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

Histone-binding protein RBBP7 (Histone acetyltransferase type B subunit 2) (Nucleosome-remodeling factor subunit RBAP46) (Retinoblastoma-binding protein 7) (RBBP-7) (Retinoblastoma-binding protein p46)

 RBBP7_HUMAN             Reviewed;         425 AA.
Q16576; Q5JP00;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
01-NOV-1997, sequence version 1.
23-MAY-2018, entry version 184.
RecName: Full=Histone-binding protein RBBP7;
AltName: Full=Histone acetyltransferase type B subunit 2;
AltName: Full=Nucleosome-remodeling factor subunit RBAP46;
AltName: Full=Retinoblastoma-binding protein 7;
Short=RBBP-7;
AltName: Full=Retinoblastoma-binding protein p46;
Name=RBBP7; Synonyms=RBAP46;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND INTERACTION WITH RB1.
PubMed=7503932; DOI=10.1074/jbc.270.43.25507;
Qian Y.-W., Lee E.Y.-H.P.;
"Dual retinoblastoma-binding proteins with properties related to a
negative regulator of ras in yeast.";
J. Biol. Chem. 270:25507-25513(1995).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Nielsen M.S., Rasmussen H.H., Dejgaard K., Celis J.E., Leffers H.;
Submitted (MAY-1993) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15772651; DOI=10.1038/nature03440;
Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A.,
Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G.,
Jones M.C., Hurles M.E., Andrews T.D., Scott C.E., Searle S.,
Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R.,
Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L.,
Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A.,
Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S.,
Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R.,
Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M.,
Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N.,
Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D.,
Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W.,
Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C.,
Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C.,
Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
Corby N., Connor R.E., David R., Davies J., Davis C., Davis J.,
Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S.,
Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I.,
Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L.,
Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P.,
Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S.,
Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A.,
Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J.,
Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J.,
Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S.,
de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z.,
Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C.,
Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W.,
Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T.,
Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I.,
Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N.,
Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J.,
Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E.,
Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S.,
Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T.,
Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S.,
Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L.,
Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A.,
Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L.,
Williams G., Williams L., Williamson A., Williamson H., Wilming L.,
Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H.,
Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A.,
Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A.,
Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T.,
Gibbs R.A., Beck S., Rogers J., Bentley D.R.;
"The DNA sequence of the human X chromosome.";
Nature 434:325-337(2005).
[5]
PARTIAL PROTEIN SEQUENCE, AND IDENTIFICATION IN THE SIN3 HDAC COMPLEX.
PubMed=9150135; DOI=10.1016/S0092-8674(00)80216-0;
Zhang Y., Iratni R., Erdjument-Bromage H., Tempst P., Reinberg D.;
"Histone deacetylases and SAP18, a novel polypeptide, are components
of a human Sin3 complex.";
Cell 89:357-364(1997).
[6]
IDENTIFICATION IN THE NURD COMPLEX.
PubMed=9790534; DOI=10.1016/S0092-8674(00)81758-4;
Zhang Y., LeRoy G., Seelig H.-P., Lane W.S., Reinberg D.;
"The dermatomyositis-specific autoantigen Mi2 is a component of a
complex containing histone deacetylase and nucleosome remodeling
activities.";
Cell 95:279-289(1998).
[7]
INTERACTION WITH HAT1 AND HISTONE H4.
PubMed=9427644; DOI=10.1016/S0960-9822(98)70040-5;
Verreault A., Kaufman P.D., Kobayashi R., Stillman B.;
"Nucleosomal DNA regulates the core-histone-binding subunit of the
human Hat1 acetyltransferase.";
Curr. Biol. 8:96-108(1998).
[8]
IDENTIFICATION IN THE SIN3 HDAC COMPLEX.
PubMed=9651585; DOI=10.1016/S1097-2765(00)80102-1;
Zhang Y., Sun Z.-W., Iratni R., Erdjument-Bromage H., Tempst P.,
Hampsey M., Reinberg D.;
"SAP30, a novel protein conserved between human and yeast, is a
component of a histone deacetylase complex.";
Mol. Cell 1:1021-1031(1998).
[9]
IDENTIFICATION IN THE NURD COMPLEX.
