[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, ACETYLATION OF HISTONE H4, AND INTERACTION WITH HAT2 AND HISTONE H4. DOI=10.1016/S0092-8674(00)81325-2; PubMed=8858151 [NCBI, ExPASy, EBI, Israel, Japan] Parthun M.R., Widom J., Gottschling D.E.; "The major cytoplasmic histone acetyltransferase in yeast: links to chromatin replication and histone metabolism."; Cell 87:85-94(1996).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION. DOI=10.1074/jbc.270.42.24674; PubMed=7559580 [NCBI, ExPASy, EBI, Israel, Japan] Kleff S., Andrulis E.D., Anderson C.W., Sternglanz R.; "Identification of a gene encoding a yeast histone H4 acetyltransferase."; J. Biol. Chem. 270:24674-24677(1995).
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=ATCC 204511 / S288c / AB972; PubMed=9169875 [NCBI, ExPASy, EBI, Israel, Japan] Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W., Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D., Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E., Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H., DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N., Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K., Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M., Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A., Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S., Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D., Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S., Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B., Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A., Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R., Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A., Vo D.H., Hani J.; "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI."; Nature 387:103-105(1997).
[4]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=ATCC 204508 / S288c; DOI=10.1101/gr.6037607; PubMed=17322287 [NCBI, ExPASy, EBI, Israel, Japan] Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J., Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J.; "Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae."; Genome Res. 17:536-543(2007).
[5]	ACETYLATION OF HISTONE H4 BY THE HAT-B COMPLEX. DOI=10.1074/jbc.273.20.12599; PubMed=9575221 [NCBI, ExPASy, EBI, Israel, Japan] Ruiz-Garcia A.B., Sendra R., Galiana M., Pamblanco M., Perez-Ortin J.E., Tordera V.; "HAT1 and HAT2 proteins are components of a yeast nuclear histone acetyltransferase enzyme specific for free histone H4."; J. Biol. Chem. 273:12599-12605(1998).
[6]	FUNCTION, AND ACETYLATION OF HISTONE H4. DOI=10.1128/MCB.20.19.7051-7058.2000; PubMed=10982821 [NCBI, ExPASy, EBI, Israel, Japan] Kelly T.J., Qin S., Gottschling D.E., Parthun M.R.; "Type B histone acetyltransferase Hat1p participates in telomeric silencing."; Mol. Cell. Biol. 20:7051-7058(2000).
[7]	FUNCTION. DOI=10.1128/MCB.22.23.8353-8365.2002; PubMed=12417736 [NCBI, ExPASy, EBI, Israel, Japan] Qin S., Parthun M.R.; "Histone H3 and the histone acetyltransferase Hat1p contribute to DNA double-strand break repair."; Mol. Cell. Biol. 22:8353-8365(2002).
[8]	INTERACTION WITH HIF1 AND HISTONE H4, FUNCTION OF THE HAT-B COMPLEX, AND SUBCELLULAR LOCATION. DOI=10.1074/jbc.M314228200; PubMed=14761951 [NCBI, ExPASy, EBI, Israel, Japan] Poveda A., Pamblanco M., Tafrov S., Tordera V., Sternglanz R., Sendra R.; "Hif1 is a component of yeast histone acetyltransferase B, a complex mainly localized in the nucleus."; J. Biol. Chem. 279:16033-16043(2004).
[9]	FUNCTION, IDENTIFICATION IN THE HAT-B COMPLEX, MASS SPECTROMETRY, INTERACTION WITH HISTONES H3 AND H4, AND SUBCELLULAR LOCATION. DOI=10.1016/S1097-2765(04)00184-4; PubMed=15099519 [NCBI, ExPASy, EBI, Israel, Japan] Ai X., Parthun M.R.; "The nuclear Hat1p/Hat2p complex: a molecular link between type B histone acetyltransferases and chromatin assembly."; Mol. Cell 14:195-205(2004).
[10]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-354, AND MASS SPECTROMETRY. DOI=10.1074/mcp.M700468-MCP200; PubMed=18407956 [NCBI, ExPASy, EBI, Israel, Japan] Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.; "A multidimensional chromatography technology for in-depth phosphoproteome analysis."; Mol. Cell. Proteomics 7:1389-1396(2008).
[11]	X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 1-320 IN COMPLEX WITH ACETYL-COENZYME A. DOI=10.1016/S0092-8674(00)81584-6; PubMed=9727486 [NCBI, ExPASy, EBI, Israel, Japan] Dutnall R.N., Tafrov S.T., Sternglanz R., Ramakrishnan V.; "Structure of the histone acetyltransferase Hat1: a paradigm for the GCN5-related N-acetyltransferase superfamily."; Cell 94:427-438(1998).

