Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Chromobox protein homolog 1 (HP1Hsbeta) (Heterochromatin protein 1 homolog beta) (HP1 beta) (Heterochromatin protein p25) (M31) (Modifier 1 protein) (p25beta)

 CBX1_HUMAN              Reviewed;         185 AA.
P83916; P23197;
07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
07-JUN-2004, sequence version 1.
05-DEC-2018, entry version 157.
RecName: Full=Chromobox protein homolog 1;
AltName: Full=HP1Hsbeta;
AltName: Full=Heterochromatin protein 1 homolog beta;
Short=HP1 beta;
AltName: Full=Heterochromatin protein p25;
AltName: Full=M31;
AltName: Full=Modifier 1 protein;
AltName: Full=p25beta;
Name=CBX1; Synonyms=CBX;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND SUBCELLULAR LOCATION.
TISSUE=Liver tumor;
PubMed=9169582; DOI=10.1007/s004120050219;
Furuta K., Chan E.K.L., Kiyosawa K., Reimer G., Luderschmidt C.,
Tan E.M.;
"Heterochromatin protein HP1Hsbeta (p25beta) and its localization with
centromeres in mitosis.";
Chromosoma 106:11-19(1997).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain, and Ovary;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[3]
PROTEIN SEQUENCE OF 8-25; 122-137; 140-150 AND 156-167, AND
IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex;
Lubec G., Afjehi-Sadat L., Chen W.-Q., Sun Y.;
Submitted (DEC-2008) to UniProtKB.
[4]
SUBCELLULAR LOCATION, AND LACK OF PHOSPHORYLATION.
PubMed=10460410; DOI=10.1007/s004120050372;
Minc E., Allory Y., Worman H.J., Courvalin J.-C., Buendia B.;
"Localization and phosphorylation of HP1 proteins during the cell
cycle in mammalian cells.";
Chromosoma 108:220-234(1999).
[5]
INTERACTION WITH SUV39H1.
PubMed=10202156; DOI=10.1093/emboj/18.7.1923;
Aagaard L., Laible G., Selenko P., Schmid M., Dorn R., Schotta G.,
Kuhfittig S., Wolf A., Lebersorger A., Singh P.B., Reuter G.,
Jenuwein T.;
"Functional mammalian homologues of the Drosophila PEV-modifier
Su(var)3-9 encode centromere-associated proteins which complex with
the heterochromatin component M31.";
EMBO J. 18:1923-1938(1999).
[6]
INTERACTION WITH EMSY.
PubMed=14651845; DOI=10.1016/S0092-8674(03)00930-9;
Hughes-Davies L., Huntsman D., Ruas M., Fuks F., Bye J., Chin S.-F.,
Milner J., Brown L.A., Hsu F., Gilks B., Nielsen T., Schulzer M.,
Chia S., Ragaz J., Cahn A., Linger L., Ozdag H., Cattaneo E.,
Jordanova E.S., Schuuring E., Yu D.S., Venkitaraman A., Ponder B.,
Doherty A., Aparicio S., Bentley D., Theillet C., Ponting C.P.,
Caldas C., Kouzarides T.;
"EMSY links the BRCA2 pathway to sporadic breast and ovarian cancer.";
Cell 115:523-535(2003).
[7]
MUTAGENESIS OF ILE-161.
PubMed=15947784; DOI=10.1038/sj.embor.7400415;
Ekblad C.M.S., Chavali G.B., Basu B.P., Freund S.M.V., Veprintsev D.,
Hughes-Davies L., Kouzarides T., Doherty A.J., Itzhaki L.S.;
"Binding of EMSY to HP1beta: implications for recruitment of HP1beta
and BS69.";
EMBO Rep. 6:675-680(2005).
[8]
INTERACTION WITH SETDB1.
PubMed=15899859; DOI=10.1128/MCB.25.11.4552-4564.2005;
Verschure P.J., van der Kraan I., de Leeuw W., van der Vlag J.,
Carpenter A.E., Belmont A.S., van Driel R.;
"In vivo HP1 targeting causes large-scale chromatin condensation and
enhanced histone lysine methylation.";
Mol. Cell. Biol. 25:4552-4564(2005).
[9]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=18318008; DOI=10.1002/pmic.200700884;
Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,
Zou H., Gu J.;
"Large-scale phosphoproteome analysis of human liver tissue by
enrichment and fractionation of phosphopeptides with strong anion
exchange chromatography.";
Proteomics 8:1346-1361(2008).
