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SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily B member 1 (BRG1-associated factor 47) (BAF47) (Integrase interactor 1 protein) (SNF5 homolog) (hSNF5)

 SNF5_HUMAN              Reviewed;         385 AA.
Q12824; O75784; O95474; Q17S11; Q38GA1; Q76N08; Q9UBH2;
01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
16-AUG-2004, sequence version 2.
22-NOV-2017, entry version 181.
RecName: Full=SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily B member 1;
AltName: Full=BRG1-associated factor 47;
Short=BAF47;
AltName: Full=Integrase interactor 1 protein;
AltName: Full=SNF5 homolog;
Short=hSNF5;
Name=SMARCB1; Synonyms=BAF47, INI1, SNF5L1;
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 A).
PubMed=7801128; DOI=10.1126/science.7801128;
Kalpana G.V., Marmon S., Wang W., Crabtree G.R., Goff S.P.;
"Binding and stimulation of HIV-1 integrase by a human homolog of
yeast transcription factor SNF5.";
Science 266:2002-2006(1994).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INVOLVEMENT IN RTPS1.
PubMed=9671307; DOI=10.1038/28212;
Versteege I., Sevenet N., Lange J., Rousseau-Merck M.-F., Ambros P.,
Handgretinger R., Aurias A., Delattre O.;
"Truncating mutations of hSNF5/INI1 in aggressive paediatric cancer.";
Nature 394:203-206(1998).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A AND B).
PubMed=10208879; DOI=10.1006/bbrc.1999.0563;
Bruder C.E., Dumanski J.P., Kedra D.;
"The mouse ortholog of the human SMARCB1 gene encodes two splice
forms.";
Biochem. Biophys. Res. Commun. 257:886-890(1999).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B).
Tozaki H., Yasuda J., Iwakura Y.;
"Human Ini1 27bp deletion form.";
Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
Beare D.M., Dunham I.;
"A genome annotation-driven approach to cloning the human ORFeome.";
Genome Biol. 5:R84.1-R84.11(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B).
TISSUE=Embryo;
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).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
NIEHS SNPs program;
Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton 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.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B).
TISSUE=Brain;
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).
[10]
IDENTIFICATION IN BAF COMPLEX.
PubMed=8895581;
Wang W., Cote J., Xue Y., Zhou S., Khavari P.A., Biggar S.R.,
Muchardt C., Kalpana G.V., Goff S.P., Yaniv M., Workman J.L.,
Crabtree G.R.;
"Purification and biochemical heterogeneity of the mammalian SWI-SNF
complex.";
EMBO J. 15:5370-5382(1996).
[11]
INTERACTION WITH EPSTEIN-BARR VIRUS EBNA2.
PubMed=8709224;
Wu D.Y., Kalpana G.V., Goff S.P., Schubach W.H.;
"Epstein-Barr virus nuclear protein 2 (EBNA2) binds to a component of
the human SNF-SWI complex, hSNF5/Ini1.";
J. Virol. 70:6020-6028(1996).
[12]
FUNCTION.
PubMed=9448295; DOI=10.1073/pnas.95.3.1120;
Morozov A., Yung E., Kalpana G.V.;
"Structure-function analysis of integrase interactor 1/hSNF5L1 reveals
differential properties of two repeat motifs present in the highly
conserved region.";
Proc. Natl. Acad. Sci. U.S.A. 95:1120-1125(1998).
[13]
INTERACTION WITH PPP1R15A.
PubMed=10490642; DOI=10.1128/MCB.19.10.7050;
Adler H.T., Chinery R., Wu D.Y., Kussick S.J., Payne J.M.,
Fornace A.J. Jr., Tkachuk D.C.;
"Leukemic HRX fusion proteins inhibit GADD34-induced apoptosis and
associate with the GADD34 and hSNF5/INI1 proteins.";
Mol. Cell. Biol. 19:7050-7060(1999).
[14]
INTERACTION WITH MYC.
PubMed=10319872; DOI=10.1038/8811;
Cheng S.-W., Davies K.P., Yung E., Beltran R.J., Yu J., Kalpana G.V.;
"c-MYC interacts with INI1/hSNF5 and requires the SWI/SNF complex for
transactivation function.";
Nat. Genet. 22:102-105(1999).
[15]
INTERACTION WITH HUMAN PAPILLOMAVIRUS-18 E1 PROTEIN.
PubMed=10365963; DOI=10.1038/20966;
Lee D., Sohn H., Kalpana G.V., Choe J.;
"Interaction of E1 and hSNF5 proteins stimulates replication of human
papillomavirus DNA.";
Nature 399:487-491(1999).
[16]
FUNCTION.
PubMed=10078207; DOI=10.1016/S1097-2765(00)80315-9;
Phelan M.L., Sif S., Narlikar G.J., Kingston R.E.;
"Reconstitution of a core chromatin remodeling complex from SWI/SNF
subunits.";
Mol. Cell 3:247-253(1999).
[17]
INVOLVEMENT IN RTPS1.
PubMed=9892189;
Biegel J.A., Zhou J.-Y., Rorke L.B., Stenstrom C., Wainwright L.M.,
Fogelgren B.;
"Germ-line and acquired mutations of INI1 in atypical teratoid and
rhabdoid tumors.";
Cancer Res. 59:74-79(1999).
[18]
INTERACTION WITH PPP1R15A.
PubMed=12016208; DOI=10.1074/jbc.M200955200;
Wu D.Y., Tkachuck D.C., Roberson R.S., Schubach W.H.;
"The human SNF5/INI1 protein facilitates the function of the growth
arrest and DNA damage-inducible protein (GADD34) and modulates GADD34-
bound protein phosphatase-1 activity.";
J. Biol. Chem. 277:27706-27715(2002).
[19]
FUNCTION IN CELL CYCLE.
PubMed=12226744; DOI=10.1038/sj.onc.1205841;
Versteege I., Medjkane S., Rouillard D., Delattre O.;
"A key role of the hSNF5/INI1 tumour suppressor in the control of the
G1-S transition of the cell cycle.";
Oncogene 21:6403-6412(2002).
[20]
FUNCTION IN CELL CYCLE.
PubMed=14604992; DOI=10.1074/jbc.M309333200;
Oruetxebarria I., Venturini F., Kekarainen T., Houweling A.,
Zuijderduijn L.M.P., Mohd-Sarip A., Vries R.G.J., Hoeben R.C.,
Verrijzer C.P.;
"P16INK4a is required for hSNF5 chromatin remodeler-induced cellular
senescence in malignant rhabdoid tumor cells.";
J. Biol. Chem. 279:3807-3816(2004).
[21]
FUNCTION IN ACTIVATION OF COLONY STIMULATING FACTOR 1 PROMOTER.
PubMed=16267391;
Pan X., Song Z., Zhai L., Li X., Zeng X.;
"Chromatin-remodeling factor INI1/hSNF5/BAF47 is involved in
activation of the colony stimulating factor 1 promoter.";
Mol. Cells 20:183-188(2005).
[22]
DISEASE.
PubMed=15899790; DOI=10.1158/0008-5472.CAN-04-3050;
Modena P., Lualdi E., Facchinetti F., Galli L., Teixeira M.R.,
Pilotti S., Sozzi G.;
"SMARCB1/INI1 tumor suppressor gene is frequently inactivated in
epithelioid sarcomas.";
Cancer Res. 65:4012-4019(2005).
[23]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-129, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic kidney;
PubMed=17525332; DOI=10.1126/science.1140321;
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
"ATM and ATR substrate analysis reveals extensive protein networks
responsive to DNA damage.";
Science 316:1160-1166(2007).
[24]
INTERACTION WITH CEBPB.
PubMed=20111005; DOI=10.1038/emboj.2010.3;
Kowenz-Leutz E., Pless O., Dittmar G., Knoblich M., Leutz A.;
"Crosstalk between C/EBPbeta phosphorylation, arginine methylation,
and SWI/SNF/Mediator implies an indexing transcription factor code.";
EMBO J. 29:1105-1115(2010).
[25]
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).
