P59226 (H32_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Histone H3.2

Alternative name(s):
Histone H3.1

Gene names

Name:	HTR2
Ordered Locus Names:	At1g09200
ORF Names:	T12M4.9
AND
Name:	HTR3
Ordered Locus Names:	At3g27360
ORF Names:	K1G2.8
AND
Name:	HTR13
Ordered Locus Names:	At5g10390
ORF Names:	F12B17_260
AND
Name:	HTR9
Ordered Locus Names:	At5g10400
ORF Names:	F12B17_250
AND
Name:	HTR1
Ordered Locus Names:	At5g65360
ORF Names:	MNA5.9

Organism

Arabidopsis thaliana (Mouse-ear cress) [Reference proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Viridiplantae › Streptophyta › Streptophytina › Embryophyta › Tracheophyta › Euphyllophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length	136 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.
Subunit structure	The nucleosome is a histone octamer containing two molecules each of H2A, H2B, H3 and H4 assembled in one H3-H4 heterotetramer and two H2A-H2B heterodimers. The octamer wraps approximately 147 bp of DNA. The H3K9meK27me dimethylated N-terminal tail of histone H3 can directly interact with the chromodomains of CMT3 and/or LHP1. Interacts with ORTH2. Ref.12 Ref.17 Ref.29
Subcellular location	Nucleus. Chromosome Ref.30.
Tissue specificity	Expressed in inflorescences, buds and seedlings. Ref.24
Developmental stage	Expressed during the S phase. Ref.14
Post-translational modification	Can be acetylated to form H3K9ac, H3K14ac, H3K18ac and H3K23ac. H3K9ac could compete with H3K9me and prevent gene silencing. H3K9acK14ac molecules are 30-fold less abundant than H3K9ac or H3K14ac. Very low level of H3K9meK14ac. H3K14 is specifically acetylated by HAG1 and deacetylated by HDA6. H3K9ac is deacetylated by HDT1. H3K9ac is restricted to euchromatin. H3K18ac, but not H3K9ac, is cell-cycle dependent and linked to replication. Reduced H4R3me2s increases H3K14ac in the FLC chromatin and activates or maintains its transcription. Vernalization decreases H3K9/14ac in the promoter region of FLC. Mono-, di- or trimethylated to form mainly H3K4me1/2/3, H3K9me1/2/3, H3K27me1/2/3 and H3K36me1/2/3. Very low monomethylation at H3K18me1 or H3K23me1. H3K4me1/2/3, H3K9me3, H3K27me3 and H3K36me1/2/3 are typical marks for euchromatin, whereas heterochromatic chromocenters are enriched in H3K9me1/2 and H3K27me1/2. H3K27me3 is largely restricted to the transcribed regions of single genes and not associated with low-nucleosome density regions. SUVR1 to SUVR5, ASHH1 to ASHH3 and ASHR1 to ASHR3 methylate H3, with ASHH2 methylating specifically H3K4 and H3K36. The Su(var)3-9 homolog proteins (SUVH1 to SUVH10) are H3K9-specific methyltransferases. Among them, KRYPTONITE (SUVH4) is only involved in di- or trimethylation. Regarding H3K9, the major forms are H3K9me1 (20%) and H3K9me2 (10%), while H3K9me3 is rare (0.2%). H3K9me is controlled by DNA methylation and is not required for the formation of constitutive heterochromatin, but double methylation H3K9meK27me is required for the recruitment of CMT3 to methylate heterochromatin and silence euchromatic loci. Very low level of H3K9meK14ac. 60% of H3K27 is found under the form of H3K27me1, 16% of H3K27me2 and 5% of H3K27me3. When associated with H3K27me, H3K36 can only be mono- or di-methylated. H327me2K36me1 or H3K27me1K36me2 are both found in 3% of the proteins. When not associated with H3K27me, H3K36 is only trimethylated. H3K36me3 is found in 3% of the proteins. H2BK143ub1 is probably prerequisite for H3K4me. Elevated H3K4me3 and H3K36me2 formed by ASHH2 are required for high FLC expression. Vernalization increases H3K9me2 and H3K27me2/3 and decreases H3K4me2 at the FLC locus, resulting in the epigenetic silencing of this floral repressor. Ref.11 Ref.13 Ref.16 Ref.19 Ref.20 Ref.21 Ref.22 Ref.27 Ref.30 In meta- and anaphase, H3T11ph is found on the entire length of the condensed chromosomes, whereas H3S10ph and H3S28ph are confined to the pericentromeric regions. During the first meiotic division, H3S10ph and H3S28ph are found on the entire length of the chromosome. Both sites may be involved in sister chromatid cohesion. No phosphorylation detected during interphase. AUR1 and AUR2 phosphorylate only H3S10, while AUR3 phosphorylates both H3S10 and H3S28.
Sequence similarities	Belongs to the histone H3 family.
Caution	To ensure consistency between histone entries, we follow the 'Brno' nomenclature for histone modifications, with positions referring to those used in the literature for the 'closest' model organism. Due to slight variations in histone sequences between organisms and to the presence of initiator methionine in UniProtKB/Swiss-Prot sequences, the actual positions of modified amino acids in the sequence generally differ. In this entry the following conventions are used: H3K4me1/2/3 = mono-, di- and trimethylated Lys-5; H3K9me1/2/3 = mono-, di- and trimethylated Lys-10; H3K9ac = acetylated Lys-10; H3S10ph = phosphorylated Ser-11; H3T11ph = phosphorylated Thr-12; H3K14ac = acetylated Lys-15; H3K18ac = acetylated Lys-19; H3K18me1 = monomethylated Lys-19; H3K23ac = acetylated Lys-24; H3K23me1 = monomethylated Lys-24; H3K27me1/2/3 = mono-, di- and trimethylated Lys-28; H3S28ph = phosphorylated Ser-29; H3K36me1/2/3 = mono-, di- and trimethylated Lys-37.

