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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.
02-JUN-2021, entry version 163.
RecName: Full=Histone H2B type 1-A;
AltName: Full=Histone H2B, testis;
AltName: Full=Testis-specific histone H2B {ECO:0000303|PubMed:23884607};
Name=H2bc1 {ECO:0000312|MGI:MGI:2448375};
Synonyms=Hist1h2ba {ECO:0000312|MGI:MGI:2448375},
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 H2AB1.
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).
[8]
LACTYLATION AT LYS-6; LYS-12; LYS-16; LYS-17; LYS-21; LYS-86; LYS-109 AND
LYS-117.
PubMed=31645732; DOI=10.1038/s41586-019-1678-1;
Zhang D., Tang Z., Huang H., Zhou G., Cui C., Weng Y., Liu W., Kim S.,
Lee S., Perez-Neut M., Ding J., Czyz D., Hu R., Ye Z., He M., Zheng Y.G.,
Shuman H.A., Dai L., Ren B., Roeder R.G., Becker L., Zhao Y.;
"Metabolic regulation of gene expression by histone lactylation.";
Nature 574:575-580(2019).
-!- 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
H2AB1 and H2BC1/TH2B is loaded onto the nucleosomes and promotes
loading of transition proteins (TNP1 and TNP2) onto the nucleosomes
(PubMed:28366643). Inclusion of the H2AB1-H2BC1/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 H2AB1;
preferentially dimerizes with H2AB1 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}.
-!- PTM: Lactylated in macrophages by EP300/P300 by using lactoyl-CoA
directly derived from endogenous or exogenous lactate, leading to
stimulates gene transcription. {ECO:0000250|UniProtKB:P33778}.
-!- 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; -; NOT_ANNOTATED_CDS; Genomic_DNA.
CCDS; CCDS26373.1; -.
RefSeq; NP_783594.1; NM_175663.2.
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; -.
SMR; P70696; -.
BioGRID; 235096; 2.
CORUM; P70696; -.
IntAct; P70696; 1.
MINT; P70696; -.
STRING; 10090.ENSMUSP00000056604; -.
iPTMnet; P70696; -.
PhosphoSitePlus; P70696; -.
SwissPalm; P70696; -.
EPD; P70696; -.
jPOST; P70696; -.
MaxQB; P70696; -.
PaxDb; P70696; -.
PeptideAtlas; P70696; -.
PRIDE; P70696; -.
ProteomicsDB; 269793; -.
TopDownProteomics; P70696; -.
Antibodypedia; 3172; 310 antibodies.
DNASU; 319177; -.
Ensembl; ENSMUST00000052776; ENSMUSP00000056604; ENSMUSG00000050799.
GeneID; 319177; -.
KEGG; mmu:319177; -.
UCSC; uc007pvi.2; mouse.
CTD; 255626; -.
MGI; MGI:2448375; H2bc1.
eggNOG; KOG1744; Eukaryota.
GeneTree; ENSGT01030000234632; -.
HOGENOM; CLU_075666_2_1_1; -.
InParanoid; P70696; -.
OMA; THKSGIS; -.
OrthoDB; 1536672at2759; -.
PhylomeDB; P70696; -.
TreeFam; TF300212; -.
Reactome; R-MMU-110330; Recognition and association of DNA glycosylase with site containing an affected purine.
Reactome; R-MMU-110331; Cleavage of the damaged purine.
Reactome; R-MMU-212300; PRC2 methylates histones and DNA.
Reactome; R-MMU-2299718; Condensation of Prophase Chromosomes.
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-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-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.
Reactome; R-MMU-9670095; Inhibition of DNA recombination at telomere.
BioGRID-ORCS; 319177; 7 hits in 54 CRISPR screens.
PRO; PR:P70696; -.
Proteomes; UP000000589; Chromosome 13.
RNAct; P70696; protein.
Bgee; ENSMUSG00000050799; Expressed in spermatocyte and 28 other tissues.
GO; GO:0044815; C:DNA packaging complex; IDA:MGI.
GO; GO:0019897; C:extrinsic component of plasma membrane; IDA:MGI.
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; IDA:MGI.
GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
GO; GO:0006325; P:chromatin organization; IDA:MGI.
GO; GO:0006323; P:DNA packaging; 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; IDA:MGI.