[26]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-106; LYS-108; LYS-124 AND
LYS-161, 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).
[27]
FUNCTION OF BAF COMPLEX IN CHROMATIN REMODELING.
PubMed=16314535; DOI=10.1128/MCB.25.24.11156-11170.2005;
Ulyanova N.P., Schnitzler G.R.;
"Human SWI/SNF generates abundant, structurally altered dinucleosomes
on polynucleosomal templates.";
Mol. Cell. Biol. 25:11156-11170(2005).
[28]
IDENTIFICATION IN THE BAF COMPLEX, AND IDENTIFICATION BY MASS
SPECTROMETRY.
PubMed=18765789; DOI=10.1101/gad.471408;
Lange M., Kaynak B., Forster U.B., Toenjes M., Fischer J.J., Grimm C.,
Schlesinger J., Just S., Dunkel I., Krueger T., Mebus S., Lehrach H.,
Lurz R., Gobom J., Rottbauer W., Abdelilah-Seyfried S., Sperling S.;
"Regulation of muscle development by DPF3, a novel histone acetylation
and methylation reader of the BAF chromatin remodeling complex.";
Genes Dev. 22:2370-2384(2008).
[29]
INVOLVEMENT IN SWNTS1.
PubMed=17357086; DOI=10.1086/513207;
Hulsebos T.J.M., Plomp A.S., Wolterman R.A., Robanus-Maandag E.C.,
Baas F., Wesseling P.;
"Germline mutation of INI1/SMARCB1 in familial schwannomatosis.";
Am. J. Hum. Genet. 80:805-810(2007).
[30]
INVOLVEMENT IN SWNTS1.
PubMed=18072270; DOI=10.1002/humu.20679;
Sestini R., Bacci C., Provenzano A., Genuardi M., Papi L.;
"Evidence of a four-hit mechanism involving SMARCB1 and NF2 in
schwannomatosis-associated schwannomas.";
Hum. Mutat. 29:227-231(2008).
[31]
INTERACTION WITH PIH1D1.
PubMed=22368283; DOI=10.1093/jmcb/mjs003;
Zhai N., Zhao Z.L., Cheng M.B., Di Y.W., Yan H.X., Cao C.Y., Dai H.,
Zhang Y., Shen Y.F.;
"Human PIH1 associates with histone H4 to mediate the glucose-
dependent enhancement of pre-rRNA synthesis.";
J. Mol. Cell Biol. 4:231-241(2012).
[32]
REVIEW ON SWI/SNF CHROMATIN REMODELING COMPLEXES.
PubMed=22952240; DOI=10.1074/jbc.R111.309302;
Euskirchen G., Auerbach R.K., Snyder M.;
"SWI/SNF chromatin-remodeling factors: multiscale analyses and diverse
functions.";
J. Biol. Chem. 287:30897-30905(2012).
[33]
REVIEW ON SWI/SNF CHROMATIN REMODELING COMPLEXES.
PubMed=26601204; DOI=10.1126/sciadv.1500447;
Kadoch C., Crabtree G.R.;
"Mammalian SWI/SNF chromatin remodeling complexes and cancer:
Mechanistic insights gained from human genomics.";
Sci. Adv. 1:E1500447-E1500447(2015).
[34]
INVOLVEMENT IN CSS3, AND VARIANTS CSS3 CYS-366 AND GLN-374.
PubMed=23906836; DOI=10.1093/hmg/ddt366;
Wieczorek D., Boegershausen N., Beleggia F., Steiner-Haldenstaett S.,
Pohl E., Li Y., Milz E., Martin M., Thiele H., Altmueller J.,
Alanay Y., Kayserili H., Klein-Hitpass L., Boehringer S.,
Wollstein A., Albrecht B., Boduroglu K., Caliebe A., Chrzanowska K.,
Cogulu O., Cristofoli F., Czeschik J.C., Devriendt K., Dotti M.T.,
Elcioglu N., Gener B., Goecke T.O., Krajewska-Walasek M.,
Guillen-Navarro E., Hayek J., Houge G., Kilic E., Simsek-Kiper P.O.,
Lopez-Gonzalez V., Kuechler A., Lyonnet S., Mari F., Marozza A.,
Mathieu Dramard M., Mikat B., Morin G., Morice-Picard F., Ozkinay F.,
Rauch A., Renieri A., Tinschert S., Utine G.E., Vilain C.,
Vivarelli R., Zweier C., Nuernberg P., Rahmann S., Vermeesch J.,
Luedecke H.J., Zeschnigk M., Wollnik B.;
"A comprehensive molecular study on Coffin-Siris and Nicolaides-
Baraitser syndromes identifies a broad molecular and clinical spectrum
converging on altered chromatin remodeling.";
Hum. Mol. Genet. 22:5121-5135(2013).
