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Chromobox protein homolog 5 (Antigen p25) (Heterochromatin protein 1 homolog alpha) (HP1 alpha)

 CBX5_HUMAN              Reviewed;         191 AA.
P45973; B2R8T9;
01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
01-NOV-1995, sequence version 1.
25-APR-2018, entry version 184.
RecName: Full=Chromobox protein homolog 5;
AltName: Full=Antigen p25;
AltName: Full=Heterochromatin protein 1 homolog alpha;
Short=HP1 alpha;
Name=CBX5; Synonyms=HP1A;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=8505380;
Saunders W.S., Chue C., Goebl M., Craig C., Clark R.F., Powers J.A.,
Eissenberg J.C., Elgin S.C.R., Rothfield N.F., Earnshaw W.C.;
"Molecular cloning of a human homologue of Drosophila heterochromatin
protein HP1 using anti-centromere autoantibodies with anti-chromo
specificity.";
J. Cell Sci. 104:573-582(1993).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Kidney;
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).
[3]
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.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Placenta;
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).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 2-191.
PubMed=8663349; DOI=10.1074/jbc.271.25.14653;
Ye Q., Worman H.J.;
"Interaction between an integral protein of the nuclear envelope inner
membrane and human chromodomain proteins homologous to Drosophila
HP1.";
J. Biol. Chem. 271:14653-14656(1996).
[6]
PROTEIN SEQUENCE OF 33-40; 56-68; 126-154 AND 160-184, AND
IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Fetal brain cortex;
Lubec G., Chen W.-Q., Sun Y.;
Submitted (DEC-2008) to UniProtKB.
[7]
INTERACTION WITH LBR AND CBX3.
PubMed=9169472; DOI=10.1074/jbc.272.23.14983;
Ye Q., Callebaut I., Pezhman A., Courvalin J.-C., Worman H.J.;
"Domain-specific interactions of human HP1-type chromodomain proteins
and inner nuclear membrane protein LBR.";
J. Biol. Chem. 272:14983-14989(1997).
[8]
SUBCELLULAR LOCATION, AND 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).
[9]
INTERACTION WITH TRIM24.
PubMed=11313457; DOI=10.1128/MCB.21.10.3314-3324.2001;
Seeler J.-S., Marchio A., Losson R., Desterro J.M.P., Hay R.T.,
Chambon P., Dejean A.;
"Common properties of nuclear protein SP100 and TIF1alpha chromatin
factor: role of SUMO modification.";
Mol. Cell. Biol. 21:3314-3324(2001).
[10]
INTERACTION WITH HISTONE H3 LYS-9.
PubMed=11242053; DOI=10.1038/35065132;
Lachner M., O'Carroll D., Rea S., Mechtler K., Jenuwein T.;
"Methylation of histone H3 lysine 9 creates a binding site for HP1
proteins.";
Nature 410:116-120(2001).
[11]
INTERACTION WITH MIS12 AND DSN1.
PubMed=15502821; DOI=10.1038/ncb1187;
Obuse C., Iwasaki O., Kiyomitsu T., Goshima G., Toyoda Y.,
Yanagida M.;
"A conserved Mis12 centromere complex is linked to heterochromatic HP1
and outer kinetochore protein Zwint-1.";
Nat. Cell Biol. 6:1135-1141(2004).
[12]
INTERACTION WITH ATRX; CHAF1A; LBR; NIPBL; SP100; STAM2 AND TRIM28.
PubMed=15882967; DOI=10.1016/j.bbrc.2005.04.016;
Lechner M.S., Schultz D.C., Negorev D., Maul G.G., Rauscher F.J. III;
"The mammalian heterochromatin protein 1 binds diverse nuclear
proteins through a common motif that targets the chromoshadow
domain.";
Biochem. Biophys. Res. Commun. 331:929-937(2005).
[13]
INTERACTION WITH JC VIRUS AGNOPROTEIN.
