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Protein

Histone acetyltransferase of the MYST family 1

Gene

HAM1

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Histone acetyltransferase which may be involved in transcriptional activation. Acetylates 'Lys-5' of histone H4 (H4K5ac) (PubMed:17877703, PubMed:19040736, PubMed:22170978, PubMed:23273925). Essential for gametophyte development (PubMed:19040736). Involved in DNA repair after UV-B exposure (PubMed:22170978). Negative regulator of flowering controlling the H4K5ac levels in the FLC chromatin (PubMed:23273925).4 Publications

Catalytic activityi

Acetyl-CoA + [histone] = CoA + acetyl-[histone].By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei345 – 3451Proton donor/acceptorBy similarity
Binding sitei349 – 3491Acetyl-CoABy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri203 – 22523C2HC-typeAdd
BLAST

GO - Molecular functioni

  1. histone acetyltransferase activity Source: TAIR
  2. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. DNA repair Source: TAIR
  2. histone acetylation Source: GOC
  3. regulation of transcription, DNA-templated Source: UniProtKB-KW
  4. response to UV-B Source: TAIR
  5. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Activator, Acyltransferase, Chromatin regulator, Transferase

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BioCyciARA:AT5G64610-MONOMER.
BRENDAi2.3.1.48. 399.

Names & Taxonomyi

Protein namesi
Recommended name:
Histone acetyltransferase of the MYST family 11 Publication (EC:2.3.1.48UniRule annotation)
Alternative name(s):
Histone acetyltransferase of the GNAT/MYST superfamily 41 Publication
MYST-like histone acetyltransferase 11 Publication
Gene namesi
Name:HAM11 Publication
Synonyms:HAG41 Publication
Ordered Locus Names:At5g64610Imported
ORF Names:MUB3.13Imported
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548 Componenti: Chromosome 5

Organism-specific databases

TAIRiAT5G64610.

Subcellular locationi

  1. Nucleus 1 Publication

GO - Cellular componenti

  1. nucleus Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Disruption phenotypei

No visible phenotype, due to the redundancy with HAM2. Ham1 and ham2 double mutants are lethal.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 445445Histone acetyltransferase of the MYST family 1PRO_0000238464Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei269 – 2691N6-acetyllysine; by autocatalysisBy similarity

Post-translational modificationi

Autoacetylation at Lys-269 is required for proper function.By similarity

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiQ9FLF7.
PRIDEiQ9FLF7.

Expressioni

Tissue specificityi

Expressed in cotyledons, leaves, stems, roots and, at higher levels in developing flowers, particularly in the anthers and gynoecia (PubMed:19040736). Constitutively expressed in all tissues, predominantly in shoot apical meristem (PubMed:23273925).2 Publications

Inductioni

Up-regulated upon UV-B exposure.1 Publication

Gene expression databases

ExpressionAtlasiQ9FLF7. baseline and differential.
GenevestigatoriQ9FLF7.

Interactioni

Subunit structurei

Interacts with MRG1 and MRG2 (PubMed:25183522). Component of the NuA4 histone acetyltransferase complex (Ref. 11).2 Publications

Protein-protein interaction databases

BioGridi21824. 1 interaction.
IntActiQ9FLF7. 1 interaction.

Structurei

3D structure databases

ProteinModelPortaliQ9FLF7.
SMRiQ9FLF7. Positions 172-440.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini74 – 13360ChromoAdd
BLAST
Domaini169 – 440272MYST-type HATAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni312 – 3143Acetyl-CoA bindingBy similarity
Regioni319 – 3257Acetyl-CoA bindingBy similarity

Sequence similaritiesi

Belongs to the MYST (SAS/MOZ) family.Curated
Contains 1 C2HC-type zinc finger.Curated
Contains 1 chromo domain.Curated

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri203 – 22523C2HC-typeAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiCOG5027.
HOGENOMiHOG000182457.
InParanoidiQ9FLF7.
KOiK11308.
OMAiEYNDSPK.
PhylomeDBiQ9FLF7.

