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Histone H2A

 H2A_DROME               Reviewed;         124 AA.
P84051; P02267; Q4ABC7;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
10-OCT-2018, entry version 133.
RecName: Full=Histone H2A;
Name=His2A; Synonyms=H2a;
and
Name=His2A:CG31618; ORFNames=CG31618;
and
Name=His2A:CG33808; ORFNames=CG33808;
and
Name=His2A:CG33814; ORFNames=CG33814;
and
Name=His2A:CG33817; ORFNames=CG33817;
and
Name=His2A:CG33820; ORFNames=CG33820;
and
Name=His2A:CG33823; ORFNames=CG33823;
and
Name=His2A:CG33826; ORFNames=CG33826;
and
Name=His2A:CG33829; ORFNames=CG33829;
and
Name=His2A:CG33832; ORFNames=CG33832;
and
Name=His2A:CG33835; ORFNames=CG33835;
and
Name=His2A:CG33838; ORFNames=CG33838;
and
Name=His2A:CG33841; ORFNames=CG33841;
and
Name=His2A:CG33844; ORFNames=CG33844;
and
Name=His2A:CG33847; ORFNames=CG33847;
and
Name=His2A:CG33850; ORFNames=CG33850;
and
Name=His2A:CG33862; ORFNames=CG33862;
and
Name=His2A:CG33865; ORFNames=CG33865;
Drosophila melanogaster (Fruit fly).
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
Ephydroidea; Drosophilidae; Drosophila; Sophophora.
NCBI_TaxID=7227;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (HIS2A).
STRAIN=AK-194;
PubMed=2536150; DOI=10.1093/nar/17.1.225;
Matsuo Y., Yamazaki T.;
"tRNA derived insertion element in histone gene repeating unit of
Drosophila melanogaster.";
Nucleic Acids Res. 17:225-238(1989).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (HIS2A:CG31618;
HIS2A:CG33808; HIS2A:CG33814; HIS2A:CG33817; HIS2A:CG33820;
HIS2A:CG33823; HIS2A:CG33826; HIS2A:CG33829; HIS2A:CG33832;
HIS2A:CG33835; HIS2A:CG33838; HIS2A:CG33841; HIS2A:CG33844;
HIS2A:CG33847; HIS2A:CG33850; HIS2A:CG33862 AND HIS2A:CG33865).
STRAIN=Berkeley;
PubMed=10731132; DOI=10.1126/science.287.5461.2185;
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X.,
Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D.,
Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G.,
Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D.,
Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J.,
Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C.,
Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z.,
Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X.,
Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H.,
Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
Spier E., Spradling A.C., Stapleton M., Strong R., Sun E.,
Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A.,
Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X.,
Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
"The genome sequence of Drosophila melanogaster.";
Science 287:2185-2195(2000).
[3]
GENOME REANNOTATION.
STRAIN=Berkeley;
PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q.,
Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
Lewis S.E.;
"Annotation of the Drosophila melanogaster euchromatic genome: a
systematic review.";
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
[4]
PROTEIN SEQUENCE OF 96-122, AND PHOSPHORYLATION AT THR-120.
STRAIN=Berkeley; TISSUE=Embryo;
PubMed=15078818; DOI=10.1101/gad.1184604;
Aihara H., Nakagawa T., Yasui K., Ohta T., Hirose S., Dhomae N.,
Takio K., Kaneko M., Takeshima Y., Muramatsu M., Ito T.;
"Nucleosomal histone kinase-1 phosphorylates H2A Thr 119 during
mitosis in the early Drosophila embryo.";
Genes Dev. 18:877-888(2004).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-122 (HIS2A).
Goldberg M.L.;
Thesis (1979), University of Stanford, United States.
[6]
PHOSPHORYLATION AT SER-2.
PubMed=15133681; DOI=10.1007/s00412-004-0281-9;
Barber C.M., Turner F.B., Wang Y., Hagstrom K., Taverna S.D.,
Mollah S., Ueberheide B., Meyer B.J., Hunt D.F., Cheung P.,
Allis C.D.;
"The enhancement of histone H4 and H2A serine 1 phosphorylation during
mitosis and S-phase is evolutionarily conserved.";
Chromosoma 112:360-371(2004).
[7]
UBIQUITINATION.
PubMed=15386022; DOI=10.1038/nature02985;
Wang H., Wang L., Erdjument-Bromage H., Vidal M., Tempst P.,
Jones R.S., Zhang Y.;
"Role of histone H2A ubiquitination in Polycomb silencing.";
Nature 431:873-878(2004).
[8]
PHOSPHORYLATION AT THR-120.
