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Histone H2B type 1-J (Histone H2B.1) (Histone H2B.r) (H2B/r)

 H2B1J_HUMAN             Reviewed;         126 AA.
P06899; B2R4J4; O60816;
01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
22-NOV-2017, entry version 177.
RecName: Full=Histone H2B type 1-J;
AltName: Full=Histone H2B.1;
AltName: Full=Histone H2B.r;
Short=H2B/r;
Name=HIST1H2BJ; Synonyms=H2BFR;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=6647026; DOI=10.1093/nar/11.21.7409;
Zhong R., Roeder R.G., Heintz N.;
"The primary structure and expression of four cloned human histone
genes.";
Nucleic Acids Res. 11:7409-7425(1983).
[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 MRNA].
TISSUE=Hippocampus;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=14574404; DOI=10.1038/nature02055;
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
"The DNA sequence and analysis of human chromosome 6.";
Nature 425:805-811(2003).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[6]
PROTEIN SEQUENCE OF 2-27.
PubMed=2917990;
Alnemri E.S., Litwack G.;
"Glucocorticoid-induced lymphocytolysis is not mediated by an induced
endonuclease.";
J. Biol. Chem. 264:4104-4111(1989).
[7]
PROTEIN SEQUENCE OF 2-21, AND FUNCTION.
PubMed=11859126; DOI=10.4049/jimmunol.168.5.2356;
Kim H.S., Cho J.H., Park H.W., Yoon H., Kim M.S., Kim S.C.;
"Endotoxin-neutralizing antimicrobial proteins of the human
placenta.";
J. Immunol. 168:2356-2364(2002).
[8]
PROTEIN SEQUENCE OF 2-13.
PubMed=8620898; DOI=10.1111/j.1432-1033.1996.0086n.x;
Frohm M., Gunne H., Bergman A.-C., Agerberth B., Bergman T., Boman A.,
Liden S., Joernvall H., Boman H.G.;
"Biochemical and antibacterial analysis of human wound and blister
fluid.";
Eur. J. Biochem. 237:86-92(1996).
[9]
PROTEIN SEQUENCE OF 2-13, AND FUNCTION.
PubMed=12860195; DOI=10.1016/S0196-9781(03)00114-1;
Tollin M., Bergman P., Svenberg T., Joernvall H., Gudmundsson G.H.,
Agerberth B.;
"Antimicrobial peptides in the first line defence of human colon
mucosa.";
Peptides 24:523-530(2003).
[10]
PROTEIN SEQUENCE OF 2-13, AND FUNCTION.
PubMed=15019208; DOI=10.1016/j.peptides.2003.07.028;
Howell S.J., Wilk D., Yadav S.P., Bevins C.L.;
"Antimicrobial polypeptides of the human colonic epithelium.";
Peptides 24:1763-1770(2003).
[11]
PROTEIN SEQUENCE OF 7-24, ACETYLATION AT LYS-6; LYS-12; LYS-13;
LYS-16; LYS-17 AND LYS-21, METHYLATION AT LYS-47; LYS-58 AND LYS-109,
UBIQUITINATION AT LYS-121, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=16627869; DOI=10.1074/mcp.M600007-MCP200;
Beck H.C., Nielsen E.C., Matthiesen R., Jensen L.H., Sehested M.,
Finn P., Grauslund M., Hansen A.M., Jensen O.N.;
"Quantitative proteomic analysis of post-translational modifications
of human histones.";
Mol. Cell. Proteomics 5:1314-1325(2006).
[12]
IDENTIFICATION BY MASS SPECTROMETRY, AND METHYLATION.
PubMed=11709551; DOI=10.1074/jbc.M107894200;
Galasinski S.C., Louie D.F., Gloor K.K., Resing K.A., Ahn N.G.;
"Global regulation of post-translational modifications on core
histones.";
J. Biol. Chem. 277:2579-2588(2002).
[13]
PHOSPHORYLATION AT SER-15.
PubMed=12757711; DOI=10.1016/S0092-8674(03)00355-6;
Cheung W.L., Ajiro K., Samejima K., Kloc M., Cheung P., Mizzen C.A.,
Beeser A., Etkin L.D., Chernoff J., Earnshaw W.C., Allis C.D.;
"Apoptotic phosphorylation of histone H2B is mediated by mammalian
sterile twenty kinase.";
Cell 113:507-517(2003).