Family and domain databases

Gene3Di3.40.630.30. 1 hit.
InterProiIPR016181. Acyl_CoA_acyltransferase.
IPR000953. Chromo/shadow_dom.
IPR016197. Chromodomain-like.
IPR002717. MOZ_SAS.
IPR025995. Tudor-knot.
IPR015880. Znf_C2H2-like.
[Graphical view]
PfamiPF01853. MOZ_SAS. 1 hit.
PF11717. Tudor-knot. 1 hit.
[Graphical view]
SMARTiSM00298. CHROMO. 1 hit.
SM00355. ZnF_C2H2. 1 hit.
[Graphical view]
SUPFAMiSSF54160. SSF54160. 1 hit.
SSF55729. SSF55729. 1 hit.
PROSITEiPS51726. MYST_HAT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9FLF7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGSSADTETA MIIATPASNH NNPATNGGDA NQNHTSGAIL ALTNSESDAS
60 70 80 90 100
KKRRMGVLPL EVGTRVMCQW RDGKYHPVKV IERRKNYNGG HNDYEYYVHY
110 120 130 140 150
TEFNRRLDEW IKLEQLDLDS VECALDEKVE DKVTSLKMTR HQKRKIDETH
160 170 180 190 200
VEGHEELDAA SLREHEEFTK VKNIATIELG KYEIETWYFS PFPPEYNDCV
210 220 230 240 250
KLFFCEFCLS FMKRKEQLQR HMRKCDLKHP PGDEIYRSST LSMFEVDGKK
260 270 280 290 300
NKVYAQNLCY LAKLFLDHKT LYYDVDLFLF YILCECDDRG CHMVGYFSKE
310 320 330 340 350
KHSEEAYNLA CILTLPPYQR KGYGKFLIAF SYELSKKEGK VGTPERPLSD
360 370 380 390 400
LGLVSYRGYW TRILLDILKK HKGNISIKEL SDMTAIKAED ILSTLQSLEL
410 420 430 440
IQYRKGQHVI CADPKVLDRH LKAAGRGGLD VDVSKMIWTP YKEQS
Length:445
Mass (Da):51,438
Last modified:March 1, 2001 - v1
Checksum:iF2243F5808ADE207
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB010076 Genomic DNA. Translation: BAB11428.1.
CP002688 Genomic DNA. Translation: AED97926.1.
AY099684 mRNA. Translation: AAM20535.1.
BT000277 mRNA. Translation: AAN15596.1.
AB493812 mRNA. Translation: BAH30650.1.
RefSeqiNP_201266.1. NM_125857.2.
UniGeneiAt.28949.
At.49220.

Genome annotation databases

EnsemblPlantsiAT5G64610.1; AT5G64610.1; AT5G64610.
GeneIDi836582.
KEGGiath:AT5G64610.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB010076 Genomic DNA. Translation: BAB11428.1.
CP002688 Genomic DNA. Translation: AED97926.1.
AY099684 mRNA. Translation: AAM20535.1.
BT000277 mRNA. Translation: AAN15596.1.
AB493812 mRNA. Translation: BAH30650.1.
RefSeqiNP_201266.1. NM_125857.2.
UniGeneiAt.28949.
At.49220.

3D structure databases

ProteinModelPortaliQ9FLF7.
SMRiQ9FLF7. Positions 172-440.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi21824. 1 interaction.
IntActiQ9FLF7. 1 interaction.

Proteomic databases

PaxDbiQ9FLF7.
PRIDEiQ9FLF7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT5G64610.1; AT5G64610.1; AT5G64610.
GeneIDi836582.
KEGGiath:AT5G64610.

Organism-specific databases

TAIRiAT5G64610.

Phylogenomic databases

eggNOGiCOG5027.
HOGENOMiHOG000182457.
InParanoidiQ9FLF7.
KOiK11308.
OMAiEYNDSPK.
PhylomeDBiQ9FLF7.

Enzyme and pathway databases

BioCyciARA:AT5G64610-MONOMER.
BRENDAi2.3.1.48. 399.

Miscellaneous databases

PROiQ9FLF7.

Gene expression databases

ExpressionAtlasiQ9FLF7. baseline and differential.
GenevestigatoriQ9FLF7.

Family and domain databases

Gene3Di3.40.630.30. 1 hit.
InterProiIPR016181. Acyl_CoA_acyltransferase.
IPR000953. Chromo/shadow_dom.
IPR016197. Chromodomain-like.
IPR002717. MOZ_SAS.
IPR025995. Tudor-knot.
IPR015880. Znf_C2H2-like.
[Graphical view]
PfamiPF01853. MOZ_SAS. 1 hit.
PF11717. Tudor-knot. 1 hit.
[Graphical view]
SMARTiSM00298. CHROMO. 1 hit.
SM00355. ZnF_C2H2. 1 hit.
[Graphical view]
SUPFAMiSSF54160. SSF54160. 1 hit.
SSF55729. SSF55729. 1 hit.
PROSITEiPS51726. MYST_HAT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Structural analysis of Arabidopsis thaliana chromosome 5. IV. Sequence features of the regions of 1,456,315 bp covered by nineteen physically assigned P1 and TAC clones."
    Sato S., Kaneko T., Kotani H., Nakamura Y., Asamizu E., Miyajima N., Tabata S.
    DNA Res. 5:41-54(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  2. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  3. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
    Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.
    , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
    Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  4. "ORF cloning and analysis of Arabidopsis transcription factor genes."
    Fujita M., Mizukado S., Seki M., Shinozaki K., Mitsuda N., Takiguchi Y., Takagi M.
    Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  5. "Analysis of histone acetyltransferase and histone deacetylase families of Arabidopsis thaliana suggests functional diversification of chromatin modification among multicellular eukaryotes."
    Pandey R., Mueller A., Napoli C.A., Selinger D.A., Pikaard C.S., Richards E.J., Bender J., Mount D.W., Jorgensen R.A.
    Nucleic Acids Res. 30:5036-5055(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION, NOMENCLATURE.
  6. "In vitro specificities of Arabidopsis co-activator histone acetyltransferases: implications for histone hyperacetylation in gene activation."
    Earley K.W., Shook M.S., Brower-Toland B., Hicks L., Pikaard C.S.
    Plant J. 52:615-626(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  7. "The MYST histone acetyltransferases are essential for gametophyte development in Arabidopsis."
    Latrasse D., Benhamed M., Henry Y., Domenichini S., Kim W., Zhou D.X., Delarue M.
    BMC Plant Biol. 8:121-121(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY.
  8. "Participation of chromatin-remodeling proteins in the repair of ultraviolet-B-damaged DNA."
    Campi M., D'Andrea L., Emiliani J., Casati P.
    Plant Physiol. 158:981-995(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INDUCTION BY UV.
  9. "Requirement of histone acetyltransferases HAM1 and HAM2 for epigenetic modification of FLC in regulating flowering in Arabidopsis."
    Xiao J., Zhang H., Xing L., Xu S., Liu H., Chong K., Xu Y.
    J. Plant Physiol. 170:444-451(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY.
  10. "Arabidopsis MRG domain proteins bridge two histone modifications to elevate expression of flowering genes."
    Xu Y., Gan E.S., Zhou J., Wee W.Y., Zhang X., Ito T.
    Nucleic Acids Res. 42:10960-10974(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MRG1 AND MRG2.
    Strain: cv. Columbia.
  11. "AtEAF1 is a potential platform protein for Arabidopsis NuA4 acetyltransferase complex."
    Bieluszewski T., Galganski L., Sura W., Bieluszewska A., Abram M., Ludwikow A., Ziolkowski P., Sadowski J.
    BMC Plant Biol. 15:0-0(2015)
    Cited for: IDENTIFICATION IN THE NUA4 COMPLEX.

Entry informationi

Entry nameiMYST1_ARATH
AccessioniPrimary (citable) accession number: Q9FLF7
Secondary accession number(s): C0SVV9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2006
Last sequence update: March 1, 2001
Last modified: April 29, 2015
This is version 104 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Miscellaneous

Knockdown expression of both HAM1 and HAM2 results in earlier flowering.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.