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Search results 101 to 200 out of 285 for Hat1

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Type Details Score
GXD Expression
GXD Expression
 
Probe: MGI:527977
Assay Type: RNA in situ
Annotation Date: 2010-09-14
Strength: Moderate
Sex: Not Specified
Emaps: EMAPS:1684623
Pattern: Regionally restricted
Stage: TS23
Assay Id: MGI:4825324
Age: embryonic day 14.5
Image: euxassay_000115_10
Specimen Label: euxassay_000115_10
Detected: true
Specimen Num: 10
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•
GXD Expression
GXD Expression
 
Probe: MGI:527977
Assay Type: RNA in situ
Annotation Date: 2010-09-14
Strength: Moderate
Sex: Not Specified
Emaps: EMAPS:1684623
Pattern: Spotted
Stage: TS23
Assay Id: MGI:4825324
Age: embryonic day 14.5
Image: euxassay_000115_11
Specimen Label: euxassay_000115_11
Detected: true
Specimen Num: 11
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•
•
GXD Expression
GXD Expression
 
Probe: MGI:527977
Assay Type: RNA in situ
Annotation Date: 2010-09-14
Strength: Moderate
Sex: Not Specified
Emaps: EMAPS:1684623
Pattern: Spotted
Stage: TS23
Assay Id: MGI:4825324
Age: embryonic day 14.5
Image: euxassay_000115_12
Specimen Label: euxassay_000115_12
Detected: true
Specimen Num: 12
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•
•
GXD Expression
GXD Expression
 
Probe: MGI:527977
Assay Type: RNA in situ
Annotation Date: 2010-09-14
Strength: Moderate
Sex: Not Specified
Emaps: EMAPS:1684623
Pattern: Spotted
Stage: TS23
Assay Id: MGI:4825324
Age: embryonic day 14.5
Image: euxassay_000115_13
Specimen Label: euxassay_000115_13
Detected: true
Specimen Num: 13
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•
•
GXD Expression
GXD Expression
 
Probe: MGI:527977
Assay Type: RNA in situ
Annotation Date: 2010-09-14
Strength: Moderate
Sex: Not Specified
Emaps: EMAPS:1684623
Pattern: Spotted
Stage: TS23
Assay Id: MGI:4825324
Age: embryonic day 14.5
Image: euxassay_000115_14
Specimen Label: euxassay_000115_14
Detected: true
Specimen Num: 14
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•
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•
•
GXD Expression
GXD Expression
 
Probe: MGI:527977
Assay Type: RNA in situ
Annotation Date: 2010-09-14
Strength: Moderate
Sex: Not Specified
Emaps: EMAPS:1684623
Pattern: Spotted
Stage: TS23
Assay Id: MGI:4825324
Age: embryonic day 14.5
Image: euxassay_000115_15
Specimen Label: euxassay_000115_15
Detected: true
Specimen Num: 15
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•
•
•
•
GXD Expression
GXD Expression
 
Probe: MGI:527977
Assay Type: RNA in situ
Annotation Date: 2010-09-14
Strength: Moderate
Sex: Not Specified
Emaps: EMAPS:1684623
Pattern: Spotted
Stage: TS23
Assay Id: MGI:4825324
Age: embryonic day 14.5
Image: euxassay_000115_16
Specimen Label: euxassay_000115_16
Detected: true
Specimen Num: 16
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•
•
•
GXD Expression
GXD Expression
 
Probe: MGI:527977
Assay Type: RNA in situ
Annotation Date: 2010-09-14
Strength: Moderate
Sex: Not Specified
Emaps: EMAPS:1684623
Pattern: Spotted
Stage: TS23
Assay Id: MGI:4825324
Age: embryonic day 14.5
Image: euxassay_000115_17
Specimen Label: euxassay_000115_17
Detected: true
Specimen Num: 17
•
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•
•
GXD Expression
GXD Expression
 
Probe: MGI:527977
Assay Type: RNA in situ
Annotation Date: 2010-09-14
Strength: Moderate
Sex: Not Specified
Emaps: EMAPS:1684623
Pattern: Spotted
Stage: TS23
Assay Id: MGI:4825324
Age: embryonic day 14.5
Image: euxassay_000115_18
Specimen Label: euxassay_000115_18
Detected: true
Specimen Num: 18
•
•
•
•
•
GXD Expression
GXD Expression
 
Probe: MGI:527977
Assay Type: RNA in situ
Annotation Date: 2010-09-14
Strength: Moderate
Sex: Not Specified
Emaps: EMAPS:1684623
Pattern: Spotted
Stage: TS23
Assay Id: MGI:4825324
Age: embryonic day 14.5
Image: euxassay_000115_19
Specimen Label: euxassay_000115_19
Detected: true
Specimen Num: 19
•
•
•
•
•
GXD Expression
GXD Expression
 
Probe: MGI:527977
Assay Type: RNA in situ
Annotation Date: 2010-09-14
Strength: Moderate
Sex: Not Specified
Emaps: EMAPS:1684623
Pattern: Spotted
Stage: TS23
Assay Id: MGI:4825324
Age: embryonic day 14.5
Image: euxassay_000115_20
Specimen Label: euxassay_000115_20
Detected: true
Specimen Num: 20
•
•
•
•
•
GXD Expression
GXD Expression
 
