GenomeNet

Database: UniProt
Entry: E4XJ06_OIKDI
LinkDB: E4XJ06_OIKDI
Original site: E4XJ06_OIKDI 
ID   E4XJ06_OIKDI            Unreviewed;       103 AA.
AC   E4XJ06;
DT   08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT   08-FEB-2011, sequence version 1.
DT   27-MAR-2024, entry version 51.
DE   RecName: Full=Histone H4 {ECO:0000256|ARBA:ARBA00020836, ECO:0000256|RuleBase:RU000528};
GN   ORFNames=GSOID_T00012586001 {ECO:0000313|EMBL:CBY10449.1};
OS   Oikopleura dioica (Tunicate).
OC   Eukaryota; Metazoa; Chordata; Tunicata; Appendicularia; Copelata;
OC   Oikopleuridae; Oikopleura.
OX   NCBI_TaxID=34765 {ECO:0000313|EMBL:CBY10449.1};
RN   [1] {ECO:0000313|EMBL:CBY10449.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=21097902; DOI=10.1126/science.1194167;
RA   Denoeud F., Henriet S., Mungpakdee S., Aury J.M., Da Silva C.,
RA   Brinkmann H., Mikhaleva J., Olsen L.C., Jubin C., Canestro C.,
RA   Bouquet J.M., Danks G., Poulain J., Campsteijn C., Adamski M., Cross I.,
RA   Yadetie F., Muffato M., Louis A., Butcher S., Tsagkogeorga G., Konrad A.,
RA   Singh S., Jensen M.F., Cong E.H., Eikeseth-Otteraa H., Noel B.,
RA   Anthouard V., Porcel B.M., Kachouri-Lafond R., Nishino A., Ugolini M.,
RA   Chourrout P., Nishida H., Aasland R., Huzurbazar S., Westhof E., Delsuc F.,
RA   Lehrach H., Reinhardt R., Weissenbach J., Roy S.W., Artiguenave F.,
RA   Postlethwait J.H., Manak J.R., Thompson E.M., Jaillon O., Du Pasquier L.,
RA   Boudinot P., Liberles D.A., Volff J.N., Philippe H., Lenhard B.,
RA   Roest Crollius H., Wincker P., Chourrout D.;
RT   "Plasticity of animal genome architecture unmasked by rapid evolution of a
RT   pelagic tunicate.";
RL   Science 330:1381-1385(2010).
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       {ECO:0000256|ARBA:ARBA00002001, ECO:0000256|RuleBase:RU000528}.
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. {ECO:0000256|RuleBase:RU000528}.
CC   -!- SUBCELLULAR LOCATION: Chromosome {ECO:0000256|ARBA:ARBA00004286}.
CC       Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the histone H4 family.
CC       {ECO:0000256|ARBA:ARBA00006564, ECO:0000256|RuleBase:RU000528}.
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; FN653057; CBY10449.1; -; Genomic_DNA.
DR   AlphaFoldDB; E4XJ06; -.
DR   InParanoid; E4XJ06; -.
DR   Proteomes; UP000001307; 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   CDD; cd00076; H4; 1.
DR   Gene3D; 1.10.20.10; Histone, subunit A; 1.
DR   InterPro; IPR035425; CENP-T/H4_C.
DR   InterPro; IPR009072; Histone-fold.
DR   InterPro; IPR001951; Histone_H4.
DR   InterPro; IPR019809; Histone_H4_CS.
DR   InterPro; IPR004823; TAF_TATA-bd_Histone-like_dom.
DR   PANTHER; PTHR10484; HISTONE H4; 1.
DR   PANTHER; PTHR10484:SF0; HISTONE H4; 1.
DR   Pfam; PF15511; CENP-T_C; 1.
DR   PRINTS; PR00623; HISTONEH4.
DR   SMART; SM00417; H4; 1.
DR   SMART; SM00803; TAF; 1.
DR   SUPFAM; SSF47113; Histone-fold; 1.
DR   PROSITE; PS00047; HISTONE_H4; 1.
PE   3: Inferred from homology;
KW   Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW   Chromosome {ECO:0000256|ARBA:ARBA00022454, ECO:0000256|RuleBase:RU000528};
KW   Citrullination {ECO:0000256|ARBA:ARBA00022934};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU000528};
KW   Hydroxylation {ECO:0000256|ARBA:ARBA00023278};
KW   Nucleosome core {ECO:0000256|ARBA:ARBA00023269,
KW   ECO:0000256|RuleBase:RU000528};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU000528};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001307}.
FT   DOMAIN          28..93
FT                   /note="TATA box binding protein associated factor (TAF)
FT                   histone-like fold"
FT                   /evidence="ECO:0000259|SMART:SM00803"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   103 AA;  11379 MW;  09F1CA0888B96EEE CRC64;
     MSGRGKGGKG LGKGGAKRHR KVLRDNIQGI TKPAIRRLAR RGGVKRISSL IYEETRGVLK
     VFLENVIRDA VTYTEHAKRK TVTALDVVYA LKRQGRTLYG FGG
//
DBGET integrated database retrieval system