Ontologies

Keywords
Cellular component	Chromosome Nucleosome core Nucleus
Ligand	DNA-binding
PTM	Acetylation Methylation Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	nucleosome assembly Inferred from electronic annotation. Source: InterPro
Cellular_component	nucleosome Inferred from electronic annotation. Source: UniProtKB-KW nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	DNA binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 136	135	Histone H3.2		PRO_0000221267
Sites
	Site	15	1	Not N6-methylated
	Site	28	1	Not N6-acetylated
	Site	37	1	Not N6-acetylated
Amino acid modifications
	Modified residue	5	1	N6,N6,N6-trimethyllysine; alternate Ref.13 Ref.19 Ref.20 Ref.21
	Modified residue	5	1	N6,N6-dimethyllysine; alternate Ref.13 Ref.19 Ref.20 Ref.21
	Modified residue	5	1	N6-methyllysine; alternate Ref.13 Ref.19 Ref.20 Ref.21
	Modified residue	10	1	N6,N6,N6-trimethyllysine; alternate Ref.11 Ref.13 Ref.16 Ref.19 Ref.20
	Modified residue	10	1	N6,N6-dimethyllysine; alternate Ref.11 Ref.13 Ref.16 Ref.19 Ref.20
	Modified residue	10	1	N6-acetyllysine; alternate Ref.13 Ref.19
	Modified residue	10	1	N6-methyllysine; alternate Ref.11 Ref.13 Ref.16 Ref.19 Ref.20
	Modified residue	11	1	Phosphoserine Ref.15 Ref.23
	Modified residue	12	1	Phosphothreonine Ref.23
	Modified residue	15	1	N6-acetyllysine Ref.19 Ref.25 Ref.28
	Modified residue	19	1	N6-acetyllysine; alternate Ref.13 Ref.19
	Modified residue	19	1	N6-methyllysine; alternate Ref.19
	Modified residue	24	1	N6-acetyllysine; alternate Ref.19
	Modified residue	24	1	N6-methyllysine; alternate Ref.19
	Modified residue	28	1	N6,N6,N6-trimethyllysine; alternate Ref.19 Ref.20 Ref.27 Ref.30
	Modified residue	28	1	N6,N6-dimethyllysine; alternate Ref.19 Ref.20 Ref.27 Ref.30
	Modified residue	28	1	N6-methyllysine; alternate Ref.19 Ref.20 Ref.27 Ref.30
	Modified residue	29	1	Phosphoserine Ref.15 Ref.23
	Modified residue	37	1	N6,N6,N6-trimethyllysine; alternate Ref.19 Ref.22
	Modified residue	37	1	N6,N6-dimethyllysine; alternate Ref.19 Ref.22
	Modified residue	37	1	N6-methyllysine; alternate Ref.19 Ref.22