[14]
UBIQUITINATION AT LYS-121.
PubMed=16307923; DOI=10.1016/j.molcel.2005.09.025;
Zhu B., Zheng Y., Pham A.-D., Mandal S.S., Erdjument-Bromage H.,
Tempst P., Reinberg D.;
"Monoubiquitination of human histone H2B: the factors involved and
their roles in HOX gene regulation.";
Mol. Cell 20:601-611(2005).
[15]
ACETYLATION AT LYS-6; LYS-13; LYS-16 AND LYS-21.
PubMed=16283522; DOI=10.1007/s11010-005-8285-1;
Golebiowski F., Kasprzak K.S.;
"Inhibition of core histones acetylation by carcinogenic nickel(II).";
Mol. Cell. Biochem. 279:133-139(2005).
[16]
UBIQUITINATION AT LYS-121.
PubMed=16713563; DOI=10.1016/j.cell.2006.04.029;
Pavri R., Zhu B., Li G., Trojer P., Mandal S., Shilatifard A.,
Reinberg D.;
"Histone H2B monoubiquitination functions cooperatively with FACT to
regulate elongation by RNA polymerase II.";
Cell 125:703-717(2006).
[17]
CROTONYLATION AT LYS-6; LYS-12; LYS-13; LYS-16; LYS-17; LYS-21; LYS-24
AND LYS-35.
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).
[18]
UBIQUITINATION AT LYS-35.
PubMed=21726816; DOI=10.1016/j.molcel.2011.05.015;
Wu L., Zee B.M., Wang Y., Garcia B.A., Dou Y.;
"The RING finger protein MSL2 in the MOF complex is an E3 ubiquitin
ligase for H2B K34 and is involved in crosstalk with H3 K4 and K79
methylation.";
Mol. Cell 43:132-144(2011).
[19]
SUCCINYLATION AT LYS-35; LYS-117 AND LYS-121, AND MALONYLATION AT
LYS-117.
PubMed=22389435; DOI=10.1074/mcp.M111.015875;
Xie Z., Dai J., Dai L., Tan M., Cheng Z., Wu Y., Boeke J.D., Zhao Y.;
"Lysine succinylation and lysine malonylation in histones.";
Mol. Cell. Proteomics 11:100-107(2012).
[20]
UBIQUITINATION, AND DEUBIQUITINATION BY USP49.
PubMed=23824326; DOI=10.1101/gad.211037.112;
Zhang Z., Jones A., Joo H.Y., Zhou D., Cao Y., Chen S.,
Erdjument-Bromage H., Renfrow M., He H., Tempst P., Townes T.M.,
Giles K.E., Ma L., Wang H.;
"USP49 deubiquitinates histone H2B and regulates cotranscriptional
pre-mRNA splicing.";
Genes Dev. 27:1581-1595(2013).
[21]
X-RAY CRYSTALLOGRAPHY (1.48 ANGSTROMS) OF 31-126 IN COMPLEX WITH H2AFZ
AND ANP32E.
PubMed=24463511; DOI=10.1038/nature12922;
Obri A., Ouararhni K., Papin C., Diebold M.L., Padmanabhan K.,
Marek M., Stoll I., Roy L., Reilly P.T., Mak T.W., Dimitrov S.,
Romier C., Hamiche A.;
"ANP32E is a histone chaperone that removes H2A.Z from chromatin.";
Nature 505:648-653(2014).
[22]
HYDROXYBUTYRYLATION AT LYS-6; LYS-13; LYS-21; LYS-24; LYS-25; LYS-35;
LYS-44; LYS-47; LYS-58; LYS-86; LYS-109; LYS-117 AND LYS-121.
PubMed=24681537; DOI=10.1038/nchembio.1497;
Dai L., Peng C., Montellier E., Lu Z., Chen Y., Ishii H.,
Debernardi A., Buchou T., Rousseaux S., Jin F., Sabari B.R., Deng Z.,
Allis C.D., Ren B., Khochbin S., Zhao Y.;
"Lysine 2-hydroxyisobutyrylation is a widely distributed active
histone mark.";
Nat. Chem. Biol. 10:365-370(2014).
[23]
BUTYRYLATION AT LYS-6 AND LYS-21.