PubMed=16230526; DOI=10.1101/gad.1348905;
Ivanovska I., Khandan T., Ito T., Orr-Weaver T.L.;
"A histone code in meiosis: the histone kinase, NHK-1, is required for
proper chromosomal architecture in Drosophila oocytes.";
Genes Dev. 19:2571-2582(2005).
[9]
SUCCINYLATION AT LYS-36.
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).
-!- 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.
-!- 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.
-!- INTERACTION:
Q9V6Q2:cid; NbExp=2; IntAct=EBI-182580, EBI-129287;
-!- SUBCELLULAR LOCATION: Nucleus. Chromosome.
-!- PTM: The chromatin-associated form, but not the free cytoplasmic
form, is phosphorylated on Thr-120 by NHK-1 during mitosis, and
dephosphorylated during S-phase. Also phosphorylated on Thr-120 by
NHK-1 during prophase I of meiosis; which is required for
acetylation of H3 'Lys-14' and H4 'Lys-5', diassembly of the
synaptonemal complex, and karyosome formation.
{ECO:0000269|PubMed:15078818, ECO:0000269|PubMed:15133681,
ECO:0000269|PubMed:16230526}.
-!- PTM: Monoubiquitination of Lys-119 by sce/dRING gives a specific
tag for epigenetic transcriptional repression.
-!- PTM: Phosphorylation on Ser-2 is enhanced during mitosis.
Phosphorylation on Ser-2 directly represses transcription (By
similarity). {ECO:0000250}.
-!- SIMILARITY: Belongs to the histone H2A family. {ECO:0000305}.
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EMBL; X14215; CAA32431.1; -; Genomic_DNA.
EMBL; X14215; CAA32436.1; -; Genomic_DNA.
EMBL; AE014134; AAN11125.1; -; Genomic_DNA.
EMBL; AE014134; AAZ66488.1; -; Genomic_DNA.
EMBL; AE014134; AAZ66497.1; -; Genomic_DNA.
EMBL; AE014134; AAZ66502.1; -; Genomic_DNA.
EMBL; AE014134; AAZ66507.1; -; Genomic_DNA.
EMBL; AE014134; AAZ66512.1; -; Genomic_DNA.
EMBL; AE014134; AAZ66517.1; -; Genomic_DNA.
EMBL; AE014134; AAZ66522.1; -; Genomic_DNA.
EMBL; AE014134; AAZ66527.1; -; Genomic_DNA.
EMBL; AE014134; AAZ66532.1; -; Genomic_DNA.
EMBL; AE014134; AAZ66537.1; -; Genomic_DNA.
EMBL; AE014134; AAZ66542.1; -; Genomic_DNA.
EMBL; AE014134; AAZ66547.1; -; Genomic_DNA.
EMBL; AE014134; AAZ66552.1; -; Genomic_DNA.
EMBL; AE014134; AAZ66557.1; -; Genomic_DNA.
EMBL; AE014134; AAZ66577.1; -; Genomic_DNA.
EMBL; AE014134; AAZ66582.1; -; Genomic_DNA.
PIR; S10094; HSFF2.
RefSeq; NP_001027292.1; NM_001032121.2.
RefSeq; NP_001027301.1; NM_001032130.2.
RefSeq; NP_001027306.1; NM_001032135.2.
RefSeq; NP_001027311.1; NM_001032140.2.
RefSeq; NP_001027316.1; NM_001032145.2.
RefSeq; NP_001027321.1; NM_001032150.2.
RefSeq; NP_001027326.1; NM_001032155.2.
RefSeq; NP_001027331.1; NM_001032160.2.
RefSeq; NP_001027336.1; NM_001032165.2.
RefSeq; NP_001027341.1; NM_001032170.2.
RefSeq; NP_001027346.1; NM_001032175.2.
RefSeq; NP_001027351.1; NM_001032180.2.
RefSeq; NP_001027356.1; NM_001032185.2.
RefSeq; NP_001027361.1; NM_001032190.2.
RefSeq; NP_001027381.1; NM_001032210.2.
RefSeq; NP_001027386.1; NM_001032215.2.
RefSeq; NP_724343.1; NM_165382.3.
PDB; 2NQB; X-ray; 2.30 A; C/G=2-124.
PDB; 2PYO; X-ray; 2.43 A; C/G=2-121.
PDB; 4QLC; X-ray; 3.50 A; C/G=2-124.
PDB; 4X23; X-ray; 3.50 A; C/G/M/Q=16-117.
PDBsum; 2NQB; -.
PDBsum; 2PYO; -.
PDBsum; 4QLC; -.
PDBsum; 4X23; -.
ProteinModelPortal; P84051; -.
SMR; P84051; -.