Probe: MGI:527977
Assay Type: RNA in situ
Annotation Date: 2010-09-14
Strength: Moderate
Sex: Not Specified
Emaps: EMAPS:1684623
Pattern: Spotted
Stage: TS23
Assay Id: MGI:4825324
Age: embryonic day 14.5
Image: euxassay_000115_21
Specimen Label: euxassay_000115_21
Detected: true
Specimen Num: 21
•
•
•
•
•
GXD Expression
GXD Expression
 
Probe: MGI:527977
Assay Type: RNA in situ
Annotation Date: 2010-09-14
Strength: Moderate
Sex: Not Specified
Emaps: EMAPS:1684623
Pattern: Spotted
Stage: TS23
Assay Id: MGI:4825324
Age: embryonic day 14.5
Image: euxassay_000115_22
Specimen Label: euxassay_000115_22
Detected: true
Specimen Num: 22
•
•
•
•
•
GXD Expression
GXD Expression
 
Probe: MGI:527977
Assay Type: RNA in situ
Annotation Date: 2010-09-14
Strength: Moderate
Sex: Not Specified
Emaps: EMAPS:1684623
Pattern: Spotted
Stage: TS23
Assay Id: MGI:4825324
Age: embryonic day 14.5
Image: euxassay_000115_23
Specimen Label: euxassay_000115_23
Detected: true
Specimen Num: 23
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•
•
•
•
GXD Expression
GXD Expression
 
Probe: MGI:527977
Assay Type: RNA in situ
Annotation Date: 2010-09-14
Strength: Moderate
Sex: Not Specified
Emaps: EMAPS:1684623
Pattern: Spotted
Stage: TS23
Assay Id: MGI:4825324
Age: embryonic day 14.5
Image: euxassay_000115_24
Specimen Label: euxassay_000115_24
Detected: true
Specimen Num: 24
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•
•
GXD Expression
GXD Expression
 
Probe: MGI:527977
Assay Type: RNA in situ
Annotation Date: 2010-09-14
Strength: Moderate
Sex: Not Specified
Emaps: EMAPS:1797223
Pattern: Regionally restricted
Stage: TS23
Assay Id: MGI:4825324
Age: embryonic day 14.5
Image: euxassay_000115_05
Specimen Label: euxassay_000115_05
Detected: true
Specimen Num: 5
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•
•
•
GXD Expression
GXD Expression
 
Probe: MGI:527977
Assay Type: RNA in situ
Annotation Date: 2010-09-14
Strength: Moderate
Sex: Not Specified
Emaps: EMAPS:1797223
Pattern: Regionally restricted
Stage: TS23
Assay Id: MGI:4825324
Age: embryonic day 14.5
Image: euxassay_000115_06
Specimen Label: euxassay_000115_06
Detected: true
Specimen Num: 6
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•
•
•
•
GXD Expression
GXD Expression
 
Probe: MGI:527977
Assay Type: RNA in situ
Annotation Date: 2010-09-14
Strength: Moderate
Sex: Not Specified
Emaps: EMAPS:1797223
Pattern: Regionally restricted
Stage: TS23
Assay Id: MGI:4825324
Age: embryonic day 14.5
Image: euxassay_000115_07
Specimen Label: euxassay_000115_07
Detected: true
Specimen Num: 7
•
•
•
•
•
GXD Expression
GXD Expression
 
Probe: MGI:527977
Assay Type: RNA in situ
Annotation Date: 2010-09-14
Strength: Moderate
Sex: Not Specified
Emaps: EMAPS:1797223
Pattern: Regionally restricted
Stage: TS23
Assay Id: MGI:4825324
Age: embryonic day 14.5
Image: euxassay_000115_08
Specimen Label: euxassay_000115_08
Detected: true
Specimen Num: 8
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•
•
•
GXD Expression
GXD Expression
 
Probe: MGI:527977
Assay Type: RNA in situ
Annotation Date: 2010-09-14
Strength: Moderate
Sex: Not Specified
Emaps: EMAPS:1797223
Pattern: Regionally restricted
Stage: TS23
Assay Id: MGI:4825324
Age: embryonic day 14.5
Image: euxassay_000115_09
Specimen Label: euxassay_000115_09
Detected: true
Specimen Num: 9
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•
GXD Expression
GXD Expression
   
Probe: MGI:527977
Assay Type: RNA in situ
Annotation Date: 2023-10-17
Strength: Present
Sex: Not Specified
Emaps: EMAPS:1754722
Pattern: Not Specified
Stage: TS22
Assay Id: MGI:7540511
Age: embryonic day 14.5
Specimen Label: Supplementary table 2
Detected: true
Specimen Num: 1
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•
•
GXD Expression
GXD Expression
 
Probe: MGI:527977
Assay Type: RNA in situ
Annotation Date: 2010-09-14
Strength: Moderate
Sex: Not Specified
Emaps: EMAPS:1757523
Pattern: Regionally restricted
Stage: TS23
Assay Id: MGI:4825324
Age: embryonic day 14.5
Image: euxassay_000115_01
Specimen Label: euxassay_000115_01
Detected: true
Specimen Num: 1
•
•
•
•
•
GXD Expression
GXD Expression
 
