H2B10_ARATH
ID H2B10_ARATH Reviewed; 145 AA.
AC Q9FFC0; Q96516;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Histone H2B.10;
DE AltName: Full=HTB2;
GN OrderedLocusNames=At5g22880; ORFNames=MRN17.11;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Columbia;
RA Phillips G.;
RL Submitted (JUL-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9330910; DOI=10.1093/dnares/4.3.215;
RA Sato S., Kotani H., Nakamura Y., Kaneko T., Asamizu E., Fukami M.,
RA Miyajima N., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. I. Sequence
RT features of the 1.6 Mb regions covered by twenty physically assigned P1
RT clones.";
RL DNA Res. 4:215-230(1997).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP INTERACTION WITH ORTH2.
RX PubMed=17242155; DOI=10.1101/gad.1512007;
RA Woo H.R., Pontes O., Pikaard C.S., Richards E.J.;
RT "VIM1, a methylcytosine-binding protein required for centromeric
RT heterochromatinization.";
RL Genes Dev. 21:267-277(2007).
RN [5]
RP UBIQUITINATION AT LYS-141, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=17554311; DOI=10.1038/nature05864;
RA Sridhar V.V., Kapoor A., Zhang K., Zhu J., Zhou T., Hasegawa P.M.,
RA Bressan R.A., Zhu J.-K.;
RT "Control of DNA methylation and heterochromatic silencing by histone H2B
RT deubiquitination.";
RL Nature 447:735-738(2007).
RN [6]
RP ACETYLATION AT LYS-6; LYS-11; LYS-16; LYS-28; LYS-34 AND LYS-35,
RP METHYLATION AT LYS-12, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=17691833; DOI=10.1021/pr0702159;
RA Bergmueller E., Gehrig P.M., Gruissem W.;
RT "Characterization of post-translational modifications of histone H2B-
RT variants isolated from Arabidopsis thaliana.";
RL J. Proteome Res. 6:3655-3668(2007).
CC -!- FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact
CC DNA into chromatin, limiting DNA accessibility to the cellular
CC machineries which require DNA as a template. Histones thereby play a
CC central role in transcription regulation, DNA repair, DNA replication
CC and chromosomal stability. DNA accessibility is regulated via a complex
CC set of post-translational modifications of histones, also called
CC histone code, and nucleosome remodeling.
CC -!- SUBUNIT: The nucleosome is a histone octamer containing two molecules
CC each of H2A, H2B, H3 and H4 assembled in one H3-H4 heterotetramer and
CC two H2A-H2B heterodimers. The octamer wraps approximately 147 bp of
CC DNA. Interacts with ORTH2. {ECO:0000269|PubMed:17242155}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome {ECO:0000250}.
CC -!- PTM: Can be acetylated to form H2BK5ac, H2BK10ac, H2BK15ac, H2BK27ac,
CC H2BK33ac and H2BK34ac. {ECO:0000269|PubMed:17691833}.
CC -!- PTM: Dimethylated to form H2BK11me2.
CC -!- PTM: Monoubiquitinated by BRE1 to form H2BK143ub1 and deubiquitinated
CC by UBP26. Required for heterochromatic histone H3 di- and
CC trimethylation at H3K4me. May give a specific tag for epigenetic
CC transcriptional activation.
CC -!- SIMILARITY: Belongs to the histone H2B family. {ECO:0000305}.
CC -!- CAUTION: To ensure consistency between histone entries, we follow the
CC 'Brno' nomenclature for histone modifications, with positions referring
CC to those used in the literature for the 'closest' model organism. Due
CC to slight variations in histone sequences between organisms and to the
CC presence of initiator methionine in UniProtKB/Swiss-Prot sequences, the
CC actual positions of modified amino acids in the sequence generally
CC differ. In this entry the following conventions are used: H2BK6ac =
CC acetylated Lys-6; H2BK11ac = acetylated Lys-11; H2BK12me2 =
CC dimethylated Lys-12; H2BK16ac = acetylated Lys-16; H2BK27ac =
CC acetylated Lys-28; H2BK33ac = acetylated Lys-34; H2BK34ac = acetylated
CC Lys-35; H2BK143ub1 = monoubiquitinated Lys-141. {ECO:0000305}.
