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

AT-rich interactive domain-containing protein 4B (ARID domain-containing protein 4B) (180 kDa Sin3-associated polypeptide) (Sin3-associated polypeptide p180) (Breast cancer-associated antigen BRCAA1) (Histone deacetylase complex subunit SAP180) (Retinoblastoma-binding protein 1-like 1)

 ARI4B_HUMAN             Reviewed;        1312 AA.
Q4LE39; A1L465; Q3MHV4; Q5HY99; Q5T2C2; Q5T2C3; Q5T2C4; Q5T2C5;
Q5T2C6; Q6P600; Q86UX1; Q86WR4; Q9H915; Q9NYU3; Q9NZB6; Q9NZG4;
Q9P2W4; Q9UF62; Q9Y6E1;
03-APR-2007, integrated into UniProtKB/Swiss-Prot.
03-APR-2007, sequence version 2.
20-JUN-2018, entry version 127.
RecName: Full=AT-rich interactive domain-containing protein 4B;
Short=ARID domain-containing protein 4B;
AltName: Full=180 kDa Sin3-associated polypeptide;
Short=Sin3-associated polypeptide p180;
AltName: Full=Breast cancer-associated antigen BRCAA1;
AltName: Full=Histone deacetylase complex subunit SAP180;
AltName: Full=Retinoblastoma-binding protein 1-like 1;
Name=ARID4B; Synonyms=BRCAA1, RBBP1L1, RBP1L1, SAP180;
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 2), SUBCELLULAR LOCATION, AND
TISSUE SPECIFICITY.
PubMed=11481388; DOI=10.1093/jnci/93.15.1159;
Cao J.-N., Gao T.-W., Stanbridge E.J., Irie R.;
"RBP1L1, a retinoblastoma-binding protein-related gene encoding an
antigenic epitope abundantly expressed in human carcinomas and normal
testis.";
J. Natl. Cancer Inst. 93:1159-1165(2001).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, DOMAIN, TISSUE
SPECIFICITY, AND IDENTIFICATION IN A MSIN3A COREPRESSOR COMPLEX WITH
SIN3A; SAP130; SUDS3; ARID4B; HDAC1 AND HDAC2.
PubMed=12724404; DOI=10.1128/MCB.23.10.3456-3467.2003;
Fleischer T.C., Yun U.J., Ayer D.E.;
"Identification and characterization of three new components of the
mSin3A corepressor complex.";
Mol. Cell. Biol. 23:3456-3467(2003).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), SUBCELLULAR LOCATION, AND
TISSUE SPECIFICITY.
PubMed=15247124;
Cui D., Jin G., Gao T.W., Sun T., Tian F., Estrada G.G., Gao H.,
Sarai A.;
"Characterization of BRCAA1 and its novel antigen epitope
identification.";
Cancer Epidemiol. Biomarkers Prev. 13:1136-1145(2004).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
TISSUE=Synovium;
Tanaka M.;
"Rheumatoid arthritis antigenic protein similar to retinoblastoma
binding protein 1 (RBP1).";
Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain;
Nakajima D., Saito K., Yamakawa H., Kikuno R.F., Nakayama M.,
Ohara R., Okazaki N., Koga H., Nagase T., Ohara O.;
"Preparation of a set of expression-ready clones of mammalian long
cDNAs encoding large proteins by the ORF trap cloning method.";
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), NUCLEOTIDE
SEQUENCE [LARGE SCALE MRNA] OF 1-651 (ISOFORM 2), AND NUCLEOTIDE
SEQUENCE [LARGE SCALE MRNA] OF 1-424.
TISSUE=Hippocampus, Kidney, and Lung;
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).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1149 (ISOFORM 2), AND
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1147-1312.
TISSUE=Adipose tissue, and Testis;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[9]
NUCLEOTIDE SEQUENCE [MRNA] OF 440-1312 (ISOFORM 1).
Cao J., Irie R.F., Stanbridge E.J.;
"Human breast carcinoma-associated antigen isoform I.";
Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases.
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 547-1312.
Liu T., Tao J., Zhang J., Li W., Ye M., Zhou J., Wu J., Shen Y.,
Yu M., Chen S., Mao M., Chen Z.;
"Human Rb binding protein homolog gene, partial CDS.";
Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
[11]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 828-1312.
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).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-717, AND 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).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-666; SER-675; SER-790;
THR-793; THR-1150; SER-1152; SER-1153; SER-1155 AND SER-1159, 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).
[14]
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).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-790; THR-793; SER-1014
AND THR-1026, 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).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-675; SER-778; SER-790
AND THR-793, 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).
[17]
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).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-276; SER-778; SER-790
AND THR-793, 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).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-483; SER-666; SER-675;
SER-778; SER-1029 AND SER-1153, 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).
[20]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-429, 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).
[21]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-429, 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).
[22]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-429 AND LYS-440, 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).
[23]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-429; LYS-440; LYS-462;
LYS-517 AND LYS-751, 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).
-!- FUNCTION: Acts as a transcriptional repressor. May function in the
assembly and/or enzymatic activity of the Sin3A corepressor
complex or in mediating interactions between the complex and other
regulatory complexes. {ECO:0000269|PubMed:12724404}.
-!- SUBUNIT: Component of a Sin3A corepressor complex consisting of
SIN3A, SAP130, SUDS3/SAP45, SAP180, HDAC1 and HDAC2.
{ECO:0000269|PubMed:12724404}.
-!- INTERACTION:
Q96JC9:EAF1; NbExp=4; IntAct=EBI-11957452, EBI-769261;
P14921:ETS1; NbExp=2; IntAct=EBI-2680990, EBI-913209;
Q5HYW2:NHSL2; NbExp=4; IntAct=EBI-11957452, EBI-2859639;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-
ProRule:PRU00355}. Cytoplasm {ECO:0000269|PubMed:11481388,
ECO:0000269|PubMed:15247124}. Note=Cytoplasmic in breast cancer
cells.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1;
IsoId=Q4LE39-1; Sequence=Displayed;
Name=2;
IsoId=Q4LE39-2; Sequence=VSP_024231;
Name=3;
IsoId=Q4LE39-3; Sequence=VSP_024234, VSP_024235;
Name=4;
IsoId=Q4LE39-4; Sequence=VSP_024230, VSP_024232, VSP_024233;
-!- TISSUE SPECIFICITY: Highly expressed in the testis and in breast,
lung, colon, pancreatic and ovarian cancers. Expressed at low
levels in the thymus, prostate and ovary.
{ECO:0000269|PubMed:11481388, ECO:0000269|PubMed:12724404,
ECO:0000269|PubMed:15247124}.
-!- DOMAIN: The C-terminus mediates interaction with mSin3A
corepressor complex. {ECO:0000269|PubMed:12724404}.
-!- DOMAIN: The N-terminus is involved in transcriptional repression
by HDAC-independent mechanisms. {ECO:0000269|PubMed:12724404}.
-!- DOMAIN: The ARID domain is involved in stabilizing the mSin3A
corepressor complex on DNA. {ECO:0000269|PubMed:12724404}.
-!- SEQUENCE CAUTION:
Sequence=AAD41239.1; Type=Frameshift; Positions=859, 869, 1287, 1311; Evidence={ECO:0000305};
Sequence=AAF23433.3; Type=Frameshift; Positions=1287, 1311; Evidence={ECO:0000305};
Sequence=BAB14428.1; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=BAE06114.1; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=CAI13751.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AF214114; AAF28341.2; -; mRNA.
EMBL; AY220790; AAO63590.1; -; mRNA.
EMBL; AF208045; AAF23433.3; ALT_FRAME; mRNA.
EMBL; AB030181; BAA89794.1; -; mRNA.
EMBL; AB210032; BAE06114.1; ALT_INIT; mRNA.
EMBL; AL391994; CAI13747.2; -; Genomic_DNA.
EMBL; AL133418; CAI13747.2; JOINED; Genomic_DNA.
EMBL; AL391994; CAI13749.1; -; Genomic_DNA.
EMBL; AL391994; CAI13751.1; ALT_SEQ; Genomic_DNA.
EMBL; AL133418; CAI13751.1; JOINED; Genomic_DNA.
EMBL; AL133418; CAI22961.2; -; Genomic_DNA.
EMBL; AL391994; CAI22961.2; JOINED; Genomic_DNA.
EMBL; AL133418; CAI22962.1; -; Genomic_DNA.
EMBL; AL391994; CAI22962.1; JOINED; Genomic_DNA.
EMBL; BC048959; AAH48959.1; ALT_TERM; mRNA.
EMBL; BC062536; AAH62536.1; ALT_TERM; mRNA.
EMBL; BC104632; AAI04633.1; ALT_TERM; mRNA.
EMBL; BC130418; AAI30419.1; -; mRNA.
EMBL; BX648820; CAI46047.1; -; mRNA.
EMBL; AL133594; CAB63731.1; -; mRNA.
EMBL; AF227899; AAF36964.1; -; mRNA.
EMBL; AF083249; AAD41239.1; ALT_FRAME; mRNA.
EMBL; AK023144; BAB14428.1; ALT_INIT; mRNA.
CCDS; CCDS31060.1; -. [Q4LE39-2]
CCDS; CCDS31061.1; -. [Q4LE39-1]
PIR; T43497; T43497.
RefSeq; NP_001193723.1; NM_001206794.1. [Q4LE39-1]
RefSeq; NP_057458.4; NM_016374.5. [Q4LE39-1]
RefSeq; NP_112739.2; NM_031371.3. [Q4LE39-2]
RefSeq; XP_011542514.1; XM_011544212.2. [Q4LE39-1]
UniGene; Hs.575782; -.
ProteinModelPortal; Q4LE39; -.
SMR; Q4LE39; -.
BioGrid; 119708; 39.
CORUM; Q4LE39; -.
IntAct; Q4LE39; 33.
MINT; Q4LE39; -.
STRING; 9606.ENSP00000264183; -.
iPTMnet; Q4LE39; -.
PhosphoSitePlus; Q4LE39; -.
BioMuta; ARID4B; -.
DMDM; 143955276; -.
EPD; Q4LE39; -.
MaxQB; Q4LE39; -.
PaxDb; Q4LE39; -.
PeptideAtlas; Q4LE39; -.
PRIDE; Q4LE39; -.
ProteomicsDB; 62238; -.
ProteomicsDB; 62239; -. [Q4LE39-2]
ProteomicsDB; 62240; -. [Q4LE39-3]
ProteomicsDB; 62241; -. [Q4LE39-4]
DNASU; 51742; -.
Ensembl; ENST00000264183; ENSP00000264183; ENSG00000054267. [Q4LE39-1]
Ensembl; ENST00000349213; ENSP00000264184; ENSG00000054267. [Q4LE39-2]
Ensembl; ENST00000366603; ENSP00000355562; ENSG00000054267. [Q4LE39-1]
Ensembl; ENST00000421364; ENSP00000394663; ENSG00000054267. [Q4LE39-3]
GeneID; 51742; -.
KEGG; hsa:51742; -.
UCSC; uc001hwq.3; human. [Q4LE39-1]
CTD; 51742; -.
DisGeNET; 51742; -.
EuPathDB; HostDB:ENSG00000054267.20; -.
GeneCards; ARID4B; -.
HGNC; HGNC:15550; ARID4B.
HPA; HPA027333; -.
HPA; HPA053692; -.
MIM; 609696; gene.
neXtProt; NX_Q4LE39; -.
OpenTargets; ENSG00000054267; -.
PharmGKB; PA134940494; -.
eggNOG; KOG2744; Eukaryota.
eggNOG; KOG3001; Eukaryota.
eggNOG; ENOG410Y2AP; LUCA.
GeneTree; ENSGT00900000140901; -.
HOVERGEN; HBG058247; -.
InParanoid; Q4LE39; -.
KO; K19195; -.
OMA; FRLVHKL; -.
OrthoDB; EOG091G0EG4; -.
PhylomeDB; Q4LE39; -.
TreeFam; TF106427; -.
Reactome; R-HSA-3214815; HDACs deacetylate histones.
Reactome; R-HSA-427413; NoRC negatively regulates rRNA expression.