Probe: MGI:527977
Assay Type: RNA in situ
Annotation Date: 2010-09-14
Strength: Strong
Sex: Not Specified
Emaps: EMAPS:1689423
Pattern: Regionally restricted
Stage: TS23
Assay Id: MGI:4825324
Age: embryonic day 14.5
Image: euxassay_000115_14
Specimen Label: euxassay_000115_14
Detected: true
Specimen Num: 14
•
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•
•
•
GXD Expression
GXD Expression
 
Probe: MGI:527977
Assay Type: RNA in situ
Annotation Date: 2010-09-14
Strength: Strong
Sex: Not Specified
Emaps: EMAPS:1689423
Pattern: Regionally restricted
Stage: TS23
Assay Id: MGI:4825324
Age: embryonic day 14.5
Image: euxassay_000115_17
Specimen Label: euxassay_000115_17
Detected: true
Specimen Num: 17
•
•
•
•
•
GXD Expression
GXD Expression
 
Probe: MGI:527977
Assay Type: RNA in situ
Annotation Date: 2010-09-14
Strength: Strong
Sex: Not Specified
Emaps: EMAPS:1689423
Pattern: Regionally restricted
Stage: TS23
Assay Id: MGI:4825324
Age: embryonic day 14.5
Image: euxassay_000115_18
Specimen Label: euxassay_000115_18
Detected: true
Specimen Num: 18
•
•
•
•
•
GXD Expression
GXD Expression
 
Probe: MGI:527977
Assay Type: RNA in situ
Annotation Date: 2010-09-14
Strength: Strong
Sex: Not Specified
Emaps: EMAPS:1689423
Pattern: Regionally restricted
Stage: TS23
Assay Id: MGI:4825324
Age: embryonic day 14.5
Image: euxassay_000115_19
Specimen Label: euxassay_000115_19
Detected: true
Specimen Num: 19
•
•
•
•
•
GXD Expression
GXD Expression
 
Probe: MGI:527977
Assay Type: RNA in situ
Annotation Date: 2010-09-14
Strength: Strong
Sex: Not Specified
Emaps: EMAPS:1689423
Pattern: Regionally restricted
Stage: TS23
Assay Id: MGI:4825324
Age: embryonic day 14.5
Image: euxassay_000115_20
Specimen Label: euxassay_000115_20
Detected: true
Specimen Num: 20
•
•
•
•
•
GXD Expression
GXD Expression
 
Probe: MGI:527977
Assay Type: RNA in situ
Annotation Date: 2010-09-14
Strength: Strong
Sex: Not Specified
Emaps: EMAPS:1689423
Pattern: Regionally restricted
Stage: TS23
Assay Id: MGI:4825324
Age: embryonic day 14.5
Image: euxassay_000115_21
Specimen Label: euxassay_000115_21
Detected: true
Specimen Num: 21
•
•
•
•
•
GXD Expression
GXD Expression
 
Probe: MGI:527977
Assay Type: RNA in situ
Annotation Date: 2010-09-14
Strength: Strong
Sex: Not Specified
Emaps: EMAPS:1689423
Pattern: Regionally restricted
Stage: TS23
Assay Id: MGI:4825324
Age: embryonic day 14.5
Image: euxassay_000115_22
Specimen Label: euxassay_000115_22
Detected: true
Specimen Num: 22
•
•
•
•
•
GXD Expression
GXD Expression
 
Probe: MGI:527977
Assay Type: RNA in situ
Annotation Date: 2010-09-14
Strength: Strong
Sex: Not Specified
Emaps: EMAPS:1689423
Pattern: Regionally restricted
Stage: TS23
Assay Id: MGI:4825324
Age: embryonic day 14.5
Image: euxassay_000115_23
Specimen Label: euxassay_000115_23
Detected: true
Specimen Num: 23
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Publication
18022353 | J:126799
First Author: Allis CD
Year: 2007
Journal: Cell
Title: New nomenclature for chromatin-modifying enzymes.
Volume: 131
Issue: 4
Pages: 633-6
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Publication
30186101 | J:266522
 
First Author: Elsen GE
Year: 2018
Journal: Front Neurosci
Title: The Epigenetic Factor Landscape of Developing Neocortex Is Regulated by Transcription Factors Pax6→ Tbr2→ Tbr1.
Volume: 12
Pages: 571
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Publication
- | J:165963
     
First Author: Centre for Modeling Human Disease
Year: 2010
Journal: MGI Direct Data Submission
Title: Alleles produced for the NorCOMM project by the Centre for Modeling Human Disease (Cmhd), Institute of Biomaterials & Biomedical Engineering, University of Toronto
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Publication
- | J:15839
       