Comments

FUNCTION: Catalytic component of the histone acetylase B (HAT-B) complex. Acetylates 'Lys-12' of free histone H4 in the cytoplasm. The complex is also found in the nucleus, however it is not certain that it modifies histone H4 when packaged in chromatin. Histone H4 'Lys-12' acetylation is required for telomeric silencing. Has intrinsic substrate specificity that modifies lysine in recognition sequence GXGKXG. Involved in DNA double-strand break repair.
CATALYTIC ACTIVITY: Acetyl-CoA + histone = CoA + acetylhistone.
SUBUNIT: Component of the HAT-B complex composed of at least HAT1 and HAT2. In the cytoplasm, this complex binds to the histone H4 tail. In the nucleus, the HAT-B complex has an additional component, the histone H3/H4 chaperone HIF1.
INTERACTION:
P53861:ELA1; NbExp=1; IntAct=EBI-8176, EBI-29191;
P39984:HAT2; NbExp=1; IntAct=EBI-8176, EBI-8185;
SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
SIMILARITY: Belongs to the HAT1 family.
SIMILARITY: Contains 1 N-acetyltransferase domain.

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

Z48483; CAA88385.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
Z71255; CAA95040.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U33335; AAB68104.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AY558042; AAS56368.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A57583; A57583.

RefSeq

NP_015324.1; -.

3D structure databases

PDB

1BOB; X-ray; 2.30 A; A=1-320.

[ExPASy / RCSB / EBI]

PDBsum

1BOB; -.

ModBase

Q12341.

Protein-protein interaction databases

DIP

DIP:2362N; -.

IntAct

Q12341; 17.

Organism-specific databases

YPL001w; -.

S000005922; HAT1.

Gene expression databases

ArrayExpress

Q12341; -.

GermOnline

YPL001W; Saccharomyces cerevisiae.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from electronic annotation from UniProtKB-KW).
GO:0000123;	Cellular component: histone acetyltransferase complex (inferred from electronic annotation from InterPro).
GO:0004406;	Molecular function: H3/H4 histone acetyltransferase activity (inferred from direct assay from SGD).
GO:0005515;	Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0006348;	Biological process: chromatin silencing at telomere (inferred from electronic annotation from InterPro).
GO:0006281;	Biological process: DNA repair (inferred from electronic annotation from UniProtKB-KW).
GO:0016573;	Biological process: histone acetylation (inferred from electronic annotation from InterPro).
QuickGo view.

Family and domain databases

InterPro

IPR016181; Acyl_CoA_acyltransferase.
IPR000182; GCN5-rel_AcTrfase.
IPR017380; Hist_AcTrfase_B-typ_cat_su.
IPR013523; Hist_AcTrfase_HAT1_C.
Graphical view of domain structure.

Gene3D

G3DSA:3.40.630.30; Acyl_CoA_acyltransferase; 1.
G3DSA:1.10.10.390; Histone_AcTrfase_HAT1_C; 1.

PIRSF

PIRSF038084; HAT-B_cat; 1.

