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O14929 (HAT1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 120. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Histone acetyltransferase type B catalytic subunit

EC=2.3.1.48
Alternative name(s):
Histone acetyltransferase 1
Gene names
Name:HAT1
Synonyms:KAT1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length419 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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.9

Catalytic activity

Acetyl-CoA + [histone] = CoA + acetyl-[histone]. Ref.1 Ref.5

Subunit structure

Catalytic subunit of the type B histone acetyltransferase (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.9

Subcellular location

Isoform A: Nucleus matrix.

Isoform B: Cytoplasm. Nucleus. Nucleus matrix. Nucleusnucleoplasm. 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.8 Ref.9

Developmental stage

Highly expressed in mitotic cells (at protein level). Ref.8

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.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

HIST2H4BP628054EBI-2339359,EBI-302023
vprP125203EBI-2339359,EBI-6164519From 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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.7
Chain2 – 419418Histone acetyltransferase type B catalytic subunit
PRO_0000083902

Amino acid modifications

Modified residue21N-acetylalanine Ref.7 Ref.11
Modified residue91N6-acetyllysine By similarity
Modified residue151N6-acetyllysine By similarity

Natural variations

Alternative sequence1 – 8585Missing in isoform B.
VSP_041129
Natural variant3171A → P in a colorectal cancer sample; somatic mutation. Ref.12
VAR_035997

Secondary structure

....................................................... 419
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform A (a) (Nuclear) [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: 509DF06E0E4E2647

FASTA41949,513
        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 

« Hide

Isoform B (b) [UniParc].

Checksum: 40E4B9925CD5DF81
Show »

FASTA33439,786

References

« Hide '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. expand/collapse author list , 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. expand/collapse author list , 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]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[8]"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.
[9]"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.
[10]"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].
[11]"Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"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. expand/collapse author list , 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.
RefSeqNP_003633.1. NM_003642.3.
UniGeneHs.632532.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2P0WX-ray1.90A/B20-341[»]
ProteinModelPortalO14929.
SMRO14929. Positions 23-341.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114092. 26 interactions.
DIPDIP-52811N.
IntActO14929. 12 interactions.
MINTMINT-2795393.
STRING9606.ENSP00000264108.

PTM databases

PhosphoSiteO14929.

Proteomic databases

PaxDbO14929.
PeptideAtlasO14929.
PRIDEO14929.

Protocols and materials databases

DNASU8520.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000264108; ENSP00000264108; ENSG00000128708. [O14929-1]
ENST00000392584; ENSP00000376363; ENSG00000128708. [O14929-2]
GeneID8520.
KEGGhsa:8520.
UCSCuc002uhi.3. human. [O14929-1]
uc010fqi.2. human. [O14929-2]

Organism-specific databases

CTD8520.
GeneCardsGC02P172742.
HGNCHGNC:4821. HAT1.
HPAHPA036788.
MIM603053. gene.
neXtProtNX_O14929.
PharmGKBPA29197.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG326277.
HOGENOMHOG000231943.
HOVERGENHBG005945.
InParanoidO14929.
KOK11303.
OMAHRYYIAS.
PhylomeDBO14929.
TreeFamTF314995.

Enzyme and pathway databases

ReactomeREACT_172623. Chromatin organization.

Gene expression databases

ArrayExpressO14929.
BgeeO14929.
CleanExHS_HAT1.
GenevestigatorO14929.

Family and domain databases

Gene3D3.40.630.30. 1 hit.
3.90.360.10. 1 hit.
InterProIPR016181. Acyl_CoA_acyltransferase.
IPR019467. Hat1_N.
IPR017380. Hist_AcTrfase_B-typ_cat-su.
[Graphical view]
PANTHERPTHR12046. PTHR12046. 1 hit.
PfamPF10394. Hat1_N. 1 hit.
[Graphical view]
PIRSFPIRSF038084. HAT-B_cat. 1 hit.
SUPFAMSSF55729. SSF55729. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceO14929.
GeneWikiHAT1.
GenomeRNAi8520.
NextBio31898.
PROO14929.
SOURCESearch...

Entry information

Entry nameHAT1_HUMAN
AccessionPrimary (citable) accession number: O14929
Secondary accession number(s): Q49A44 expand/collapse secondary AC list , Q53QF0, Q53SU4, Q6P594, Q8WWB9
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: January 1, 1998
Last modified: April 16, 2014
This is version 120 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM