H2B1A_MOUSE
ID H2B1A_MOUSE Reviewed; 127 AA.
AC P70696; Q5NCL9;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Histone H2B type 1-A;
DE AltName: Full=Histone H2B, testis;
DE AltName: Full=Testis-specific histone H2B {ECO:0000303|PubMed:23884607};
GN Name=H2bc1 {ECO:0000312|MGI:MGI:2448375};
GN Synonyms=Hist1h2ba {ECO:0000312|MGI:MGI:2448375},
GN Th2b {ECO:0000303|PubMed:23884607};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
RC TISSUE=Kidney;
RX PubMed=8672246; DOI=10.1089/dna.1996.15.495;
RA Choi Y.C., Gu W., Hecht N.B., Feinberg A.P., Chae C.-B.;
RT "Molecular cloning of mouse somatic and testis-specific H2B histone genes
RT containing a methylated CpG island.";
RL DNA Cell Biol. 15:495-504(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=12408966; DOI=10.1006/geno.2002.6850;
RA Marzluff W.F., Gongidi P., Woods K.R., Jin J., Maltais L.J.;
RT "The human and mouse replication-dependent histone genes.";
RL Genomics 80:487-498(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP CROTONYLATION AT LYS-7; LYS-13; LYS-14; LYS-17; LYS-18; LYS-22; LYS-25 AND
RP LYS-36.
RX PubMed=21925322; DOI=10.1016/j.cell.2011.08.008;
RA Tan M., Luo H., Lee S., Jin F., Yang J.S., Montellier E., Buchou T.,
RA Cheng Z., Rousseaux S., Rajagopal N., Lu Z., Ye Z., Zhu Q., Wysocka J.,
RA Ye Y., Khochbin S., Ren B., Zhao Y.;
RT "Identification of 67 histone marks and histone lysine crotonylation as a
RT new type of histone modification.";
RL Cell 146:1016-1028(2011).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RX PubMed=23884607; DOI=10.1101/gad.220095.113;
RA Montellier E., Boussouar F., Rousseaux S., Zhang K., Buchou T.,
RA Fenaille F., Shiota H., Debernardi A., Hery P., Curtet S., Jamshidikia M.,
RA Barral S., Holota H., Bergon A., Lopez F., Guardiola P., Pernet K.,
RA Imbert J., Petosa C., Tan M., Zhao Y., Gerard M., Khochbin S.;
RT "Chromatin-to-nucleoprotamine transition is controlled by the histone H2B
RT variant TH2B.";
RL Genes Dev. 27:1680-1692(2013).
RN [7]
RP FUNCTION, AND INTERACTION WITH H2AB1.
RX PubMed=28366643; DOI=10.1016/j.molcel.2017.02.025;
RA Barral S., Morozumi Y., Tanaka H., Montellier E., Govin J.,
RA de Dieuleveult M., Charbonnier G., Coute Y., Puthier D., Buchou T.,
RA Boussouar F., Urahama T., Fenaille F., Curtet S., Hery P.,
RA Fernandez-Nunez N., Shiota H., Gerard M., Rousseaux S., Kurumizaka H.,
RA Khochbin S.;
RT "Histone variant H2A.L.2 guides transition protein-dependent protamine
RT assembly in male germ cells.";
RL Mol. Cell 66:89-101(2017).
RN [8]
RP LACTYLATION AT LYS-6; LYS-12; LYS-16; LYS-17; LYS-21; LYS-86; LYS-109 AND
RP LYS-117.
RX PubMed=31645732; DOI=10.1038/s41586-019-1678-1;
RA Zhang D., Tang Z., Huang H., Zhou G., Cui C., Weng Y., Liu W., Kim S.,
RA Lee S., Perez-Neut M., Ding J., Czyz D., Hu R., Ye Z., He M., Zheng Y.G.,
RA Shuman H.A., Dai L., Ren B., Roeder R.G., Becker L., Zhao Y.;
RT "Metabolic regulation of gene expression by histone lactylation.";
RL Nature 574:575-580(2019).
