ID H2B4_ORYSI Reviewed; 153 AA. AC A2WKP5; DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot. DT 20-MAR-2007, sequence version 1. DT 27-MAR-2024, entry version 77. DE RecName: Full=Histone H2B.4; GN Name=H2B.4; ORFNames=OsI_000388; OS Oryza sativa subsp. indica (Rice). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade; OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa. OX NCBI_TaxID=39946; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. 93-11; RX PubMed=15685292; DOI=10.1371/journal.pbio.0030038; RA Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S., RA Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L., RA Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J., RA Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X., RA Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y., RA Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L., RA Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H., RA Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z., RA Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L., RA Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F., RA Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q., RA Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J., RA Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M., RA McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.; RT "The genomes of Oryza sativa: a history of duplications."; RL PLoS Biol. 3:266-281(2005). 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 -!- PTM: Can be acetylated to form H2BK6ac and H2BK33ac. {ECO:0000250}. 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 (By similarity). {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-37; H2BK143ub1 = CC monoubiquitinated Lys-149. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CM000126; EAY72541.1; -; Genomic_DNA. DR AlphaFoldDB; A2WKP5; -. DR SMR; A2WKP5; -. DR STRING; 39946.A2WKP5; -. DR EnsemblPlants; BGIOSGA002785-TA; BGIOSGA002785-PA; BGIOSGA002785. DR Gramene; BGIOSGA002785-TA; BGIOSGA002785-PA; BGIOSGA002785. DR HOGENOM; CLU_075666_1_0_1; -. DR OMA; MHSSDRN; -. DR Proteomes; UP000007015; Chromosome 1. 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; IEA:UniProtKB-KW. DR GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro. DR GO; GO:0030527; F:structural constituent of chromatin; IEA:InterPro. DR Gene3D; 1.10.20.10; Histone, subunit A; 1. DR InterPro; IPR009072; Histone-fold. DR InterPro; IPR007125; Histone_H2A/H2B/H3. DR InterPro; IPR000558; Histone_H2B. DR PANTHER; PTHR23428; HISTONE H2B; 1. DR PANTHER; PTHR23428:SF397; HISTONE H2B.11; 1. DR Pfam; PF00125; Histone; 1. DR PRINTS; PR00621; HISTONEH2B. DR SMART; SM00427; H2B; 1. DR SUPFAM; SSF47113; Histone-fold; 1. DR PROSITE; PS00357; HISTONE_H2B; 1. PE 3: Inferred from homology; 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..153 FT /note="Histone H2B.4" FT /id="PRO_0000294182" FT REGION 1..61 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1..52 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 7 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250" FT MOD_RES 37 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250" FT CROSSLNK 149 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in ubiquitin)" FT /evidence="ECO:0000250" SQ SEQUENCE 153 AA; 16502 MW; 5D5EB9234988EA50 CRC64; MAPKAEKKPA AKKPAEEEPA AEKAEKAPAG KKPKAEKRLP AGKAEKGSGE GKKAGRKKAK KSVETYKIYI FKVLKQVHPD IGISSKAMSI MNSFINDIFE KLAGESAKLA RYNKKPTITS REIQTSVRLV LPGELAKHAV SEGTKAVTKF TSA //