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; DNA-binding; Isopeptide bond;
Methylation; Nucleosome core; Nucleus; Phosphoprotein; Reference proteome;
Ubl conjugation.
INIT_MET 1
/note="Removed"
/evidence="ECO:0000250|UniProtKB:P23527"
CHAIN 2..127
/note="Histone H2B type 1-A"
/id="PRO_0000071843"
MOD_RES 2
/note="N-acetylproline"
/evidence="ECO:0000250|UniProtKB:P23527"
MOD_RES 7
/note="N6-acetyllysine; alternate"
/evidence="ECO:0000250|UniProtKB:Q96A08"
MOD_RES 7
/note="N6-crotonyllysine; alternate"
/evidence="ECO:0000269|PubMed:21925322"
MOD_RES 7
/note="N6-lactoyllysine; alternate"
/evidence="ECO:0000269|PubMed:31645732"
MOD_RES 13
/note="N6-acetyllysine; alternate"
/evidence="ECO:0000250|UniProtKB:P62807"
MOD_RES 13
/note="N6-crotonyllysine; alternate"
/evidence="ECO:0000269|PubMed:21925322"
MOD_RES 13
/note="N6-lactoyllysine; alternate"
/evidence="ECO:0000269|PubMed:31645732"
MOD_RES 14
/note="N6-acetyllysine; alternate"
/evidence="ECO:0000250|UniProtKB:Q96A08"
MOD_RES 14
/note="N6-crotonyllysine; alternate"
/evidence="ECO:0000269|PubMed:21925322"
MOD_RES 17
/note="N6-acetyllysine; alternate"
/evidence="ECO:0000250|UniProtKB:Q96A08"
MOD_RES 17
/note="N6-crotonyllysine; alternate"
/evidence="ECO:0000269|PubMed:21925322"
MOD_RES 17
/note="N6-lactoyllysine; alternate"
/evidence="ECO:0000269|PubMed:31645732"
MOD_RES 18
/note="N6-acetyllysine; alternate"
/evidence="ECO:0000250|UniProtKB:Q00729"
MOD_RES 18
/note="N6-crotonyllysine; alternate"
/evidence="ECO:0000269|PubMed:21925322"
MOD_RES 18
/note="N6-lactoyllysine; alternate"
/evidence="ECO:0000269|PubMed:31645732"
MOD_RES 22
/note="N6-acetyllysine; alternate"
/evidence="ECO:0000250|UniProtKB:Q96A08"
MOD_RES 22
/note="N6-crotonyllysine; alternate"
/evidence="ECO:0000269|PubMed:21925322"
MOD_RES 22
/note="N6-lactoyllysine; alternate"
/evidence="ECO:0000269|PubMed:31645732"
MOD_RES 25
/note="N6-acetyllysine; alternate"
/evidence="ECO:0000250|UniProtKB:P33778"
MOD_RES 25
/note="N6-crotonyllysine; alternate"
/evidence="ECO:0000269|PubMed:21925322"
MOD_RES 25
/note="N6-lactoyllysine; alternate"
/evidence="ECO:0000250|UniProtKB:P33778"
MOD_RES 36
/note="N6-crotonyllysine; alternate"
/evidence="ECO:0000269|PubMed:21925322"
MOD_RES 36
/note="N6-succinyllysine; alternate"
/evidence="ECO:0000250|UniProtKB:P33778"
MOD_RES 38
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:Q64475"
MOD_RES 45
/note="N6-lactoyllysine; alternate"
/evidence="ECO:0000250|UniProtKB:P33778"
MOD_RES 48
/note="N6-methyllysine"
/evidence="ECO:0000250|UniProtKB:P62807"
MOD_RES 59
/note="N6,N6-dimethyllysine"
/evidence="ECO:0000250|UniProtKB:P62807"
MOD_RES 81
/note="Dimethylated arginine"
/evidence="ECO:0000250|UniProtKB:Q96A08"
MOD_RES 87
/note="N6,N6,N6-trimethyllysine; alternate"
/evidence="ECO:0000250|UniProtKB:Q96A08"
MOD_RES 87
/note="N6-acetyllysine; alternate"
/evidence="ECO:0000250|UniProtKB:Q96A08"
MOD_RES 87
/note="N6-lactoyllysine; alternate"
/evidence="ECO:0000269|PubMed:31645732"
MOD_RES 88
/note="Omega-N-methylarginine"
/evidence="ECO:0000250|UniProtKB:Q96A08"