PROSITE

PS51186; GNAT; 1.
PROSITE graphical view of domain structure (profiles).

Proteomic databases

PeptideAtlas

Q12341; -.

Proteomics databases

PRIDE

Q12341; -.

Genome annotation databases

Ensembl

YPL001W; Saccharomyces cerevisiae. [Contig view]

856106; -.

U00094_GR; YPL001W.

sce:YPL001W; -.

fig|4932.3.peg.6458; -.

Phylogenomic databases

HOGENOM

Q12341; -.

Other

Q12341; -.

981164; -.

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

Keywords

3D-structure; Acyltransferase; Chromatin regulator; Complete proteome; Cytoplasm; Direct protein sequencing; DNA damage; DNA repair; Nucleus; Phosphoprotein; Transferase.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 374`	`374`	`Histone acetyltransferase type B catalytic subunit.`	`PRO_0000083903`
`DOMAIN`	`135 303`	`169`	`N-acetyltransferase.`
`COMPBIAS`	`314 317`	`4`	`Poly-Leu.`
`MOD_RES`	`354 354`		`Phosphoserine.`
`CONFLICT`	`87 87`		`L -> V (in Ref. 4; AAS56368).`
`HELIX`	`8 10`	`3`
`STRAND`	`11 14`	`4`
`HELIX`	`15 18`	`4`
`STRAND`	`19 31`	`13`
`HELIX`	`37 40`	`4`
`TURN`	`41 44`	`4`
`STRAND`	`45 51`	`7`
`STRAND`	`53 59`	`7`
`TURN`	`60 62`	`3`
`STRAND`	`65 70`	`6`
`STRAND`	`72 74`	`3`
`HELIX`	`83 88`	`6`
`STRAND`	`97 99`	`3`
`HELIX`	`101 111`	`11`
`TURN`	`112 114`	`3`
`TURN`	`117 120`	`4`
`STRAND`	`121 129`	`9`
`STRAND`	`132 139`	`8`
`HELIX`	`144 153`	`10`
`HELIX`	`155 160`	`6`
`STRAND`	`174 181`	`8`
`TURN`	`182 184`	`3`
`STRAND`	`187 196`	`10`
`STRAND`	`213 222`	`10`
`HELIX`	`224 226`	`3`
`STRAND`	`228 230`	`3`
`HELIX`	`231 245`	`15`
`STRAND`	`249 256`	`8`
`HELIX`	`259 275`	`17`
`HELIX`	`278 281`	`4`
`HELIX`	`290 300`	`11`
`HELIX`	`304 317`	`14`

Sequence information

Length: 374 AA [This is the length of the unprocessed precursor]

Molecular weight: 43873 Da [This is the MW of the unprocessed precursor]

CRC64: 8DECA134274413E6 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSANDFKPET WTSSANEALR VSIVGENAVQ FSPLFTYPIY GDSEKIYGYK DLIIHLAFDS 

        70         80         90        100        110        120 
VTFKPYVNVK YSAKLGDDNI VDVEKKLLSF LPKDDVIVRD EAKWVDCFAE ERKTHNLSDV 

       130        140        150        160        170        180 
FEKVSEYSLN GEEFVVYKSS LVDDFARRMH RRVQIFSLLF IEAANYIDET DPSWQIYWLL 

       190        200        210        220        230        240 
NKKTKELIGF VTTYKYWHYL GAKSFDEDID KKFRAKISQF LIFPPYQNKG HGSCLYEAII 

       250        260        270        280        290        300 
QSWLEDKSIT EITVEDPNEA FDDLRDRNDI QRLRKLGYDA VFQKHSDLSD EFLESSRKSL 

       310        320        330        340        350        360 
KLEERQFNRL VEMLLLLNNS PSFELKVKNR LYIKNYDALD QTDPEKAREA LQNSFILVKD 

       370 
DYRRIIESIN KSQG

Q12341 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