BioGrid; 534102; 1.
BioGrid; 77146; 22.
DIP; DIP-29504N; -.
IntAct; P84051; 9.
MINT; P84051; -.
STRING; 7227.FBpp0091111; -.
iPTMnet; P84051; -.
PaxDb; P84051; -.
PRIDE; P84051; -.
EnsemblMetazoa; FBtr0085893; FBpp0085249; FBgn0051618.
EnsemblMetazoa; FBtr0091812; FBpp0091055; FBgn0053808.
EnsemblMetazoa; FBtr0091818; FBpp0091060; FBgn0053814.
EnsemblMetazoa; FBtr0091821; FBpp0091063; FBgn0053817.
EnsemblMetazoa; FBtr0091824; FBpp0091066; FBgn0053820.
EnsemblMetazoa; FBtr0091827; FBpp0091069; FBgn0053823.
EnsemblMetazoa; FBtr0091830; FBpp0091072; FBgn0053826.
EnsemblMetazoa; FBtr0091833; FBpp0091075; FBgn0053829.
EnsemblMetazoa; FBtr0091836; FBpp0091078; FBgn0053832.
EnsemblMetazoa; FBtr0091839; FBpp0091081; FBgn0053835.
EnsemblMetazoa; FBtr0091842; FBpp0091084; FBgn0053838.
EnsemblMetazoa; FBtr0091845; FBpp0091087; FBgn0053841.
EnsemblMetazoa; FBtr0091848; FBpp0091090; FBgn0053844.
EnsemblMetazoa; FBtr0091851; FBpp0091093; FBgn0053847.
EnsemblMetazoa; FBtr0091854; FBpp0091096; FBgn0053850.
EnsemblMetazoa; FBtr0091866; FBpp0091108; FBgn0053862.
EnsemblMetazoa; FBtr0091869; FBpp0091111; FBgn0053865.
GeneID; 318855; -.
GeneID; 3771774; -.
GeneID; 3771783; -.
GeneID; 3771785; -.
GeneID; 3772148; -.
GeneID; 3772278; -.
GeneID; 3772282; -.
GeneID; 3772345; -.
GeneID; 3772351; -.
GeneID; 3772360; -.
GeneID; 3772447; -.
GeneID; 3772448; -.
GeneID; 3772505; -.
GeneID; 3772541; -.
GeneID; 3772565; -.
GeneID; 3772618; -.
GeneID; 3772632; -.
KEGG; dme:Dmel_CG31618; -.
KEGG; dme:Dmel_CG33808; -.
KEGG; dme:Dmel_CG33814; -.
KEGG; dme:Dmel_CG33817; -.
KEGG; dme:Dmel_CG33820; -.
KEGG; dme:Dmel_CG33823; -.
KEGG; dme:Dmel_CG33826; -.
KEGG; dme:Dmel_CG33829; -.
KEGG; dme:Dmel_CG33832; -.
KEGG; dme:Dmel_CG33835; -.
KEGG; dme:Dmel_CG33838; -.
KEGG; dme:Dmel_CG33841; -.
KEGG; dme:Dmel_CG33844; -.
KEGG; dme:Dmel_CG33847; -.
KEGG; dme:Dmel_CG33850; -.
KEGG; dme:Dmel_CG33862; -.
KEGG; dme:Dmel_CG33865; -.
UCSC; CG31618-RA; d. melanogaster.
CTD; 318855; -.
CTD; 3771774; -.
CTD; 3771783; -.
CTD; 3771785; -.
CTD; 3772148; -.
CTD; 3772278; -.
CTD; 3772282; -.
CTD; 3772345; -.
CTD; 3772351; -.
CTD; 3772360; -.
CTD; 3772447; -.
CTD; 3772448; -.
CTD; 3772505; -.
CTD; 3772541; -.
CTD; 3772565; -.
CTD; 3772618; -.
CTD; 3772632; -.
FlyBase; FBgn0001196; His2A.
FlyBase; FBgn0051618; His2A:CG31618.
FlyBase; FBgn0053808; His2A:CG33808.
FlyBase; FBgn0053814; His2A:CG33814.
FlyBase; FBgn0053817; His2A:CG33817.
FlyBase; FBgn0053820; His2A:CG33820.
FlyBase; FBgn0053823; His2A:CG33823.
FlyBase; FBgn0053826; His2A:CG33826.
FlyBase; FBgn0053829; His2A:CG33829.
FlyBase; FBgn0053832; His2A:CG33832.
FlyBase; FBgn0053835; His2A:CG33835.
FlyBase; FBgn0053838; His2A:CG33838.
FlyBase; FBgn0053841; His2A:CG33841.
