H2B_ZHASC
ID H2B_ZHASC Reviewed; 126 AA.
AC Q75VN4;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=Histone H2B;
GN Name=histh2b {ECO:0000312|EMBL:BAC99977.1};
OS Zhangixalus schlegelii (Japanese gliding frog) (Rhacophorus schlegelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Neobatrachia; Ranoidea; Rhacophoridae; Rhacophorinae;
OC Zhangixalus.
OX NCBI_TaxID=210202;
RN [1] {ECO:0000305, ECO:0000312|EMBL:BAC99977.1}
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 2-94 AND 107-126,
RP SUBCELLULAR LOCATION, AND FUNCTION.
RC TISSUE=Skin {ECO:0000269|PubMed:14651982};
RX PubMed=14651982; DOI=10.1016/j.bbrc.2003.11.052;
RA Kawasaki H., Isaacson T., Iwamuro S., Conlon J.M.;
RT "A protein with antimicrobial activity in the skin of Schlegel's green tree
RT frog Rhacophorus schlegelii (Rhacophoridae) identified as histone H2B.";
RL Biochem. Biophys. Res. Commun. 312:1082-1086(2003).
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. {ECO:0000269|PubMed:14651982}.
CC -!- FUNCTION: Has antibacterial activity against the Gram-negative bacteria
CC E.coli and the Gram-positive bacteria S.aureus.
CC {ECO:0000269|PubMed:14651982}.
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:0000269|PubMed:14651982}. Secreted
CC {ECO:0000269|PubMed:14651982}. Chromosome
CC {ECO:0000269|PubMed:14651982}.
CC -!- TISSUE SPECIFICITY: Expressed by the skin granular glands.
CC {ECO:0000305}.
CC -!- PTM: Monoubiquitination of Lys-121 by BRE1 gives a specific tag for
CC epigenetic transcriptional activation and is also prerequisite for
CC histone H3 'Lys-4' and 'Lys-79' methylation.
CC {ECO:0000250|UniProtKB:P33778}.
CC -!- PTM: Phosphorylated on Ser-15 during apoptosis; which facilitates
CC apoptotic chromatin condensation. {ECO:0000250|UniProtKB:P06900}.
CC -!- PTM: GlcNAcylation at Ser-113 promotes monoubiquitination of Lys-121.
CC It fluctuates in response to extracellular glucose, and associates with
CC transcribed genes (By similarity). {ECO:0000250|UniProtKB:P62807}.
CC -!- SIMILARITY: Belongs to the histone H2B family. {ECO:0000255}.
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DR EMBL; AB124798; BAC99977.1; -; mRNA.
DR AlphaFoldDB; Q75VN4; -.
DR SMR; Q75VN4; -.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0000786; C:nucleosome; NAS:UniProtKB.
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:0044877; F:protein-containing complex binding; ISS:UniProtKB.
DR GO; GO:0030527; F:structural constituent of chromatin; IEA:InterPro.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; IDA:UniProtKB.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; IDA:UniProtKB.
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; Amphibian defense peptide; Antibiotic; Antimicrobial;
KW Chromosome; Direct protein sequencing; DNA-binding; Glycoprotein;
KW Isopeptide bond; Nucleosome core; Nucleus; Phosphoprotein; Secreted;
KW Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:14651982"
FT CHAIN 2..126
FT /note="Histone H2B"
FT /id="PRO_0000071853"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 17..35
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 6
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P0C1H4"
FT MOD_RES 13
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P0C1H4"
FT MOD_RES 15
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P06900"
FT MOD_RES 16
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P0C1H4"
FT MOD_RES 21
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P0C1H4"
FT CARBOHYD 113
FT /note="O-linked (GlcNAc) serine"
FT /evidence="ECO:0000250|UniProtKB:P62807"
FT CROSSLNK 121
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P0C1H4"
SQ SEQUENCE 126 AA; 13906 MW; C2976C2F866D3FF3 CRC64;
MPEPAKSAPA AKKGSKKAVS KVQKKDGKKR RKSRKESYAI YVYKVLKQVH PDTGISSKAM
SIMNSFVNDI FERIAGEASR LAHYNKRSTI TSREIQTAVR LLLPGELAKH AVSEGTKAVT
KYTSAK