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DR EMBL; Y07745; CAA69025.1; -; mRNA.
DR EMBL; AB005243; BAB10609.1; -; Genomic_DNA.
DR EMBL; CP002688; AED93093.1; -; Genomic_DNA.
DR RefSeq; NP_197679.1; NM_122194.3.
DR AlphaFoldDB; Q9FFC0; -.
DR SMR; Q9FFC0; -.
DR BioGRID; 17627; 5.
DR STRING; 3702.AT5G22880.1; -.
DR iPTMnet; Q9FFC0; -.
DR PaxDb; Q9FFC0; -.
DR PRIDE; Q9FFC0; -.
DR ProteomicsDB; 222370; -.
DR EnsemblPlants; AT5G22880.1; AT5G22880.1; AT5G22880.
DR GeneID; 832352; -.
DR Gramene; AT5G22880.1; AT5G22880.1; AT5G22880.
DR KEGG; ath:AT5G22880; -.
DR Araport; AT5G22880; -.
DR TAIR; locus:2172691; AT5G22880.
DR eggNOG; KOG1744; Eukaryota.
DR HOGENOM; CLU_075666_1_0_1; -.
DR InParanoid; Q9FFC0; -.
DR OMA; WSEAMSI; -.
DR OrthoDB; 1536672at2759; -.
DR PhylomeDB; Q9FFC0; -.
DR PRO; PR:Q9FFC0; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FFC0; baseline and differential.
DR Genevisible; Q9FFC0; AT.
DR GO; GO:0005730; C:nucleolus; HDA:TAIR.
DR GO; GO:0000786; C:nucleosome; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR GO; GO:0030527; F:structural constituent of chromatin; IEA:InterPro.
DR GO; GO:0006334; P:nucleosome assembly; IBA:GO_Central.
DR Gene3D; 1.10.20.10; -; 1.
DR InterPro; IPR009072; Histone-fold.
DR InterPro; IPR007125; Histone_H2A/H2B/H3.
DR InterPro; IPR000558; Histone_H2B.
DR PANTHER; PTHR23428; PTHR23428; 1.
DR Pfam; PF00125; Histone; 1.
DR PRINTS; PR00621; HISTONEH2B.
DR SMART; SM00427; H2B; 1.
DR SUPFAM; SSF47113; SSF47113; 1.
DR PROSITE; PS00357; HISTONE_H2B; 1.
PE 1: Evidence at protein level;
KW Acetylation; Chromosome; DNA-binding; Isopeptide bond; Methylation;
KW Nucleosome core; Nucleus; Reference proteome; Ubl conjugation.
FT CHAIN 1..145
FT /note="Histone H2B.10"
FT /id="PRO_0000238697"
FT REGION 1..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 27..53
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 3
FT /note="N6-methyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9LZT0"
FT MOD_RES 6
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:17691833"
FT MOD_RES 11
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:17691833"
FT MOD_RES 12
FT /note="N6,N6-dimethyllysine"
FT /evidence="ECO:0000269|PubMed:17691833"
FT MOD_RES 16
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:17691833"
FT MOD_RES 28
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:17691833"
FT MOD_RES 34
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:17691833"
FT MOD_RES 35
FT /note="N6-acetyllysine; partial"
FT /evidence="ECO:0000269|PubMed:17691833"
FT CROSSLNK 141
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q9LQQ4"
FT CONFLICT 38
FT /note="K -> E (in Ref. 1; CAA69025)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 145 AA; 15732 MW; CC8421B559D42B30 CRC64;
MAKADKKPAE KKPAEKTPAA EPAAAAEKKP KAGKKLPKEP AGAGDKKKKR SKKNVETYKI
YIFKVLKQVH PDIGISSKAM GIMNSFINDI FEKLAGESSK LARYNKKPTI TSREIQTAVR
LVLPGELAKH AVSEGTKAVT KFTSS