FlyBase; FBgn0053844; His2A:CG33844.
FlyBase; FBgn0053847; His2A:CG33847.
FlyBase; FBgn0053850; His2A:CG33850.
FlyBase; FBgn0053862; His2A:CG33862.
FlyBase; FBgn0053865; His2A:CG33865.
eggNOG; KOG1756; Eukaryota.
eggNOG; COG5262; LUCA.
GeneTree; ENSGT00910000143981; -.
InParanoid; P84051; -.
KO; K11251; -.
OMA; HAYLYSA; -.
OrthoDB; EOG091G0XGD; -.
PhylomeDB; P84051; -.
Reactome; R-DME-201722; Formation of the beta-catenin:TCF transactivating complex.
Reactome; R-DME-212300; PRC2 methylates histones and DNA.
Reactome; R-DME-2299718; Condensation of Prophase Chromosomes.
Reactome; R-DME-2559580; Oxidative Stress Induced Senescence.
Reactome; R-DME-2559582; Senescence-Associated Secretory Phenotype (SASP).
Reactome; R-DME-3214815; HDACs deacetylate histones.
Reactome; R-DME-3214847; HATs acetylate histones.
Reactome; R-DME-3214858; RMTs methylate histone arginines.
Reactome; R-DME-427359; SIRT1 negatively regulates rRNA expression.
Reactome; R-DME-427413; NoRC negatively regulates rRNA expression.
Reactome; R-DME-5578749; Transcriptional regulation by small RNAs.
Reactome; R-DME-5625886; Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3.
Reactome; R-DME-5689603; UCH proteinases.
Reactome; R-DME-5689880; Ub-specific processing proteases.
Reactome; R-DME-5689901; Metalloprotease DUBs.
Reactome; R-DME-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
Reactome; R-DME-5693571; Nonhomologous End-Joining (NHEJ).
Reactome; R-DME-8936459; RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function.
Reactome; R-DME-9018519; Estrogen-dependent gene expression.
ChiTaRS; His2Av; fly.
EvolutionaryTrace; P84051; -.
PRO; PR:P84051; -.
Proteomes; UP000000803; Chromosome 2L.
Bgee; FBgn0051618; Expressed in 2 organ(s), highest expression level in adult organism.
Genevisible; P84051; DM.
GO; GO:0005694; C:chromosome; IDA:FlyBase.
GO; GO:0000790; C:nuclear chromatin; IBA:GO_Central.
GO; GO:0000788; C:nuclear nucleosome; ISS:FlyBase.
GO; GO:0000786; C:nucleosome; TAS:FlyBase.
GO; GO:0005634; C:nucleus; IDA:FlyBase.
GO; GO:0005700; C:polytene chromosome; IDA:FlyBase.
GO; GO:0005704; C:polytene chromosome band; IDA:FlyBase.
GO; GO:0003677; F:DNA binding; ISS:FlyBase.
GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
GO; GO:0006325; P:chromatin organization; ISS:FlyBase.
GO; GO:0006342; P:chromatin silencing; IBA:GO_Central.
GO; GO:0007526; P:larval somatic muscle development; IMP:FlyBase.
GO; GO:0006334; P:nucleosome assembly; NAS:UniProtKB.
CDD; cd00074; H2A; 1.
Gene3D; 1.10.20.10; -; 1.
InterPro; IPR009072; Histone-fold.
InterPro; IPR002119; Histone_H2A.
InterPro; IPR007125; Histone_H2A/H2B/H3.
InterPro; IPR032454; Histone_H2A_C.
InterPro; IPR032458; Histone_H2A_CS.
Pfam; PF00125; Histone; 1.
Pfam; PF16211; Histone_H2A_C; 1.
PRINTS; PR00620; HISTONEH2A.
SMART; SM00414; H2A; 1.
SUPFAM; SSF47113; SSF47113; 1.
PROSITE; PS00046; HISTONE_H2A; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Chromosome; Complete proteome;
Direct protein sequencing; DNA-binding; Isopeptide bond; Methylation;
Nucleosome core; Nucleus; Phosphoprotein; Reference proteome;
Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000250}.
CHAIN 2 124 Histone H2A.
/FTId=PRO_0000055222.
MOD_RES 2 2 N-acetylserine. {ECO:0000250}.
MOD_RES 2 2 Phosphoserine.
{ECO:0000305|PubMed:15133681}.
MOD_RES 36 36 N6-succinyllysine.
{ECO:0000269|PubMed:22389435}.
MOD_RES 104 104 N5-methylglutamine. {ECO:0000250}.
MOD_RES 120 120 Phosphothreonine.
