O14929 (HAT1_HUMAN) 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 1

Gene names

Name:	HAT1
Synonyms:	KAT1

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	419 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Acetylates soluble but not nucleosomal histone H4 at 'Lys-5' (H4K5ac) and 'Lys-12' (H4K12ac) and, to a lesser extent, acetylates histone H2A at 'Lys-5' (H2AK5ac). Has intrinsic substrate specificity that modifies lysine in recognition sequence GXGKXG. May be involved in nucleosome assembly during DNA replication and repair as part of the histone H3.1 and H3.3 complexes. May play a role in DNA repair in response to free radical damage. Ref.1 Ref.5 Ref.8
Catalytic activity	Acetyl-CoA + [histone] = CoA + acetyl-[histone]. Ref.1 Ref.5
Subunit structure	Catalytic subunit of the type B histone acetlytransferase (HAT) complex, composed of RBBP7 and HAT1. Interacts with histones H4 and H2A. The interaction is dependent of the ability of RBBP7 to bind to the N-terminus of histones. Component of the histone H3.1 and H3.3 complexes. Ref.1 Ref.8
Subcellular location	Isoform A: Nucleus matrix. Isoform B: Cytoplasm. Nucleus. Nucleus matrix. Nucleus › nucleoplasm. Note: Localization is predominantly nuclear in normal cells. Treatment with hydrogen peroxide or ionizing radiation enhances nuclear localization through redistribution of existing protein. Ref.1 Ref.7 Ref.8
Developmental stage	Highly expressed in mitotic cells (at protein level). Ref.7
Induction	Up-regulated by estrogen. Ref.6
Sequence similarities	Belongs to the HAT1 family.
Sequence caution	The sequence AAH18682.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Molecular function	Acyltransferase Transferase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	DNA packaging Traceable author statement Ref.1. Source: ProtInc chromatin silencing at telomere Inferred from electronic annotation. Source: InterPro response to nutrient Inferred from electronic annotation. Source: Compara
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell nuclear matrix Inferred from electronic annotation. Source: UniProtKB-SubCell nucleoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from direct assay. Source: HPA
Molecular_function	histone acetyltransferase activity Traceable author statement Ref.1. Source: ProtInc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
HIST1H4A	P62805	4	EBI-2339359,EBI-302023
vpr	P12520	3	EBI-2339359,EBI-6164519	From a different organism.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform A (identifier: O14929-1)

Also known as: a; Nuclear;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform B (identifier: O14929-2)

Also known as: b;

The sequence of this isoform differs from the canonical sequence as follows:
     1-85: Missing.

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

Natural variations

Alternative sequence

1 – 85

85

Missing in isoform B.

VSP_041129

Natural variant

317

1

A → P in a colorectal cancer sample; somatic mutation. Ref.10

VAR_035997

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

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)
	Isoform A (a) (Nuclear) [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
	Isoform B (b) [UniParc]. Checksum: 40E4B9925CD5DF81	FASTA	334	39,786
	10 20 30 40 50 60 MFRVEYASKV DENFDCVEAD DVEGKIRQII PPGFCTNTND FLSLLEKEVD FKPFGTLLHT 70 80 90 100 110 120 YSVLSPTGGE NFTFQIYKAD MTCRGFREYH ERLQTFLMWF IETASFIDVD DERWHYFLVF 130 140 150 160 170 180 EKYNKDGATL FATVGYMTVY NYYVYPDKTR PRVSQMLILT PFQGQGHGAQ LLETVHRYYT 190 200 210 220 230 240 EFPTVLDITA EDPSKSYVKL RDFVLVKLCQ DLPCFSREKL MQGFNEDMAI EAQQKFKINK 250 260 270 280 290 300 QHARRVYEIL RLLVTDMSDA EQYRSYRLDI KRRLISPYKK KQRDLAKMRK CLRPEELTNQ 310 320 330 MNQIEISMQH EQLEESFQEL VEDYRRVIER LAQE