MOD_RES 94
/note="Omega-N-methylarginine"
/evidence="ECO:0000250|UniProtKB:Q96A08"
MOD_RES 110
/note="N6-lactoyllysine; alternate"
/evidence="ECO:0000269|PubMed:31645732"
MOD_RES 110
/note="N6-methyllysine"
/evidence="ECO:0000250|UniProtKB:P62807"
MOD_RES 117
/note="Phosphothreonine"
/evidence="ECO:0000250|UniProtKB:Q00729"
MOD_RES 118
/note="N6-lactoyllysine; alternate"
/evidence="ECO:0000269|PubMed:31645732"
MOD_RES 118
/note="N6-methylated lysine; alternate"
/evidence="ECO:0000250|UniProtKB:Q00729"
MOD_RES 118
/note="N6-succinyllysine; alternate"
/evidence="ECO:0000250|UniProtKB:P33778"
MOD_RES 122
/note="N6-lactoyllysine; alternate"
/evidence="ECO:0000250|UniProtKB:P33778"
MOD_RES 122
/note="N6-succinyllysine; alternate"
/evidence="ECO:0000250|UniProtKB:P33778"
CROSSLNK 7
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO2); alternate"
/evidence="ECO:0000250|UniProtKB:P58876"
CROSSLNK 22
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in SUMO2); alternate"
/evidence="ECO:0000250|UniProtKB:Q5QNW6"
CROSSLNK 36
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in ubiquitin); alternate"
/evidence="ECO:0000250|UniProtKB:P33778"
CROSSLNK 122
/note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
G-Cter in ubiquitin); alternate"
/evidence="ECO:0000250|UniProtKB:Q96A08"
HELIX 40..50
/evidence="ECO:0007829|PDB:3X1T"
HELIX 58..85
/evidence="ECO:0007829|PDB:3X1T"
STRAND 89..91
/evidence="ECO:0007829|PDB:3X1V"
HELIX 93..103
/evidence="ECO:0007829|PDB:3X1T"
HELIX 106..124
/evidence="ECO:0007829|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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WP1017: Type II interferon signaling (IFNG)
WP1289: Type II interferon signaling (IFNG)
WP2113: Type III interferon signaling
WP585: Interferon type I
WP900: Type II interferon signaling (IFNG)
WP1253: Type II interferon signaling (IFNG)
WP1584: Type II diabetes mellitus
WP786: Type II interferon signaling (IFNG)
WP1136: Type II interferon signaling (IFNG)
WP1350: Type II interferon signaling (IFNG)
WP2272: Pathogenic Escherichia coli infection
WP619: Type II interferon signaling (IFNG)

Related Genes :
[H2BC1 HIST1H2BA TSH2B] Histone H2B type 1-A (Histone H2B, testis) (TSH2B.1) (hTSH2B) (Testis-specific histone H2B)
[H2bc1 Hist1h2ba Th2b] Histone H2B type 1-A (Histone H2B, testis) (Testis-specific histone H2B)
[H2bc1 Hist1h2ba Th2b] Histone H2B type 1-A (Histone H2B, testis) (Testis-specific histone H2B)
[H2BC4 H2BFL HIST1H2BC; H2BC6 H2BFH HIST1H2BE; H2BC7 H2BFG HIST1H2BF; H2BC8 H2BFA HIST1H2BG; H2BC10 H2BFK HIST1H2BI] Histone H2B type 1-C/E/F/G/I (Histone H2B.1 A) (Histone H2B.a) (H2B/a) (Histone H2B.g) (H2B/g) (Histone H2B.h) (H2B/h) (Histone H2B.k) (H2B/k) (Histone H2B.l) (H2B/l)
[H2BC5 H2BFB HIRIP2 HIST1H2BD] Histone H2B type 1-D (H2B-clustered histone 5) (HIRA-interacting protein 2) (Histone H2B.1 B) (Histone H2B.b) (H2B/b)
[H2BC3 H2BFF HIST1H2BB] Histone H2B type 1-B (H2B-clustered histone 3) (Histone H2B.1) (Histone H2B.f) (H2B/f)