[35]
STRUCTURE BY NMR OF 2-113, DOMAIN, AND DNA-BINDING.
PubMed=26073604; DOI=10.1016/j.str.2015.04.021;
Allen M.D., Freund S.M., Zinzalla G., Bycroft M.;
"The SWI/SNF subunit INI1 contains an N-terminal winged helix DNA
binding domain that is a target for mutations in schwannomatosis.";
Structure 23:1344-1349(2015).
[36]
VARIANTS CSS3 LYS-364 DEL AND HIS-377.
PubMed=22426308; DOI=10.1038/ng.2219;
Tsurusaki Y., Okamoto N., Ohashi H., Kosho T., Imai Y., Hibi-Ko Y.,
Kaname T., Naritomi K., Kawame H., Wakui K., Fukushima Y., Homma T.,
Kato M., Hiraki Y., Yamagata T., Yano S., Mizuno S., Sakazume S.,
Ishii T., Nagai T., Shiina M., Ogata K., Ohta T., Niikawa N.,
Miyatake S., Okada I., Mizuguchi T., Doi H., Saitsu H., Miyake N.,
Matsumoto N.;
"Mutations affecting components of the SWI/SNF complex cause Coffin-
Siris syndrome.";
Nat. Genet. 44:376-378(2012).
-!- FUNCTION: Core component of the BAF (hSWI/SNF) complex. This ATP-
dependent chromatin-remodeling complex plays important roles in
cell proliferation and differentiation, in cellular antiviral
activities and inhibition of tumor formation. The BAF complex is
able to create a stable, altered form of chromatin that constrains
fewer negative supercoils than normal. This change in supercoiling
would be due to the conversion of up to one-half of the
nucleosomes on polynucleosomal arrays into asymmetric structures,
termed altosomes, each composed of 2 histones octamers. Stimulates
in vitro the remodeling activity of SMARCA4/BRG1/BAF190A. Involved
in activation of CSF1 promoter. Belongs to the neural progenitors-
specific chromatin remodeling complex (npBAF complex) and the
neuron-specific chromatin remodeling complex (nBAF complex).
During neural development a switch from a stem/progenitor to a
postmitotic chromatin remodeling mechanism occurs as neurons exit
the cell cycle and become committed to their adult state. The
transition from proliferating neural stem/progenitor cells to
postmitotic neurons requires a switch in subunit composition of
the npBAF and nBAF complexes. As neural progenitors exit mitosis
and differentiate into neurons, npBAF complexes which contain
ACTL6A/BAF53A and PHF10/BAF45A, are exchanged for homologous
alternative ACTL6B/BAF53B and DPF1/BAF45B or DPF3/BAF45C subunits
in neuron-specific complexes (nBAF). The npBAF complex is
essential for the self-renewal/proliferative capacity of the
multipotent neural stem cells. The nBAF complex along with CREST
plays a role regulating the activity of genes essential for
dendrite growth (By similarity). Plays a key role in cell-cycle
control and causes cell cycle arrest in G0/G1.
{ECO:0000250|UniProtKB:Q9Z0H3, ECO:0000269|PubMed:10078207,
ECO:0000269|PubMed:12226744, ECO:0000269|PubMed:14604992,
ECO:0000269|PubMed:16267391, ECO:0000269|PubMed:16314535,
ECO:0000269|PubMed:9448295}.
