H2B2_TETTS
ID H2B2_TETTS Reviewed; 122 AA.
AC P08994;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Histone H2B.2;
DE Short=H2B-2;
GN Name=HTB2; ORFNames=TTHERM_00283180;
OS Tetrahymena thermophila (strain SB210).
OC Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC Oligohymenophorea; Hymenostomatida; Tetrahymenina; Tetrahymenidae;
OC Tetrahymena.
OX NCBI_TaxID=312017;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3039463; DOI=10.1093/nar/15.14.5681;
RA Nomoto M., Imai N., Saiga H., Matsui T., Mita T.;
RT "Characterization of two types of histone H2B genes from macronuclei of
RT Tetrahymena thermophila.";
RL Nucleic Acids Res. 15:5681-5697(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SB210;
RX PubMed=16933976; DOI=10.1371/journal.pbio.0040286;
RA Eisen J.A., Coyne R.S., Wu M., Wu D., Thiagarajan M., Wortman J.R.,
RA Badger J.H., Ren Q., Amedeo P., Jones K.M., Tallon L.J., Delcher A.L.,
RA Salzberg S.L., Silva J.C., Haas B.J., Majoros W.H., Farzad M.,
RA Carlton J.M., Smith R.K. Jr., Garg J., Pearlman R.E., Karrer K.M., Sun L.,
RA Manning G., Elde N.C., Turkewitz A.P., Asai D.J., Wilkes D.E., Wang Y.,
RA Cai H., Collins K., Stewart B.A., Lee S.R., Wilamowska K., Weinberg Z.,
RA Ruzzo W.L., Wloga D., Gaertig J., Frankel J., Tsao C.-C., Gorovsky M.A.,
RA Keeling P.J., Waller R.F., Patron N.J., Cherry J.M., Stover N.A.,
RA Krieger C.J., del Toro C., Ryder H.F., Williamson S.C., Barbeau R.A.,
RA Hamilton E.P., Orias E.;
RT "Macronuclear genome sequence of the ciliate Tetrahymena thermophila, a
RT model eukaryote.";
RL PLoS Biol. 4:1620-1642(2006).
RN [3]
RP ACETYLATION.
RC STRAIN=B;
RX PubMed=7061439; DOI=10.1016/s0021-9258(18)34965-2;
RA Vavra K.J., Allis C.D., Gorovsky M.A.;
RT "Regulation of histone acetylation in Tetrahymena macro- and micronuclei.";
RL J. Biol. Chem. 257:2591-2598(1982).
RN [4]
RP UBIQUITINATION.
RX PubMed=2713375; DOI=10.1021/bi00429a006;
RA Nickel B.E., Allis C.D., Davie J.R.;
RT "Ubiquitinated histone H2B is preferentially located in transcriptionally
RT active chromatin.";
RL Biochemistry 28:958-963(1989).
RN [5]
RP METHYLATION AT ALA-2, ACETYLATION AT LYS-5 AND LYS-42, AND IDENTIFICATION
RP BY MASS SPECTROMETRY.
RC STRAIN=CU427, and CU428;
RX PubMed=15199121; DOI=10.1074/mcp.m400041-mcp200;
RA Medzihradszky K.F., Zhang X., Chalkley R.J., Guan S., McFarland M.A.,
RA Chalmers M.J., Marshall A.G., Diaz R.L., Allis C.D., Burlingame A.L.;
RT "Characterization of Tetrahymena histone H2B variants and posttranslational
RT populations by electron capture dissociation (ECD) Fourier transform ion
RT cyclotron mass spectrometry (FT-ICR MS).";
RL Mol. Cell. Proteomics 3:872-886(2004).
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. Chromosome. Note=Macronuclei.
CC -!- PTM: Acetylation occurs almost exclusively in the MAC.
CC {ECO:0000269|PubMed:15199121, ECO:0000269|PubMed:7061439}.
CC -!- PTM: Monoubiquitination to form H2BK115ub1 gives a specific tag for
CC epigenetic transcriptional activation and is also prerequisite for
CC H3K4me and H3K79me formation. {ECO:0000305}.
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: H2BK4ac =
CC acetylated Lys-5; H2BK41ac = acetylated Lys-42; H2BK115ub1 =
CC monoubiquitinated Lys-116. {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; X05544; CAA29060.1; -; Genomic_DNA.
DR EMBL; GG662656; EAR97929.2; -; Genomic_DNA.
DR PIR; B27097; B27097.
DR RefSeq; XP_001018174.2; XM_001018174.2.
DR AlphaFoldDB; P08994; -.
DR SMR; P08994; -.
DR STRING; 5911.EAR97929; -.
DR iPTMnet; P08994; -.
DR GeneID; 7837957; -.
DR KEGG; tet:TTHERM_00283180; -.
DR eggNOG; KOG1744; Eukaryota.
DR InParanoid; P08994; -.
DR OrthoDB; 1536672at2759; -.
DR Proteomes; UP000009168; Unassembled WGS sequence.
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; -; 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 INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..122
FT /note="Histone H2B.2"
FT /id="PRO_0000071906"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..28
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N,N,N-trimethylalanine"
FT /evidence="ECO:0000269|PubMed:15199121"
FT MOD_RES 5
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:15199121"
FT MOD_RES 42
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:15199121"
FT CROSSLNK 116
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000305|PubMed:2713375"
SQ SEQUENCE 122 AA; 13635 MW; 1104F3CE0CA44EEA CRC64;
MAPKKAPAAT TEKKVKKAPT TEKKNKKKRS ETFAIYIFKV LKQVHPDVGI SKKAMNIMNS
FINDSFERIA LESSKLVRFN KRRTLSSREV QTAVKLLLPG ELARHAISEG TKAVTKFSSS
SN