PubMed=27105113; DOI=10.1016/j.molcel.2016.03.014;
Goudarzi A., Zhang D., Huang H., Barral S., Kwon O.K., Qi S., Tang Z.,
Buchou T., Vitte A.L., He T., Cheng Z., Montellier E., Gaucher J.,
Curtet S., Debernardi A., Charbonnier G., Puthier D., Petosa C.,
Panne D., Rousseaux S., Roeder R.G., Zhao Y., Khochbin S.;
"Dynamic competing histone H4 K5K8 acetylation and butyrylation are
hallmarks of highly active gene promoters.";
Mol. Cell 62:169-180(2016).
[24]
HYDROXYBUTYRYLATION AT LYS-6; LYS-12; LYS-17; LYS-21; LYS-35; LYS-86;
LYS-117 AND LYS-121.
PubMed=27105115; DOI=10.1016/j.molcel.2016.03.036;
Xie Z., Zhang D., Chung D., Tang Z., Huang H., Dai L., Qi S., Li J.,
Colak G., Chen Y., Xia C., Peng C., Ruan H., Kirkey M., Wang D.,
Jensen L.M., Kwon O.K., Lee S., Pletcher S.D., Tan M., Lombard D.B.,
White K.P., Zhao H., Li J., Roeder R.G., Yang X., Zhao Y.;
"Metabolic regulation of gene expression by histone lysine beta-
hydroxybutyrylation.";
Mol. Cell 62:194-206(2016).
[25]
X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) OF 31-126 IN COMPLEX WITH H2AFZ
AND VPS72, AND INTERACTION WITH H2AFZ AND VPS72.
PubMed=26974126; DOI=10.1038/NSMB.3189;
Latrick C.M., Marek M., Ouararhni K., Papin C., Stoll I.,
Ignatyeva M., Obri A., Ennifar E., Dimitrov S., Romier C., Hamiche A.;
"Molecular basis and specificity of H2A.Z-H2B recognition and
deposition by the histone chaperone YL1.";
Nat. Struct. Mol. Biol. 23:309-316(2016).
-!- FUNCTION: 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.
-!- FUNCTION: Has broad antibacterial activity. May contribute to the
formation of the functional antimicrobial barrier of the colonic
epithelium, and to the bactericidal activity of amniotic fluid.
-!- 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. The octamer wraps
approximately 147 bp of DNA. Heterodimer HIST1H2BJ and H2AFZ
interacts with VPS72 (via N-terminal domain) (PubMed:26974126).
{ECO:0000269|PubMed:24463511, ECO:0000269|PubMed:26974126}.
-!- INTERACTION:
P04908:HIST1H2AB; NbExp=9; IntAct=EBI-6150252, EBI-358971;
-!- SUBCELLULAR LOCATION: Nucleus. Chromosome.
-!- PTM: Monoubiquitination at Lys-35 (H2BK34Ub) 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 at Lys-121 (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. {ECO:0000269|PubMed:11709551,
ECO:0000269|PubMed:16627869}.
-!- PTM: Phosphorylation at Ser-37 (H2BS36ph) by AMPK in response to
stress promotes transcription (By similarity). Phosphorylated on
Ser-15 (H2BS14ph) by STK4/MST1 during apoptosis; which facilitates
apoptotic chromatin condensation. Also phosphorylated on Ser-15 in
response to DNA double strand breaks (DSBs), and in correlation
with somatic hypermutation and immunoglobulin class-switch
recombination. {ECO:0000250|UniProtKB:Q64475,
ECO:0000269|PubMed:12757711}.
-!- PTM: GlcNAcylation at Ser-113 promotes monoubiquitination of Lys-
121. It fluctuates in response to extracellular glucose, and
associates with transcribed genes (By similarity).
{ECO:0000250|UniProtKB:P62807}.
-!- 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}.
-!- SIMILARITY: Belongs to the histone H2B family. {ECO:0000305}.
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EMBL; X00088; CAA24950.1; -; Genomic_DNA.
EMBL; AF531293; AAN06693.1; -; Genomic_DNA.
EMBL; AK311849; BAG34791.1; -; mRNA.
EMBL; AL021807; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471081; EAX03080.1; -; Genomic_DNA.
CCDS; CCDS4618.1; -.
PIR; A26318; HSHUB1.
PIR; S65409; S65409.
RefSeq; NP_066402.2; NM_021058.3.
