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Histone H2B type 1-A (Histone H2B, testis) (Testis-specific histone H2B)

 H2B1A_MOUSE             Reviewed;         127 AA.
P70696; Q5NCL9;
16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
05-DEC-2018, entry version 147.
RecName: Full=Histone H2B type 1-A;
AltName: Full=Histone H2B, testis;
AltName: Full=Testis-specific histone H2B {ECO:0000303|PubMed:23884607};
Name=Hist1h2ba {ECO:0000312|MGI:MGI:2448375};
Synonyms=Th2b {ECO:0000303|PubMed:23884607};
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
TISSUE=Kidney;
PubMed=8672246; DOI=10.1089/dna.1996.15.495;
Choi Y.C., Gu W., Hecht N.B., Feinberg A.P., Chae C.-B.;
"Molecular cloning of mouse somatic and testis-specific H2B histone
genes containing a methylated CpG island.";
DNA Cell Biol. 15:495-504(1996).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=12408966; DOI=10.1006/geno.2002.6850;
Marzluff W.F., Gongidi P., Woods K.R., Jin J., Maltais L.J.;
"The human and mouse replication-dependent histone genes.";
Genomics 80:487-498(2002).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[4]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[5]
CROTONYLATION AT LYS-7; LYS-13; LYS-14; LYS-17; LYS-18; LYS-22; LYS-25
AND LYS-36.
PubMed=21925322; DOI=10.1016/j.cell.2011.08.008;
Tan M., Luo H., Lee S., Jin F., Yang J.S., Montellier E., Buchou T.,
Cheng Z., Rousseaux S., Rajagopal N., Lu Z., Ye Z., Zhu Q.,
Wysocka J., Ye Y., Khochbin S., Ren B., Zhao Y.;
"Identification of 67 histone marks and histone lysine crotonylation
as a new type of histone modification.";
Cell 146:1016-1028(2011).
[6]
FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, TISSUE SPECIFICITY, AND
DEVELOPMENTAL STAGE.
PubMed=23884607; DOI=10.1101/gad.220095.113;
Montellier E., Boussouar F., Rousseaux S., Zhang K., Buchou T.,
Fenaille F., Shiota H., Debernardi A., Hery P., Curtet S.,
Jamshidikia M., Barral S., Holota H., Bergon A., Lopez F.,
Guardiola P., Pernet K., Imbert J., Petosa C., Tan M., Zhao Y.,
Gerard M., Khochbin S.;
"Chromatin-to-nucleoprotamine transition is controlled by the histone
H2B variant TH2B.";
Genes Dev. 27:1680-1692(2013).
[7]
FUNCTION, AND INTERACTION WITH H2AFB1.
PubMed=28366643; DOI=10.1016/j.molcel.2017.02.025;
Barral S., Morozumi Y., Tanaka H., Montellier E., Govin J.,
de Dieuleveult M., Charbonnier G., Coute Y., Puthier D., Buchou T.,
Boussouar F., Urahama T., Fenaille F., Curtet S., Hery P.,
Fernandez-Nunez N., Shiota H., Gerard M., Rousseaux S., Kurumizaka H.,
Khochbin S.;
"Histone variant H2A.L.2 guides transition protein-dependent protamine
assembly in male germ cells.";
Mol. Cell 66:89-101(2017).
-!- FUNCTION: Variant histone specifically required to direct the
transformation of dissociating nucleosomes to protamine in male
germ cells (PubMed:23884607, PubMed:28366643). Entirely replaces
classical histone H2B prior nucleosome to protamine transition and
probably acts as a nucleosome dissociating factor that creates a
more dynamic chromatin, facilitating the large-scale exchange of
histones (PubMed:23884607). In condensing spermatids, the
heterodimer between H2AFB1 and HIST1H2BA/TH2B is loaded onto the
nucleosomes and promotes loading of transition proteins (TNP1 and
TNP2) onto the nucleosomes (PubMed:28366643). Inclusion of the
H2AFB1-HIST1H2BA/TH2B dimer into chromatin opens the nucleosomes,
releasing the nucleosomal DNA ends and allowing the invasion of
nucleosomes by transition proteins (TNP1 and TNP2)
(PubMed:28366643). Then, transition proteins drive the recruitment
and processing of protamines, which are responsible for histone
eviction (PubMed:28366643). Also expressed maternally and is
present in the female pronucleus, suggesting a similar role in
protamine replacement by nucleosomes at fertilization
(PubMed:23884607). Core component of nucleosome. Nucleosomes wrap
and compact DNA into chromatin, limiting DNA accessibility to the
cellular machineries which require DNA as a template. Histones
thereby play a central role in transcription regulation, DNA
repair, DNA replication and chromosomal stability. DNA
accessibility is regulated via a complex set of post-translational
modifications of histones, also called histone code, and
nucleosome remodeling. {ECO:0000269|PubMed:23884607,
ECO:0000269|PubMed:28366643}.