First Author: International Committee on Standardized Genetic Nomenclature for Mice
Year: 1993
Title: Nomenclature rule change to delete hyphens and parentheses from mouse locus symbols
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Publication
12904583 | J:85162
First Author: Hansen J
Year: 2003
Journal: Proc Natl Acad Sci U S A
Title: A large-scale, gene-driven mutagenesis approach for the functional analysis of the mouse genome.
Volume: 100
Issue: 17
Pages: 9918-22
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Publication
17967808 | J:152068
First Author: Friedel RH
Year: 2007
Journal: Brief Funct Genomic Proteomic
Title: EUCOMM--the European conditional mouse mutagenesis program.
Volume: 6
Issue: 3
Pages: 180-5
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Publication
34321999 | J:313619
 
First Author: Bedogni F
Year: 2021
Journal: Front Mol Neurosci
Title: Cell-Type-Specific Gene Expression in Developing Mouse Neocortex: Intermediate Progenitors Implicated in Axon Development.
Volume: 14
Pages: 686034
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Publication
- | J:346132
       
First Author: The Gene Ontology Consortium
Year: 2016
Title: Automatic assignment of GO terms using logical inference, based on on inter-ontology links
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Publication
- | J:80155
       
First Author: Mouse Genome Informatics Scientific Curators
Year: 2002
Title: Mouse Genome Informatics Computational Sequence to Gene Associations for FANTOM2 data
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Publication
12520002 | J:91812
First Author: Stryke D
Year: 2003
Journal: Nucleic Acids Res
Title: BayGenomics: a resource of insertional mutations in mouse embryonic stem cells.
Volume: 31
Issue: 1
Pages: 278-81
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Publication
- | J:57656
     
First Author: Lennon G
Year: 1999
Journal: Database Download
Title: WashU-HHMI Mouse EST Project
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Publication
- | J:155845
     
First Author: Wellcome Trust Sanger Institute
Year: 2010
Journal: MGI Direct Data Submission
Title: Alleles produced for the EUCOMM and EUCOMMTools projects by the Wellcome Trust Sanger Institute
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Publication
- | J:72247
       
First Author: DDB, FB, MGI, GOA, ZFIN curators
Year: 2001
Title: Gene Ontology annotation through association of InterPro records with GO terms
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Publication
18799693 | J:142754
First Author: Hansen GM
Year: 2008
Journal: Genome Res
Title: Large-scale gene trapping in C57BL/6N mouse embryonic stem cells.
Volume: 18
Issue: 10
Pages: 1670-9
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Publication
- | J:342604
       
First Author: UniProt-GOA
Year: 2012
Title: Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
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Publication
16141072 | J:99680
First Author: Carninci P
Year: 2005
Journal: Science
Title: The transcriptional landscape of the mammalian genome.
Volume: 309
Issue: 5740
Pages: 1559-63
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Publication
11217851 | J:65060
First Author: Kawai J
Year: 2001
Journal: Nature
Title: Functional annotation of a full-length mouse cDNA collection.
Volume: 409
Issue: 6821
Pages: 685-90
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Publication
14610273 | J:86696
First Author: Zambrowicz BP
Year: 2003
Journal: Proc Natl Acad Sci U S A
Title: Wnk1 kinase deficiency lowers blood pressure in mice: a gene-trap screen to identify potential targets for therapeutic intervention.
Volume: 100
Issue: 24
Pages: 14109-14
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Publication
- | J:23000
       
First Author: MGD Nomenclature Committee
Year: 1995
Title: Nomenclature Committee Use
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Publication
- | J:141210
     
First Author: Mouse Genome Informatics (MGI) and National Center for Biotechnology Information (NCBI)
Year: 2008
Journal: Database Download
Title: Mouse Gene Trap Data Load from dbGSS
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Publication
21677750 | J:173534
First Author: Skarnes WC
Year: 2011
Journal: Nature
Title: A conditional knockout resource for the genome-wide study of mouse gene function.
Volume: 474
Issue: 7351
Pages: 337-42
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Publication
- | J:293217
       
First Author: GemPharmatech
Year: 2020
Title: GemPharmatech Website.
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Publication
- | J:342587
       
First Author: AgBase, BHF-UCL, Parkinson's UK-UCL, dictyBase, HGNC, Roslin Institute, FlyBase and UniProtKB curators
Year: 2011
Title: Manual transfer of experimentally-verified manual GO annotation data to orthologs by curator judgment of sequence similarity
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Publication
- | J:68900
     
First Author: The Jackson Laboratory Mouse Radiation Hybrid Database
Year: 2004
Journal: Database Release
Title: Mouse T31 Radiation Hybrid Data Load
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Publication
12466851 | J:80000
First Author: Okazaki Y
Year: 2002
Journal: Nature
Title: Analysis of the mouse transcriptome based on functional annotation of 60,770 full-length cDNAs.
Volume: 420
Issue: 6915
Pages: 563-73
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Publication
- | J:164563
       
First Author: The Gene Ontology Consortium
Year: 2010
Title: Automated transfer of experimentally-verified manual GO annotation data to mouse-human orthologs
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Publication
21267068 | J:153498
First Author: Diez-Roux G
Year: 2011
Journal: PLoS Biol
Title: A high-resolution anatomical atlas of the transcriptome in the mouse embryo.
Volume: 9
Issue: 1
Pages: e1000582
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Publication
- | J:75000
       
First Author: Mouse Genome Informatics Scientific Curators
Year: 2002
Title: Mouse Genome Informatics Computational Sequence to Gene Associations
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Publication
- | J:57747
     