UniGene; Hs.591807; -.
UniGene; Hs.656567; -.
PDB; 2RVQ; NMR; -; D=1-126.
PDB; 3A6N; X-ray; 2.70 A; D/H=1-126.
PDB; 3AFA; X-ray; 2.50 A; D/H=1-126.
PDB; 3AN2; X-ray; 3.60 A; D/H=1-126.
PDB; 3AV1; X-ray; 2.50 A; D/H=1-126.
PDB; 3AV2; X-ray; 2.80 A; D/H=1-126.
PDB; 3AYW; X-ray; 2.90 A; D/H=1-126.
PDB; 3AZE; X-ray; 3.00 A; D/H=1-126.
PDB; 3AZF; X-ray; 2.70 A; D/H=1-126.
PDB; 3AZG; X-ray; 2.40 A; D/H=1-126.
PDB; 3AZH; X-ray; 3.49 A; D/H=1-126.
PDB; 3AZI; X-ray; 2.70 A; D/H=1-126.
PDB; 3AZJ; X-ray; 2.89 A; D/H=1-126.
PDB; 3AZK; X-ray; 3.20 A; D/H=1-126.
PDB; 3AZL; X-ray; 2.70 A; D/H=1-126.
PDB; 3AZM; X-ray; 2.89 A; D/H=1-126.
PDB; 3AZN; X-ray; 3.00 A; D/H=1-126.
PDB; 3W96; X-ray; 3.00 A; D/H=1-126.
PDB; 3W97; X-ray; 3.20 A; D/H=26-126.
PDB; 3W98; X-ray; 3.42 A; D/H=1-126.
PDB; 3W99; X-ray; 3.00 A; D/H=1-126.
PDB; 3WA9; X-ray; 3.07 A; D/H=1-126.
PDB; 3WAA; X-ray; 3.20 A; D/H=1-126.
PDB; 3WTP; X-ray; 2.67 A; D/H=1-126.
PDB; 4CAY; X-ray; 1.48 A; B=31-126.
PDB; 4YM5; X-ray; 4.00 A; D/H=1-126.
PDB; 4YM6; X-ray; 3.51 A; D/H=1-126.
PDB; 4Z5T; X-ray; 2.80 A; D/H=1-126.
PDB; 5AV5; X-ray; 2.40 A; D/H=1-126.
PDB; 5AV6; X-ray; 2.20 A; D/H=1-126.
PDB; 5AV8; X-ray; 2.20 A; D/H=1-126.
PDB; 5AV9; X-ray; 2.20 A; D/H=1-126.
PDB; 5AVB; X-ray; 2.40 A; D/H=1-126.
PDB; 5AVC; X-ray; 2.40 A; D/H=1-126.
PDB; 5AY8; X-ray; 2.80 A; D/H=1-126.
PDB; 5B0Y; X-ray; 2.56 A; D/H=1-126.
PDB; 5B0Z; X-ray; 1.99 A; D/H=1-126.
PDB; 5B24; X-ray; 3.60 A; D/H=1-126.
PDB; 5B2I; X-ray; 3.00 A; D/H=1-126.
PDB; 5B2J; X-ray; 2.60 A; D/H=1-126.
PDB; 5B31; X-ray; 2.20 A; D/H=1-126.
PDB; 5B32; X-ray; 2.35 A; D/H=1-126.
PDB; 5B33; X-ray; 2.92 A; D/H=1-126.
PDB; 5B40; X-ray; 3.33 A; D/H=1-126.
PDB; 5CPI; X-ray; 2.90 A; D/H=1-126.
PDB; 5CPJ; X-ray; 3.15 A; D/H=1-126.
PDB; 5CPK; X-ray; 2.63 A; D/H=1-126.
PDB; 5FUG; X-ray; 2.70 A; B/E/H/K=31-126.
PDB; 5GSE; X-ray; 3.14 A; D/H/N=1-126.
PDB; 5GTC; X-ray; 2.70 A; D/H=1-126.
PDB; 5GXQ; X-ray; 2.85 A; D/H=1-126.
PDB; 5JRG; X-ray; 2.50 A; D/H=1-126.
PDB; 5VEY; NMR; -; A=34-124.
PDB; 5X7X; X-ray; 2.18 A; D/H=1-126.
