Reviewed, UniProtKB/Swiss-Prot O14929 (HAT1_HUMAN)

Names and origin

Protein names

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

Gene names

Name:

HAT1

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	419 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein 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.
Catalytic activity	Acetyl-CoA + histone = CoA + acetylhistone.
Subunit structure	Heteromer of HAT1 and p46/HAT2 subunits.
Subcellular location	Nucleus. Cytoplasm. Note: Nuclear in S-phase cells and cytoplasmic.
Sequence similarities	Belongs to the HAT1 family.

Ontologies

Keywords
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Polymorphism
Molecular function	Acyltransferase Transferase
PTM	Phosphoprotein
Technical term	3D-structure
Gene Ontology (GO)
Biological process	DNA packaging Ref.1 Traceable author statement. Source: ProtInc chromatin silencing at telomere Inferred from electronic annotation. Source: InterPro histone acetylation Inferred from electronic annotation. Source: InterPro internal protein amino acid acetylation Ref.1 Traceable author statement. Source: ProtInc
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Ref.1 Traceable author statement. Source: ProtInc
Molecular function	histone acetyltransferase activity Ref.1 Traceable author statement. Source: ProtInc protein binding Ref.1 Traceable author statement. Source: ProtInc
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 419

419

Histone acetyltransferase type B catalytic subunit

PRO_0000083902

Amino acid modifications

Modified residue

361

1

Phosphoserine Ref.4 Ref.5

Natural variations

Natural variant

317

1

A → P in a colorectal cancer sample; somatic mutation. Ref.7

VAR_035997

Secondary structure

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419

Helix Strand Turn

Details...

Beta strand

26 – 28

3

Helix

29 – 32

4

Beta strand

33 – 40

8

Helix

41 – 44

4

Helix

47 – 49

3

Helix

57 – 60

4

Turn

61 – 64

4

Beta strand

65 – 71

7

Beta strand

73 – 79

7

Turn

80 – 82

3

Beta strand

85 – 90

6

Beta strand

92 – 94

3

Turn

97 – 99

3

Beta strand

100 – 102

3

Helix

107 – 112

6

Helix

123 – 131

9

Helix

132 – 135

4

Beta strand

140 – 148

9

Beta strand

157 – 164

8

Helix

171 – 185

15

Beta strand

199 – 210

12

Beta strand

213 – 229

17

Turn

230 – 232

3

Beta strand

233 – 243

11

Helix

245 – 247

3

Helix

252 – 265

14

Beta strand

273 – 277

5

Helix

280 – 294

15

Helix

298 – 300

3

Helix

302 – 305

4

Helix

311 – 321

11

Helix

325 – 339

15

Sequences

	Sequence		Length	Mass (Da)
	O14929-1 [UniParc]. Last modified January 1, 1998. Version 1. Checksum: 509DF06E0E4E2647	FASTA	419	49,513
	10 20 30 40 50 60 MAGFGAMEKF LVEYKSAVEK KLAEYKCNTN TAIELKLVRF PEDLENDIRT FFPEYTHQLF 70 80 90 100 110 120 GDDETAFGYK GLKILLYYIA GSLSTMFRVE YASKVDENFD CVEADDVEGK IRQIIPPGFC 130 140 150 160 170 180 TNTNDFLSLL EKEVDFKPFG TLLHTYSVLS PTGGENFTFQ IYKADMTCRG FREYHERLQT 190 200 210 220 230 240 FLMWFIETAS FIDVDDERWH YFLVFEKYNK DGATLFATVG YMTVYNYYVY PDKTRPRVSQ 250 260 270 280 290 300 MLILTPFQGQ GHGAQLLETV HRYYTEFPTV LDITAEDPSK SYVKLRDFVL VKLCQDLPCF 310 320 330 340 350 360 SREKLMQGFN EDMAIEAQQK FKINKQHARR VYEILRLLVT DMSDAEQYRS YRLDIKRRLI 370 380 390 400 410 SPYKKKQRDL AKMRKCLRPE ELTNQMNQIE ISMQHEQLEE SFQELVEDYR RVIERLAQE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Nucleosomal DNA regulates the core-histone-binding subunit of the human Hat1 acetyltransferase." Verreault A., Kaufman P.D., Kobayashi R., Stillman B. Curr. Biol. 8:96-108(1998) [PubMed: 9427644] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Generation and annotation of the DNA sequences of human chromosomes 2 and 4." Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K. Nature 434:724-731(2005) [PubMed: 15815621] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	"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]. Tissue: Testis.
[4]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-361, MASS SPECTROMETRY. Tissue: Epithelium.
[5]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-361, MASS SPECTROMETRY.
[6]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[7]	"The consensus coding sequences of human breast and colorectal cancers." Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E. Science 314:268-274(2006) [PubMed: 16959974] [Abstract] Cited for: VARIANT [LARGE SCALE ANALYSIS] PRO-317.
+	Additional computationally mapped references.

Web resources

Wikipedia

Histone acetyltransferase entry

Cross-references

Sequence databases

EMBLGenBankDDBJ

AF030424 mRNA. Translation: AAC02425.1.
AC114745 Genomic DNA. Translation: AAX93247.1.
AC015976 Genomic DNA. Translation: AAY14731.1.
BC045673 mRNA. Translation: AAH45673.1. Different initiation.

IPI

IPI00024719.

RefSeq

NP_003633.1.

UniGene

Hs.632532

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2P0W	X-ray	1.90	A/B	20-341	[»]

ModBase

Search...

PTM databases

PhosphoSite

O14929.

Proteomic databases

PeptideAtlas

O14929.

PRIDE

O14929.

Genome annotation databases

Ensembl

ENSG00000128708. Homo sapiens. [Contig view]

GeneID

8520.

Organism-specific databases

GeneCards

GC02P172487.

H-InvDB

HIX0002592.

HGNC

HGNC:4821. HAT1.

MIM

603053. gene.

PharmGKB

PA29197.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

O14929.

HOVERGEN

O14929.

OMA

O14929. SEDMAIE.

Enzyme and pathway databases

BRENDA

2.3.1.48. 247.

Gene expression databases

ArrayExpress

O14929.

Bgee

O14929.

CleanEx

HS_HAT1.

GermOnline

ENSG00000128708. Homo sapiens.

Family and domain databases

InterPro

IPR016181. Acyl_CoA_acyltransferase.
IPR019467. Hat1_N.
IPR017380. Hist_AcTrfase_B-typ_cat-su.
[Graphical view]

Gene3D

G3DSA:3.40.630.30. Acyl_CoA_acyltransferase. 1 hit.

Pfam

PF10394. Hat1_N. 1 hit.
[Graphical view]

PIRSF

PIRSF038084. HAT-B_cat. 1 hit.

ProtoNet

Search...

Other Resources

NextBio

31898.

SOURCE

Search...

Entry information

Entry name

HAT1_HUMAN

Accession

Primary (citable) accession number: O14929
Secondary accession number(s): Q49A44, Q53QF0, Q53SU4

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	January 1, 1998
Last modified:	June 16, 2009
This is version 69 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)