H2B_ANOGA
ID H2B_ANOGA Reviewed; 124 AA.
AC Q27442; A0NGM0; Q7PCX1; Q7Q017; Q7Q8Z1; Q7QLH5;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 5.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Histone H2B;
GN ORFNames=AGAP012199;
GN and
GN ORFNames=AGAP012201;
GN and
GN ORFNames=AGAP012202;
GN and
GN ORFNames=AGAP012710;
GN and
GN ORFNames=AGAP012894;
OS Anopheles gambiae (African malaria mosquito).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=7165;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Suakoko; TISSUE=Ovary;
RX PubMed=9013255; DOI=10.1046/j.1365-2583.1997.00156.x;
RA Zurita M., Reynaud E., Kafatos F.C.;
RT "Cloning and characterization of cDNAs preferentially expressed in the
RT ovary of the mosquito, Anopheles gambiae.";
RL Insect Mol. Biol. 6:55-62(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PEST;
RX PubMed=12364791; DOI=10.1126/science.1076181;
RA Holt R.A., Subramanian G.M., Halpern A., Sutton G.G., Charlab R.,
RA Nusskern D.R., Wincker P., Clark A.G., Ribeiro J.M.C., Wides R.,
RA Salzberg S.L., Loftus B.J., Yandell M.D., Majoros W.H., Rusch D.B., Lai Z.,
RA Kraft C.L., Abril J.F., Anthouard V., Arensburger P., Atkinson P.W.,
RA Baden H., de Berardinis V., Baldwin D., Benes V., Biedler J., Blass C.,
RA Bolanos R., Boscus D., Barnstead M., Cai S., Center A., Chaturverdi K.,
RA Christophides G.K., Chrystal M.A.M., Clamp M., Cravchik A., Curwen V.,
RA Dana A., Delcher A., Dew I., Evans C.A., Flanigan M.,
RA Grundschober-Freimoser A., Friedli L., Gu Z., Guan P., Guigo R.,
RA Hillenmeyer M.E., Hladun S.L., Hogan J.R., Hong Y.S., Hoover J.,
RA Jaillon O., Ke Z., Kodira C.D., Kokoza E., Koutsos A., Letunic I.,
RA Levitsky A.A., Liang Y., Lin J.-J., Lobo N.F., Lopez J.R., Malek J.A.,
RA McIntosh T.C., Meister S., Miller J.R., Mobarry C., Mongin E., Murphy S.D.,
RA O'Brochta D.A., Pfannkoch C., Qi R., Regier M.A., Remington K., Shao H.,
RA Sharakhova M.V., Sitter C.D., Shetty J., Smith T.J., Strong R., Sun J.,
RA Thomasova D., Ton L.Q., Topalis P., Tu Z.J., Unger M.F., Walenz B.,
RA Wang A.H., Wang J., Wang M., Wang X., Woodford K.J., Wortman J.R., Wu M.,
RA Yao A., Zdobnov E.M., Zhang H., Zhao Q., Zhao S., Zhu S.C., Zhimulev I.,
RA Coluzzi M., della Torre A., Roth C.W., Louis C., Kalush F., Mural R.J.,
RA Myers E.W., Adams M.D., Smith H.O., Broder S., Gardner M.J., Fraser C.M.,
RA Birney E., Bork P., Brey P.T., Venter J.C., Weissenbach J., Kafatos F.C.,
RA Collins F.H., Hoffman S.L.;
RT "The genome sequence of the malaria mosquito Anopheles gambiae.";
RL Science 298:129-149(2002).
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.
CC -!- PTM: Monoubiquitination of Lys-119 gives a specific tag for epigenetic
CC transcriptional activation and is also prerequisite for histone H3
CC 'Lys-4' and 'Lys-79' methylation. {ECO:0000250}.
CC -!- PTM: GlcNAcylation at Ser-111 promotes monoubiquitination of Lys-119.
CC It fluctuates in response to extracellular glucose, and associates with
CC transcribed genes (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the histone H2B family. {ECO:0000305}.
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DR EMBL; X98185; CAA66860.1; -; mRNA.
DR EMBL; AAAB01004664; EAA02466.3; -; Genomic_DNA.
DR EMBL; AAAB01007051; EAA02895.2; -; Genomic_DNA.
DR EMBL; AAAB01008986; EAA00131.2; -; Genomic_DNA.
DR EMBL; AAAB01008986; EAA00128.2; -; Genomic_DNA.
DR EMBL; AAAB01008986; EAU75797.1; -; Genomic_DNA.
DR RefSeq; XP_001238300.1; XM_001238299.1.
DR RefSeq; XP_306255.2; XM_306255.2.
DR RefSeq; XP_307082.2; XM_307082.2.
DR RefSeq; XP_320329.2; XM_320329.3.
DR RefSeq; XP_320334.2; XM_320334.3.
DR AlphaFoldDB; Q27442; -.
DR SMR; Q27442; -.
DR STRING; 7165.AGAP012199-PA; -.
DR PaxDb; Q27442; -.
DR GeneID; 1267698; -.
DR GeneID; 1268522; -.
DR GeneID; 1280483; -.
DR GeneID; 1280488; -.
DR GeneID; 4577811; -.
DR KEGG; aga:AgaP_AGAP012199; -.
DR KEGG; aga:AgaP_AGAP012201; -.
DR KEGG; aga:AgaP_AGAP012202; -.
DR KEGG; aga:AgaP_AGAP012710; -.
DR KEGG; aga:AgaP_AGAP012894; -.
DR CTD; 1267698; -.
DR CTD; 1268522; -.
DR CTD; 1280483; -.
DR CTD; 1280488; -.
DR CTD; 4577811; -.
DR VEuPathDB; VectorBase:AGAP012199; -.
DR VEuPathDB; VectorBase:AGAP012201; -.
DR VEuPathDB; VectorBase:AGAP012202; -.
DR VEuPathDB; VectorBase:AGAP012710; -.
DR VEuPathDB; VectorBase:AGAP012894; -.
DR eggNOG; KOG1744; Eukaryota.
DR HOGENOM; CLU_075666_2_1_1; -.
DR InParanoid; Q27442; -.
DR OMA; SKEMSIM; -.
DR OrthoDB; 1536672at2759; -.
DR PhylomeDB; Q27442; -.
DR Proteomes; UP000007062; 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; IBA:GO_Central.
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:0006334; P:nucleosome assembly; IBA:GO_Central.
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 2: Evidence at transcript level;
KW Chromosome; DNA-binding; Glycoprotein; Isopeptide bond; Nucleosome core;
KW Nucleus; Reference proteome; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..123
FT /note="Histone H2B"
FT /id="PRO_0000071856"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 111
FT /note="O-linked (GlcNAc) serine"
FT /evidence="ECO:0000250"
FT CROSSLNK 119
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250"
FT CONFLICT 2
FT /note="A -> P (in Ref. 1; CAA66860)"
FT /evidence="ECO:0000305"
FT CONFLICT 34..37
FT /note="ESYA -> RATP (in Ref. 1; CAA66860)"
FT /evidence="ECO:0000305"
FT CONFLICT 74..76
FT /note="AEA -> RK (in Ref. 1; CAA66860)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 124 AA; 13759 MW; 064D50C1A6850283 CRC64;
MAPKTSGKAA KKSGKAQKNI SKSDKKKKRK TRKESYAIYI YKVLKQVHPD TGISSKAMSI
MNSFVNDIFE RIAAEASRLA HYNKRSTITS REIQTAVRLL LPGELAKHAV SEGTKAVTKY
TSSK