-!- SUBUNIT: The nucleosome is a histone octamer containing two
molecules each of H2A, H2B, H3 and H4 assembled in one H3-H4
heterotetramer and two H2A-H2B heterodimers (PubMed:23884607).
Interacts with H2AFB1; preferentially dimerizes with H2AFB1 to
form nucleosomes (PubMed:28366643). {ECO:0000269|PubMed:23884607,
ECO:0000269|PubMed:28366643}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:23884607}.
Chromosome {ECO:0000269|PubMed:23884607}.
-!- TISSUE SPECIFICITY: Mainly expressed in testis, and the
corresponding protein is also present in mature sperm. Also
present in metaphase oocytes (at protein level).
{ECO:0000269|PubMed:23884607, ECO:0000269|PubMed:8672246}.
-!- DEVELOPMENTAL STAGE: Accumulates at 10 day postpartum (dpp), when
pre-leptotene/leptotene spermatocytes first appear and when H2B
expression shows a drastic decrease. Replaces H2B by 18 dpp in
spermatocytes. Also present in metaphase oocytes and in the female
pronucleus at fertilization and is also rapidly incorporated into
the male pronucleus. {ECO:0000269|PubMed:23884607}.
-!- PTM: Monoubiquitination at Lys-36 by the MSL1/MSL2 dimer is
required for histone H3 'Lys-4' (H3K4me) and 'Lys-79' (H3K79me)
methylation and transcription activation at specific gene loci,
such as HOXA9 and MEIS1 loci. Similarly, monoubiquitination of
Lys-122 (H2BK120Ub) by the RNF20/40 complex gives a specific tag
for epigenetic transcriptional activation and is also prerequisite
for histone H3 'Lys-4' and 'Lys-79' methylation. It also functions
cooperatively with the FACT dimer to stimulate elongation by RNA
polymerase II. H2BK120Ub also acts as a regulator of mRNA
splicing: deubiquitination by USP49 is required for efficient
cotranscriptional splicing of a large set of exons (By
similarity). {ECO:0000250|UniProtKB:Q96A08}.
-!- PTM: Crotonylation (Kcr) is specifically present in male germ
cells and marks testis-specific genes in post-meiotic cells,
including X-linked genes that escape sex chromosome inactivation
in haploid cells. Crotonylation marks active promoters and
enhancers and confers resistance to transcriptional repressors. It
is also associated with post-meiotically activated genes on
autosomes. {ECO:0000269|PubMed:21925322}.
-!- PTM: Acetylated during spermatogenesis. Acetylated form is most
abundant in spermatogonia compared to spermatocytes and round
spermatids (By similarity). {ECO:0000250|UniProtKB:Q00729}.
-!- PTM: Phosphorylated at Thr-117 in spermatogonia, spermatocytes and
round spermatids. {ECO:0000250|UniProtKB:Q00729}.
-!- PTM: Methylated at Lys-118 in spermatogonia, spermatocytes and
round spermatids. {ECO:0000250|UniProtKB:Q00729}.
-!- SIMILARITY: Belongs to the histone H2B family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; X90778; CAA62299.1; -; Genomic_DNA.
EMBL; AY158939; AAO06249.1; -; Genomic_DNA.
EMBL; AL606464; CAI35973.1; -; Genomic_DNA.
CCDS; CCDS26373.1; -.
RefSeq; NP_783594.1; NM_175663.2.
UniGene; Mm.377879; -.
PDB; 3X1T; X-ray; 2.81 A; D/H=2-127.
PDB; 3X1V; X-ray; 2.92 A; D/H=2-127.
PDBsum; 3X1T; -.
PDBsum; 3X1V; -.
ProteinModelPortal; P70696; -.
SMR; P70696; -.
BioGrid; 235096; 2.
CORUM; P70696; -.
IntAct; P70696; 1.
MINT; P70696; -.