{ECO:0000269|PubMed:15078818,
ECO:0000269|PubMed:16230526}.
CROSSLNK 119 119 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000305|PubMed:15386022}.
HELIX 17 21 {ECO:0000244|PDB:2NQB}.
HELIX 27 36 {ECO:0000244|PDB:2NQB}.
STRAND 41 43 {ECO:0000244|PDB:2NQB}.
HELIX 46 72 {ECO:0000244|PDB:2NQB}.
STRAND 76 78 {ECO:0000244|PDB:2NQB}.
HELIX 80 88 {ECO:0000244|PDB:2NQB}.
HELIX 91 96 {ECO:0000244|PDB:2NQB}.
TURN 97 99 {ECO:0000244|PDB:2NQB}.
STRAND 100 102 {ECO:0000244|PDB:2NQB}.
HELIX 113 115 {ECO:0000244|PDB:2NQB}.
SEQUENCE 124 AA; 13363 MW; 725BA63C393155F6 CRC64;
MSGRGKGGKV KGKAKSRSNR AGLQFPVGRI HRLLRKGNYA ERVGAGAPVY LAAVMEYLAA
EVLELAGNAA RDNKKTRIIP RHLQLAIRND EELNKLLSGV TIAQGGVLPN IQAVLLPKKT
EKKA


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25-522 UTX is a histone demethylase that specifically demethylates 'Lys-27' of histone H3, thereby playing a central role in histone code. It demethylates trimethylated and dimethylated but not monomethylate 0.05 mg
orb61320 CI-994 CI-994 is a histone deacetylase (HDAC) inhibitor and induces histone hyperacetylation in living cells. CI-994 inhibited HDAC-1 and HDAC-2 but not the prototypical histone acetyltransferase GCN5 500 mg
29-186 JMJD3 is a histone demethylase that specifically demethylates 'Lys-27' of histone H3, thereby playing a central role in histone code. It plays a central role in regulation of posterior development, by 0.1 mg
25-583 JMJD3 is a histone demethylase that specifically demethylates 'Lys-27' of histone H3, thereby playing a central role in histone code. It plays a central role in regulation of posterior development, by 0.05 mg
27-131 POLE3 is a histone-fold protein that interacts with other histone-fold proteins to bind DNA in a sequence-independent manner. These histone-fold protein dimers combine within larger enzymatic complexe 0.05 mg
27-775 POLE3 is a histone-fold protein that interacts with other histone-fold proteins to bind DNA in a sequence-independent manner. These histone-fold protein dimers combine within larger enzymatic complexe 0.1 mg
25-113 CHRAC1 is a histone-fold protein that interacts with other histone-fold proteins to bind DNA in a sequence-independent manner. These histone-fold protein dimers combine within larger enzymatic complex 0.05 mg
bs-0931P Peptides: Histone H1b(Histone H1.4) Protein Length:12-25 amino acids. 200ug lyophilized
SET3001 Histone-related : SET7_9 Histone methyltransferase Human, E.coli 0.5mg
SET3001 Histone-related : SET7_9 Histone methyltransferase Human, E.coli 100ug
E0356h ELISA H2B_s,H2BFS,Histone H2B type F-S,Histone H2B.s,Homo sapiens,Human 96T
E0356h ELISA kit H2B_s,H2BFS,Histone H2B type F-S,Histone H2B.s,Homo sapiens,Human 96T
U0356h CLIA H2B_s,H2BFS,Histone H2B type F-S,Histone H2B.s,Homo sapiens,Human 96T
303-35199 Anti_phospho Histone H3 (P_Ser10), monoclonal antibody Binds to Histone H3 phosphorylated at serine 10. 100 ul
30-333 DOT1L is a histone methyltransferase. It methylates 'Lys-79' of histone H3. Nucleosomes are preferred as substrate compared to free histones. 0.05 mg
ANTY021260 Polyclonal Antibodies: Histone H2A.X (Ab-139) ; Specificity: Histone H2A.X (Ab-139) ; Application: IHC 100ug
31-007 Histone H3, along with histone H4, plays a central role in nucleosome formation. 0.1 mg
ANTY021137 Polyclonal Antibodies: Histone H3.1 (Ab-10) ; Specificity: Histone H3.1 (Ab-10) ; Application: IHC 100ug
3623BP-50 Histone H3 Blocking Peptide target: Histone H3 50 μg
3624BP-50 Histone H4 Blocking Peptide target: Histone H4 50 μg
3621BP-50 Histone H2A Blocking Peptide target: Histone H2A 50 μg
3622BP-50 Histone H2B Blocking Peptide target: Histone H2B 50 μg


 

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