First Author: MGI Genome Annotation Group and UniGene Staff
Year: 2015
Journal: Database Download
Title: MGI-UniGene Interconnection Effort
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Publication
- | J:157972
     
First Author: Mouse Genome Informatics Scientific Curators
Year: 2010
Journal: Database Download
Title: Mouse Microarray Data Integration in Mouse Genome Informatics, the Affymetrix GeneChip Mouse Genome U74 Array Platform (A, B, C v2).
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Publication
- | J:161428
       
First Author: Marc Feuermann, Huaiyu Mi, Pascale Gaudet, Dustin Ebert, Anushya Muruganujan, Paul Thomas
Year: 2010
Title: Annotation inferences using phylogenetic trees
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Publication
- | J:63103
     
First Author: Mouse Genome Database and National Center for Biotechnology Information
Year: 2000
Journal: Database Release
Title: Entrez Gene Load
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Publication
- | J:53168
     
First Author: Bairoch A
Year: 1999
Journal: Database Release
Title: SWISS-PROT Annotated protein sequence database
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Publication
- | J:90438
       
First Author: Mouse Genome Informatics Scientific Curators
Year: 2005
Title: Obtaining and loading genome assembly coordinates from NCBI annotations
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Publication
- | J:85324
     
First Author: Mouse Genome Informatics Group
Year: 2003
Journal: Database Procedure
Title: Automatic Encodes (AutoE) Reference
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Publication
- | J:155721
     
First Author: Mouse Genome Informatics (MGI) and The National Center for Biotechnology Information (NCBI)
Year: 2010
Journal: Database Download
Title: Consensus CDS project
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Publication
- | J:155221
     
First Author: Mouse Genome Informatics
Year: 2010
Journal: Database Release
Title: Protein Ontology Association Load.
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Publication
- | J:91388
       
First Author: Mouse Genome Informatics Scientific Curators
Year: 2005
Title: Obtaining and Loading Genome Assembly Coordinates from Ensembl Annotations
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Publication
- | J:144086
     
First Author: Mouse Genome Informatics Scientific Curators
Year: 2009
Journal: Database Download
Title: Mouse Microarray Data Integration in Mouse Genome Informatics, the Affymetrix GeneChip Mouse Gene 1.0 ST Array Platform
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Publication
- | J:262123
     
First Author: Allen Institute for Brain Science
Year: 2004
Journal: Allen Institute
Title: Allen Brain Atlas: mouse riboprobes
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Publication
- | J:144087
     
First Author: Mouse Genome Informatics Scientific Curators
Year: 2009
Journal: Database Download
Title: Mouse Microarray Data Integration in Mouse Genome Informatics, the Affymetrix GeneChip Mouse Genome 430 2.0 Array Platform
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Protein Domain
IPR019467 | Hat1_N
Type: Domain
Description: This entry represents the N-terminal half of the structure of histone acetyl transferase HAT1. It is often found in association with the C-terminal part of . It seems to be motifs C and D of the structure. Histone acetyltransferases (HATs) catalyse the transfer of an acetyl group from acetyl-CoA to the lysine E-amino groups on the N-terminal tails of histones. HATs are involved in transcription since histones tend to be hyper-acetylated in actively transcribed regions of chromatin, whereas in transcriptionally silent regions histones are hypo-acetylated [].
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Protein
Q8BY71
Organism: Mus musculus/domesticus
Length: 416  
Fragment?: false
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Protein
A2ATU9
Organism: Mus musculus/domesticus
Length: 423  
Fragment?: false
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Publication
9175471 | -
First Author: Neuwald AF
Year: 1997
Journal: Trends Biochem Sci
Title: GCN5-related histone N-acetyltransferases belong to a diverse superfamily that includes the yeast SPT10 protein.
Volume: 22
Issue: 5
Pages: 154-5
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Publication
18601901 | -
First Author: Barman HK
Year: 2008
Journal: Biochem Biophys Res Commun
Title: Histone acetyltransferase-1 regulates integrity of cytosolic histone H3-H4 containing complex.
Volume: 373
Issue: 4
Pages: 624-30
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Publication
18373695 | -
First Author: Poveda A
Year: 2008
Journal: FEBS J
Title: Site specificity of yeast histone acetyltransferase B complex in vivo.
Volume: 275
Issue: 9
Pages: 2122-36
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Publication
17694075 | -
First Author: Parthun MR
Year: 2007
Journal: Oncogene
Title: Hat1: the emerging cellular roles of a type B histone acetyltransferase.
Volume: 26
Issue: 37
Pages: 5319-28
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Publication
12417736 | -
First Author: Qin S
Year: 2002
Journal: Mol Cell Biol
Title: Histone H3 and the histone acetyltransferase Hat1p contribute to DNA double-strand break repair.
Volume: 22
Issue: 23
Pages: 8353-65
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Protein Domain
IPR017380 | Hist_AcTrfase_B-typ_cat-su
Type: Family
Description: This entry represents the catalytic subunit of histone acetyltransferase type B () (also known as HAT1), which is the catalytic component of the histone acetylase B (HAT-B) complex [, , ]. The HAT-B complex is 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.This enzyme acetylates soluble but not nucleosomal H4 at Lys-12, which is required for telomeric silencing. HAT1 has intrinsic substrate specificity that modifies lysine in recognition sequence GXGKXG. It is involved in DNA double-strand break repair [].
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Publication
28143904 | J:259532
 
