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Q9LXD7 (MYST2_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 98. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
MYST-like histone acetyltransferase 2

EC=2.3.1.48
Gene names
Name:HAG5
Ordered Locus Names:At5g09740
ORF Names:F17I14.70
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length445 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Histone acetyltransferase which may be involved in transcriptional activation. Acetylates 'Lys-5' of histone H4. Ref.6

Catalytic activity

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

Subcellular location

Nucleus Probable.

Post-translational modification

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

Sequence similarities

Belongs to the MYST (SAS/MOZ) family.

Contains 1 C2HC-type zinc finger.

Contains 1 chromo domain.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9LXD7-1)

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 2 (identifier: Q9LXD7-2)

The sequence of this isoform differs from the canonical sequence as follows:
     135-135: S → N
     172-249: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 445445MYST-like histone acetyltransferase 2
PRO_0000238465

Regions

Domain74 – 13360Chromo
Zinc finger203 – 22523C2HC-type
Region319 – 3257Acetyl-CoA binding By similarity
Compositional bias14 – 4027Pro-rich

Sites

Active site2691 By similarity
Active site3111Nucleophile By similarity
Binding site3141Acetyl-CoA By similarity
Binding site3491Acetyl-CoA By similarity

Amino acid modifications

Modified residue2691N6-acetyllysine; by autocatalysis By similarity

Natural variations

Alternative sequence1351S → N in isoform 2.
VSP_018609
Alternative sequence172 – 24978Missing in isoform 2.
VSP_018610

Experimental info

Sequence conflict1291V → L in AAM63720. Ref.5

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 3BA39F07E2E47C33

FASTA44551,367
        10         20         30         40         50         60 
MGSSANTETN GNAPPPSSNQ KPPATNGVDG SHPPPPPLTP DQAIIESDPS KKRKMGMLPL 

        70         80         90        100        110        120 
EVGTRVMCRW RDGKHHPVKV IERRRIHNGG QNDYEYYVHY TEFNRRLDEW TQLDQLDLDS 

       130        140        150        160        170        180 
VECAVDEKVE DKVTSLKMTR HQKRKIDETH IEGHEELDAA SLREHEEFTK VKNISTIELG 

       190        200        210        220        230        240 
KYEIETWYFS PFPPEYNDCV KLFFCEFCLN FMKRKEQLQR HMRKCDLKHP PGDEIYRSGT 

       250        260        270        280        290        300 
LSMFEVDGKK NKVYAQNLCY LAKLFLDHKT LYYDVDLFLF YVLCECDDRG CHMVGYFSKE 

       310        320        330        340        350        360 
KHSEEAYNLA CILTLPSYQR KGYGKFLIAF SYELSKKEGK VGTPERPLSD LGLLSYRGYW 

       370        380        390        400        410        420 
TRVLLEILKK HKGNISIKEL SDVTAIKAED ILSTLQSLEL IQYRKGQHVI CADPKVLDRH 

       430        440 
LKAAGRGGLD VDASKLIWTP YKDQS 

« Hide

Isoform 2 [UniParc].

Checksum: 74D19D94047E699D
Show »

FASTA36742,007

References

« Hide 'large scale' references
[1]"Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana."
Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E., Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K. expand/collapse author list , Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L., O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D., Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M., Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L., Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B., Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P., Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M., Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D., Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A., Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I., Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T., Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A., McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U., Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G., Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W., Bevan M., Fransz P.F.
Nature 408:823-826(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[2]"Structural analysis of Arabidopsis thaliana chromosome 5. IX. Sequence features of the regions of 1,011,550 bp covered by seventeen P1 and TAC clones."
Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Kotani H., Miyajima N., Tabata S.
DNA Res. 6:183-195(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[3]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[4]"Functional annotation of a full-length Arabidopsis cDNA collection."
Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T., Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y., Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K., Shinagawa A., Shinozaki K.
Science 296:141-145(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Strain: cv. Columbia.
[5]"Full-length cDNA from Arabidopsis thaliana."
Brover V., Troukhan M., Alexandrov N., Lu Y.-P., Flavell R., Feldmann K.A.
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[6]"Erasure of histone acetylation by Arabidopsis HDA6 mediates large-scale gene silencing in nucleolar dominance."
Earley K., Lawrence R.J., Pontes O., Reuther R., Enciso A.J., Silva M., Neves N., Gross M., Viegas W., Pikaard C.S.
Genes Dev. 20:1283-1293(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[7]"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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL353994 Genomic DNA. Translation: CAB89356.1.
AB020752 Genomic DNA. Translation: BAB09532.1.
CP002688 Genomic DNA. Translation: AED91440.1.
AK117126 mRNA. Translation: BAC41804.1.
AY086663 mRNA. Translation: AAM63720.1.
PIRT49924.
RefSeqNP_196536.1. NM_121011.3. [Q9LXD7-1]
UniGeneAt.32464.

3D structure databases

ProteinModelPortalQ9LXD7.
SMRQ9LXD7. Positions 172-440.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid16112. 1 interaction.

Proteomic databases

PRIDEQ9LXD7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT5G09740.1; AT5G09740.1; AT5G09740. [Q9LXD7-1]
GeneID830834.
KEGGath:AT5G09740.

Organism-specific databases

TAIRAT5G09740.

Phylogenomic databases

eggNOGCOG5027.
HOGENOMHOG000182457.
InParanoidQ9LXD7.
KOK11308.
OMAPPEYNDS.
PhylomeDBQ9LXD7.

Enzyme and pathway databases

BioCycARA:AT5G09740-MONOMER.

Gene expression databases

GenevestigatorQ9LXD7.

Family and domain databases

Gene3D3.40.630.30. 1 hit.
InterProIPR016181. Acyl_CoA_acyltransferase.
IPR000953. Chromo_domain/shadow.
IPR016197. Chromodomain-like.
IPR002717. MOZ_SAS.
IPR025995. Tudor-knot.
IPR015880. Znf_C2H2-like.
[Graphical view]
PfamPF01853. MOZ_SAS. 1 hit.
PF11717. Tudor-knot. 1 hit.
[Graphical view]
SMARTSM00298. CHROMO. 1 hit.
SM00355. ZnF_C2H2. 1 hit.
[Graphical view]
SUPFAMSSF54160. SSF54160. 1 hit.
SSF55729. SSF55729. 1 hit.
ProtoNetSearch...

Entry information

Entry nameMYST2_ARATH
AccessionPrimary (citable) accession number: Q9LXD7
Secondary accession number(s): Q8GZ97, Q8LCD4
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2006
Last sequence update: October 1, 2000
Last modified: June 11, 2014
This is version 98 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names