[H2BC17 H2BFH H2BFN HIST1H2BO] Histone H2B type 1-O (H2B-clustered histone 17) (Histone H2B.2) (Histone H2B.n) (H2B/n)
[H2BC11 H2BFR HIST1H2BJ] Histone H2B type 1-J (Histone H2B.1) (Histone H2B.r) (H2B/r)
[H2BS1 H2BFS] Histone H2B type F-S (H2B.S histone 1) (Histone H2B.s) (H2B/s)
[H2BC9 H2BFJ HIST1H2BH] Histone H2B type 1-H (H2B-clustered histone 9) (Histone H2B.j) (H2B/j)
[H2BC21 H2BFQ HIST2H2BE] Histone H2B type 2-E (H2B-clustered histone 21) (Histone H2B-GL105) (Histone H2B.q) (H2B/q)
[H2bc7 H2b-f Hist1h2bf; H2bc11 H2b-j Hist1h2bj; H2bc13 H2b-l Hist1h2bl; H2bc15 H2b-n Hist1h2bn] Histone H2B type 1-F/J/L (H2B 291A)
[H2BU1 HIST3H2BB] Histone H2B type 3-B (H2B type 12) (H2B.U histone 1)
[H2BC14 H2BFE HIST1H2BM] Histone H2B type 1-M (Histone H2B.e) (H2B/e)
[H2BC13 H2BFC HIST1H2BL] Histone H2B type 1-L (Histone H2B.c) (H2B/c)
[H2BC15 H2BFD HIST1H2BN] Histone H2B type 1-N (Histone H2B.d) (H2B/d)
[H2bc3 Hist1h2bb] Histone H2B type 1-B (H2B-clustered histone 3) (h2B-143)
[H2bu1 H2bu1-ps Hist3h2bb Hist3h2bb-ps] Histone H2B type 3-B (H2B.U histone 1)
[H2bc9 Hist1h2bh] Histone H2B type 1-H (H2B-clustered histone 9) (h2B-221)
[H2bc21 Hist2h2be] Histone H2B type 2-E (H2B-clustered histone 21) (H2b 613)
[H2BC12 H2BFT HIRIP1 HIST1H2BK] Histone H2B type 1-K (H2B K) (HIRA-interacting protein 1)
[H2bc14 Hist1h2bm] Histone H2B type 1-M (H2B 291B)
[H2BC18 HIST2H2BF] Histone H2B type 2-F (H2B-clustered histone 18)
[Hist1h2bp] Histone H2B type 1-P
[H2BC20P HIST2H2BC] Putative histone H2B type 2-C (H2B-clustered histone 20 pseudogene) (Histone H2B.t) (H2B/t)
[H2bc4 Hist1h2bc; H2bc6 Hist1h2be; H2bc8 Hist1h2bg] Histone H2B type 1-C/E/G
[H2bc12 Hist1h2bk] Histone H2B type 1-K
[Hist2h2bb] Histone H2B type 2-B (H2b 616)
[Hist3h2ba] Histone H2B type 3-A
[H2BC19P HIST2H2BD] Putative histone H2B type 2-D (H2B-clustered histone 19 pseudogene)

Bibliography :
[30939211] Differential localization of histone variant TH2B during the first round compared with subsequent rounds of spermatogenesis.
[29453813] Association between two common transitions of H2BFWT gene and male infertility: a case-control, meta, and structural analysis.
[27992841] Structural analyses of the nucleosome complexes with human testis-specific histone variants, hTh2a and hTh2b.
[25252820] Mapping post-translational modifications of mammalian testicular specific histone variant TH2B in tetraploid and haploid germ cells and their implications on the dynamics of nucleosome structure.
[24025782] In vivo study on the effects of microcystin-LR on the apoptosis, proliferation and differentiation of rat testicular spermatogenic cells of male rats injected i.p. with toxins.
[9712314] Localization and quantitative expression of mRNAs encoding the testis-specific histone TH2B, the phosphoprotein p19, the transition proteins 1 and 2 during pubertal development and throughout the spermatogenic cycle of the rat.
[9688392] Immunoexpression of testis-specific histone 2B in human spermatozoa and testis tissue.
[8562066] Increased accessibility of the N-terminus of testis-specific histone TH2B to antibodies in elongating spermatids.