PubMed=10444591; DOI=10.1101/gad.13.15.1924;
Zhang Y., Ng H.-H., Erdjument-Bromage H., Tempst P., Bird A.,
Reinberg D.;
"Analysis of the NuRD subunits reveals a histone deacetylase core
complex and a connection with DNA methylation.";
Genes Dev. 13:1924-1935(1999).
[10]
INTERACTION WITH BRCA1 AND RB1.
PubMed=10220405; DOI=10.1073/pnas.96.9.4983;
Yarden R.I., Brody L.C.;
"BRCA1 interacts with components of the histone deacetylase complex.";
Proc. Natl. Acad. Sci. U.S.A. 96:4983-4988(1999).
[11]
FUNCTION, AND INTERACTION WITH CREBBP.
PubMed=10866654; DOI=10.1128/MCB.20.14.4970-4978.2000;
Zhang Q., Vo N., Goodman R.H.;
"Histone binding protein RbAp48 interacts with a complex of CREB
binding protein and phosphorylated CREB.";
Mol. Cell. Biol. 20:4970-4978(2000).
[12]
IDENTIFICATION IN THE NURD COMPLEX.
PubMed=11102443; DOI=10.1074/jbc.M007372200;
Humphrey G.W., Wang Y., Russanova V.R., Hirai T., Qin J., Nakatani Y.,
Howard B.H.;
"Stable histone deacetylase complexes distinguished by the presence of
SANT domain proteins CoREST/kiaa0071 and Mta-L1.";
J. Biol. Chem. 276:6817-6824(2001).
[13]
IDENTIFICATION IN THE SIN3 HDAC COMPLEX.
PubMed=11118440; DOI=10.1074/jbc.M007664200;
Skowyra D., Zeremski M., Neznanov N., Li M., Choi Y., Uesugi M.,
Hauser C.A., Gu W., Gudkov A.V., Qin J.;
"Differential association of products of alternative transcripts of
the candidate tumor suppressor ING1 with the mSin3/HDAC1
transcriptional corepressor complex.";
J. Biol. Chem. 276:8734-8739(2001).
[14]
IDENTIFICATION IN THE PRC2/EED-EZH2 COMPLEX WITH EED; EZH2; RBBP4 AND
SUZ12, AND METHYLTRANSFERASE ACTIVITY OF THE COMPLEX.
PubMed=12435631; DOI=10.1101/gad.1035902;
Kuzmichev A., Nishioka K., Erdjument-Bromage H., Tempst P.,
Reinberg D.;
"Histone methyltransferase activity associated with a human
multiprotein complex containing the Enhancer of Zeste protein.";
Genes Dev. 16:2893-2905(2002).
[15]
IDENTIFICATION IN THE SIN3 HDAC COMPLEX.
PubMed=11784859; DOI=10.1128/MCB.22.3.835-848.2002;
Kuzmichev A., Zhang Y., Erdjument-Bromage H., Tempst P., Reinberg D.;
"Role of the Sin3-histone deacetylase complex in growth regulation by
the candidate tumor suppressor p33(ING1).";
Mol. Cell. Biol. 22:835-848(2002).
[16]
IDENTIFICATION IN THE NURF COMPLEX, AND IDENTIFICATION BY MASS
SPECTROMETRY.
PubMed=14609955; DOI=10.1093/emboj/cdg582;
Barak O., Lazzaro M.A., Lane W.S., Speicher D.W., Picketts D.J.,
Shiekhattar R.;
"Isolation of human NURF: a regulator of Engrailed gene expression.";
EMBO J. 22:6089-6100(2003).
[17]
IDENTIFICATION IN THE MTA1 HDAC COMPLEX.
PubMed=12920132; DOI=10.1074/jbc.M302955200;
Yao Y.-L., Yang W.-M.;
"The metastasis-associated proteins 1 and 2 form distinct protein
complexes with histone deacetylase activity.";
J. Biol. Chem. 278:42560-42568(2003).
[18]
INTERACTION WITH MBD3L1.