ChiTaRS; ARID4B; human.
GeneWiki; ARID4B; -.
GenomeRNAi; 51742; -.
PRO; PR:Q4LE39; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000054267; -.
ExpressionAtlas; Q4LE39; baseline and differential.
Genevisible; Q4LE39; HS.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IBA:GO_Central.
GO; GO:0004407; F:histone deacetylase activity; TAS:Reactome.
GO; GO:0000981; F:RNA polymerase II transcription factor activity, sequence-specific DNA binding; ISA:NTNU_SB.
GO; GO:0044212; F:transcription regulatory region DNA binding; IBA:GO_Central.
GO; GO:0097368; P:establishment of Sertoli cell barrier; IEA:Ensembl.
GO; GO:0036124; P:histone H3-K9 trimethylation; IEA:Ensembl.
GO; GO:0034773; P:histone H4-K20 trimethylation; IEA:Ensembl.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
GO; GO:0006349; P:regulation of gene expression by genetic imprinting; IEA:Ensembl.
GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
GO; GO:0007283; P:spermatogenesis; IEA:Ensembl.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
CDD; cd00024; CHROMO; 1.
Gene3D; 1.10.150.60; -; 1.
InterPro; IPR028853; ARID4B.
InterPro; IPR001606; ARID_dom.
InterPro; IPR036431; ARID_dom_sf.
InterPro; IPR016197; Chromo-like_dom_sf.
InterPro; IPR000953; Chromo/chromo_shadow_dom.
InterPro; IPR012603; RBB1NT.
InterPro; IPR002999; Tudor.
InterPro; IPR025995; Tudor-knot.
PANTHER; PTHR13964:SF24; PTHR13964:SF24; 1.
Pfam; PF01388; ARID; 1.
Pfam; PF08169; RBB1NT; 1.
Pfam; PF11717; Tudor-knot; 1.
SMART; SM00501; BRIGHT; 1.
SMART; SM00333; TUDOR; 2.
SUPFAM; SSF46774; SSF46774; 1.
SUPFAM; SSF54160; SSF54160; 1.
PROSITE; PS51011; ARID; 1.
1: Evidence at protein level;
Alternative splicing; Coiled coil; Complete proteome; Cytoplasm;
DNA-binding; Isopeptide bond; Nucleus; Phosphoprotein;
Reference proteome; Transcription; Transcription regulation;
Ubl conjugation.
CHAIN 1 1312 AT-rich interactive domain-containing
protein 4B.
/FTId=PRO_0000282863.
DOMAIN 306 398 ARID. {ECO:0000255|PROSITE-
ProRule:PRU00355}.
REGION 465 473 Antigenic epitope.
REGION 1130 1137 Antigenic epitope.
COILED 728 754 {ECO:0000255}.
COILED 1231 1270 {ECO:0000255}.
COMPBIAS 154 159 Poly-Ser.
COMPBIAS 268 567 Glu-rich.
COMPBIAS 1095 1101 Poly-Ser.
COMPBIAS 1271 1303 Ser-rich.
MOD_RES 276 276 Phosphoserine.
{ECO:0000244|PubMed:21406692}.
MOD_RES 295 295 Phosphoserine.
{ECO:0000250|UniProtKB:Q9JKB5}.
MOD_RES 296 296 Phosphoserine.
{ECO:0000250|UniProtKB:Q9JKB5}.
MOD_RES 483 483 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 666 666 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 675 675 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 717 717 Phosphoserine.
{ECO:0000244|PubMed:17081983}.
MOD_RES 778 778 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 790 790 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692}.
MOD_RES 793 793 Phosphothreonine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692}.
MOD_RES 1014 1014 Phosphoserine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 1026 1026 Phosphothreonine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 1029 1029 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1150 1150 Phosphothreonine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 1152 1152 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 1153 1153 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 1155 1155 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 1159 1159 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
CROSSLNK 429 429 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 440 440 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25755297,
ECO:0000244|PubMed:28112733}.
CROSSLNK 462 462 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 517 517 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 751 751 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
VAR_SEQ 1 319 Missing (in isoform 4).
{ECO:0000303|Ref.4}.
/FTId=VSP_024230.
VAR_SEQ 529 614 Missing (in isoform 2).
{ECO:0000303|PubMed:11481388,
ECO:0000303|PubMed:15247124,
ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:17974005}.
/FTId=VSP_024231.
VAR_SEQ 1112 1122 ACTGQKRVKDA -> GEKENVYVDLF (in isoform
4). {ECO:0000303|Ref.4}.
/FTId=VSP_024232.
VAR_SEQ 1123 1312 Missing (in isoform 4).
{ECO:0000303|Ref.4}.
/FTId=VSP_024233.
VAR_SEQ 1150 1153 TNSS -> SAPH (in isoform 3).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_024234.
VAR_SEQ 1154 1312 Missing (in isoform 3).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_024235.
CONFLICT 15 15 D -> G (in Ref. 2; AAO63590).
{ECO:0000305}.
CONFLICT 79 79 V -> A (in Ref. 2; AAO63590).
{ECO:0000305}.
CONFLICT 330 330 R -> Q (in Ref. 1; AAF28341 and 3;
AAF23433). {ECO:0000305}.
CONFLICT 400 400 A -> P (in Ref. 4; BAA89794).
{ECO:0000305}.
CONFLICT 436 436 I -> IEFCGR (in Ref. 3; AAF23433).
{ECO:0000305}.
CONFLICT 437 437 K -> Q (in Ref. 4; BAA89794).
{ECO:0000305}.
CONFLICT 559 561 DNN -> ATI (in Ref. 4; BAA89794).
{ECO:0000305}.
CONFLICT 568 568 C -> S (in Ref. 4; BAA89794).
{ECO:0000305}.
CONFLICT 575 575 V -> A (in Ref. 4; BAA89794).
{ECO:0000305}.
CONFLICT 584 584 N -> H (in Ref. 4; BAA89794).
{ECO:0000305}.
CONFLICT 605 605 L -> S (in Ref. 9; AAF36964).
{ECO:0000305}.
CONFLICT 616 616 D -> G (in Ref. 9; AAF36964).
{ECO:0000305}.
CONFLICT 813 813 D -> G (in Ref. 2; AAO63590).
{ECO:0000305}.
CONFLICT 915 917 RLQ -> LP (in Ref. 3; AAF23433).
{ECO:0000305}.
CONFLICT 940 940 L -> R (in Ref. 3; AAF23433).
{ECO:0000305}.
CONFLICT 1000 1000 K -> E (in Ref. 1; AAF28341 and 9;
AAF36964). {ECO:0000305}.
CONFLICT 1001 1001 T -> Q (in Ref. 3; AAF23433).
{ECO:0000305}.
CONFLICT 1032 1032 S -> P (in Ref. 2; AAO63590).
{ECO:0000305}.
CONFLICT 1087 1087 S -> N (in Ref. 2; AAO63590).
{ECO:0000305}.
CONFLICT 1118 1118 R -> G (in Ref. 8; CAI46047).
{ECO:0000305}.
CONFLICT 1144 1144 K -> T (in Ref. 3; AAF23433 and 10;
AAD41239). {ECO:0000305}.
CONFLICT 1243 1244 IR -> NQ (in Ref. 3; AAF23433 and 10;
AAD41239). {ECO:0000305}.
CONFLICT 1290 1290 V -> A (in Ref. 1; AAF28341 and 9;
AAF36964). {ECO:0000305}.