PubMed=15864296; DOI=10.1038/sj.embor.7400406;
Okada Y., Suzuki T., Sunden Y., Orba Y., Kose S., Imamoto N.,
Takahashi H., Tanaka S., Hall W.W., Nagashima K., Sawa H.;
"Dissociation of heterochromatin protein 1 from lamin B receptor
induced by human polyomavirus agnoprotein: role in nuclear egress of
viral particles.";
EMBO Rep. 6:452-457(2005).
[14]
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).
[15]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-92, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11; SER-12; SER-13;
SER-14 AND SER-92, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[18]
INTERACTION WITH HNRNPU, AND SUBCELLULAR LOCATION.
PubMed=19617346; DOI=10.1074/jbc.M109.037929;
Ameyar-Zazoua M., Souidi M., Fritsch L., Robin P., Thomas A.,
Hamiche A., Percipalle P., Ait-Si-Ali S., Harel-Bellan A.;
"Physical and functional interaction between heterochromatin protein
1alpha and the RNA-binding protein heterogeneous nuclear
ribonucleoprotein U.";
J. Biol. Chem. 284:27974-27979(2009).
[19]
INTERACTION WITH RRP1B.
PubMed=19710015; DOI=10.1074/jbc.M109.023457;
Crawford N.P., Yang H., Mattaini K.R., Hunter K.W.;
"The metastasis efficiency modifier ribosomal RNA processing 1 homolog
B (RRP1B) is a chromatin-associated factor.";
J. Biol. Chem. 284:28660-28673(2009).
[20]
FUNCTION, AND HISTONE-BINDING.
PubMed=19783980; DOI=10.1038/nature08448;
Dawson M.A., Bannister A.J., Gottgens B., Foster S.D., Bartke T.,
Green A.R., Kouzarides T.;
"JAK2 phosphorylates histone H3Y41 and excludes HP1alpha from
chromatin.";
Nature 461:819-822(2009).
[21]
INTERACTION WITH BAHD1.
PubMed=19666599; DOI=10.1073/pnas.0901259106;
Bierne H., Tham T.N., Batsche E., Dumay A., Leguillou M.,
Kerneis-Golsteyn S., Regnault B., Seeler J.S., Muchardt C.,
Feunteun J., Cossart P.;
"Human BAHD1 promotes heterochromatic gene silencing.";
Proc. Natl. Acad. Sci. U.S.A. 106:13826-13831(2009).
[22]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11; SER-14; SER-92 AND
SER-97, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[23]
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).
[24]
INTERACTION WITH ASXL1.
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).
[25]
INTERACTION WITH POGZ; TRIM28; CHAF1A; NIPBL AND INCENP, AND
MUTAGENESIS OF ILE-165 AND TRP-174.
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).
[26]
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).
[27]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11; SER-12; SER-13;
SER-14; SER-92 AND SER-97, 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).
[28]
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).
[29]
INTERACTION WITH INCENP, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
TRP-174.
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).
[30]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13; SER-14; SER-95 AND
SER-97, 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).
[31]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[32]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14; SER-92 AND SER-95,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and 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).
[33]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11; SER-12; SER-13 AND
SER-14, 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).
[34]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-32 AND LYS-102, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25218447; DOI=10.1038/nsmb.2890;
Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
Vertegaal A.C.;
"Uncovering global SUMOylation signaling networks in a site-specific
manner.";
Nat. Struct. Mol. Biol. 21:927-936(2014).
[35]
INTERACTION WITH PRR14.
PubMed=25906157; DOI=10.1038/cddis.2015.103;
Yang M., Yuan Z.M.;
"A novel role of PRR14 in the regulation of skeletal myogenesis.";
Cell Death Dis. 6:E1734-E1734(2015).
[36]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-32 AND LYS-102, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
Vertegaal A.C.;
"SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
Cell Rep. 10:1778-1791(2015).
[37]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-32 AND LYS-102, 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).
[38]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-32; LYS-91; LYS-102;
LYS-106; LYS-154 AND LYS-184, 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).