PubMed=15456747; DOI=10.1074/jbc.M409149200;
Jiang C.-L., Jin S.-G., Pfeifer G.P.;
"MBD3L1 is a transcriptional repressor that interacts with methyl-CpG-
binding protein 2 (MBD2) and components of the NuRD complex.";
J. Biol. Chem. 279:52456-52464(2004).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-354, 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).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-354, 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).
[21]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[22]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-4, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[23]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2 (ISOFORM 2),
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-354, PHOSPHORYLATION
[LARGE SCALE ANALYSIS] AT SER-13 (ISOFORM 2), CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS] (ISOFORM 2), 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).
[24]
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).
[25]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE
SCALE ANALYSIS] AT SER-3, CLEAVAGE OF INITIATOR METHIONINE [LARGE
SCALE ANALYSIS], 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).
[26]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND 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).
[27]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3; THR-10 AND SER-354,
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).
[28]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-95, 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).
[29]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-159, 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).
[30]
INTERACTION WITH CENPA.
PubMed=25556658; DOI=10.1016/j.devcel.2014.11.030;
Yu Z., Zhou X., Wang W., Deng W., Fang J., Hu H., Wang Z., Li S.,
Cui L., Shen J., Zhai L., Peng S., Wong J., Dong S., Yuan Z., Ou G.,
Zhang X., Xu P., Lou J., Yang N., Chen P., Xu R.M., Li G.;
"Dynamic phosphorylation of CENP-A at Ser68 orchestrates its cell-
cycle-dependent deposition at centromeres.";
Dev. Cell 32:68-81(2015).
[31]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-4; LYS-101; LYS-155 AND
LYS-159, 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).
[32]
X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 2-411 IN COMPLEX WITH HISTONE
H4, AND DOMAINS WD REPEATS.
PubMed=18571423; DOI=10.1016/j.str.2008.05.006;
Murzina N.V., Pei X.Y., Zhang W., Sparkes M., Vicente-Garcia J.,
Pratap J.V., McLaughlin S.H., Ben-Shahar T.R., Verreault A.,
Luisi B.F., Laue E.D.;
"Structural basis for the recognition of histone H4 by the histone-
chaperone RbAp46.";
Structure 16:1077-1085(2008).
-!- FUNCTION: Core histone-binding subunit that may target chromatin
remodeling factors, histone acetyltransferases and histone
deacetylases to their histone substrates in a manner that is
regulated by nucleosomal DNA. Component of several complexes which
regulate chromatin metabolism. These include the type B histone
acetyltransferase (HAT) complex, which is required for chromatin
assembly following DNA replication; the core histone deacetylase
(HDAC) complex, which promotes histone deacetylation and
consequent transcriptional repression; the nucleosome remodeling
and histone deacetylase complex (the NuRD complex), which promotes
transcriptional repression by histone deacetylation and nucleosome
remodeling; and the PRC2/EED-EZH2 complex, which promotes
repression of homeotic genes during development; and the NURF
(nucleosome remodeling factor) complex.
{ECO:0000269|PubMed:10866654}.
-!- SUBUNIT: Binds directly to helix 1 of the histone fold of histone
H4, a region that is not accessible when H4 is in chromatin.
Subunit of the type B histone acetyltransferase (HAT) complex,
composed of RBBP7 and HAT1. Subunit of the core histone
deacetylase (HDAC) complex, which is composed of HDAC1, HDAC2,
RBBP4 and RBBP7. The core HDAC complex associates with SIN3A,
ARID4B/SAP180, SAP18, SAP30, SAP130, SUDS3/SAP45 and possibly
ARID4A/RBP1 and ING1 to form the SIN3 HDAC complex. The core HDAC
complex may also associate with MTA2, MBD3, CHD3 and CHD4 to form
the nucleosome remodeling and histone deacetylase complex (the
NuRD complex). The NuRD complex may also interact with MBD3L1 and
MBD3L2. Interacts with MTA1. Subunit of the PRC2/EED-EZH2 complex,
which is composed of at least EED, EZH2, RBBP4, RBBP7 and SUZ12
(PubMed:12435631). The PRC2/EED-EZH2 complex may also associate
with HDAC1. Part of the nucleosome remodeling factor (NURF)
complex which consists of SMARCA1; BPTF; RBBP4 and RBBP7.