CC -!- FUNCTION: Variant histone specifically required to direct the
CC transformation of dissociating nucleosomes to protamine in male germ
CC cells (PubMed:23884607, PubMed:28366643). Entirely replaces classical
CC histone H2B prior nucleosome to protamine transition and probably acts
CC as a nucleosome dissociating factor that creates a more dynamic
CC chromatin, facilitating the large-scale exchange of histones
CC (PubMed:23884607). In condensing spermatids, the heterodimer between
CC H2AB1 and H2BC1/TH2B is loaded onto the nucleosomes and promotes
CC loading of transition proteins (TNP1 and TNP2) onto the nucleosomes
CC (PubMed:28366643). Inclusion of the H2AB1-H2BC1/TH2B dimer into
CC chromatin opens the nucleosomes, releasing the nucleosomal DNA ends and
CC allowing the invasion of nucleosomes by transition proteins (TNP1 and
CC TNP2) (PubMed:28366643). Then, transition proteins drive the
CC recruitment and processing of protamines, which are responsible for
CC histone eviction (PubMed:28366643). Also expressed maternally and is
CC present in the female pronucleus, suggesting a similar role in
CC protamine replacement by nucleosomes at fertilization
CC (PubMed:23884607). Core component of nucleosome. Nucleosomes wrap and
CC compact 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. {ECO:0000269|PubMed:23884607,
CC ECO:0000269|PubMed:28366643}.
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 (PubMed:23884607). Interacts with H2AB1;
CC preferentially dimerizes with H2AB1 to form nucleosomes
CC (PubMed:28366643). {ECO:0000269|PubMed:23884607,
CC ECO:0000269|PubMed:28366643}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:23884607}. Chromosome
CC {ECO:0000269|PubMed:23884607}.
CC -!- TISSUE SPECIFICITY: Mainly expressed in testis, and the corresponding
CC protein is also present in mature sperm. Also present in metaphase
CC oocytes (at protein level). {ECO:0000269|PubMed:23884607,
CC ECO:0000269|PubMed:8672246}.
CC -!- DEVELOPMENTAL STAGE: Accumulates at 10 day postpartum (dpp), when pre-
CC leptotene/leptotene spermatocytes first appear and when H2B expression
CC shows a drastic decrease. Replaces H2B by 18 dpp in spermatocytes. Also
CC present in metaphase oocytes and in the female pronucleus at
CC fertilization and is also rapidly incorporated into the male
CC pronucleus. {ECO:0000269|PubMed:23884607}.
CC -!- PTM: Monoubiquitination at Lys-36 by the MSL1/MSL2 dimer is required
CC for histone H3 'Lys-4' (H3K4me) and 'Lys-79' (H3K79me) methylation and
CC transcription activation at specific gene loci, such as HOXA9 and MEIS1
CC loci. Similarly, monoubiquitination of Lys-122 (H2BK120Ub) by the
CC RNF20/40 complex gives a specific tag for epigenetic transcriptional
CC activation and is also prerequisite for histone H3 'Lys-4' and 'Lys-79'
CC methylation. It also functions cooperatively with the FACT dimer to
CC stimulate elongation by RNA polymerase II. H2BK120Ub also acts as a
CC regulator of mRNA splicing: deubiquitination by USP49 is required for
CC efficient cotranscriptional splicing of a large set of exons (By
CC similarity). {ECO:0000250|UniProtKB:Q96A08}.
CC -!- PTM: Crotonylation (Kcr) is specifically present in male germ cells and
CC marks testis-specific genes in post-meiotic cells, including X-linked
CC genes that escape sex chromosome inactivation in haploid cells.
CC Crotonylation marks active promoters and enhancers and confers
CC resistance to transcriptional repressors. It is also associated with
CC post-meiotically activated genes on autosomes.
CC {ECO:0000269|PubMed:21925322}.
CC -!- PTM: Acetylated during spermatogenesis. Acetylated form is most
CC abundant in spermatogonia compared to spermatocytes and round
CC spermatids (By similarity). {ECO:0000250|UniProtKB:Q00729}.
CC -!- PTM: Phosphorylated at Thr-117 in spermatogonia, spermatocytes and
CC round spermatids. {ECO:0000250|UniProtKB:Q00729}.
CC -!- PTM: Methylated at Lys-118 in spermatogonia, spermatocytes and round
CC spermatids. {ECO:0000250|UniProtKB:Q00729}.