[10]
INTERACTION WITH CHAMP1 AND POGZ.
PubMed=20850016; DOI=10.1016/j.cell.2010.08.020;
Vermeulen M., Eberl H.C., Matarese F., Marks H., Denissov S.,
Butter F., Lee K.K., Olsen J.V., Hyman A.A., Stunnenberg H.G.,
Mann M.;
"Quantitative interaction proteomics and genome-wide profiling of
epigenetic histone marks and their readers.";
Cell 142:967-980(2010).
[11]
RETRACTED PAPER.
PubMed=19880879; DOI=10.1074/jbc.M109.065862;
Lee S.W., Cho Y.S., Na J.M., Park U.H., Kang M., Kim E.J., Um S.J.;
"ASXL1 represses retinoic acid receptor-mediated transcription through
associating with HP1 and LSD1.";
J. Biol. Chem. 285:18-29(2010).
[12]
RETRACTION NOTICE FOR PUBMED:19880879.
PubMed=25750265; DOI=10.1074/jbc.A109.065862;
Lee S.W., Cho Y.S., Na J.M., Park U.H., Kang M., Kim E.J., Um S.J.;
"Retraction: 'ASXL1 represses retinoic acid receptor-mediated
transcription through associating with HP1 and LSD1'.";
J. Biol. Chem. 290:6008-6008(2015).
[13]
INTERACTION WITH POGZ.
PubMed=20562864; DOI=10.1038/ncb2075;
Nozawa R.S., Nagao K., Masuda H.T., Iwasaki O., Hirota T., Nozaki N.,
Kimura H., Obuse C.;
"Human POGZ modulates dissociation of HP1alpha from mitotic chromosome
arms through Aurora B activation.";
Nat. Cell Biol. 12:719-727(2010).
[14]
UBIQUITINATION.
PubMed=20498703; DOI=10.1371/journal.pone.0010620;
Chaturvedi P., Parnaik V.K.;
"Lamin A rod domain mutants target heterochromatin protein 1alpha and
beta for proteasomal degradation by activation of F-box protein,
FBXW10.";
PLoS ONE 5:E10620-E10620(2010).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-89, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[16]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-89; SER-91 AND SER-175,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[18]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[19]
INTERACTION WITH LRIF1.
PubMed=23542155; DOI=10.1038/nsmb.2532;
Nozawa R.S., Nagao K., Igami K.T., Shibata S., Shirai N., Nozaki N.,
Sado T., Kimura H., Obuse C.;
"Human inactive X chromosome is compacted through a PRC2-independent
SMCHD1-HBiX1 pathway.";
Nat. Struct. Mol. Biol. 20:566-573(2013).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-89, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[21]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-9, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25755297; DOI=10.1074/mcp.O114.044792;
Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
Vertegaal A.C.;
"System-wide analysis of SUMOylation dynamics in response to
replication stress reveals novel small ubiquitin-like modified target
proteins and acceptor lysines relevant for genome stability.";
Mol. Cell. Proteomics 14:1419-1434(2015).
[22]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-9; LYS-33; LYS-99 AND
LYS-150, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[23]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 104-175 IN COMPLEX WITH EMSY.
PubMed=16615912; DOI=10.1016/j.str.2006.01.007;
Huang Y., Myers M.P., Xu R.-M.;
"Crystal structure of the HP1-EMSY complex reveals an unusual mode of
HP1 binding.";
Structure 14:703-712(2006).
[24]
X-RAY CRYSTALLOGRAPHY (1.93 ANGSTROMS) OF 108-185 IN COMPLEX WITH
SGO1, AND INTERACTION WITH INCENP.
PubMed=21346195; DOI=10.1091/mbc.E11-01-0009;
Kang J., Chaudhary J., Dong H., Kim S., Brautigam C.A., Yu H.;
"Mitotic centromeric targeting of HP1 and its binding to Sgo1 are
dispensable for sister-chromatid cohesion in human cells.";
Mol. Biol. Cell 22:1181-1190(2011).
-!- FUNCTION: Component of heterochromatin. Recognizes and binds
histone H3 tails methylated at 'Lys-9', leading to epigenetic
repression. Interaction with lamin B receptor (LBR) can contribute
to the association of the heterochromatin with the inner nuclear
membrane. {ECO:0000250|UniProtKB:P83917}.