First Author: Marin TL
Year: 2017
Journal: Sci Signal
Title: AMPK promotes mitochondrial biogenesis and function by phosphorylating the epigenetic factors DNMT1, RBBP7, and HAT1.
Volume: 10
Issue: 464
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Publication
9727486 | -
First Author: Dutnall RN
Year: 1998
Journal: Cell
Title: Structure of the histone acetyltransferase Hat1: a paradigm for the GCN5-related N-acetyltransferase superfamily.
Volume: 94
Issue: 4
Pages: 427-38
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Publication
12801725 | J:84039
First Author: Carrozza MJ
Year: 2003
Journal: Trends Genet
Title: The diverse functions of histone acetyltransferase complexes.
Volume: 19
Issue: 6
Pages: 321-9
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Publication
22615379 | -
First Author: Wu H
Year: 2012
Journal: Proc Natl Acad Sci U S A
Title: Structural basis for substrate specificity and catalysis of human histone acetyltransferase 1.
Volume: 109
Issue: 23
Pages: 8925-30
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Protein Domain
IPR013523 | Hist_AcTrfase_HAT1_C
Type: Homologous_superfamily
Description: Histone acetylation is carried out by a class of enzymes known as histone acetyltransferases (HATs), which catalyse the transfer of an acetyl group from acetyl-CoA to the lysine E-amino groups on the N-terminal tails of histones [, ]. Early indication that HATs were involved in transcription came from the observation that in actively transcribed regions of chromatin, histones tend to be hyperacetylated, whereas in transcriptionally silent regions histones are hypoacetylated. The histone acetyltransferases are divided into five families. These include the Gcn5-related acetyltransferases (GNATs); the MYST (for `MOZ, Ybf2/Sas3, Sas2 and Tip60)-related HATs; p300/CBP HATs; the general transcription factor HATs, which include the TFIID subunit TAF250; and the nuclear hormone-related HATs SRC1 and ACTR (SRC3). The GCN5-related N-acetyltransferase superfamily includes such enzymes as the histone acetyltransferases GCN5 and Hat1, the elongator complex subunit Elp3, the mediator-complex subunit Nut1, and Hpa2 [].Many GNATs share several functional domains, including an N-terminal region of variable length, an acetyltransferase domain that encompasses the conserved sequence motifs described above, a region that interacts with the coactivator Ada2, and a C-terminal bromodomain that is believed to interact with acetyl-lysine residues. Members of the GNAT family are important for the regulation of cell growth and development. In mice, knockouts of Gcn5L are embryonic lethal. Yeast Gcn5 is needed for normal progression through the G2-M boundary and mitotic gene expression. The importance of GNATs is probably related to their role in transcription and DNA repair.The yeast GCN5 (yGCN5) transcriptional coactivator functions as a histone acetyltransferase (HAT) to promote transcriptional activation. The crystal structure of the yeast histone acetyltransferase Hat1-acetyl coenzyme A (AcCoA) shows that Hat1 has an elongated, curved structure, and the AcCoA molecule is bound in a cleft on the concave surface of the protein, marking the active site of the enzyme. A channel of variable width and depth that runs across the protein is probably the binding site for the histone substrate []. The central protein core associated with AcCoA binding that appears to be structurally conserved among a superfamily of N-acetyltransferases, including yeast histone acetyltransferase 1 and Serratia marcescens aminoglycoside 3-N-acetyltransferase [].This entry represents the C-terminal region of histone acetyltransferase type B () (also known as HAT1) from fungi and metazoa, which is required for telomeric silencing and has intrinsic substrate specificity that modifies lysine in recognition sequence GXGKXG. It is also involved in DNA double-strand break repair. The structure from human HAT1 revealed that this domain consists of a bundle of helices with one short β-strand [].
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Protein Domain
IPR006855 | Vertebrate-like_GNAT_dom
Type: Domain
Description: The N-acetyltransferases (NAT) (EC 2.3.1.-) are enzymes that use acetylcoenzyme A (CoA) to transfer an acetyl group to a substrate, a reactionimplicated in various functions from bacterial antibiotic resistance tomammalian circadian rhythm and chromatin remodeling. The Gcn5-relatedN-acetyltransferases (GNAT) catalyze the transfer of the acetyl from the CoAdonor to a primary amine of the acceptor. The GNAT proteins share a domaincomposed of four conserved sequence motifs A-D [, ]. This GNAT domain isnamed after yeast GCN5 (from General Control Nonrepressed) and related histoneacetyltransferases (HATs) like Hat1 and PCAF. HATs acetylate lysine residuesof amino terminal histone tails, resulting in transcription activation.Another category of GNAT, the aminoglycoside N-acetyltransferases, conferantibiotic resistance by catalyzing the acetylation of amino groups inaminoglycoside antibiotics []. GNAT proteins can also have anabolic andcatabolic functions in both prokaryotes and eukaryotes [, , , , ].The acetyltransferase/GNAT domain forms a structurally conserved fold of 6 to7 beta strands (B) and 4 helices (H) in the topologyB1-H1-H2-B2-B3-B4-H3-B5-H4-B6, followed by a C-terminal strand which may befrom the same monomer or contributed by another [, ]. MotifsD (B2-B3), A (B4-H3) and B (B5-H4) are collectively called the HAT core[, , ], while the N-terminal motif C (B1-H1) is less conserved.This entry represents the vertebrate-likeNAGS-type GNAT domain [].
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Protein Domain
IPR031165 | GNAT_YJDJ
Type: Domain
Description: The N-acetyltransferases (NAT) ([intenz:2.3.1.-]) are enzymes that use acetyl coenzyme A (CoA) to transfer an acetyl group to a substrate, a reaction implicated in various functions from bacterial antibiotic resistance to mammalian circadian rhythm and chromatin remodeling. The Gcn5-related N-acetyltransferases (GNAT) catalyse the transfer of the acetyl from the CoA donor to a primary amine of the acceptor. The GNAT proteins share a domain composed of four conserved sequence motifs A-D [, ]. This GNAT domain is named after yeast GCN5 (from General Control Nonrepressed) and related histone acetyltransferases (HATs) like Hat1 and PCAF. HATs acetylate lysine residuesof amino terminal histone tails, resulting in transcription activation. Another category of GNAT, the aminoglycoside N-acetyltransferases, confer antibiotic resistance by catalysing the acetylation of amino groups in aminoglycoside antibiotics []. GNAT proteins can also have anabolic and catabolic functions in both prokaryotes and eukaryotes [, , , , ].The acetyltransferase/GNAT domain forms a structurally conserved fold of 6 to 7 beta strands (B) and 4 helices (H) in the topology B1-H1-H2-B2-B3-B4-H3-B5-H4-B6, followed by a C-terminal strand which may be from the same monomer or contributed by another [, ]. MotifsD (B2-B3), A (B4-H3) and B (B5-H4) are collectively called the HAT core [, , ], while the N-terminal motif C (B1-H1) is less conserved.The entry represents the NAGS-type GNAT domain [, ].
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Publication
10430873 | -
First Author: Trievel RC
Year: 1999
Journal: Proc Natl Acad Sci U S A
Title: Crystal structure and mechanism of histone acetylation of the yeast GCN5 transcriptional coactivator.
Volume: 96
Issue: 16
Pages: 8931-6
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Publication
12527305 | -
First Author: He H
Year: 2003
Journal: J Mol Biol
Title: Crystal structure of tabtoxin resistance protein complexed with acetyl coenzyme A reveals the mechanism for beta-lactam acetylation.
Volume: 325
Issue: 5
Pages: 1019-30
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Publication
12592013 | -
First Author: Burk DL
Year: 2003
Journal: Protein Sci
Title: X-ray structure of the AAC(6')-Ii antibiotic resistance enzyme at 1.8 A resolution; examination of oligomeric arrangements in GNAT superfamily members.
Volume: 12
Issue: 3
Pages: 426-37
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Publication
10940244 | -
 