[39]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 18-75 IN COMPLEX WITH
TRIMETHYLATED HISTONE H3 PEPTIDE, SUBUNIT, AND X-RAY CRYSTALLOGRAPHY
(2.48 ANGSTROMS) OF 110-173.
PubMed=21047797; DOI=10.1074/jbc.M110.191411;
Kaustov L., Ouyang H., Amaya M., Lemak A., Nady N., Duan S.,
Wasney G.A., Li Z., Vedadi M., Schapira M., Min J., Arrowsmith C.H.;
"Recognition and specificity determinants of the human cbx
chromodomains.";
J. Biol. Chem. 286:521-529(2011).
[40]
INTERACTION WITH HP1BP3, AND MUTAGENESIS OF TRP-174.
PubMed=20042602; DOI=10.1074/jbc.M109.092833;
Hayashihara K., Uchiyama S., Shimamoto S., Kobayashi S., Tomschik M.,
Wakamatsu H., No D., Sugahara H., Hori N., Noda M., Ohkubo T.,
Zlatanova J., Matsunaga S., Fukui K.;
"The middle region of an HP1-binding protein, HP1-BP74, associates
with linker DNA at the entry/exit site of nucleosomal DNA.";
J. Biol. Chem. 285:6498-6507(2010).
-!- FUNCTION: Component of heterochromatin that recognizes and binds
histone H3 tails methylated at 'Lys-9' (H3K9me), leading to
epigenetic repression. In contrast, it is excluded from chromatin
when 'Tyr-41' of histone H3 is phosphorylated (H3Y41ph). Can
interact with lamin-B receptor (LBR). This interaction can
contribute to the association of the heterochromatin with the
inner nuclear membrane. Involved in the formation of functional
kinetochore through interaction with MIS12 complex proteins.
{ECO:0000269|PubMed:19783980}.
-!- SUBUNIT: Interacts with KMT5B and KMT5C (By similarity). Interacts
with HP1BP3 (PubMed:20042602). Interacts directly with ATRX,
CHAF1A, LBR, NIPBL, SP100, STAM2 and TRIM28 via the chromoshadow
domain (PubMed:15882967, PubMed:9169472). Can interact directly
with CBX3 via the chromoshadow domain (PubMed:9169472). Interacts
with histone H3 methylated at 'Lys-9' (PubMed:11242053,
PubMed:21047797). Interacts with BAHD1, MIS12 and DSN1
(PubMed:15502821, PubMed:19666599). Interacts with POGZ; POGZ and
PXVXL motif-containing proteins such as INCENP and TRIM28 compete
for interaction with CBX5 (PubMed:20562864, PubMed:20850016,
PubMed:21346195). Interacts with INCENP and TRIM24
(PubMed:11313457). Interacts with JC virus agnoprotein; this
interaction induces the dissociation of CBX5 from LBR, resulting
in destabilization of the nuclear envelope (PubMed:15864296).
Interacts with CHAMP1 (PubMed:20850016). Interacts with ASXL1
(PubMed:19880879). Interacts with PRR14 (via N-terminus)
(PubMed:25906157). Interacts with RRP1B (PubMed:19710015).
Interacts with HNRNPU (via C-terminus); this interaction is, at
least in part, RNA-dependent (PubMed:19617346).
{ECO:0000250|UniProtKB:Q61686, ECO:0000269|PubMed:11242053,
ECO:0000269|PubMed:11313457, ECO:0000269|PubMed:15502821,
ECO:0000269|PubMed:15864296, ECO:0000269|PubMed:15882967,
ECO:0000269|PubMed:15899859, ECO:0000269|PubMed:19617346,
ECO:0000269|PubMed:19666599, ECO:0000269|PubMed:19710015,
ECO:0000269|PubMed:19880879, ECO:0000269|PubMed:20042602,
ECO:0000269|PubMed:20562864, ECO:0000269|PubMed:20850016,
ECO:0000269|PubMed:21047797, ECO:0000269|PubMed:21346195,
ECO:0000269|PubMed:25906157, ECO:0000269|PubMed:9169472}.
