H2B2_ARATH
ID H2B2_ARATH Reviewed; 243 AA.
AC Q9SGE3;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Histone H2B.2;
DE AltName: Full=HTB8;
GN OrderedLocusNames=At1g08170; ORFNames=T23G18.3, T6D22.26;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Underwood B.A., Xiao Y.-L., Moskal W.A. Jr., Monaghan E.L., Wang W.,
RA Redman J.C., Wu H.C., Utterback T., Town C.D.;
RL Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases.
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 {ECO:0000250}. Chromosome {ECO:0000250}.
CC -!- PTM: Can be acetylated to form H2BK6ac. {ECO:0000250}.
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: H2BK6ac =
CC acetylated Lys-7. {ECO:0000305}.
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DR EMBL; AC011438; AAF18256.1; -; Genomic_DNA.
DR EMBL; AC026875; AAF79830.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE28257.1; -; Genomic_DNA.
DR EMBL; DQ056448; AAY78605.1; -; mRNA.
DR RefSeq; NP_172295.1; NM_100691.2.
DR AlphaFoldDB; Q9SGE3; -.
DR SMR; Q9SGE3; -.
DR STRING; 3702.AT1G08170.1; -.
DR MetOSite; Q9SGE3; -.
DR PaxDb; Q9SGE3; -.
DR PRIDE; Q9SGE3; -.
DR ProteomicsDB; 230179; -.
DR EnsemblPlants; AT1G08170.1; AT1G08170.1; AT1G08170.
DR GeneID; 837338; -.
DR Gramene; AT1G08170.1; AT1G08170.1; AT1G08170.
DR KEGG; ath:AT1G08170; -.
DR Araport; AT1G08170; -.
DR TAIR; locus:2199988; AT1G08170.
DR eggNOG; KOG1744; Eukaryota.
DR HOGENOM; CLU_075666_0_0_1; -.
DR InParanoid; Q9SGE3; -.
DR OMA; ANDQETQ; -.
DR OrthoDB; 1536672at2759; -.
DR PhylomeDB; Q9SGE3; -.
DR PRO; PR:Q9SGE3; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9SGE3; baseline and differential.
DR Genevisible; Q9SGE3; AT.
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: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.
PE 2: Evidence at transcript level;
KW Acetylation; Chromosome; DNA-binding; Methylation; Nucleosome core;
KW Nucleus; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9LQQ4"
FT CHAIN 2..243
FT /note="Histone H2B.2"
FT /id="PRO_0000238689"
FT REGION 67..145
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 99..113
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N,N,N-trimethylalanine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9LQQ4"
FT MOD_RES 2
FT /note="N,N-dimethylalanine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9LQQ4"
FT MOD_RES 2
FT /note="N-methylalanine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9LQQ4"
SQ SEQUENCE 243 AA; 27221 MW; 046E8F086B20C069 CRC64;
MAPRKPKVVS VTKKKKVVEE TIKVTVTEEG DPCVITETAN DQETQDLTFS IPVGENVTTV
EIPVEVPDER SLPVGENVTT VKIPVDDRDE SSPQPPETPV EVRDEPSPQP PETPASKSEG
TLKKTDKVEK KQENKKKKKK KKRDDLAGDE YRRYVYKVMK QVHPDLGITS KAMTVVNMFM
GDMFERIAQE AARLSDYTKR RTLSSREIEA AVRLVLPGEL SRHAVAEGSK AVSNFVGYDS
RKR