Sequences

	Sequence		Length	Mass (Da)
	P59226 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: F1FB03A849777A61	FASTA	136	15,268
	10 20 30 40 50 60 MARTKQTARK STGGKAPRKQ LATKAARKSA PATGGVKKPH RFRPGTVALR EIRKYQKSTE 70 80 90 100 110 120 LLIRKLPFQR LVREIAQDFK TDLRFQSSAV AALQEAAEAY LVGLFEDTNL CAIHAKRVTI 130 MPKDIQLARR IRGERA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Histone genes in higher plants: organization and expression." Chaubet N., Chaboute M.-E., Philipps G., Gigot C. Dev. Genet. 8:461-473(1987) Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (AT1G09200).
[2]	"Genomic organization and nucleotide sequences of two histone H3 and two histone H4 genes of Arabidopsis thaliana." Chaboute M.-E., Chaubet N., Philipps G., Ehling M., Gigot C. Plant Mol. Biol. 8:179-191(1987) Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (AT1G09200 AND AT5G65360).
[3]	"Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana." Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K. , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W. Nature 408:816-820(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (AT1G09200). Strain: cv. Columbia.
[4]	"Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence features of the regions of 4,504,864 bp covered by sixty P1 and TAC clones." Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S. DNA Res. 7:131-135(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (AT3G27360). Strain: cv. Columbia.
[5]	"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. , 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] (AT5G10390 AND AT5G10400). Strain: cv. Columbia.
[6]	"Structural analysis of Arabidopsis thaliana chromosome 5. V. Sequence features of the regions of 1,381,565 bp covered by twenty one physically assigned P1 and TAC clones." Kaneko T., Kotani H., Nakamura Y., Sato S., Asamizu E., Miyajima N., Tabata S. DNA Res. 5:131-145(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (AT5G65360). Strain: cv. Columbia.
[7]	The Arabidopsis Information Resource (TAIR) Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: cv. Columbia.
[8]	"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] (AT5G65360). Strain: cv. Columbia.
[9]	"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] (AT1G09200; AT3G27360; AT5G10390; AT5G10400 AND AT5G65360). Strain: cv. Columbia.
[10]	"Full-length cDNA from Arabidopsis thaliana." Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A. Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[11]	"DNA methylation controls histone H3 lysine 9 methylation and heterochromatin assembly in Arabidopsis." Soppe W.J.J., Jasencakova Z., Houben A., Kakutani T., Meister A., Huang M.S., Jacobsen S.E., Schubert I., Fransz P.F. EMBO J. 21:6549-6559(2002) [PubMed] [Europe PMC] [Abstract] Cited for: METHYLATION AT LYS-10.
[12]	"Control of CpNpG DNA methylation by the KRYPTONITE histone H3 methyltransferase." Jackson J.P., Lindroth A.M., Cao X., Jacobsen S.E. Nature 416:556-560(2002) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH LHP1.
[13]	"Histone modifications in Arabidopsis -- high methylation of H3 lysine 9 is dispensable for constitutive heterochromatin." Jasencakova Z., Soppe W.J.J., Meister A., Gernand D., Turner B.M., Schubert I. Plant J. 33:471-480(2003) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION AT LYS-10 AND LYS-19, METHYLATION AT LYS-5 AND LYS-10.
[14]	"Genome-wide gene expression in an Arabidopsis cell suspension." Menges M., Hennig L., Gruissem W., Murray J.A.H. Plant Mol. Biol. 53:423-442(2003) [PubMed] [Europe PMC] [Abstract] Cited for: DEVELOPMENTAL STAGE.
[15]	"The temporal and spatial pattern of histone H3 phosphorylation at serine 28 and serine 10 is similar in plants but differs between mono- and polycentric chromosomes." Gernand D., Demidov D., Houben A. Cytogenet. Genome Res. 101:172-176(2003) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT SER-11 AND SER-29.
[16]	"Dimethylation of histone H3 lysine 9 is a critical mark for DNA methylation and gene silencing in Arabidopsis thaliana." Jackson J.P., Johnson L., Jasencakova Z., Zhang X., PerezBurgos L., Singh P.B., Cheng X., Schubert I., Jenuwein T., Jacobsen S.E. Chromosoma 112:308-315(2004) [PubMed] [Europe PMC] [Abstract] Cited for: METHYLATION AT LYS-10.
[17]	"Dual histone H3 methylation marks at lysines 9 and 27 required for interaction with CHROMOMETHYLASE3." Lindroth A.M., Shultis D., Jasencakova Z., Fuchs J., Johnson L., Schubert D., Patnaik D., Pradhan S., Goodrich J., Schubert I., Jenuwein T., Khorasanizadeh S., Jacobsen S.E. EMBO J. 23:4286-4296(2004) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH CMT3.
