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O14929

- HAT1_HUMAN

UniProt

O14929 - HAT1_HUMAN

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Protein

Histone acetyltransferase type B catalytic subunit

Gene
HAT1, KAT1
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.3 Publications

Catalytic activityi

Acetyl-CoA + [histone] = CoA + acetyl-[histone].2 Publications

GO - Molecular functioni

  1. histone acetyltransferase activity Source: ProtInc
  2. protein binding Source: IntAct

GO - Biological processi

  1. chromatin organization Source: Reactome
  2. chromatin silencing at telomere Source: InterPro
  3. DNA packaging Source: ProtInc
  4. DNA replication-dependent nucleosome assembly Source: UniProt
  5. DNA replication-independent nucleosome assembly Source: UniProt
  6. internal protein amino acid acetylation Source: ProtInc
  7. response to nutrient Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Enzyme and pathway databases

ReactomeiREACT_172610. HATs acetylate histones.

Names & Taxonomyi

Protein namesi
Recommended name:
Histone acetyltransferase type B catalytic subunit (EC:2.3.1.48)
Alternative name(s):
Histone acetyltransferase 1
Gene namesi
Name:HAT1
Synonyms:KAT1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 2

Organism-specific databases

HGNCiHGNC:4821. HAT1.

Subcellular locationi

Isoform A : Nucleus matrix 3 Publications
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.3 Publications

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
  2. intracellular membrane-bounded organelle Source: HPA
  3. nuclear chromatin Source: UniProt
  4. nuclear matrix Source: UniProtKB-SubCell
  5. nucleoplasm Source: Reactome
  6. nucleus Source: HPA
  7. protein complex Source: UniProt
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA29197.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 419418Histone acetyltransferase type B catalytic subunitPRO_0000083902Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine2 Publications
Modified residuei9 – 91N6-acetyllysine By similarity
Modified residuei15 – 151N6-acetyllysine By similarity

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiO14929.
PaxDbiO14929.
PeptideAtlasiO14929.
PRIDEiO14929.

PTM databases

PhosphoSiteiO14929.

Expressioni

Developmental stagei

Highly expressed in mitotic cells (at protein level).1 Publication

Inductioni

Up-regulated by estrogen.1 Publication

Gene expression databases

ArrayExpressiO14929.
BgeeiO14929.
CleanExiHS_HAT1.
GenevestigatoriO14929.

Organism-specific databases

HPAiHPA036788.

Interactioni

Subunit structurei

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.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
HIST2H4BP628054EBI-2339359,EBI-302023
vprP125203EBI-2339359,EBI-6164519From a different organism.

Protein-protein interaction databases

BioGridi114092. 26 interactions.
DIPiDIP-52811N.
IntActiO14929. 12 interactions.
MINTiMINT-2795393.
STRINGi9606.ENSP00000264108.

Structurei

Secondary structure

1
419
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi26 – 283
Helixi29 – 324
Beta strandi33 – 408
Helixi41 – 444
Helixi47 – 493
Helixi57 – 604
Turni61 – 644
Beta strandi65 – 717
Beta strandi73 – 797
Turni80 – 823
Beta strandi85 – 906
Beta strandi92 – 943
Turni97 – 993
Beta strandi100 – 1023
Helixi107 – 1126
Helixi123 – 1319
Helixi132 – 1354
Beta strandi140 – 1489
Beta strandi157 – 1648
Helixi171 – 18515
Beta strandi199 – 21012
Beta strandi213 – 22917
Turni230 – 2323
Beta strandi233 – 24311
Helixi245 – 2473
Helixi252 – 26514
Beta strandi273 – 2775
Helixi280 – 29415
Helixi298 – 3003
Helixi302 – 3054
Helixi311 – 32111
Helixi325 – 33915

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2P0WX-ray1.90A/B20-341[»]
ProteinModelPortaliO14929.
SMRiO14929. Positions 23-341.

Miscellaneous databases

EvolutionaryTraceiO14929.

Family & Domainsi

Sequence similaritiesi

Belongs to the HAT1 family.

Phylogenomic databases

eggNOGiNOG326277.
HOGENOMiHOG000231943.
HOVERGENiHBG005945.
InParanoidiO14929.
KOiK11303.
OMAiHRYYIAS.
PhylomeDBiO14929.
TreeFamiTF314995.

Family and domain databases

Gene3Di3.40.630.30. 1 hit.
3.90.360.10. 1 hit.
InterProiIPR016181. Acyl_CoA_acyltransferase.
IPR019467. Hat1_N.
IPR017380. Hist_AcTrfase_B-typ_cat-su.
[Graphical view]
PANTHERiPTHR12046. PTHR12046. 1 hit.
PfamiPF10394. Hat1_N. 1 hit.
[Graphical view]
PIRSFiPIRSF038084. HAT-B_cat. 1 hit.
SUPFAMiSSF55729. SSF55729. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform A (identifier: O14929-1) [UniParc]FASTAAdd to Basket

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.