PDB; 5XF3; X-ray; 2.60 A; D/H=1-126.
PDB; 5XF4; X-ray; 2.87 A; D/H=1-126.
PDB; 5XF5; X-ray; 2.82 A; D/H=1-126.
PDBsum; 2RVQ; -.
PDBsum; 3A6N; -.
PDBsum; 3AFA; -.
PDBsum; 3AN2; -.
PDBsum; 3AV1; -.
PDBsum; 3AV2; -.
PDBsum; 3AYW; -.
PDBsum; 3AZE; -.
PDBsum; 3AZF; -.
PDBsum; 3AZG; -.
PDBsum; 3AZH; -.
PDBsum; 3AZI; -.
PDBsum; 3AZJ; -.
PDBsum; 3AZK; -.
PDBsum; 3AZL; -.
PDBsum; 3AZM; -.
PDBsum; 3AZN; -.
PDBsum; 3W96; -.
PDBsum; 3W97; -.
PDBsum; 3W98; -.
PDBsum; 3W99; -.
PDBsum; 3WA9; -.
PDBsum; 3WAA; -.
PDBsum; 3WTP; -.
PDBsum; 4CAY; -.
PDBsum; 4YM5; -.
PDBsum; 4YM6; -.
PDBsum; 4Z5T; -.
PDBsum; 5AV5; -.
PDBsum; 5AV6; -.
PDBsum; 5AV8; -.
PDBsum; 5AV9; -.
PDBsum; 5AVB; -.
PDBsum; 5AVC; -.
PDBsum; 5AY8; -.
PDBsum; 5B0Y; -.
PDBsum; 5B0Z; -.
PDBsum; 5B24; -.
PDBsum; 5B2I; -.
PDBsum; 5B2J; -.
PDBsum; 5B31; -.
PDBsum; 5B32; -.
PDBsum; 5B33; -.
PDBsum; 5B40; -.
PDBsum; 5CPI; -.
PDBsum; 5CPJ; -.
PDBsum; 5CPK; -.
PDBsum; 5FUG; -.
PDBsum; 5GSE; -.
PDBsum; 5GTC; -.
PDBsum; 5GXQ; -.
PDBsum; 5JRG; -.
PDBsum; 5VEY; -.
PDBsum; 5X7X; -.
PDBsum; 5XF3; -.
PDBsum; 5XF4; -.
PDBsum; 5XF5; -.
ProteinModelPortal; P06899; -.
SMR; P06899; -.
BioGrid; 114460; 29.
DIP; DIP-421N; -.
IntAct; P06899; 10.
MINT; MINT-4822927; -.
STRING; 9606.ENSP00000342886; -.
iPTMnet; P06899; -.
PhosphoSitePlus; P06899; -.
SwissPalm; P06899; -.
BioMuta; HIST1H2BJ; -.
DMDM; 7404367; -.
EPD; P06899; -.
MaxQB; P06899; -.
PaxDb; P06899; -.
PeptideAtlas; P06899; -.
PRIDE; P06899; -.
TopDownProteomics; P06899; -.
Ensembl; ENST00000339812; ENSP00000342886; ENSG00000124635.
Ensembl; ENST00000607124; ENSP00000476136; ENSG00000124635.
GeneID; 8970; -.
KEGG; hsa:8970; -.
UCSC; uc003niv.4; human.
CTD; 8970; -.
DisGeNET; 8970; -.
EuPathDB; HostDB:ENSG00000124635.8; -.
GeneCards; HIST1H2BJ; -.
HGNC; HGNC:4761; HIST1H2BJ.
HPA; HPA042205; -.
HPA; HPA043013; -.
HPA; HPA048671; -.
MIM; 615044; gene.
neXtProt; NX_P06899; -.
OpenTargets; ENSG00000124635; -.
PharmGKB; PA29136; -.
eggNOG; KOG1744; Eukaryota.
eggNOG; ENOG4111NV5; LUCA.
GeneTree; ENSGT00760000118976; -.
HOGENOM; HOG000231213; -.
HOVERGEN; HBG007774; -.
InParanoid; P06899; -.
KO; K11252; -.
OMA; SANIACN; -.
OrthoDB; EOG091G0XGD; -.
PhylomeDB; P06899; -.
TreeFam; TF300212; -.
Reactome; R-HSA-1221632; Meiotic synapsis.