Interacts with the viral protein-binding domain of the
retinoblastoma protein (RB1) (PubMed:7503932, PubMed:10220405).
Interacts with CREBBP, and this interaction may be enhanced by the
binding of phosphorylated CREB1 to CREBBP. Interacts with BRCA1,
HDAC7 and SUV39H1. Interacts with CENPA (PubMed:25556658).
{ECO:0000269|PubMed:10220405, ECO:0000269|PubMed:10444591,
ECO:0000269|PubMed:10866654, ECO:0000269|PubMed:11102443,
ECO:0000269|PubMed:11118440, ECO:0000269|PubMed:11784859,
ECO:0000269|PubMed:12435631, ECO:0000269|PubMed:12920132,
ECO:0000269|PubMed:14609955, ECO:0000269|PubMed:15456747,
ECO:0000269|PubMed:18571423, ECO:0000269|PubMed:25556658,
ECO:0000269|PubMed:7503932, ECO:0000269|PubMed:9150135,
ECO:0000269|PubMed:9427644, ECO:0000269|PubMed:9651585,
ECO:0000269|PubMed:9790534}.
-!- INTERACTION:
P62799:- (xeno); NbExp=2; IntAct=EBI-352227, EBI-302085;
Q13547:HDAC1; NbExp=6; IntAct=EBI-352227, EBI-301834;
P62805:HIST2H4B; NbExp=8; IntAct=EBI-352227, EBI-302023;
O94776:MTA2; NbExp=7; IntAct=EBI-352227, EBI-1783035;
Q17R98:ZNF827; NbExp=2; IntAct=EBI-352227, EBI-5564776;
-!- SUBCELLULAR LOCATION: Nucleus.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q16576-1; Sequence=Displayed;
Name=2;
IsoId=Q16576-2; Sequence=VSP_043016;
Note=No experimental confirmation available. Initiator Met-1 is
removed. Contains a N-acetylalanine at position 2. Contains a
phosphoserine at position 13. {ECO:0000244|PubMed:20068231};
-!- SIMILARITY: Belongs to the WD repeat RBAP46/RBAP48/MSI1 family.
{ECO:0000305}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/RBBP7ID42065chXp22.html";
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; U35143; AAC50231.1; -; mRNA.
EMBL; X72841; CAA51360.1; -; mRNA.
EMBL; AK091911; BAG52439.1; -; mRNA.
EMBL; AL929302; -; NOT_ANNOTATED_CDS; Genomic_DNA.
CCDS; CCDS14179.1; -. [Q16576-1]
CCDS; CCDS56598.1; -. [Q16576-2]
PIR; I39181; I39181.
RefSeq; NP_001185648.1; NM_001198719.1. [Q16576-2]
RefSeq; NP_002884.1; NM_002893.3. [Q16576-1]
UniGene; Hs.495755; -.
PDB; 3CFS; X-ray; 2.40 A; B=1-411.
PDB; 3CFV; X-ray; 2.60 A; A/B=1-411.
PDBsum; 3CFS; -.
PDBsum; 3CFV; -.
ProteinModelPortal; Q16576; -.
SMR; Q16576; -.
BioGrid; 111866; 168.
CORUM; Q16576; -.
DIP; DIP-436N; -.
IntAct; Q16576; 96.
MINT; Q16576; -.
STRING; 9606.ENSP00000369424; -.
ChEMBL; CHEMBL3301388; -.
iPTMnet; Q16576; -.
PhosphoSitePlus; Q16576; -.
SwissPalm; Q16576; -.
BioMuta; RBBP7; -.
DMDM; 2494891; -.
EPD; Q16576; -.
PaxDb; Q16576; -.
PeptideAtlas; Q16576; -.
PRIDE; Q16576; -.
Ensembl; ENST00000380084; ENSP00000369424; ENSG00000102054. [Q16576-2]
Ensembl; ENST00000380087; ENSP00000369427; ENSG00000102054. [Q16576-1]
GeneID; 5931; -.
KEGG; hsa:5931; -.
