES. DOI=10.1016/0014-5793(96)00401-2; PubMed=8635608 [NCBI, ExPASy, EBI, Israel, Japan] Eberharter A., Lechner T., Goralik-Schramel M., Loidl P.; "Purification and characterization of the cytoplasmic histone acetyltransferase B of maize embryos."; FEBS Lett. 386:75-81(1996).
[4]	SUBSTRATE SPECIFICITY. DOI=10.1016/S0014-5793(97)01544-5; PubMed=9468289 [NCBI, ExPASy, EBI, Israel, Japan] Koelle D., Sarg B., Lindner H., Loidl P.; "Substrate and sequential site specificity of cytoplasmic histone acetyltransferases of maize and rat liver."; FEBS Lett. 421:109-114(1998).

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 + acetylhistone.
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.
BIOPHYSICOCHEMICAL PROPERTIES:

Kinetic parameters:   K_M=25 µM for core histones;
K_M=9 µM for acetyl-CoA;
pH dependence:   Optimum pH is 8.2-8.5;
Temperature dependence:   Optimum temperature is 37 degrees Celsius;
SUBUNIT: Heteromer of HAT1/p50 and p45 subunits.
SUBCELLULAR LOCATION: Nucleus. Cytoplasm.
DEVELOPMENTAL STAGE: Found in the dry embryo (at protein level). Maximum level of expression 22 hours after start of seed imbibition.
SIMILARITY: Belongs to the HAT1 family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

U90274; AAC03423.2; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF171927; AAF06742.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AY093417; AAM28228.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

T02064; T02064.

NP_001105187.1; -.

3D structure databases

HSSP

Q12341; 1BOB. [HSSP ENTRY / PDB]

ModBase

Q8LPU4.

Organism-specific databases

Gramene

Q8LPU4; -.

MaizeGDB

273678; -.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from electronic annotation from UniProtKB-KW).
GO:0005634;	Cellular component: nucleus (inferred from electronic annotation from UniProtKB-KW).
GO:0004402;	Molecular function: histone acetyltransferase activity (inferred from electronic annotation from EC).
QuickGo view.

Family and domain databases

InterPro

IPR016181; Acyl_CoA_acyltransferase.
IPR017380; Hist_AcTrfase_B-typ_cat_su.
Graphical view of domain structure.

Gene3D

G3DSA:3.40.630.30; Acyl_CoA_acyltransferase; 1.

PIRSF

PIRSF038084; HAT-B_cat; 1.

ProtoNet

Q8LPU4.

Genome annotation databases

GeneID

542083; -.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Acyltransferase; Cytoplasm; Nucleus; Transferase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 468`	`468`	`Histone acetyltransferase type B catalytic subunit.`	`PRO_0000232126`
`CONFLICT`	`354 354`		`V -> I (in Ref. 2; AAM28228).`

Sequence information

Length: 468 AA [This is the length of the unprocessed precursor]

Molecular weight: 52721 Da [This is the MW of the unprocessed precursor]

CRC64: 049F68157ED8443C [This is a checksum on the sequence]

        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

Q8LPU4 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools