H2BV3_DICDI
ID H2BV3_DICDI Reviewed; 154 AA.
AC Q54LP8;
DT 24-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Histone H2B.v3;
GN Name=H2Bv3; ORFNames=DDB_G0286509;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
CC -!- FUNCTION: Core component of nucleosome which plays a central role in
CC DNA double strand break (DSB) repair. Nucleosomes wrap and compact DNA
CC into chromatin, limiting DNA accessibility to the cellular machineries
CC which require DNA as a template. Histones thereby play a central role
CC in transcription regulation, DNA repair, DNA replication and
CC chromosomal stability. DNA accessibility is regulated via a complex set
CC of post-translational modifications of histones, also called histone
CC code, and nucleosome remodeling (By similarity). {ECO:0000250}.
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 DNA
CC (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the histone H2B family. {ECO:0000305}.
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DR EMBL; AAFI02000087; EAL64181.1; -; Genomic_DNA.
DR RefSeq; XP_637684.1; XM_632592.1.
DR AlphaFoldDB; Q54LP8; -.
DR SMR; Q54LP8; -.
DR STRING; 44689.DDB0231622; -.
DR PaxDb; Q54LP8; -.
DR EnsemblProtists; EAL64181; EAL64181; DDB_G0286509.
DR GeneID; 8625650; -.
DR KEGG; ddi:DDB_G0286509; -.
DR dictyBase; DDB_G0286509; H2Bv3.
DR eggNOG; KOG1744; Eukaryota.
DR HOGENOM; CLU_075666_1_3_1; -.
DR InParanoid; Q54LP8; -.
DR OMA; AQLCQTT; -.
DR PhylomeDB; Q54LP8; -.
DR Reactome; R-DDI-2299718; Condensation of Prophase Chromosomes.
DR Reactome; R-DDI-2559580; Oxidative Stress Induced Senescence.
DR Reactome; R-DDI-3214815; HDACs deacetylate histones.
DR Reactome; R-DDI-427359; SIRT1 negatively regulates rRNA expression.
DR Reactome; R-DDI-5689880; Ub-specific processing proteases.
DR Reactome; R-DDI-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
DR Reactome; R-DDI-68616; Assembly of the ORC complex at the origin of replication.
DR Reactome; R-DDI-73772; RNA Polymerase I Promoter Escape.
DR PRO; PR:Q54LP8; -.
DR Proteomes; UP000002195; Chromosome 4.
DR GO; GO:0031012; C:extracellular matrix; HDA:dictyBase.
DR GO; GO:0000786; C:nucleosome; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IDA:dictyBase.
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 GO; GO:0046689; P:response to mercury ion; IDA:dictyBase.
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 SMART; SM00427; H2B; 1.
DR SUPFAM; SSF47113; SSF47113; 1.
PE 3: Inferred from homology;
KW Chromosome; DNA-binding; Nucleosome core; Nucleus; Reference proteome.
FT CHAIN 1..154
FT /note="Histone H2B.v3"
FT /id="PRO_0000389160"
FT REGION 1..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..32
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 33..48
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 154 AA; 17100 MW; D51108A3120C4768 CRC64;
MVFVKGQKKA TKGSTQSGEE KTASTTPKVT KTPTEGGEKK RKKRKSDYTS FSTYIHKLLK
QITPPTNAKS NEKGDRKFTI SSKAMSVMNS FVHDIFDRIA TEASGLAKKK KRQTLHSRDI
QVAVRIILTG ELAKHAILQG MTAVNKYNPT ESKN