SEQUENCE 1312 AA; 147809 MW; E4175FF80F5217EE CRC64;
MKALDEPPYL TVGTDVSAKY RGAFCEAKIK TAKRLVKVKV TFRHDSSTVE VQDDHIKGPL
KVGAIVEVKN LDGAYQEAVI NKLTDASWYT VVFDDGDEKT LRRSSLCLKG ERHFAESETL
DQLPLTNPEH FGTPVIGKKT NRGRRSNHIP EEESSSSSSD EDEDDRKQID ELLGKVVCVD
YISLDKKKAL WFPALVVCPD CSDEIAVKKD NILVRSFKDG KFTSVPRKDV HEITSDTAPK
PDAVLKQAFE QALEFHKSRT IPANWKTELK EDSSSSEAEE EEEEEDDEKE KEDNSSEEEE
EIEPFPEERE NFLQQLYKFM EDRGTPINKR PVLGYRNLNL FKLFRLVHKL GGFDNIESGA
VWKQVYQDLG IPVLNSAAGY NVKCAYKKYL YGFEEYCRSA NIEFQMALPE KVVNKQCKEC
ENVKEIKVKE ENETEIKEIK MEEERNIIPR EEKPIEDEIE RKENIKPSLG SKKNLLESIP
THSDQEKEVN IKKPEDNENL DDKDDDTTRV DESLNIKVEA EEEKAKSGDE TNKEEDEDDE
EAEEEEEEEE EEEDEDDDDN NEEEEFECYP PGMKVQVRYG RGKNQKMYEA SIKDSDVEGG
EVLYLVHYCG WNVRYDEWIK ADKIVRPADK NVPKIKHRKK IKNKLDKEKD KDEKYSPKNC
KLRRLSKPPF QTNPSPEMVS KLDLTDAKNS DTAHIKSIEI TSILNGLQAS ESSAEDSEQE
DERGAQDMDN NGKEESKIDH LTNNRNDLIS KEEQNSSSLL EENKVHADLV ISKPVSKSPE
RLRKDIEVLS EDTDYEEDEV TKKRKDVKKD TTDKSSKPQI KRGKRRYCNT EECLKTGSPG
KKEEKAKNKE SLCMENSSNS SSDEDEEETK AKMTPTKKYN GLEEKRKSLR TTGFYSGFSE
VAEKRIKLLN NSDERLQNSR AKDRKDVWSS IQGQWPKKTL KELFSDSDTE AAASPPHPAP
EEGVAEESLQ TVAEEESCSP SVELEKPPPV NVDSKPIEEK TVEVNDRKAE FPSSGSNSVL
NTPPTTPESP SSVTVTEGSR QQSSVTVSEP LAPNQEEVRS IKSETDSTIE VDSVAGELQD
LQSEGNSSPA GFDASVSSSS SNQPEPEHPE KACTGQKRVK DAQGGGSSSK KQKRSHKATV
VNNKKKGKGT NSSDSEELSA GESITKSQPV KSVSTGMKSH STKSPARTQS PGKCGKNGDK
DPDLKEPSNR LPKVYKWSFQ MSDLENMTSA ERITILQEKL QEIRKHYLSL KSEVASIDRR
RKRLKKKERE SAATSSSSSS PSSSSITAAV MLTLAEPSMS SASQNGMSVE CR


Related products :

Catalog number Product name Quantity
18-783-78579 GOAT ANTI RBP1-LIKE PROTEIN - ARID domain-containing protein 4B; Histone deacetylase complex subunit SAP180; 180 kDa Sin3-associated polypeptide; Sin3-associated polypeptide p180; Retinoblastoma-bindi 0.1 mg
18-003-44088 Histone deacetylase complex subunit SAP18 - Sin3-associated polypeptide. 18 kDa; Sin3-associated polypeptide p18; Cell growth-inhibiting protein 38; 2HOR0202 Polyclonal 0.05 mg Aff Pur
EIAAB37270 18 kDa Sin3-associated polypeptide,2HOR0202,Cell growth-inhibiting gene 38 protein,GIG38,Histone deacetylase complex subunit SAP18,Homo sapiens,Human,SAP18,Sin3-associated polypeptide p18
EIAAB37273 25 kDa Sin3-associated polypeptide,Histone deacetylase complex subunit SAP25,Mouse,mSin3A-binding protein,Mus musculus,Sap25,Sin3 corepressor complex subunit SAP25
EIAAB37277 30 kDa Sin3-associated polypeptide,Histone deacetylase complex subunit SAP30,Homo sapiens,Human,SAP30,Sin3 corepressor complex subunit SAP30,Sin3-associated polypeptide p30
EIAAB37276 30 kDa Sin3-associated polypeptide,Histone deacetylase complex subunit SAP30,Mouse,Mus musculus,Sap30,Sin3 corepressor complex subunit SAP30,Sin3-associated polypeptide p30
EIAAB39316 130 kDa Sin3-associated polypeptide,Histone deacetylase complex subunit SAP130,Homo sapiens,Human,SAP130,Sin3-associated polypeptide p130
EIAAB39317 130 kDa Sin3-associated polypeptide,Histone deacetylase complex subunit SAP130,Mouse,Mus musculus,Sap130,Sin3-associated polypeptide p130