-!- INTERACTION:
Self; NbExp=2; IntAct=EBI-78219, EBI-78219;
Q9H2P0:ADNP; NbExp=3; IntAct=EBI-78219, EBI-1764854;
P46100:ATRX; NbExp=2; IntAct=EBI-78219, EBI-396461;
Q13111:CHAF1A; NbExp=7; IntAct=EBI-78219, EBI-1020839;
P84243:H3F3B; NbExp=2; IntAct=EBI-78219, EBI-120658;
P68431:HIST1H3D; NbExp=9; IntAct=EBI-78219, EBI-79722;
Q9NQS7:INCENP; NbExp=11; IntAct=EBI-78219, EBI-307907;
P28838:LAP3; NbExp=4; IntAct=EBI-78219, EBI-2339312;
Q14739:LBR; NbExp=4; IntAct=EBI-78219, EBI-1055147;
Q5ZUS4:legAS4 (xeno); NbExp=6; IntAct=EBI-78219, EBI-8871796;
Q5T3J3:LRIF1; NbExp=3; IntAct=EBI-78219, EBI-473196;
Q9UIS9:MBD1; NbExp=6; IntAct=EBI-78219, EBI-867196;
Q7Z3K3:POGZ; NbExp=7; IntAct=EBI-78219, EBI-1389308;
Q9BWN1:PRR14; NbExp=5; IntAct=EBI-78219, EBI-748167;
Q9BQF6:SENP7; NbExp=4; IntAct=EBI-78219, EBI-766251;
Q5FBB7:SGO1; NbExp=3; IntAct=EBI-78219, EBI-989069;
P23497-2:SP100; NbExp=6; IntAct=EBI-78219, EBI-6589365;
O43463:SUV39H1; NbExp=9; IntAct=EBI-78219, EBI-349968;
Q13263:TRIM28; NbExp=10; IntAct=EBI-78219, EBI-78139;
Q14191:WRN; NbExp=3; IntAct=EBI-78219, EBI-368417;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10460410,
ECO:0000269|PubMed:19617346}. Chromosome
{ECO:0000269|PubMed:10460410}. Chromosome, centromere
{ECO:0000269|PubMed:10460410, ECO:0000269|PubMed:21346195}.
Note=Colocalizes with HNRNPU in the nucleus (PubMed:19617346).
Component of centromeric and pericentromeric heterochromatin.
Associates with chromosomes during mitosis. Associates
specifically with chromatin during metaphase and anaphase.
{ECO:0000269|PubMed:19617346}.
-!- PTM: Phosphorylation of HP1 and LBR may be responsible for some of
the alterations in chromatin organization and nuclear structure
which occur at various times during the cell cycle (By
similarity). Phosphorylated during interphase and possibly hyper-
phosphorylated during mitosis. {ECO:0000250,
ECO:0000269|PubMed:10460410}.
-!- PTM: Ubiquitinated. {ECO:0000269|PubMed:20498703}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; S62077; AAB26994.1; -; mRNA.
EMBL; L07515; AAA72327.1; -; mRNA.
EMBL; AK313506; BAG36286.1; -; mRNA.
EMBL; CH471054; EAW96759.1; -; Genomic_DNA.
EMBL; BC006821; AAH06821.1; -; mRNA.
EMBL; U26311; AAC50553.1; -; mRNA.
CCDS; CCDS8875.1; -.
PIR; G01808; G01808.
RefSeq; NP_001120793.1; NM_001127321.1.
RefSeq; NP_001120794.1; NM_001127322.1.
RefSeq; NP_036249.1; NM_012117.2.
UniGene; Hs.349283; -.
PDB; 3FDT; X-ray; 2.00 A; A=18-75.
PDB; 3I3C; X-ray; 2.48 A; A/B/C/D=110-173.