[18]	"A concerted DNA methylation/histone methylation switch regulates rRNA gene dosage control and nucleolar dominance." Lawrence R.J., Earley K., Pontes O., Silva M., Chen Z.J., Neves N., Viegas W., Pikaard C.S. Mol. Cell 13:599-609(2004) [PubMed] [Europe PMC] [Abstract] Cited for: DEACETYLATION BY HDT1.
[19]	"Mass spectrometry analysis of Arabidopsis histone H3 reveals distinct combinations of post-translational modifications." Johnson L., Mollah S., Garcia B.A., Muratore T.L., Shabanowitz J., Hunt D.F., Jacobsen S.E. Nucleic Acids Res. 32:6511-6518(2004) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION AT LYS-10; LYS-15; LYS-19 AND LYS-24, ABSENCE OF ACETYLATION AT LYS-28 AND LYS-37, METHYLATION AT LYS-5; LYS-10; LYS-19; LYS-24; LYS-28 AND LYS-37, ABSENCE OF METHYLATION AT LYS-15, MASS SPECTROMETRY.
[20]	"Vernalization requires epigenetic silencing of FLC by histone methylation." Bastow R., Mylne J.S., Lister C., Lippman Z., Martienssen R.A., Dean C. Nature 427:164-167(2004) [PubMed] [Europe PMC] [Abstract] Cited for: METHYLATION AT LYS-5; LYS-10 AND LYS-28.
[21]	"Establishment of the vernalization-responsive, winter-annual habit in Arabidopsis requires a putative histone H3 methyl transferase." Kim S.Y., He Y., Jacob Y., Noh Y.-S., Michaels S., Amasino R. Plant Cell 17:3301-3310(2005) [PubMed] [Europe PMC] [Abstract] Cited for: METHYLATION AT LYS-5.
[22]	"Prevention of early flowering by expression of FLOWERING LOCUS C requires methylation of histone H3 K36." Zhao Z., Yu Y., Meyer D., Wu C., Shen W.-H. Nat. Cell Biol. 7:1256-1260(2005) [PubMed] [Europe PMC] [Abstract] Cited for: METHYLATION AT LYS-37.
[23]	"Novel phosphorylation of histone H3 at threonine 11 that temporally correlates with condensation of mitotic and meiotic chromosomes in plant cells." Houben A., Demidov D., Rutten T., Scheidtmann K.H. Cytogenet. Genome Res. 109:148-155(2005) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT SER-11; THR-12 AND SER-29.
[24]	"Analysis of the histone H3 gene family in Arabidopsis and identification of the male-gamete-specific variant AtMGH3." Okada T., Endo M., Singh M.B., Bhalla P.L. Plant J. 44:557-568(2005) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION, TISSUE SPECIFICITY.
[25]	"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: ACETYLATION AT LYS-15 BY HAG1, DEACETYLATION BY HDA6.
[26]	"Chromosomal histone modification patterns -- from conservation to diversity." Fuchs J., Demidov D., Houben A., Schubert I. Trends Plant Sci. 11:199-208(2006) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW.
[27]	"The PHD finger protein VRN5 functions in the epigenetic silencing of Arabidopsis FLC." Greb T., Mylne J.S., Crevillen P., Geraldo N., An H., Gendall A.R., Dean C. Curr. Biol. 17:73-78(2007) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION, METHYLATION AT LYS-28.
[28]	"SKB1-mediated symmetric dimethylation of histone H4R3 controls flowering time in Arabidopsis." Wang X., Zhang Y., Ma Q., Zhang Z., Xue Y., Bao S., Chong K. EMBO J. 26:1934-1941(2007) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION AT LYS-15.
[29]	"VIM1, a methylcytosine-binding protein required for centromeric heterochromatinization." Woo H.R., Pontes O., Pikaard C.S., Richards E.J. Genes Dev. 21:267-277(2007) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH ORTH2.
[30]	"Whole-genome analysis of histone H3 lysine 27 trimethylation in Arabidopsis." Zhang X., Clarenz O., Cokus S., Bernatavichute Y.V., Pellegrini M., Goodrich J., Jacobsen S.E. PLoS Biol. 5:1026-1035(2007) [PubMed] [Europe PMC] [Abstract] Cited for: METHYLATION AT LYS-28, SUBCELLULAR LOCATION.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M35387 Genomic DNA. Translation: AAA79889.1.
M17131 Genomic DNA. Translation: AAA32809.1.
M17130 Genomic DNA. Translation: AAA32808.1.
AC003114 Genomic DNA. Translation: AAC24084.1.
AB024028 Genomic DNA. Translation: BAA95712.1.
AL353995 Genomic DNA. Translation: CAB89403.1.
AL353995 Genomic DNA. Translation: CAB89404.1.
AB011479 Genomic DNA. Translation: BAB11558.1.
CP002684 Genomic DNA. Translation: AEE28413.1.
CP002686 Genomic DNA. Translation: AEE77308.1.
CP002688 Genomic DNA. Translation: AED91535.1.
CP002688 Genomic DNA. Translation: AED91536.1.
CP002688 Genomic DNA. Translation: AED98043.1.
AK117157 mRNA. Translation: BAC41835.1.
AF370577 mRNA. Translation: AAK49583.1.
AY037250 mRNA. Translation: AAK59851.1.
AY039904 mRNA. Translation: AAK64008.1.
AY077654 mRNA. Translation: AAL76132.1.
AY081741 mRNA. Translation: AAL87394.1.
BT003051 mRNA. Translation: AAO23616.1.
BT003162 mRNA. Translation: AAO24594.1.
BT005805 mRNA. Translation: AAO64207.1.
BT006068 mRNA. Translation: AAP04053.1.
AY084316 mRNA. Translation: AAM60903.1.