UCSC; uc004cxs.3; human. [Q16576-1]
CTD; 5931; -.
DisGeNET; 5931; -.
EuPathDB; HostDB:ENSG00000102054.17; -.
GeneCards; RBBP7; -.
HGNC; HGNC:9890; RBBP7.
HPA; CAB037084; -.
HPA; HPA060710; -.
HPA; HPA060724; -.
MIM; 300825; gene.
neXtProt; NX_Q16576; -.
OpenTargets; ENSG00000102054; -.
PharmGKB; PA34254; -.
eggNOG; KOG0264; Eukaryota.
eggNOG; ENOG410XNU9; LUCA.
GeneTree; ENSGT00570000079069; -.
HOGENOM; HOG000160330; -.
HOVERGEN; HBG053236; -.
InParanoid; Q16576; -.
KO; K11659; -.
OMA; WQMADNI; -.
OrthoDB; EOG091G0A20; -.
PhylomeDB; Q16576; -.
TreeFam; TF106485; -.
Reactome; R-HSA-212300; PRC2 methylates histones and DNA.
Reactome; R-HSA-2559580; Oxidative Stress Induced Senescence.
Reactome; R-HSA-3214815; HDACs deacetylate histones.
Reactome; R-HSA-3214841; PKMTs methylate histone lysines.
Reactome; R-HSA-3214847; HATs acetylate histones.
Reactome; R-HSA-3214858; RMTs methylate histone arginines.
Reactome; R-HSA-427389; ERCC6 (CSB) and EHMT2 (G9a) positively regulate rRNA expression.
Reactome; R-HSA-5617472; Activation of anterior HOX genes in hindbrain development during early embryogenesis.
Reactome; R-HSA-606279; Deposition of new CENPA-containing nucleosomes at the centromere.
Reactome; R-HSA-6804758; Regulation of TP53 Activity through Acetylation.
Reactome; R-HSA-73762; RNA Polymerase I Transcription Initiation.
Reactome; R-HSA-8943724; Regulation of PTEN gene transcription.
Reactome; R-HSA-8951664; Neddylation.
Reactome; R-HSA-8953750; Transcriptional Regulation by E2F6.
SignaLink; Q16576; -.
ChiTaRS; RBBP7; human.
EvolutionaryTrace; Q16576; -.
GeneWiki; RBBP7; -.
GenomeRNAi; 5931; -.
PMAP-CutDB; Q16576; -.
PRO; PR:Q16576; -.
Proteomes; UP000005640; Chromosome X.
Bgee; ENSG00000102054; -.
CleanEx; HS_RBBP7; -.
ExpressionAtlas; Q16576; baseline and differential.
Genevisible; Q16576; HS.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0035098; C:ESC/E(Z) complex; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0016581; C:NuRD complex; IDA:UniProtKB.
GO; GO:0004407; F:histone deacetylase activity; TAS:Reactome.
GO; GO:0003723; F:RNA binding; IEA:Ensembl.
GO; GO:0008283; P:cell proliferation; TAS:ProtInc.
GO; GO:0070370; P:cellular heat acclimation; IDA:UniProtKB.
GO; GO:0034080; P:CENP-A containing nucleosome assembly; TAS:Reactome.
GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
GO; GO:0007275; P:multicellular organism development; TAS:ProtInc.
GO; GO:0030308; P:negative regulation of cell growth; IDA:UniProtKB.
GO; GO:0070317; P:negative regulation of G0 to G1 transition; TAS:Reactome.
GO; GO:0045814; P:negative regulation of gene expression, epigenetic; TAS:Reactome.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:Ensembl.
GO; GO:0043687; P:post-translational protein modification; TAS:Reactome.
GO; GO:0048545; P:response to steroid hormone; IEA:Ensembl.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
Gene3D; 2.130.10.10; -; 1.
InterPro; IPR020472; G-protein_beta_WD-40_rep.
InterPro; IPR022052; Histone-bd_RBBP4_N.
InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
InterPro; IPR001680; WD40_repeat.
InterPro; IPR019775; WD40_repeat_CS.
InterPro; IPR017986; WD40_repeat_dom.