PDBsum; 3FDT; -.
PDBsum; 3I3C; -.
ProteinModelPortal; P45973; -.
SMR; P45973; -.
BioGrid; 117030; 185.
CORUM; P45973; -.
DIP; DIP-5986N; -.
IntAct; P45973; 155.
MINT; P45973; -.
STRING; 9606.ENSP00000209875; -.
ChEMBL; CHEMBL3826867; -.
iPTMnet; P45973; -.
PhosphoSitePlus; P45973; -.
BioMuta; CBX5; -.
DMDM; 1170338; -.
EPD; P45973; -.
PaxDb; P45973; -.
PeptideAtlas; P45973; -.
PRIDE; P45973; -.
TopDownProteomics; P45973; -.
DNASU; 23468; -.
Ensembl; ENST00000209875; ENSP00000209875; ENSG00000094916.
Ensembl; ENST00000439541; ENSP00000401009; ENSG00000094916.
Ensembl; ENST00000550411; ENSP00000449207; ENSG00000094916.
GeneID; 23468; -.
KEGG; hsa:23468; -.
CTD; 23468; -.
DisGeNET; 23468; -.
EuPathDB; HostDB:ENSG00000094916.13; -.
GeneCards; CBX5; -.
HGNC; HGNC:1555; CBX5.
HPA; CAB017548; -.
HPA; HPA016699; -.
MIM; 604478; gene.
neXtProt; NX_P45973; -.
OpenTargets; ENSG00000094916; -.
PharmGKB; PA26130; -.
eggNOG; ENOG410IUAB; Eukaryota.
eggNOG; ENOG4111I3N; LUCA.
GeneTree; ENSGT00510000046310; -.
HOGENOM; HOG000220852; -.
HOVERGEN; HBG000400; -.
InParanoid; P45973; -.
KO; K11587; -.
OMA; YSEKHNT; -.
OrthoDB; EOG091G0RBS; -.
PhylomeDB; P45973; -.
TreeFam; TF350503; -.
Reactome; R-HSA-4551638; SUMOylation of chromatin organization proteins.
Reactome; R-HSA-8953750; Transcriptional Regulation by E2F6.
Reactome; R-HSA-983231; Factors involved in megakaryocyte development and platelet production.
SIGNOR; P45973; -.
ChiTaRS; CBX5; human.
EvolutionaryTrace; P45973; -.
GeneWiki; CBX5_(gene); -.
GenomeRNAi; 23468; -.
PRO; PR:P45973; -.
Proteomes; UP000005640; Chromosome 12.
Bgee; ENSG00000094916; -.
CleanEx; HS_CBX5; -.
ExpressionAtlas; P45973; baseline and differential.
Genevisible; P45973; HS.
GO; GO:0010369; C:chromocenter; IEA:Ensembl.
GO; GO:0000118; C:histone deacetylase complex; ISS:BHF-UCL.
GO; GO:0035097; C:histone methyltransferase complex; ISS:BHF-UCL.
GO; GO:0000776; C:kinetochore; IEA:Ensembl.
GO; GO:0000784; C:nuclear chromosome, telomeric region; HDA:BHF-UCL.
GO; GO:0005635; C:nuclear envelope; TAS:ProtInc.
GO; GO:0005720; C:nuclear heterochromatin; TAS:ProtInc.
GO; GO:0031618; C:nuclear pericentric heterochromatin; NAS:BHF-UCL.
GO; GO:0005730; C:nucleolus; IDA:BHF-UCL.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0005721; C:pericentric heterochromatin; ISS:BHF-UCL.
GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
GO; GO:1990904; C:ribonucleoprotein complex; IDA:UniProtKB.
GO; GO:0017053; C:transcriptional repressor complex; ISS:BHF-UCL.
GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
GO; GO:0042826; F:histone deacetylase binding; IEA:Ensembl.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0035064; F:methylated histone binding; IDA:UniProtKB.