« Hide

MAGFGAMEKF LVEYKSAVEK KLAEYKCNTN TAIELKLVRF PEDLENDIRT    50
FFPEYTHQLF GDDETAFGYK GLKILLYYIA GSLSTMFRVE YASKVDENFD 100
CVEADDVEGK IRQIIPPGFC TNTNDFLSLL EKEVDFKPFG TLLHTYSVLS 150
PTGGENFTFQ IYKADMTCRG FREYHERLQT FLMWFIETAS FIDVDDERWH 200
YFLVFEKYNK DGATLFATVG YMTVYNYYVY PDKTRPRVSQ MLILTPFQGQ 250
GHGAQLLETV HRYYTEFPTV LDITAEDPSK SYVKLRDFVL VKLCQDLPCF 300
SREKLMQGFN EDMAIEAQQK FKINKQHARR VYEILRLLVT DMSDAEQYRS 350
YRLDIKRRLI SPYKKKQRDL AKMRKCLRPE ELTNQMNQIE ISMQHEQLEE 400
SFQELVEDYR RVIERLAQE 419
Length:419
Mass (Da):49,513
Last modified:January 1, 1998 - v1
Checksum:i509DF06E0E4E2647
GO
Isoform B (identifier: O14929-2) [UniParc]FASTAAdd to Basket

Also known as: b

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

Show »
Length:334
Mass (Da):39,786
Checksum:i40E4B9925CD5DF81
GO

Sequence cautioni

The sequence AAH18682.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti317 – 3171A → P in a colorectal cancer sample; somatic mutation. 1 Publication
VAR_035997

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 8585Missing in isoform B. VSP_041129Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS2245.1. [O14929-1]
RefSeqiNP_003633.1. NM_003642.3. [O14929-1]
UniGeneiHs.632532.

Genome annotation databases

EnsembliENST00000264108; ENSP00000264108; ENSG00000128708. [O14929-1]
ENST00000392584; ENSP00000376363; ENSG00000128708. [O14929-2]
GeneIDi8520.
KEGGihsa:8520.
UCSCiuc002uhi.3. human. [O14929-1]
uc010fqi.2. human. [O14929-2]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Wikipedia

Histone acetyltransferase entry

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS2245.1. [O14929-1 ]
RefSeqi NP_003633.1. NM_003642.3. [O14929-1 ]
UniGenei Hs.632532.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2P0W X-ray 1.90 A/B 20-341 [» ]
ProteinModelPortali O14929.
SMRi O14929. Positions 23-341.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 114092. 26 interactions.
DIPi DIP-52811N.
IntActi O14929. 12 interactions.
MINTi MINT-2795393.
STRINGi 9606.ENSP00000264108.

PTM databases

PhosphoSitei O14929.

Proteomic databases

MaxQBi O14929.
PaxDbi O14929.
PeptideAtlasi O14929.
PRIDEi O14929.

Protocols and materials databases

DNASUi 8520.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000264108 ; ENSP00000264108 ; ENSG00000128708 . [O14929-1 ]
ENST00000392584 ; ENSP00000376363 ; ENSG00000128708 . [O14929-2 ]
GeneIDi 8520.
KEGGi hsa:8520.
UCSCi uc002uhi.3. human. [O14929-1 ]
uc010fqi.2. human. [O14929-2 ]

Organism-specific databases

CTDi 8520.
GeneCardsi GC02P172742.
HGNCi HGNC:4821. HAT1.
HPAi HPA036788.
MIMi 603053. gene.
neXtProti NX_O14929.
PharmGKBi PA29197.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG326277.
HOGENOMi HOG000231943.
HOVERGENi HBG005945.
InParanoidi O14929.
KOi K11303.
OMAi HRYYIAS.
PhylomeDBi O14929.
TreeFami TF314995.

Enzyme and pathway databases

Reactomei REACT_172610. HATs acetylate histones.

Miscellaneous databases

EvolutionaryTracei O14929.
GeneWikii HAT1.
GenomeRNAii 8520.
NextBioi 31898.
PROi O14929.
SOURCEi Search...

Gene expression databases

ArrayExpressi O14929.
Bgeei O14929.
CleanExi HS_HAT1.
Genevestigatori O14929.

Family and domain databases

Gene3Di 3.40.630.30. 1 hit.
3.90.360.10. 1 hit.
InterProi IPR016181. Acyl_CoA_acyltransferase.
IPR019467. Hat1_N.
IPR017380. Hist_AcTrfase_B-typ_cat-su.
[Graphical view ]
PANTHERi PTHR12046. PTHR12046. 1 hit.
Pfami PF10394. Hat1_N. 1 hit.
[Graphical view ]
PIRSFi PIRSF038084. HAT-B_cat. 1 hit.
SUPFAMi SSF55729. SSF55729. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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. Cited for: FUNCTION, SUBUNIT, SUBCELLULAR LOCATION.
  10. 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. Cited for: VARIANT [LARGE SCALE ANALYSIS] PRO-317.

Entry informationi

Entry nameiHAT1_HUMAN
AccessioniPrimary (citable) accession number: O14929
Secondary accession number(s): Q49A44
, Q53QF0, Q53SU4, Q6P594, Q8WWB9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: January 1, 1998
Last modified: September 3, 2014
This is version 124 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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