Reactome; R-HSA-171306; Packaging Of Telomere Ends.
Reactome; R-HSA-201722; Formation of the beta-catenin:TCF transactivating complex.
Reactome; R-HSA-212300; PRC2 methylates histones and DNA.
Reactome; R-HSA-2299718; Condensation of Prophase Chromosomes.
Reactome; R-HSA-2559580; Oxidative Stress Induced Senescence.
Reactome; R-HSA-2559582; Senescence-Associated Secretory Phenotype (SASP).
Reactome; R-HSA-2559586; DNA Damage/Telomere Stress Induced Senescence.
Reactome; R-HSA-3214815; HDACs deacetylate histones.
Reactome; R-HSA-3214847; HATs acetylate histones.
Reactome; R-HSA-427359; SIRT1 negatively regulates rRNA expression.
Reactome; R-HSA-427389; ERCC6 (CSB) and EHMT2 (G9a) positively regulate rRNA expression.
Reactome; R-HSA-427413; NoRC negatively regulates rRNA expression.
Reactome; R-HSA-5250924; B-WICH complex positively regulates rRNA expression.
Reactome; R-HSA-5334118; DNA methylation.
Reactome; R-HSA-5578749; Transcriptional regulation by small RNAs.
Reactome; R-HSA-5617472; Activation of anterior HOX genes in hindbrain development during early embryogenesis.
Reactome; R-HSA-5625886; Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3.
Reactome; R-HSA-5689880; Ub-specific processing proteases.
Reactome; R-HSA-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
Reactome; R-HSA-5693571; Nonhomologous End-Joining (NHEJ).
Reactome; R-HSA-5693607; Processing of DNA double-strand break ends.
Reactome; R-HSA-606279; Deposition of new CENPA-containing nucleosomes at the centromere.
Reactome; R-HSA-69473; G2/M DNA damage checkpoint.
Reactome; R-HSA-73728; RNA Polymerase I Promoter Opening.
Reactome; R-HSA-73777; RNA Polymerase I Chain Elongation.
Reactome; R-HSA-8866654; E3 ubiquitin ligases ubiquitinate target proteins.
Reactome; R-HSA-8936459; RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function.
Reactome; R-HSA-8939236; RUNX1 regulates transcription of genes involved in differentiation of HSCs.
Reactome; R-HSA-912446; Meiotic recombination.
Reactome; R-HSA-977225; Amyloid fiber formation.
EvolutionaryTrace; P06899; -.
GeneWiki; HIST1H2BJ; -.
GenomeRNAi; 8970; -.
PRO; PR:P06899; -.
Proteomes; UP000005640; Chromosome 6.
Bgee; ENSG00000124635; -.
CleanEx; HS_HIST1H2BJ; -.
ExpressionAtlas; P06899; baseline and differential.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0000786; C:nucleosome; NAS:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0003677; F:DNA binding; IBA:GO_Central.
GO; GO:0001530; F:lipopolysaccharide binding; IDA:UniProtKB.
GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
GO; GO:0019731; P:antibacterial humoral response; IDA:UniProtKB.
GO; GO:0061844; P:antimicrobial humoral immune response mediated by antimicrobial peptide; IDA:UniProtKB.
GO; GO:0050829; P:defense response to Gram-negative bacterium; IDA:UniProtKB.
GO; GO:0050830; P:defense response to Gram-positive bacterium; IDA:UniProtKB.
GO; GO:0002227; P:innate immune response in mucosa; IDA:UniProtKB.
GO; GO:0031640; P:killing of cells of other organism; IDA:UniProtKB.
GO; GO:0010804; P:negative regulation of tumor necrosis factor-mediated signaling pathway; IDA:UniProtKB.
GO; GO:0006334; P:nucleosome assembly; IBA:GO_Central.
GO; GO:0016567; P:protein ubiquitination; TAS:Reactome.
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; Antibiotic; Antimicrobial; Chromosome;
Complete proteome; Direct protein sequencing; DNA-binding;
Glycoprotein; Hydroxylation; Isopeptide bond; Methylation;
Nucleosome core; Nucleus; Phosphoprotein; Reference proteome;
Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:P23527,
ECO:0000269|PubMed:11859126,
ECO:0000269|PubMed:12860195,
ECO:0000269|PubMed:15019208,
ECO:0000269|PubMed:2917990,
ECO:0000269|PubMed:8620898}.