IPI

IPI00517184.

PIR

S06250.

RefSeq

NP_189372.1. NM_113651.2.
NP_201339.1. NM_125934.2.
NP_563838.1. NM_100790.2.
NP_568227.1. NM_121077.3.
NP_568228.1. NM_121078.2.

UniGene

At.17610.
At.1824.
At.20804.
At.21310.
At.21486.
At.22540.
At.32384.
At.63772.
At.71559.
At.73076.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
4FT2	X-ray	3.20	P	2-16	[»]
4FT4	X-ray	2.70	P/Q	2-33	[»]

ProteinModelPortal

P59226.

SMR

P59226. Positions 17-136.

ModBase

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Protein-protein interaction databases

DIP

DIP-48531N.

STRING

3702.AT5G10390.1-P.

Proteomic databases

PRIDE

P59226.

Protocols and materials databases

StructuralBiologyKnowledgebase

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Genome annotation databases

EnsemblPlants

AT1G09200.1; AT1G09200.1; AT1G09200.
AT3G27360.1; AT3G27360.1; AT3G27360.
AT5G10390.1; AT5G10390.1; AT5G10390.
AT5G10400.1; AT5G10400.1; AT5G10400.
AT5G65360.1; AT5G65360.1; AT5G65360.

GeneID

822357.
830903.
830904.
836661.
837440.

KEGG

ath:AT1G09200.
ath:AT3G27360.
ath:AT5G10390.
ath:AT5G10400.
ath:AT5G65360.

Organism-specific databases

TAIR

At1g09200.
At3g27360.
At5g10390.
At5g10400.
At5g65360.

Phylogenomic databases

eggNOG

COG2036.

HOGENOM

HOG000155290.

InParanoid

P59226.

KO

K11253.

OMA

RISKMAR.

PhylomeDB

P59226.

ProtClustDB

PLN00121.

Gene expression databases

ArrayExpress

P59226.

Genevestigator

P59226.

GermOnline

AT1G09200. Arabidopsis thaliana.

Family and domain databases

Gene3D

1.10.20.10. 1 hit.

InterPro

IPR009072. Histone-fold.
IPR007125. Histone_core_D.
IPR000164. Histone_H3.
[Graphical view]

PANTHER

PTHR11426. PTHR11426. 1 hit.

Pfam

PF00125. Histone. 1 hit.
[Graphical view]

PRINTS

PR00622. HISTONEH3.

SMART

SM00428. H3. 1 hit.
[Graphical view]

SUPFAM

SSF47113. Histone-fold. 1 hit.

PROSITE

PS00322. HISTONE_H3_1. 1 hit.
PS00959. HISTONE_H3_2. 1 hit.
[Graphical view]

ProtoNet

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Entry information

Entry name

H32_ARATH

Accession

Primary (citable) accession number: P59226

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 17, 2003
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 102 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program