-!- SUBUNIT: Homodimer (By similarity). Interacts directly with
CHAF1A, EMSY, LBR, TIF1/TIF1A and TRIM28/TIF1B PXVXL motif via the
chromoshadow domain (PubMed:14651845, PubMed:16615912). Interacts
directly with histone H3 methylated at 'Lys-9' via the chromo
domain (By similarity). Interacts with SUV39H1 and SETDB1, KMT5B
and KMT5C (PubMed:10202156, PubMed:15899859). Interacts with PRDM6
(By similarity). Interacts with POGZ (PubMed:20850016,
PubMed:20562864). Interacts with CHAMP1 (PubMed:20850016).
Interacts with INCENP (PubMed:21346195). Interacts with SGO1; the
CBX1 homodimer binds to one molecule of SGO1 (PubMed:21346195).
Interacts with LRIF1 (via PxVxL motif) (PubMed:23542155).
{ECO:0000250|UniProtKB:P83917, ECO:0000269|PubMed:10202156,
ECO:0000269|PubMed:14651845, ECO:0000269|PubMed:15899859,
ECO:0000269|PubMed:16615912, ECO:0000269|PubMed:20562864,
ECO:0000269|PubMed:20850016, ECO:0000269|PubMed:21346195,
ECO:0000269|PubMed:23542155}.
-!- INTERACTION:
Q9H2P0:ADNP; NbExp=3; IntAct=EBI-78129, EBI-1764854;
Q6IQ32:ADNP2; NbExp=3; IntAct=EBI-78129, EBI-2838654;
Q7Z589:EMSY; NbExp=3; IntAct=EBI-78129, EBI-6598631;
P68431:HIST1H3D; NbExp=12; IntAct=EBI-78129, EBI-79722;
P10588:NR2F6; NbExp=2; IntAct=EBI-78129, EBI-2681496;
Q5FBB7:SGO1; NbExp=2; IntAct=EBI-78129, EBI-989069;
O43463:SUV39H1; NbExp=3; IntAct=EBI-78129, EBI-349968;
Q8ND82:ZNF280C; NbExp=3; IntAct=EBI-78129, EBI-8831272;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10460410,
ECO:0000269|PubMed:9169582}. Note=Unassociated with chromosomes
during mitosis.
-!- TISSUE SPECIFICITY: Expressed in all adult and embryonic tissues.
-!- PTM: Not phosphorylated.
-!- PTM: Ubiquitinated. {ECO:0000269|PubMed:20498703}.
-!- CAUTION: Was previously reported to interact with ASXL1. However,
this publication has been retracted. {ECO:0000305|PubMed:19880879,
ECO:0000305|PubMed:25750265}.
-!- WEB RESOURCE: Name=Wikipedia; Note=Heterochromatin protein 1
entry;
URL="https://en.wikipedia.org/wiki/Heterochromatin_Protein_1";
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; U35451; AAB81548.1; -; mRNA.
EMBL; BC002609; AAH02609.1; -; mRNA.
EMBL; BC021302; AAH21302.1; -; mRNA.
CCDS; CCDS11525.1; -.
PIR; G02080; G02080.
RefSeq; NP_001120700.1; NM_001127228.1.
RefSeq; NP_006798.1; NM_006807.4.
UniGene; Hs.77254; -.
PDB; 2FMM; X-ray; 1.80 A; A/B/C/D=104-175.
PDB; 3F2U; X-ray; 1.80 A; A=20-73.
PDB; 3Q6S; X-ray; 1.93 A; A/B/C/D=108-185.
PDB; 5T1G; X-ray; 1.90 A; A=108-185.
PDBsum; 2FMM; -.
PDBsum; 3F2U; -.
PDBsum; 3Q6S; -.
PDBsum; 5T1G; -.
ProteinModelPortal; P83916; -.
SMR; P83916; -.
BioGrid; 116151; 115.
DIP; DIP-28135N; -.
IntAct; P83916; 112.
MINT; P83916; -.
STRING; 9606.ENSP00000225603; -.
BindingDB; P83916; -.
ChEMBL; CHEMBL1741193; -.
iPTMnet; P83916; -.
PhosphoSitePlus; P83916; -.
SwissPalm; P83916; -.
BioMuta; CBX1; -.
DMDM; 48428808; -.
EPD; P83916; -.
PaxDb; P83916; -.
PeptideAtlas; P83916; -.
PRIDE; P83916; -.
ProteomicsDB; 57742; -.
TopDownProteomics; P83916; -.
DNASU; 10951; -.
Ensembl; ENST00000225603; ENSP00000225603; ENSG00000108468.
Ensembl; ENST00000393408; ENSP00000377060; ENSG00000108468.
GeneID; 10951; -.
KEGG; hsa:10951; -.
CTD; 10951; -.
DisGeNET; 10951; -.
EuPathDB; HostDB:ENSG00000108468.14; -.
GeneCards; CBX1; -.
HGNC; HGNC:1551; CBX1.
HPA; CAB012265; -.
MIM; 604511; gene.
neXtProt; NX_P83916; -.
OpenTargets; ENSG00000108468; -.
PharmGKB; PA26126; -.
eggNOG; ENOG410KDV3; Eukaryota.
eggNOG; ENOG4111H4A; LUCA.
GeneTree; ENSGT00940000154152; -.
HOGENOM; HOG000220852; -.
HOVERGEN; HBG000400; -.
InParanoid; P83916; -.
KO; K11585; -.
OMA; QTWEPED; -.
OrthoDB; EOG091G0RBS; -.
PhylomeDB; P83916; -.
TreeFam; TF350503; -.
SIGNOR; P83916; -.
ChiTaRS; CBX1; human.
EvolutionaryTrace; P83916; -.
GeneWiki; CBX1; -.
GenomeRNAi; 10951; -.
PRO; PR:P83916; -.
Proteomes; UP000005640; Chromosome 17.
Bgee; ENSG00000108468; Expressed in 237 organ(s), highest expression level in amniotic fluid.
CleanEx; HS_CBX1; -.
ExpressionAtlas; P83916; baseline and differential.
Genevisible; P83916; HS.
GO; GO:0000785; C:chromatin; IDA:UniProtKB.
GO; GO:0010369; C:chromocenter; IEA:Ensembl.
GO; GO:0000775; C:chromosome, centromeric region; IDA:UniProtKB.
GO; GO:0001939; C:female pronucleus; IEA:Ensembl.
GO; GO:0001940; C:male pronucleus; IEA:Ensembl.
GO; GO:0000784; C:nuclear chromosome, telomeric region; HDA:BHF-UCL.
GO; GO:0005720; C:nuclear heterochromatin; TAS:ProtInc.
GO; GO:0005654; C:nucleoplasm; TAS:ProtInc.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0005721; C:pericentric heterochromatin; IEA:Ensembl.
GO; GO:0090734; C:site of DNA damage; IMP:UniProtKB.
GO; GO:0005819; C:spindle; IDA:UniProtKB.
GO; GO:0003682; F:chromatin binding; TAS:ProtInc.
GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
GO; GO:1990226; F:histone methyltransferase binding; IPI:BHF-UCL.
GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
GO; GO:0006974; P:cellular response to DNA damage stimulus; IMP:UniProtKB.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IEA:Ensembl.
CDD; cd00024; CHROMO; 1.
InterPro; IPR016197; Chromo-like_dom_sf.
InterPro; IPR000953; Chromo/chromo_shadow_dom.
InterPro; IPR017984; Chromo_dom_subgr.
InterPro; IPR023780; Chromo_domain.
InterPro; IPR008251; Chromo_shadow_dom.
InterPro; IPR023779; Chromodomain_CS.
Pfam; PF00385; Chromo; 1.
Pfam; PF01393; Chromo_shadow; 1.
PRINTS; PR00504; CHROMODOMAIN.
SMART; SM00298; CHROMO; 2.
SMART; SM00300; ChSh; 1.
SUPFAM; SSF54160; SSF54160; 2.
PROSITE; PS00598; CHROMO_1; 1.
PROSITE; PS50013; CHROMO_2; 2.
1: Evidence at protein level;
3D-structure; Complete proteome; Direct protein sequencing;
Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome; Repeat;
Ubl conjugation.
CHAIN 1 185 Chromobox protein homolog 1.
/FTId=PRO_0000080199.
DOMAIN 21 79 Chromo 1. {ECO:0000255|PROSITE-
ProRule:PRU00053}.
DOMAIN 117 175 Chromo 2; shadow subtype.
{ECO:0000255|PROSITE-ProRule:PRU00053}.
BINDING 21 21 Histone H3K9me2. {ECO:0000250}.
BINDING 23 23 Histone H3A7. {ECO:0000250}.
BINDING 40 40 Histone H3A7. {ECO:0000250}.
BINDING 42 42 Histone H3A7. {ECO:0000250}.
BINDING 42 42 Histone H3K9me2. {ECO:0000250}.
BINDING 45 45 Histone H3K9me2. {ECO:0000250}.
BINDING 58 58 Histone H3A7. {ECO:0000250}.
BINDING 60 60 Histone H3A7. {ECO:0000250}.
BINDING 125 125 PxVxL motif. {ECO:0000250}.
BINDING 126 126 PxVxL motif. {ECO:0000250}.
BINDING 135 135 PxVxL motif. {ECO:0000250}.
BINDING 146 146 PxVxL motif. {ECO:0000250}.
BINDING 163 163 PxVxL motif. {ECO:0000250}.
BINDING 167 167 PxVxL motif. {ECO:0000250}.
BINDING 168 168 PxVxL motif. {ECO:0000250}.
BINDING 170 170 PxVxL motif. {ECO:0000250}.
MOD_RES 89 89 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:24275569}.
MOD_RES 91 91 Phosphoserine.
{ECO:0000244|PubMed:21406692}.
MOD_RES 175 175 Phosphoserine.
{ECO:0000244|PubMed:21406692}.
CROSSLNK 9 9 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25755297,
ECO:0000244|PubMed:28112733}.
CROSSLNK 33 33 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 99 99 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 150 150 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
MUTAGEN 161 161 I->E: Abolishes homodimer formation and
binding to EMSY.
{ECO:0000269|PubMed:15947784}.
STRAND 23 32 {ECO:0000244|PDB:3F2U}.
STRAND 35 42 {ECO:0000244|PDB:3F2U}.
HELIX 47 49 {ECO:0000244|PDB:3F2U}.
STRAND 51 54 {ECO:0000244|PDB:3F2U}.
HELIX 55 57 {ECO:0000244|PDB:3F2U}.
HELIX 61 68 {ECO:0000244|PDB:3F2U}.
HELIX 112 115 {ECO:0000244|PDB:2FMM}.
STRAND 119 128 {ECO:0000244|PDB:2FMM}.
STRAND 131 138 {ECO:0000244|PDB:2FMM}.
STRAND 145 148 {ECO:0000244|PDB:2FMM}.
HELIX 149 155 {ECO:0000244|PDB:2FMM}.
HELIX 157 165 {ECO:0000244|PDB:2FMM}.
STRAND 168 172 {ECO:0000244|PDB:2FMM}.
SEQUENCE 185 AA; 21418 MW; BE687AF9C66E48E3 CRC64;
MGKKQNKKKV EEVLEEEEEE YVVEKVLDRR VVKGKVEYLL KWKGFSDEDN TWEPEENLDC
PDLIAEFLQS QKTAHETDKS EGGKRKADSD SEDKGEESKP KKKKEESEKP RGFARGLEPE
RIIGATDSSG ELMFLMKWKN SDEADLVPAK EANVKCPQVV ISFYEERLTW HSYPSEDDDK
KDDKN


Related products :

Catalog number Product name Quantity
EIAAB05641 CBX,CBX1,Chromobox protein homolog 1,Heterochromatin protein 1 homolog beta,Heterochromatin protein p25,Homo sapiens,HP1 beta,HP1Hsbeta,Human,M31,Modifier 1 protein,p25beta
18-003-43118 Chromobox protein homolog 1 - Heterochromatin protein 1 homolog beta; HP1 beta; Modifier 1 protein; M31; Heterochromatin protein p25; HP1Hsbeta; p25beta Polyclonal 0.1 mg Protein A
EIAAB05642 Cbx,Cbx1,Chromobox protein homolog 1,Heterochromatin protein 1 homolog beta,Heterochromatin protein p25,HP1 beta,M31,Modifier 1 protein,Mouse,Mus musculus
EIAAB05645 CBX3,Chromobox protein homolog 3,HECH,Heterochromatin protein 1 homolog gamma,Homo sapiens,HP1 gamma,Human,Modifier 2 protein
EIAAB05646 Cbx3,Chromobox protein homolog 3,Heterochromatin protein 1 homolog gamma,HP1 gamma,M32,Modifier 2 protein,Mouse,Mus musculus
18-003-43449 Chromobox protein homolog 3 - Heterochromatin protein 1 homolog gamma; HP1 gamma; Modifier 2 protein; HECH Polyclonal 0.1 mg Protein A
18-003-43123 Chromobox protein homolog 3 - Heterochromatin protein 1 homolog gamma; HP1 gamma; Modifier 2 protein; HECH Polyclonal 0.05 mg Aff Pur
EIAAB05649 Antigen p25,CBX5,Chromobox protein homolog 5,Heterochromatin protein 1 homolog alpha,Homo sapiens,HP1 alpha,HP1A,Human