CHAIN 2 126 Histone H2B type 1-J.
/FTId=PRO_0000071836.
MOD_RES 2 2 N-acetylproline.
{ECO:0000250|UniProtKB:P23527}.
MOD_RES 6 6 N6-(2-hydroxyisobutyryl)lysine;
alternate. {ECO:0000269|PubMed:24681537}.
MOD_RES 6 6 N6-(beta-hydroxybutyryl)lysine;
alternate. {ECO:0000269|PubMed:27105115}.
MOD_RES 6 6 N6-acetyllysine; alternate.
{ECO:0000269|PubMed:16283522,
ECO:0000269|PubMed:16627869}.
MOD_RES 6 6 N6-butyryllysine; alternate.
{ECO:0000269|PubMed:27105113}.
MOD_RES 6 6 N6-crotonyllysine; alternate.
{ECO:0000269|PubMed:21925322}.
MOD_RES 12 12 N6-(beta-hydroxybutyryl)lysine;
alternate. {ECO:0000269|PubMed:27105115}.
MOD_RES 12 12 N6-acetyllysine; alternate.
{ECO:0000269|PubMed:16627869}.
MOD_RES 12 12 N6-crotonyllysine; alternate.
{ECO:0000269|PubMed:21925322}.
MOD_RES 13 13 N6-(2-hydroxyisobutyryl)lysine;
alternate. {ECO:0000269|PubMed:24681537}.
MOD_RES 13 13 N6-acetyllysine; alternate.
{ECO:0000269|PubMed:16283522,
ECO:0000269|PubMed:16627869}.
MOD_RES 13 13 N6-crotonyllysine; alternate.
{ECO:0000269|PubMed:21925322}.
MOD_RES 15 15 Phosphoserine; by STK4/MST1.
{ECO:0000269|PubMed:12757711}.
MOD_RES 16 16 N6-acetyllysine; alternate.
{ECO:0000269|PubMed:16283522,
ECO:0000269|PubMed:16627869}.
MOD_RES 16 16 N6-crotonyllysine; alternate.
{ECO:0000269|PubMed:21925322}.
MOD_RES 17 17 N6-(beta-hydroxybutyryl)lysine;
alternate. {ECO:0000269|PubMed:27105115}.
MOD_RES 17 17 N6-acetyllysine; alternate.
{ECO:0000269|PubMed:16627869}.
MOD_RES 17 17 N6-crotonyllysine; alternate.
{ECO:0000269|PubMed:21925322}.
MOD_RES 21 21 N6-(2-hydroxyisobutyryl)lysine;
alternate. {ECO:0000269|PubMed:24681537}.
MOD_RES 21 21 N6-(beta-hydroxybutyryl)lysine;
alternate. {ECO:0000269|PubMed:27105115}.
MOD_RES 21 21 N6-acetyllysine; alternate.
{ECO:0000269|PubMed:16283522,
ECO:0000269|PubMed:16627869}.
MOD_RES 21 21 N6-butyryllysine; alternate.
{ECO:0000269|PubMed:27105113}.
MOD_RES 21 21 N6-crotonyllysine; alternate.
{ECO:0000269|PubMed:21925322}.
MOD_RES 24 24 N6-(2-hydroxyisobutyryl)lysine;
alternate. {ECO:0000269|PubMed:24681537}.
MOD_RES 24 24 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P33778}.
MOD_RES 24 24 N6-crotonyllysine; alternate.
{ECO:0000269|PubMed:21925322}.
MOD_RES 25 25 N6-(2-hydroxyisobutyryl)lysine.
{ECO:0000269|PubMed:24681537}.
MOD_RES 35 35 N6-(2-hydroxyisobutyryl)lysine;
alternate. {ECO:0000269|PubMed:24681537}.
MOD_RES 35 35 N6-(beta-hydroxybutyryl)lysine;
alternate. {ECO:0000269|PubMed:27105115}.
MOD_RES 35 35 N6-crotonyllysine; alternate.
{ECO:0000269|PubMed:21925322}.
MOD_RES 35 35 N6-succinyllysine; alternate.
{ECO:0000269|PubMed:22389435}.
MOD_RES 37 37 Phosphoserine; by AMPK.
{ECO:0000250|UniProtKB:Q64475}.
