Reviewed, UniProtKB/Swiss-Prot Q8BY71 (HAT1_MOUSE)

Names and origin

Protein names

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

Gene names

Name:

Hat1

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

Sequence length	416 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Function	May play a role in telomeric silencing. Acetylates soluble but not nucleosomal H4 at 'Lys-5' and 'Lys-12' and acetylates histone H2A at 'Lys-5'. HAT1 has intrinsic substrate specificity that modifies lysine in recognition sequence GXGKXG By similarity.
Catalytic activity	Acetyl-CoA + histone = CoA + acetylhistone.
Subunit structure	Heteromer of HAT1 and p46/HAT2 subunits By similarity.
Subcellular location	Nucleus By similarity. Cytoplasm By similarity. Note: Nuclear in S-phase cells and cytoplasmic By similarity.
Sequence similarities	Belongs to the HAT1 family.

Ontologies

Keywords
Cellular component	Cytoplasm Nucleus
Molecular function	Acyltransferase Transferase
PTM	Phosphoprotein
Gene Ontology (GO)
Biological process	chromatin silencing at telomere Inferred from electronic annotation. Source: InterPro histone acetylation Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	histone acetyltransferase activity Inferred from electronic annotation. Source: EC protein 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 – 416	416	Histone acetyltransferase type B catalytic subunit		PRO_0000227729
Amino acid modifications
	Modified residue	358	1	Phosphoserine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q8BY71-1 [UniParc]. Last modified March 1, 2003. Version 1. Checksum: A20D53ABF1A7C824	FASTA	416	49,278
	10 20 30 40 50 60 MAALEKFLVE YKSAVEKKLA EYKCNTNTAI ELKLVRFPED LENDIRTFFP EYTHQLFGDD 70 80 90 100 110 120 ETAFGYKGLK ILLYYIAGSL STLFRVEYSS KVDENFDCVE ADDVEGKIRQ IIPPGFCTNT 130 140 150 160 170 180 NDFLSLLEKE TNFKPFGTLL HTYTVPSQTG GETFTFQIHK ADMTCRGFRE YHERLQTFLM 190 200 210 220 230 240 WFIETASFID VDDERWHYFL VFEKYNKDGA TLFATVGYMT VYNYYVYPDK TRPRVSQMLI 250 260 270 280 290 300 LTPFQGQGHG AQLLETVHRY YISFPTVLDI TAEDPSRSYL KLRDFVLVKF CQFLPSFSRE 310 320 330 340 350 360 RLLQGFSEDM AIQAQQMFKI NKQHARRVYE ILRLLVTDMS DAEQYRSYRL DIKRRLISPY 370 380 390 400 410 KKKQRDLAKM KKCLRPEELT NQMNQIEISV QHEQLEERFQ ELVEDYRRVI ERLAQE

References

[1]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Heart and Thymus.
[2]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: FVB/N. Tissue: Mammary tumor.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AK041700 mRNA. Translation: BAC31038.1. AK169315 mRNA. Translation: BAE41070.1. BC055460 mRNA. Translation: AAH55460.1.
IPI	IPI00226930.
RefSeq	NP_080391.2.
UniGene	Mm.272472
3D structure databases
SMR	Q8BY71. Positions 20-338.
ModBase	Search...
Protein-protein interaction databases
STRING	Q8BY71.
PTM databases
PhosphoSite	Q8BY71.
Proteomic databases
PRIDE	Q8BY71.
Genome annotation databases
Ensembl	ENSMUST00000028408; ENSMUSP00000028408; ENSMUSG00000027018; Mus musculus. [Genome view] ENSMUST00000112122; ENSMUSP00000107750; ENSMUSG00000027018; Mus musculus. [Genome view]
GeneID	107435.
KEGG	mmu:107435.
UCSC	uc008kaq.1. mouse.
Organism-specific databases
CTD	107435.
MGI	MGI:96013. Hat1.
Phylogenomic databases
HOGENOM	Q8BY71.
HOVERGEN	Q8BY71.
Enzyme and pathway databases
BRENDA	2.3.1.48. 244.
Gene expression databases
ArrayExpress	Q8BY71.
Bgee	Q8BY71.
CleanEx	MM_HAT1.
Genevestigator	Q8BY71.
GermOnline	ENSMUSG00000027018. Mus musculus.
Family and domain databases
InterPro	IPR019467. Hat1_N. IPR017380. Hist_AcTrfase_B-typ_cat-su. [Graphical view]
Pfam	PF10394. Hat1_N. 1 hit. [Graphical view]
PIRSF	PIRSF038084. HAT-B_cat. 1 hit.
ProtoNet	Search...
Other Resources
NextBio	358792.
SOURCE	Search...

Entry information

Entry name

HAT1_MOUSE

Accession

Primary (citable) accession number: Q8BY71

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 21, 2006
Last sequence update:	March 1, 2003
Last modified:	October 13, 2009
This is version 52 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)