EIAAB05650 Cbx5,Chromobox protein homolog 5,Heterochromatin protein 1 homolog alpha,HP1 alpha,Hp1a,Mouse,Mus musculus
18-003-42225 Chromobox protein homolog 5 - Heterochromatin protein 1 homolog alpha; HP1 alpha; Antigen p25 Polyclonal 0.1 mg Protein A
15-288-21281 Chromobox protein homolog 5 - Heterochromatin protein 1 homolog alpha; HP1 alpha; Antigen p25 Polyclonal 0.05 mg
15-288-21281 Chromobox protein homolog 5 - Heterochromatin protein 1 homolog alpha; HP1 alpha; Antigen p25 Polyclonal 0.1 mg
EIAAB05644 Cbx2,Chromobox protein homolog 2,M33,M33,Modifier 3 protein,Mouse,Mus musculus
EIAAB43748 Homo sapiens,hTRA2-beta,Human,SFRS10,Splicing factor, arginine_serine-rich 10,TRA-2 beta,TRA2B,TRA2-beta,Transformer-2 protein homolog B,Transformer-2 protein homolog beta
63-101 anti_Swi6(fission yeast)antibody, rabbit serum Swi6 protein of fission yeast is a functional and structural homolog of HP1 (Heterochromatin Protein 1) of animals and is involved in the formation of he 50 ul
63-102 anti_Swi6(fission yeast)antibody, rabbit serum Swi6 protein of fission yeast is a functional and structural homolog of HP1 (Heterochromatin Protein 1) of animals and is involved in the formation of he 250 ul
EIAAB43751 Mouse,Mus musculus,Sfrs10,SIG-41,Silg41,Silica-induced gene 41 protein,Splicing factor, arginine_serine-rich 10,TRA-2 beta,Tra2b,TRA2-beta,Transformer-2 protein homolog B,Transformer-2 protein homolog
EIAAB43749 RA301,Rat,Rattus norvegicus,Sfrs10,Splicing factor, arginine_serine-rich 10,TRA-2 beta,Tra2b,TRA2-beta,Transformer-2 protein homolog B,Transformer-2 protein homolog beta
EIAAB43750 Bos taurus,Bovine,SFRS10,Splicing factor, arginine_serine-rich 10,TRA-2 beta,TRA2B,TRA2-beta,Transformer-2 protein homolog B,Transformer-2 protein homolog beta
E0093c ELISA kit C-C motif chemokine 4 homolog,CCL4,Chicken,Gallus gallus,Macrophage inflammatory protein 1-beta homolog,MIP-1-beta,SCYA4,Small-inducible cytokine A4 homolog 96T
E0093c ELISA C-C motif chemokine 4 homolog,CCL4,Chicken,Gallus gallus,Macrophage inflammatory protein 1-beta homolog,MIP-1-beta,SCYA4,Small-inducible cytokine A4 homolog 96T
U0093c CLIA C-C motif chemokine 4 homolog,CCL4,Chicken,Gallus gallus,Macrophage inflammatory protein 1-beta homolog,MIP-1-beta,SCYA4,Small-inducible cytokine A4 homolog 96T
CSB-EL010692BO Bovine Heterochromatin protein 1-binding protein 3(HP1BP3) ELISA kit SpeciesBovine 96T
CSB-EL010692CH Chicken Heterochromatin protein 1-binding protein 3(HP1BP3) ELISA kit SpeciesChicken 96T
CSB-EL010692MO Mouse Heterochromatin protein 1-binding protein 3(HP1BP3) ELISA kit SpeciesMouse 96T


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur | Gentaur





GENTAUR Ltd.
Unicorn House, Station Cl
Hertfordshire, Potters Bar EN6 1TL
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017
RIB 30004 00187 00010092253 10
BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG
IBAN FR76 3000 4001 8700 0100 9225 310
france@gentaur.com | Gentaur | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: +49 0241 40 08 90 86, +49 0241 95 78 94 78, +49 0241 40 08 90 86
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur | Gentaur