MOD_RES 44 44 N6-(2-hydroxyisobutyryl)lysine.
{ECO:0000269|PubMed:24681537}.
MOD_RES 47 47 N6-(2-hydroxyisobutyryl)lysine;
alternate. {ECO:0000269|PubMed:24681537}.
MOD_RES 47 47 N6-methyllysine; alternate.
{ECO:0000269|PubMed:16627869}.
MOD_RES 58 58 N6,N6-dimethyllysine; alternate.
{ECO:0000269|PubMed:16627869}.
MOD_RES 58 58 N6-(2-hydroxyisobutyryl)lysine;
alternate. {ECO:0000269|PubMed:24681537}.
MOD_RES 80 80 Dimethylated arginine.
{ECO:0000250|UniProtKB:Q96A08}.
MOD_RES 86 86 N6,N6,N6-trimethyllysine; alternate.
{ECO:0000250|UniProtKB:Q96A08}.
MOD_RES 86 86 N6-(2-hydroxyisobutyryl)lysine;
alternate. {ECO:0000269|PubMed:24681537}.
MOD_RES 86 86 N6-(beta-hydroxybutyryl)lysine;
alternate. {ECO:0000269|PubMed:27105115}.
MOD_RES 86 86 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q96A08}.
MOD_RES 87 87 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:Q96A08}.
MOD_RES 93 93 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:Q96A08}.
MOD_RES 109 109 N6-(2-hydroxyisobutyryl)lysine;
alternate. {ECO:0000269|PubMed:24681537}.
MOD_RES 109 109 N6-methyllysine; alternate.
{ECO:0000269|PubMed:16627869}.
MOD_RES 116 116 Phosphothreonine.
{ECO:0000250|UniProtKB:Q00729}.
MOD_RES 117 117 N6-(2-hydroxyisobutyryl)lysine;
alternate. {ECO:0000269|PubMed:24681537}.
MOD_RES 117 117 N6-(beta-hydroxybutyryl)lysine;
alternate. {ECO:0000269|PubMed:27105115}.
MOD_RES 117 117 N6-malonyllysine; alternate.
{ECO:0000269|PubMed:22389435}.
MOD_RES 117 117 N6-methylated lysine; alternate.
{ECO:0000250|UniProtKB:Q00729}.
MOD_RES 117 117 N6-succinyllysine; alternate.
{ECO:0000269|PubMed:22389435}.
MOD_RES 121 121 N6-(2-hydroxyisobutyryl)lysine;
alternate. {ECO:0000269|PubMed:24681537}.
MOD_RES 121 121 N6-(beta-hydroxybutyryl)lysine;
alternate. {ECO:0000269|PubMed:27105115}.
MOD_RES 121 121 N6-succinyllysine; alternate.
{ECO:0000269|PubMed:22389435}.
CARBOHYD 113 113 O-linked (GlcNAc) serine.
{ECO:0000250|UniProtKB:P62807}.
CROSSLNK 6 6 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:P58876}.
CROSSLNK 21 21 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:Q5QNW6}.
CROSSLNK 35 35 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin);
alternate. {ECO:0000269|PubMed:21726816}.
CROSSLNK 121 121 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000269|PubMed:16307923,
ECO:0000269|PubMed:16627869,
ECO:0000269|PubMed:16713563}.
CONFLICT 29 33 KRKRS -> SAAH (in Ref. 1; CAA24950).
{ECO:0000305}.
HELIX 39 49 {ECO:0000244|PDB:4CAY}.
STRAND 54 56 {ECO:0000244|PDB:4CAY}.
HELIX 57 83 {ECO:0000244|PDB:4CAY}.
TURN 84 86 {ECO:0000244|PDB:5B33}.
STRAND 88 90 {ECO:0000244|PDB:5B0Z}.
HELIX 92 102 {ECO:0000244|PDB:4CAY}.
HELIX 105 124 {ECO:0000244|PDB:4CAY}.
SEQUENCE 126 AA; 13904 MW; 0408C881ABBE6647 CRC64;
MPEPAKSAPA PKKGSKKAVT KAQKKDGKKR KRSRKESYSI YVYKVLKQVH PDTGISSKAM
GIMNSFVNDI FERIAGEASR LAHYNKRSTI TSREIQTAVR LLLPGELAKH AVSEGTKAVT
KYTSAK


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