First Author: Dyda F
Year: 2000
Journal: Annu Rev Biophys Biomol Struct
Title: GCN5-related N-acetyltransferases: a structural overview.
Volume: 29
Pages: 81-103
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Publication
15581578 | -
First Author: Vetting MW
Year: 2005
Journal: Arch Biochem Biophys
Title: Structure and functions of the GNAT superfamily of acetyltransferases.
Volume: 433
Issue: 1
Pages: 212-26
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Publication
18709443 | -
First Author: Cort JR
Year: 2008
Journal: J Struct Funct Genomics
Title: Structure of an acetyl-CoA binding protein from Staphylococcus aureus representing a novel subfamily of GCN5-related N-acetyltransferase-like proteins.
Volume: 9
Issue: 1-4
Pages: 7-20
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Protein Domain
IPR000182 | GNAT_dom
Type: Domain
Description: The N-acetyltransferases (NAT) ([intenz:2.3.1.-]) are enzymes that use acetyl coenzyme A (CoA) to transfer an acetyl group to a substrate, a reaction implicated in various functions from bacterial antibiotic resistance to mammalian circadian rhythm and chromatin remodelling. The Gcn5-related N-acetyltransferases (GNAT) catalyse the transfer of the acetyl from the CoA donor to a primary amine of the acceptor. The GNAT proteins share a domain composed of four conserved sequence motifs A-D [, ]. This GNAT domain is named after yeast GCN5 (from General Control Nonrepressed) and related histone acetyltransferases (HATs) like Hat1 and PCAF. HATs acetylate lysine residues of N-terminal histone tails, resulting in transcription activation. Another category of GNAT, the aminoglycoside N-acetyltransferases, confer antibiotic resistance by catalysing the acetylation of amino groups in aminoglycoside antibiotics []. GNAT proteins can also have anabolic and catabolic functions in both prokaryotes and eukaryotes [, , , , ].The acetyltransferase/GNAT domain forms a structurally conserved fold of 6 to 7 β-strands (B) and 4 helices (H) in the topology B1-H1-H2-B2-B3-B4-H3-B5-H4-B6, followed by a C-terminal strand which may be from the same monomer or contributed by another [, ]. Motifs D (B2-B3), A (B4-H3) and B (B5-H4) are collectively called the HAT core [, , ], while the N-terminal motif C (B1-H1) is less conserved.Some proteins known to contain a GNAT domain:Actinobacterial mycothiol acetyltransferase (MshD), which catalyses the transfer of acetyl from acetyl-CoA to desacetylmycothiol to form mycothiol. Yeast GCN5 and Hat1, which are histone acetyltransferases (EC 2.3.1.48).Human PCAF, a histone acetyltransferase.Mammalian serotonin N-acetyltransferase (SNAT) or arylalkylamine NAT(AANAT), which acetylates serotonin into a circadian neurohormone that mayparticipate in light-dark rhythms, and human mood and behaviour.Mammalian glucosamine 6-phosphate N-acetyltransferase (GNA1) (EC 2.3.1.4).Escherichia coli RimI and RimJ, which acetylate the N-terminal alanine ofribosomal proteins S18 and S5, respectively (EC 2.3.1.128).Mycobacterium tuberculosis aminoglycoside 2'-N-acetyltransferase (Aac),which acetylates the 2' hydroxyl or amino group of a broad spectrum ofaminoglycoside antibiotics.Bacillus subtilis BltD and PaiA, which acetylate spermine and spermidine.This entry represents the entire GNAT domain.
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Protein Domain
IPR007965 | GNAT_ATAT
Type: Domain
Description: The N-acetyltransferases (NAT) (EC 2.3.1.-) are enzymes that use acetylcoenzyme A (CoA) to transfer an acetyl group to a substrate, a reactionimplicated in various functions from bacterial antibiotic resistance tomammalian circadian rhythm and chromatin remodeling. The Gcn5-relatedN-acetyltransferases (GNAT) catalyze the transfer of the acetyl from the CoAdonor to a primary amine of the acceptor. The GNAT proteins share a domaincomposed of four conserved sequence motifs A-D [, ]. This GNAT domain is named after yeast GCN5 (from General Control Nonrepressed) and related histone acetyltransferases (HATs) like Hat1 and PCAF. HATs acetylate lysine residues of amino terminal histone tails, resulting in transcription activation. Another category of GNAT, the aminoglycoside N-acetyltransferases, confer antibiotic resistance by catalyzing the acetylation of amino groups in aminoglycoside antibiotics []. GNAT proteins can also have anabolic and catabolic functions in both prokaryotes and eukaryotes [, , , , ].The acetyltransferase/GNAT domain forms a structurally conserved fold of 6 to7 beta strands (B) and 4 helices (H) in the topologyB1-H1-H2-B2-B3-B4-H3-B5-H4-B6, followed by a C-terminal strand which may befrom the same monomer or contributed by another [, ]. MotifsD (B2-B3), A (B4-H3) and B (B5-H4) are collectively called the HAT core[, , ], while the N-terminal motif C (B1-H1) is less conserved.This entry represents the ATAT-type of the GNAT domain []. Proteins containing this domain include alpha-tubulin N-acetyltransferase, originally known as mechanosensory abnormality protein 17 (Mec-17), as it is the protein product of one of the 18 genes required for the development and function of the touch receptor neuron for gentle touch []. Mec-17 specifically acetylates 'Lys-40' in alpha-tubulin on the lumenal side of microtubules []. It is inefficient, and its activity is enhanced when tubulin is incorporated in microtubules []. It may affect microtubule stability and regulate microtubule dynamics.
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Publication
23894642 | -
First Author: Zhao G
Year: 2013
Journal: PLoS One
Title: Crystal structure of the N-acetyltransferase domain of human N-acetyl-L-glutamate synthase in complex with N-acetyl-L-glutamate provides insights into its catalytic and regulatory mechanisms.
Volume: 8
Issue: 7
Pages: e70369
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Publication
20829795 | J:164738
First Author: Akella JS
Year: 2010
Journal: Nature
Title: MEC-17 is an alpha-tubulin acetyltransferase.
Volume: 467
Issue: 7312
Pages: 218-22
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Protein
Q8K341
Organism: Mus musculus/domesticus
Length: 421  
Fragment?: false
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Protein
F7BUT2
Organism: Mus musculus/domesticus
Length: 131  
Fragment?: true
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Protein
Q9DCR0
Organism: Mus musculus/domesticus
Length: 254  
Fragment?: false
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MouseMine is a collaboration between MGI at The Jackson Laboratory and the InterMine project at the Cambridge Systems Biology Centre. MouseMine is funded through a grant from the NIH/NHGRI.The Jackson Laboratory makes no representation about the suitability or accuracy of this software or data for any purpose, and makes no warranties, either express or implied, including merchantability and fitness for a particular purpose or that the use of this software or data will not infringe any third party patents, copyrights, trademarks, or other rights. the software and data are provided "as is". This software and data are provided to enhance knowledge and encourage progress in the scientific community and are to be used only for research and educational purposes. Any reproduction or use for commercial purpose is prohibited without the prior express written permission of the Jackson Laboratory.

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