EIAAB37271 18 kDa Sin3-associated polypeptide,Histone deacetylase complex subunit SAP18,Mouse,Mus musculus,Sap18,Sin3-associated polypeptide p18
EIAAB37269 18 kDa Sin3-associated polypeptide,Bos taurus,Bovine,Histone deacetylase complex subunit SAP18,SAP18,Sin3-associated polypeptide p18
EIAAB39315 130 kDa Sin3-associated polypeptide,Chicken,Gallus gallus,Histone deacetylase complex subunit SAP130,RCJMB04_7d5,SAP130,Sin3-associated polypeptide p130
EIAAB37751 45 kDa Sin3-associated polypeptide,Homo sapiens,Human,SAP45,SDS3,Sin3 histone deacetylase corepressor complex component SDS3,SUDS3,Suppressor of defective silencing 3 protein homolog
18-003-43340 Histone deacetylase complex subunit SAP30 - Sin3-associated polypeptide. 30 kDa; Sin3 corepressor complex subunit SAP30 Polyclonal 0.1 mg Protein A
EIAAB37272 25 kDa Sin3-associated polypeptide,Histone deacetylase complex subunit SAP25,Homo sapiens,Human,SAP25,Sin3 corepressor complex subunit SAP25
EIAAB39326 HCV non-structural protein 4A-transactivated protein 2,Histone deacetylase complex subunit SAP30L,Homo sapiens,Human,NS4ATP2,SAP30L,Sin3 corepressor complex subunit SAP30L,Sin3-associated protein p30-
18-003-42333 AT-rich interactive domain-containing protein 4A - ARID domain-containing protein 4A; Retinoblastoma-binding protein 1; RBBP-1 Polyclonal 0.1 mg Protein A
EIAAB39327 Histone deacetylase complex subunit SAP30L,Mouse,Mus musculus,Sap30l,Sin3 corepressor complex subunit SAP30L,Sin3-associated protein p30-like
18-003-43093 AT-rich interactive domain-containing protein 3A - ARID domain-containing protein 3A; B-cell regulator of IgH transcription; Bright; E2F-binding protein 1 Polyclonal 0.05 mg Aff Pur
20-372-60070 AT rich interactive domain 3A (BRIGHT- like) - Mouse monoclonal anti-human ARID3A antibody; ARID domain-containing protein 3A; Dead ringer-like protein 1; Bright; E2F-binding protein 1 Monoclonal 0.1 mg
18-272-196234 SAP30 - Rabbit polyclonal to SAP30; Sin3-associated polypeptide. 30 kDa; Sin3 corepressor complex subunit SAP30 Polyclonal 0.1 mg
18-272-196233 SAP30 - Rabbit polyclonal to SAP30; Sin3-associated polypeptide. 30 kDa; Sin3 corepressor complex subunit SAP30 Polyclonal 0.05 mg
18-003-44091 AT-rich interactive domain-containing protein 3B - ARID domain-containing protein 3B; Bright-like; Bright and dead ringer protein Polyclonal 0.05 mg Aff Pur
EIAAB37753 Mouse,Mus musculus,Sds3,Sin3 histone deacetylase corepressor complex component SDS3,Suds3,Suppressor of defective silencing 3 protein homolog
EIAAB37752 Bos taurus,Bovine,SDS3,Sin3 histone deacetylase corepressor complex component SDS3,SUDS3,Suppressor of defective silencing 3 protein homolog
20-372-60127 AT rich interactive domain 1A (SWI- like) (ARID1A). transcript variant 1. mRNA - Mouse monoclonal anti-human ARID1A antibody; ARID domain-containing protein 1A; SWI_SNF-related. matrix-associated. act 0.1 mg


 

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