H2B2_SOLLC
ID H2B2_SOLLC Reviewed; 140 AA.
AC O65818;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Histone H2B.2;
DE AltName: Full=LeH2B-2;
GN Name=H2B-2;
OS Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum;
OC Solanum subgen. Lycopersicon.
OX NCBI_TaxID=4081;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND INDUCTION.
RC STRAIN=cv. Moneymaker; TISSUE=Anther;
RX PubMed=10344194; DOI=10.1023/a:1006157718263;
RA van den Heuvel K.J.P.T., van Esch R.J., Barendse G.W.M., Wullems G.J.;
RT "Isolation and molecular characterization of gibberellin-regulated H1 and
RT H2B histone cDNAs in the leaf of the gibberellin-deficient tomato.";
RL Plant Mol. Biol. 39:883-890(1999).
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.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. Highest level in shoots, fruits and
CC young flower buds, including petals, anthers and ovules.
CC {ECO:0000269|PubMed:10344194}.
CC -!- INDUCTION: By gibberellins GA1, GA3, GA4 and GA9.
CC {ECO:0000269|PubMed:10344194}.
CC -!- PTM: Can be acetylated to form H2BK6ac, H2BK33ac and H2BK34ac.
CC {ECO:0000250}.
CC -!- PTM: Monoubiquitinated to form H2BK143ub1; may give a specific tag for
CC epigenetic transcriptional activation. {ECO:0000250}.
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-7; H2BK33ac = acetylated Lys-28; H2BK34ac = acetylated
CC Lys-29; H2BK143ub1 = monoubiquitinated Lys-136. {ECO:0000305}.
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DR EMBL; AJ224931; CAA12230.1; -; mRNA.
DR PIR; T06389; T06389.
DR RefSeq; NP_001296295.1; NM_001309366.1.
DR AlphaFoldDB; O65818; -.
DR SMR; O65818; -.
DR STRING; 4081.Solyc11g066430.1.1; -.
DR PaxDb; O65818; -.
DR PRIDE; O65818; -.
DR EnsemblPlants; Solyc11g066430.1.1; Solyc11g066430.1.1.1; Solyc11g066430.1.
DR GeneID; 778354; -.
DR Gramene; Solyc11g066430.1.1; Solyc11g066430.1.1.1; Solyc11g066430.1.
DR KEGG; sly:778354; -.
DR eggNOG; KOG1744; Eukaryota.
DR HOGENOM; CLU_075666_1_0_1; -.
DR InParanoid; O65818; -.
DR OMA; YTSANIM; -.
DR OrthoDB; 1536672at2759; -.
DR PhylomeDB; O65818; -.
DR Proteomes; UP000004994; Chromosome 11.
DR GO; GO:0000786; C:nucleosome; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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 2: Evidence at transcript level;
KW Acetylation; Chromosome; DNA-binding; Isopeptide bond; Nucleosome core;
KW Nucleus; Reference proteome; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..140
FT /note="Histone H2B.2"
FT /id="PRO_0000240450"
FT REGION 1..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 7
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250"
FT MOD_RES 28
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250"
FT MOD_RES 29
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250"
FT CROSSLNK 136
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250"
SQ SEQUENCE 140 AA; 15411 MW; 1A94B1A17012D087 CRC64;
MAPKAEKKPA EKKPAEEKKA EKTPKAGKKL PKESGSSGAD KKKKKSKKSI ETYKIYIFKV
LKQVHPDIGI SSKSMGIMNS FINDIFEKLA QESSRLARIN KKPTITSREI QTAVRLVLPG
ELAKHAVSEG TKAVTKFTSS