STRING; 10090.ENSMUSP00000056604; -.
iPTMnet; P70696; -.
PhosphoSitePlus; P70696; -.
EPD; P70696; -.
MaxQB; P70696; -.
PaxDb; P70696; -.
PeptideAtlas; P70696; -.
PRIDE; P70696; -.
TopDownProteomics; P70696; -.
Ensembl; ENSMUST00000052776; ENSMUSP00000056604; ENSMUSG00000050799.
GeneID; 319177; -.
KEGG; mmu:319177; -.
UCSC; uc007pvi.2; mouse.
CTD; 255626; -.
MGI; MGI:2448375; Hist1h2ba.
eggNOG; KOG1744; Eukaryota.
eggNOG; ENOG4111NV5; LUCA.
GeneTree; ENSGT00940000153443; -.
HOGENOM; HOG000231213; -.
HOVERGEN; HBG007774; -.
InParanoid; P70696; -.
KO; K11252; -.
OMA; CKGTTIS; -.
OrthoDB; EOG091G0XGD; -.
PhylomeDB; P70696; -.
TreeFam; TF300212; -.
Reactome; R-MMU-171306; Packaging Of Telomere Ends.
Reactome; R-MMU-201722; Formation of the beta-catenin:TCF transactivating complex.
Reactome; R-MMU-212300; PRC2 methylates histones and DNA.
Reactome; R-MMU-2299718; Condensation of Prophase Chromosomes.
Reactome; R-MMU-2559580; Oxidative Stress Induced Senescence.
Reactome; R-MMU-2559582; Senescence-Associated Secretory Phenotype (SASP).
Reactome; R-MMU-2559586; DNA Damage/Telomere Stress Induced Senescence.
Reactome; R-MMU-3214815; HDACs deacetylate histones.
Reactome; R-MMU-3214847; HATs acetylate histones.
Reactome; R-MMU-427359; SIRT1 negatively regulates rRNA expression.
Reactome; R-MMU-427413; NoRC negatively regulates rRNA expression.
Reactome; R-MMU-5250924; B-WICH complex positively regulates rRNA expression.
Reactome; R-MMU-5578749; Transcriptional regulation by small RNAs.
Reactome; R-MMU-5625886; Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3.
Reactome; R-MMU-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
Reactome; R-MMU-5693571; Nonhomologous End-Joining (NHEJ).
Reactome; R-MMU-5693607; Processing of DNA double-strand break ends.
Reactome; R-MMU-606279; Deposition of new CENPA-containing nucleosomes at the centromere.
Reactome; R-MMU-69473; G2/M DNA damage checkpoint.
Reactome; R-MMU-73728; RNA Polymerase I Promoter Opening.
Reactome; R-MMU-73777; RNA Polymerase I Chain Elongation.
Reactome; R-MMU-8866654; E3 ubiquitin ligases ubiquitinate target proteins.
Reactome; R-MMU-8936459; RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function.
Reactome; R-MMU-9018519; Estrogen-dependent gene expression.
PRO; PR:P70696; -.
Proteomes; UP000000589; Chromosome 13.
Bgee; ENSMUSG00000050799; Expressed in 7 organ(s), highest expression level in testis.
CleanEx; MM_HIST1H2BA; -.
GO; GO:0019897; C:extrinsic component of plasma membrane; IDA:MGI.
GO; GO:0000788; C:nuclear nucleosome; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0000786; C:nucleosome; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:MGI.
GO; GO:0003677; F:DNA binding; ISO:MGI.
GO; GO:0042393; F:histone binding; IPI:UniProtKB.
GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
GO; GO:0006325; P:chromatin organization; IDA:MGI.
GO; GO:0006954; P:inflammatory response; IMP:MGI.
GO; GO:0071674; P:mononuclear cell migration; IMP:MGI.
GO; GO:0006334; P:nucleosome assembly; IMP:UniProtKB.
GO; GO:0006337; P:nucleosome disassembly; IMP:UniProtKB.
GO; GO:0031639; P:plasminogen activation; IMP:MGI.
GO; GO:0051099; P:positive regulation of binding; IMP:MGI.
GO; GO:0035093; P:spermatogenesis, exchange of chromosomal proteins; IMP:UniProtKB.
Gene3D; 1.10.20.10; -; 1.
InterPro; IPR009072; Histone-fold.
InterPro; IPR007125; Histone_H2A/H2B/H3.