GO; GO:0030674; F:protein binding, bridging; ISS:BHF-UCL.
GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
GO; GO:0044877; F:protein-containing complex binding; IDA:UniProtKB.
GO; GO:0070491; F:repressing transcription factor binding; ISS:BHF-UCL.
GO; GO:0043021; F:ribonucleoprotein complex binding; IDA:UniProtKB.
GO; GO:0007596; P:blood coagulation; TAS:Reactome.
GO; GO:0070317; P:negative regulation of G0 to G1 transition; TAS:Reactome.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:UniProtKB.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
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; Acetylation; Centromere; Chromosome; Complete proteome;
Direct protein sequencing; Host-virus interaction; Isopeptide bond;
Nucleus; Phosphoprotein; Reference proteome; Repeat; Ubl conjugation.
CHAIN 1 191 Chromobox protein homolog 5.
/FTId=PRO_0000080208.
DOMAIN 20 78 Chromo 1. {ECO:0000255|PROSITE-
ProRule:PRU00053}.
DOMAIN 121 179 Chromo 2; shadow subtype.
{ECO:0000255|PROSITE-ProRule:PRU00053}.
REGION 116 191 Interaction with ASXL1.
{ECO:0000269|PubMed:19880879}.
COMPBIAS 11 14 Poly-Ser.
MOD_RES 11 11 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:24275569}.
MOD_RES 12 12 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:24275569}.
MOD_RES 13 13 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:24275569}.
MOD_RES 14 14 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 40 40 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q13185}.
MOD_RES 92 92 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 95 95 Phosphoserine.
{ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 97 97 Phosphoserine.
{ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692}.
CROSSLNK 32 32 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:25755297,
ECO:0000244|PubMed:25772364,
ECO:0000244|PubMed:28112733}.
CROSSLNK 91 91 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 102 102 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:25755297,
ECO:0000244|PubMed:25772364,
ECO:0000244|PubMed:28112733}.
CROSSLNK 106 106 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 154 154 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 184 184 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
MUTAGEN 165 165 I->E: No effect on interaction with POGZ.
Abolishes interaction with TRIM28, CHAF1A
and NIPBL. {ECO:0000269|PubMed:20562864}.
MUTAGEN 174 174 W->A: Abolishes interaction with TRIM28,
CHAF1A, NIPBL and HP1BP3, fails to
localize to centromeres in mitosis.
{ECO:0000269|PubMed:20042602,
ECO:0000269|PubMed:20562864,
ECO:0000269|PubMed:21346195}.
STRAND 19 31 {ECO:0000244|PDB:3FDT}.
STRAND 34 41 {ECO:0000244|PDB:3FDT}.
HELIX 46 48 {ECO:0000244|PDB:3FDT}.
STRAND 50 53 {ECO:0000244|PDB:3FDT}.
HELIX 54 56 {ECO:0000244|PDB:3FDT}.
HELIX 60 67 {ECO:0000244|PDB:3FDT}.
HELIX 116 119 {ECO:0000244|PDB:3I3C}.
STRAND 123 130 {ECO:0000244|PDB:3I3C}.
STRAND 137 142 {ECO:0000244|PDB:3I3C}.
STRAND 148 152 {ECO:0000244|PDB:3I3C}.
HELIX 153 159 {ECO:0000244|PDB:3I3C}.
HELIX 161 168 {ECO:0000244|PDB:3I3C}.
SEQUENCE 191 AA; 22225 MW; 16FFC476367093B1 CRC64;
MGKKTKRTAD SSSSEDEEEY VVEKVLDRRV VKGQVEYLLK WKGFSEEHNT WEPEKNLDCP
ELISEFMKKY KKMKEGENNK PREKSESNKR KSNFSNSADD IKSKKKREQS NDIARGFERG
LEPEKIIGAT DSCGDLMFLM KWKDTDEADL VLAKEANVKC PQIVIAFYEE RLTWHAYPED
AENKEKETAK S


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