InterPro; IPR036322; WD40_repeat_dom_sf.
Pfam; PF12265; CAF1C_H4-bd; 1.
Pfam; PF00400; WD40; 5.
PRINTS; PR00320; GPROTEINBRPT.
SMART; SM00320; WD40; 6.
SUPFAM; SSF50978; SSF50978; 1.
PROSITE; PS00678; WD_REPEATS_1; 3.
PROSITE; PS50082; WD_REPEATS_2; 5.
PROSITE; PS50294; WD_REPEATS_REGION; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Chaperone;
Chromatin regulator; Complete proteome; Direct protein sequencing;
DNA replication; Isopeptide bond; Nucleus; Phosphoprotein;
Reference proteome; Repeat; Repressor; Transcription;
Transcription regulation; Ubl conjugation; WD repeat.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:22814378}.
CHAIN 2 425 Histone-binding protein RBBP7.
/FTId=PRO_0000051195.
REPEAT 47 122 WD 1.
REPEAT 128 173 WD 2.
REPEAT 181 217 WD 3.
REPEAT 228 269 WD 4.
REPEAT 275 312 WD 5.
REPEAT 318 369 WD 6.
REPEAT 376 403 WD 7.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:22814378}.
MOD_RES 3 3 Phosphoserine.
{ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 4 4 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:19608861}.
MOD_RES 10 10 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 95 95 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 119 119 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q60973}.
MOD_RES 159 159 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q60973}.
MOD_RES 354 354 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
CROSSLNK 4 4 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate. {ECO:0000244|PubMed:28112733}.
CROSSLNK 4 4 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin);
alternate.
CROSSLNK 101 101 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 155 155 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 159 159 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate. {ECO:0000244|PubMed:25772364,
ECO:0000244|PubMed:28112733}.
VAR_SEQ 1 6 MASKEM -> MAAEAGVVGAGASPDGDWRDQACGLLLHVHL
SSRLGRAAPVRTGRHLRTV (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_043016.
HELIX 10 30 {ECO:0000244|PDB:3CFS}.
STRAND 31 38 {ECO:0000244|PDB:3CFS}.
STRAND 46 53 {ECO:0000244|PDB:3CFS}.
STRAND 59 67 {ECO:0000244|PDB:3CFS}.
STRAND 72 74 {ECO:0000244|PDB:3CFS}.
STRAND 76 86 {ECO:0000244|PDB:3CFS}.
STRAND 113 124 {ECO:0000244|PDB:3CFS}.
STRAND 127 131 {ECO:0000244|PDB:3CFS}.
STRAND 138 142 {ECO:0000244|PDB:3CFS}.
STRAND 144 146 {ECO:0000244|PDB:3CFS}.
STRAND 148 152 {ECO:0000244|PDB:3CFS}.
HELIX 153 155 {ECO:0000244|PDB:3CFS}.
STRAND 169 173 {ECO:0000244|PDB:3CFS}.
STRAND 182 184 {ECO:0000244|PDB:3CFS}.
STRAND 186 188 {ECO:0000244|PDB:3CFS}.
STRAND 191 195 {ECO:0000244|PDB:3CFS}.
STRAND 201 205 {ECO:0000244|PDB:3CFS}.
STRAND 214 217 {ECO:0000244|PDB:3CFS}.
STRAND 219 222 {ECO:0000244|PDB:3CFS}.
STRAND 229 234 {ECO:0000244|PDB:3CFS}.
STRAND 241 246 {ECO:0000244|PDB:3CFS}.
STRAND 249 259 {ECO:0000244|PDB:3CFS}.
STRAND 261 263 {ECO:0000244|PDB:3CFS}.
STRAND 265 269 {ECO:0000244|PDB:3CFS}.
STRAND 275 280 {ECO:0000244|PDB:3CFS}.
STRAND 287 292 {ECO:0000244|PDB:3CFS}.
STRAND 295 301 {ECO:0000244|PDB:3CFS}.
STRAND 305 307 {ECO:0000244|PDB:3CFV}.
STRAND 310 313 {ECO:0000244|PDB:3CFS}.