CC -!- PTM: Lactylated in macrophages by EP300/P300 by using lactoyl-CoA
CC directly derived from endogenous or exogenous lactate, leading to
CC stimulates gene transcription. {ECO:0000250|UniProtKB:P33778}.
CC -!- SIMILARITY: Belongs to the histone H2B family. {ECO:0000305}.
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DR EMBL; X90778; CAA62299.1; -; Genomic_DNA.
DR EMBL; AY158939; AAO06249.1; -; Genomic_DNA.
DR EMBL; AL606464; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS26373.1; -.
DR RefSeq; NP_783594.1; NM_175663.2.
DR PDB; 3X1T; X-ray; 2.81 A; D/H=2-127.
DR PDB; 3X1V; X-ray; 2.92 A; D/H=2-127.
DR PDBsum; 3X1T; -.
DR PDBsum; 3X1V; -.
DR AlphaFoldDB; P70696; -.
DR SMR; P70696; -.
DR BioGRID; 235096; 2.
DR CORUM; P70696; -.
DR IntAct; P70696; 1.
DR MINT; P70696; -.
DR STRING; 10090.ENSMUSP00000056604; -.
DR iPTMnet; P70696; -.
DR PhosphoSitePlus; P70696; -.
DR SwissPalm; P70696; -.
DR EPD; P70696; -.
DR jPOST; P70696; -.
DR MaxQB; P70696; -.
DR PaxDb; P70696; -.
DR PeptideAtlas; P70696; -.
DR PRIDE; P70696; -.
DR ProteomicsDB; 269793; -.
DR TopDownProteomics; P70696; -.
DR Antibodypedia; 3172; 319 antibodies from 21 providers.
DR DNASU; 319177; -.
DR Ensembl; ENSMUST00000052776; ENSMUSP00000056604; ENSMUSG00000050799.
DR GeneID; 319177; -.
DR KEGG; mmu:319177; -.
DR UCSC; uc007pvi.2; mouse.
DR CTD; 255626; -.
DR MGI; MGI:2448375; H2bc1.
DR VEuPathDB; HostDB:ENSMUSG00000050799; -.
DR eggNOG; KOG1744; Eukaryota.
DR GeneTree; ENSGT01050000244921; -.
DR HOGENOM; CLU_075666_2_1_1; -.
DR InParanoid; P70696; -.
DR OMA; ELAKHAX; -.
DR OrthoDB; 1536672at2759; -.
DR PhylomeDB; P70696; -.
DR TreeFam; TF300212; -.
DR BioGRID-ORCS; 319177; 8 hits in 74 CRISPR screens.
DR PRO; PR:P70696; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; P70696; protein.
DR Bgee; ENSMUSG00000050799; Expressed in spermatocyte and 12 other tissues.
DR GO; GO:0044815; C:DNA packaging complex; IDA:MGI.
DR GO; GO:0019897; C:extrinsic component of plasma membrane; IDA:MGI.
DR GO; GO:0001674; C:female germ cell nucleus; IDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0000786; C:nucleosome; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0003677; F:DNA binding; ISO:MGI.
DR GO; GO:0042393; F:histone binding; IDA:MGI.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR GO; GO:0030527; F:structural constituent of chromatin; IEA:InterPro.
DR GO; GO:0006325; P:chromatin organization; IDA:MGI.
DR GO; GO:0051276; P:chromosome organization; IDA:MGI.
DR GO; GO:0006954; P:inflammatory response; IMP:MGI.
DR GO; GO:0071674; P:mononuclear cell migration; IMP:MGI.
DR GO; GO:0006334; P:nucleosome assembly; IDA:MGI.
DR GO; GO:0006337; P:nucleosome disassembly; IMP:UniProtKB.
DR GO; GO:0031639; P:plasminogen activation; IMP:MGI.
DR GO; GO:0051099; P:positive regulation of binding; IMP:MGI.
DR GO; GO:0035093; P:spermatogenesis, exchange of chromosomal proteins; IMP:UniProtKB.