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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), FUNCTION, ENZYME ACTIVITY, SUBUNIT, SUBCELLULAR LOCATION. Tissue: Teratocarcinoma.
[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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2-419 (ISOFORM A). Tissue: Brain, Lung and Testis.
[5]	"Effects of acetylation of histone H4 at lysines 8 and 16 on activity of the Hat1 histone acetyltransferase." Makowski A.M., Dutnall R.N., Annunziato A.T. J. Biol. Chem. 276:43499-43502(2001) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, CATALYTIC ACTIVITY.
[6]	"Quantitative real-time RT-PCR analysis of eight novel estrogen-regulated genes in breast cancer." Sorbello V., Fuso L., Sfiligoi C., Scafoglio C., Ponzone R., Biglia N., Weisz A., Sismondi P., De Bortoli M. Int. J. Biol. Markers 18:123-129(2003) [PubMed] [Europe PMC] [Abstract] Cited for: INDUCTION BY ESTROGEN.
[7]	"Irradiation with heavy-ion particles changes the cellular distribution of human histone acetyltransferase HAT1." Lebel E.A., Boukamp P., Tafrov S.T. Mol. Cell. Biochem. 339:271-284(2010) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE.
[8]	"The program for processing newly synthesized histones H3.1 and H4." Campos E.I., Fillingham J., Li G., Zheng H., Voigt P., Kuo W.H., Seepany H., Gao Z., Day L.A., Greenblatt J.F., Reinberg D. Nat. Struct. Mol. Biol. 17:1343-1351(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBUNIT, SUBCELLULAR LOCATION.
[9]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[10]	"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] [Europe PMC] [Abstract] Cited for: VARIANT [LARGE SCALE ANALYSIS] PRO-317.
+	Additional computationally mapped references.

Web resources

Wikipedia

Histone acetyltransferase entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF030424 mRNA. Translation: AAC02425.1.
AC015976 Genomic DNA. Translation: AAY14731.1.
AC114745 Genomic DNA. Translation: AAX93247.1.
CH471058 Genomic DNA. Translation: EAX11195.1.
BC018682 mRNA. Translation: AAH18682.1. Different initiation.
BC045673 mRNA. No translation available.
BC063003 mRNA. Translation: AAH63003.1.

IPI

IPI00024719.
IPI00651621.

RefSeq

NP_003633.1. NM_003642.3.

UniGene

Hs.632532.

3D structure databases

PDBe
RCSB PDB
PDBj

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

ProteinModelPortal

O14929.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-52811N.

IntAct

O14929. 10 interactions.

MINT

MINT-2795393.

STRING

9606.ENSP00000264108.

PTM databases

PhosphoSite

O14929.

Proteomic databases

PaxDb

O14929.

PeptideAtlas

O14929.

PRIDE

O14929.

Protocols and materials databases

DNASU

8520.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000264108; ENSP00000264108; ENSG00000128708.
ENST00000392584; ENSP00000376363; ENSG00000128708.

GeneID

8520.

KEGG

hsa:8520.

UCSC

uc002uhi.3. human.
uc010fqi.2. human.

Organism-specific databases

CTD

8520.

GeneCards

GC02P172742.

HGNC

HGNC:4821. HAT1.

HPA

HPA036788.

MIM

603053. gene.

neXtProt

NX_O14929.

PharmGKB

PA29197.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG326277.

HOGENOM

HOG000231943.

HOVERGEN

HBG005945.

InParanoid

O14929.

KO

K11303.

OMA

HRYYIAS.

OrthoDB

EOG4NCMCS.

PhylomeDB

O14929.

Gene expression databases

ArrayExpress

O14929.

Bgee

O14929.

CleanEx

HS_HAT1.

Genevestigator

O14929.

GermOnline

ENSG00000128708. Homo sapiens.

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...

Other

EvolutionaryTrace

O14929.

GenomeRNAi

8520.

NextBio

31898.

SOURCE

Search...

Entry information

Entry name

HAT1_HUMAN

Accession

Primary (citable) accession number: O14929
Secondary accession number(s): Q49A44 , Q53QF0, Q53SU4, Q6P594, Q8WWB9

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	January 1, 1998
Last modified:	May 29, 2013
This is version 110 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.