InterPro; IPR000558; Histone_H2B.
PANTHER; PTHR23428; PTHR23428; 1.
Pfam; PF00125; Histone; 1.
PRINTS; PR00621; HISTONEH2B.
SMART; SM00427; H2B; 1.
SUPFAM; SSF47113; SSF47113; 1.
PROSITE; PS00357; HISTONE_H2B; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Chromosome; Complete proteome; DNA-binding;
Isopeptide bond; Methylation; Nucleosome core; Nucleus;
Phosphoprotein; Reference proteome; Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:P23527}.
CHAIN 2 127 Histone H2B type 1-A.
/FTId=PRO_0000071843.
MOD_RES 2 2 N-acetylproline.
{ECO:0000250|UniProtKB:P23527}.
MOD_RES 7 7 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q96A08}.
MOD_RES 7 7 N6-crotonyllysine; alternate.
{ECO:0000269|PubMed:21925322}.
MOD_RES 13 13 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P62807}.
MOD_RES 13 13 N6-crotonyllysine; alternate.
{ECO:0000269|PubMed:21925322}.
MOD_RES 14 14 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q96A08}.
MOD_RES 14 14 N6-crotonyllysine; alternate.
{ECO:0000269|PubMed:21925322}.
MOD_RES 17 17 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q96A08}.
MOD_RES 17 17 N6-crotonyllysine; alternate.
{ECO:0000269|PubMed:21925322}.
MOD_RES 18 18 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q00729}.
MOD_RES 18 18 N6-crotonyllysine; alternate.
{ECO:0000269|PubMed:21925322}.
MOD_RES 22 22 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q96A08}.
MOD_RES 22 22 N6-crotonyllysine; alternate.
{ECO:0000269|PubMed:21925322}.
MOD_RES 25 25 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P33778}.
MOD_RES 25 25 N6-crotonyllysine; alternate.
{ECO:0000269|PubMed:21925322}.
MOD_RES 36 36 N6-crotonyllysine; alternate.
{ECO:0000269|PubMed:21925322}.
MOD_RES 36 36 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P33778}.
MOD_RES 38 38 Phosphoserine.
{ECO:0000250|UniProtKB:Q64475}.
MOD_RES 48 48 N6-methyllysine.
{ECO:0000250|UniProtKB:P62807}.
MOD_RES 59 59 N6,N6-dimethyllysine.
{ECO:0000250|UniProtKB:P62807}.
MOD_RES 81 81 Dimethylated arginine.
{ECO:0000250|UniProtKB:Q96A08}.
MOD_RES 87 87 N6,N6,N6-trimethyllysine; alternate.
{ECO:0000250|UniProtKB:Q96A08}.
MOD_RES 87 87 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q96A08}.
MOD_RES 88 88 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:Q96A08}.
MOD_RES 94 94 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:Q96A08}.
MOD_RES 110 110 N6-methyllysine.
{ECO:0000250|UniProtKB:P62807}.
MOD_RES 117 117 Phosphothreonine.
{ECO:0000250|UniProtKB:Q00729}.
MOD_RES 118 118 N6-methylated lysine; alternate.
{ECO:0000250|UniProtKB:Q00729}.
MOD_RES 118 118 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P33778}.
MOD_RES 122 122 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P33778}.
CROSSLNK 7 7 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:P58876}.
CROSSLNK 22 22 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:Q5QNW6}.
CROSSLNK 36 36 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin);
alternate.
{ECO:0000250|UniProtKB:P33778}.
CROSSLNK 122 122 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin);
alternate.
{ECO:0000250|UniProtKB:Q96A08}.
HELIX 40 50 {ECO:0000244|PDB:3X1T}.
HELIX 58 85 {ECO:0000244|PDB:3X1T}.
STRAND 89 91 {ECO:0000244|PDB:3X1V}.
HELIX 93 103 {ECO:0000244|PDB:3X1T}.
HELIX 106 124 {ECO:0000244|PDB:3X1T}.
SEQUENCE 127 AA; 14237 MW; F9A6180E4D005AF5 CRC64;
MPEVAVKGAT ISKKGFKKAV TKTQKKEGRK RKRCRKESYS IYIYKVLKQV HPDTGISSKA
MSIMNSFVTD IFERIASEAS RLAHYNKRST ITSREIQTAV RLLLPGELAK HAVSEGTKAV
TKYTSSK


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