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 3D-structure; Acetylation; Chromosome; DNA-binding; Isopeptide bond;
KW Methylation; Nucleosome core; Nucleus; Phosphoprotein; Reference proteome;
KW Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P23527"
FT CHAIN 2..127
FT /note="Histone H2B type 1-A"
FT /id="PRO_0000071843"
FT MOD_RES 2
FT /note="N-acetylproline"
FT /evidence="ECO:0000250|UniProtKB:P23527"
FT MOD_RES 7
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q96A08"
FT MOD_RES 7
FT /note="N6-crotonyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:21925322"
FT MOD_RES 7
FT /note="N6-lactoyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:31645732"
FT MOD_RES 13
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P62807"
FT MOD_RES 13
FT /note="N6-crotonyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:21925322"
FT MOD_RES 13
FT /note="N6-lactoyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:31645732"
FT MOD_RES 14
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q96A08"
FT MOD_RES 14
FT /note="N6-crotonyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:21925322"
FT MOD_RES 17
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q96A08"
FT MOD_RES 17
FT /note="N6-crotonyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:21925322"
FT MOD_RES 17
FT /note="N6-lactoyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:31645732"
FT MOD_RES 18
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q00729"
FT MOD_RES 18
FT /note="N6-crotonyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:21925322"
FT MOD_RES 18
FT /note="N6-lactoyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:31645732"
FT MOD_RES 22
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q96A08"
FT MOD_RES 22
FT /note="N6-crotonyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:21925322"
FT MOD_RES 22
FT /note="N6-lactoyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:31645732"
FT MOD_RES 25
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P33778"
FT MOD_RES 25
FT /note="N6-crotonyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:21925322"
FT MOD_RES 25
FT /note="N6-lactoyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P33778"
FT MOD_RES 36
FT /note="N6-crotonyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:21925322"
FT MOD_RES 36
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P33778"
FT MOD_RES 38
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q64475"
FT MOD_RES 45
FT /note="N6-lactoyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P33778"
FT MOD_RES 48
FT /note="N6-methyllysine"
FT /evidence="ECO:0000250|UniProtKB:P62807"
FT MOD_RES 59
FT /note="N6,N6-dimethyllysine"
FT /evidence="ECO:0000250|UniProtKB:P62807"
FT MOD_RES 81
FT /note="Dimethylated arginine"
FT /evidence="ECO:0000250|UniProtKB:Q96A08"
FT MOD_RES 87
FT /note="N6,N6,N6-trimethyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q96A08"
FT MOD_RES 87
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q96A08"
FT MOD_RES 87
FT /note="N6-lactoyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:31645732"
FT MOD_RES 88
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q96A08"
FT MOD_RES 94
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q96A08"
FT MOD_RES 110
FT /note="N6-lactoyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:31645732"
FT MOD_RES 110
FT /note="N6-methyllysine"
FT /evidence="ECO:0000250|UniProtKB:P62807"
FT MOD_RES 117
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q00729"
FT MOD_RES 118
FT /note="N6-lactoyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:31645732"
FT MOD_RES 118
FT /note="N6-methylated lysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q00729"
FT MOD_RES 118
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P33778"
FT MOD_RES 122
FT /note="N6-lactoyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P33778"
FT MOD_RES 122
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P33778"
FT CROSSLNK 7
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P58876"
FT CROSSLNK 22
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q5QNW6"
FT CROSSLNK 36
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin); alternate"
FT /evidence="ECO:0000250|UniProtKB:P33778"
FT CROSSLNK 122
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q96A08"
FT HELIX 40..50
FT /evidence="ECO:0007829|PDB:3X1T"
FT HELIX 58..85
FT /evidence="ECO:0007829|PDB:3X1T"
FT STRAND 89..91
FT /evidence="ECO:0007829|PDB:3X1V"
FT HELIX 93..103
FT /evidence="ECO:0007829|PDB:3X1T"
FT HELIX 106..124
FT /evidence="ECO:0007829|PDB:3X1T"
SQ SEQUENCE 127 AA; 14237 MW; F9A6180E4D005AF5 CRC64;
MPEVAVKGAT ISKKGFKKAV TKTQKKEGRK RKRCRKESYS IYIYKVLKQV HPDTGISSKA
MSIMNSFVTD IFERIASEAS RLAHYNKRST ITSREIQTAV RLLLPGELAK HAVSEGTKAV
TKYTSSK