STRAND 319 324 {ECO:0000244|PDB:3CFS}.
STRAND 331 336 {ECO:0000244|PDB:3CFS}.
STRAND 341 345 {ECO:0000244|PDB:3CFS}.
HELIX 346 348 {ECO:0000244|PDB:3CFS}.
HELIX 355 358 {ECO:0000244|PDB:3CFS}.
STRAND 365 369 {ECO:0000244|PDB:3CFS}.
STRAND 376 381 {ECO:0000244|PDB:3CFS}.
STRAND 383 385 {ECO:0000244|PDB:3CFS}.
STRAND 388 393 {ECO:0000244|PDB:3CFS}.
STRAND 396 403 {ECO:0000244|PDB:3CFS}.
HELIX 405 408 {ECO:0000244|PDB:3CFS}.
SEQUENCE 425 AA; 47820 MW; 1A4B4CD1A8E96815 CRC64;
MASKEMFEDT VEERVINEEY KIWKKNTPFL YDLVMTHALQ WPSLTVQWLP EVTKPEGKDY
ALHWLVLGTH TSDEQNHLVV ARVHIPNDDA QFDASHCDSD KGEFGGFGSV TGKIECEIKI
NHEGEVNRAR YMPQNPHIIA TKTPSSDVLV FDYTKHPAKP DPSGECNPDL RLRGHQKEGY
GLSWNSNLSG HLLSASDDHT VCLWDINAGP KEGKIVDAKA IFTGHSAVVE DVAWHLLHES
LFGSVADDQK LMIWDTRSNT TSKPSHLVDA HTAEVNCLSF NPYSEFILAT GSADKTVALW
DLRNLKLKLH TFESHKDEIF QVHWSPHNET ILASSGTDRR LNVWDLSKIG EEQSAEDAED
GPPELLFIHG GHTAKISDFS WNPNEPWVIC SVSEDNIMQI WQMAENIYND EESDVTTSEL
EGQGS


Related products :

Catalog number Product name Quantity
EIAAB33915 Histone acetyltransferase type B subunit 2,Histone-binding protein RBBP7,Homo sapiens,Human,Nucleosome-remodeling factor subunit RBAP46,RBAP46,RBBP7,RBBP-7,Retinoblastoma-binding protein 7,Retinoblast
EIAAB33917 Histone acetyltransferase type B subunit 2,Histone-binding protein RBBP7,Mouse,Mus musculus,Nucleosome-remodeling factor subunit RBAP46,Rbap46,Rbbp7,RBBP-7,Retinoblastoma-binding protein 7,Retinoblast
EIAAB33913 Bos taurus,Bovine,Histone-binding protein RBBP7,Nucleosome-remodeling factor subunit RBAP46,RBBP7,RBBP-7,Retinoblastoma-binding protein 7
EIAAB33916 Histone-binding protein RBBP7,Nucleosome-remodeling factor subunit RBAP46,Rat,Rattus norvegicus,Rbbp7,RBBP-7,Retinoblastoma-binding protein 7
EIAAB33907 Bos taurus,Bovine,Histone-binding protein RBBP4,Nucleosome-remodeling factor subunit RBAP48,RBBP4,RBBP-4,Retinoblastoma-binding protein 4
EIAAB33914 Chicken,Gallus gallus,Histone-binding protein RBBP7,RBAP46,RBBP7,RBBP-7,Retinoblastoma-binding protein 7,Retinoblastoma-binding protein p46
18-003-42905 Transcription factor E2F1 - E2F-1; Retinoblastoma-binding protein 3; RBBP-3; PRB-binding protein E2F-1; PBR3; Retinoblastoma-associated protein 1; RBAP-1 Polyclonal 0.05 mg Aff Pur
18-003-43023 Transcription factor E2F1 - E2F-1; Retinoblastoma-binding protein 3; RBBP-3; PRB-binding protein E2F-1; PBR3; Retinoblastoma-associated protein 1; RBAP-1 Polyclonal 0.1 mg Protein A
EIAAB33918 B5T-overexpressed gene protein,BOG,Homo sapiens,Human,Protein BOG,Putative hydrolase RBBP9,RBBP10,RBBP-10,RBBP9,RBBP-9,Retinoblastoma-binding protein 10,Retinoblastoma-binding protein 9
EIAAB33908 CAF-1 subunit C,CAF-I 48 kDa subunit,CAF-I p48,Chromatin assembly factor 1 subunit C,Chromatin assembly factor I p48 subunit,Histone-binding protein RBBP4,Homo sapiens,Human,Nucleosome-remodeling fact
EIAAB33905 CAF-1 subunit C,CAF-I 48 kDa subunit,CAF-I p48,Chromatin assembly factor 1 subunit C,Chromatin assembly factor I p48 subunit,Histone-binding protein RBBP4,Mouse,Mus musculus,Nucleosome-remodeling fact
EIAAB12253 E2F1,E2F-1,Homo sapiens,Human,PBR3,PRB-binding protein E2F-1,RBAP-1,RBBP3,RBBP-3,Retinoblastoma-associated protein 1,Retinoblastoma-binding protein 3,Transcription factor E2F1
EIAAB33910 Homo sapiens,Human,RBBP5,RBBP-5,RBQ3,Retinoblastoma-binding protein 5,Retinoblastoma-binding protein RBQ-3
20-272-190684 E2F1 - Mouse monoclonal [KH129] to E2F1; E2F-1; Retinoblastoma-binding protein 3; RBBP-3; PRB-binding protein E2F-1; PBR3; Retinoblastoma-associated protein 1; RBAP-1 Monoclonal 0.05 ml
18-272-195543 E2F1 - Rabbit polyclonal to E2F1; E2F-1; Retinoblastoma-binding protein 3; RBBP-3; PRB-binding protein E2F-1; PBR3; Retinoblastoma-associated protein 1; RBAP-1 Polyclonal 0.1 ml
EIAAB33906 CAF-1 subunit C,CAF-I 48 kDa subunit,CAF-I p48,chCAF-1 p48,Chicken,Chromatin assembly factor 1 subunit C,Chromatin assembly factor I p48 subunit,Gallus gallus,Histone-binding protein RBBP4,RBAP48,RBBP
TM-1101Y-55 Anti-human Histone Binding Protein or Retinoblastoma Binding Protein p46 (RBA p46) IgG fraction (monoclonal) 150
TM-1101Y-55 Anti_human Histone Binding Protein or Retinoblastoma Binding Protein p46 (RBA p46) IgG fraction (monoclonal) 150µg
EIAAB08542 CtBP-interacting protein,CtIP,CTIP,DNA endonuclease RBBP8,Homo sapiens,Human,RBBP8,RBBP-8,Retinoblastoma-binding protein 8,Retinoblastoma-interacting protein and myosin-like,RIM,SAE2,Sporulation in th
RBBP7 RBBP7 Gene retinoblastoma binding protein 7
CSB-EL019392RA Rat retinoblastoma binding protein 7 (RBBP7) ELISA kit, Species Rat, Sample Type serum, plasma 96T
EIAAB33909 Mouse,Mus musculus,Rbbp5,RBBP-5,Retinoblastoma-binding protein 5
EIAAB46626 CBF-A,CCAAT-binding transcription factor I subunit A,DBPB,DNA-binding protein B,EFI-A,Enhancer factor I subunit A,Homo sapiens,Human,NSEP1,Nuclease-sensitive element-binding protein 1,YB1,YB-1,Y-box t
EIAAB46625 CBF-A,CCAAT-binding transcription factor I subunit A,DBPB,DNA-binding protein B,EFI-A,Enhancer factor I subunit A,Mouse,Msy1,Msy-1,Mus musculus,Nsep1,Nuclease-sensitive element-binding protein 1,Yb1,Y
EIAAB46624 CBF-A,CCAAT-binding transcription factor I subunit A,DBPB,DNA-binding protein B,EFI-A,Enhancer factor I subunit A,Msy-1,Nsep1,Nuclease-sensitive element-binding protein 1,Rat,Rattus norvegicus,Yb1,YB-


 

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 Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | 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

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
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 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
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | 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
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

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