-!- SUBUNIT: Component of the multiprotein chromatin-remodeling
complexes SWI/SNF: SWI/SNF-A (BAF), SWI/SNF-B (PBAF) and related
complexes. The canonical complex contains a catalytic subunit
(either SMARCA4/BRG1/BAF190A or SMARCA2/BRM/BAF190B) and at least
SMARCE1, ACTL6A/BAF53, SMARCC1/BAF155, SMARCC2/BAF170, and
SMARCB1/SNF5/BAF47. Other subunits specific to each of the
complexes may also be present permitting several possible
combinations developmentally and tissue specific (Probable).
Component of the BAF complex, which includes at least actin
(ACTB), ARID1A/BAF250A, ARID1B/BAF250B, SMARCA2/BRM,
SMARCA4/BRG1/BAF190A, ACTL6A/BAF53, ACTL6B/BAF53B, SMARCE1/BAF57
SMARCC1/BAF155, SMARCC2/BAF170, SMARCB1/SNF5/INI1, and one or more
SMARCD1/BAF60A, SMARCD2/BAF60B, or SMARCD3/BAF60C. In muscle
cells, the BAF complex also contains DPF3 (PubMed:8895581,
PubMed:18765789). Component of neural progenitors-specific
chromatin remodeling complex (npBAF complex) composed of at least,
ARID1A/BAF250A or ARID1B/BAF250B, SMARCD1/BAF60A, SMARCD3/BAF60C,
SMARCA2/BRM/BAF190B, SMARCA4/BRG1/BAF190A, SMARCB1/BAF47,
SMARCC1/BAF155, SMARCE1/BAF57, SMARCC2/BAF170, PHF10/BAF45A,
ACTL6A/BAF53A and actin. Component of neuron-specific chromatin
remodeling complex (nBAF complex) composed of at least,
ARID1A/BAF250A or ARID1B/BAF250B, SMARCD1/BAF60A, SMARCD3/BAF60C,
SMARCA2/BRM/BAF190B, SMARCA4/BRG1/BAF190A, SMARCB1/BAF47,
SMARCC1/BAF155, SMARCE1/BAF57, SMARCC2/BAF170, DPF1/BAF45B,
DPF3/BAF45C, ACTL6B/BAF53B and actin (By similarity). Component of
the SWI/SNF-B (PBAF) chromatin remodeling complex, at least
composed of SMARCA4/BRG1, SMARCB1/BAF47/SNF5, ACTL6A/BAF53A or
ACTL6B/BAF53B, SMARCE1/BAF57, SMARCD1/BAF60A, SMARCD2/BAF60B,
perhaps SMARCD3/BAF60C, SMARCC1/BAF155, SMARCC2/BAF170,
PBRM1/BAF180, ARID2/BAF200 and actin (PubMed:26601204). Binds to
double-stranded DNA. Interacts with CEBPB (when not methylated)
(PubMed:20111005). Interacts with PIH1D1 (PubMed:22368283).
Interacts with MYK and MAEL (PubMed:10319872). Interacts with
PPP1R15A (PubMed:10490642, PubMed:12016208).
{ECO:0000250|UniProtKB:Q9Z0H3, ECO:0000269|PubMed:10319872,
ECO:0000269|PubMed:10490642, ECO:0000269|PubMed:12016208,
ECO:0000269|PubMed:18765789, ECO:0000269|PubMed:20111005,
ECO:0000269|PubMed:22368283, ECO:0000269|PubMed:8895581,
ECO:0000303|PubMed:22952240, ECO:0000303|PubMed:26601204}.
-!- SUBUNIT: (Microbial infection) Binds tightly to the human
immunodeficiency virus-type 1 (HIV-1) integrase in vitro and
stimulates its DNA-joining activity. Interacts with human
papillomavirus 18 E1 protein to stimulate its viral replication
(PubMed:10365963). Interacts with Epstein-Barr virus protein EBNA-
2 (PubMed:8709224). {ECO:0000269|PubMed:10365963,
ECO:0000269|PubMed:8709224}.
-!- INTERACTION:
P04326:- (xeno); NbExp=3; IntAct=EBI-358419, EBI-7333987;
Q68CP9:ARID2; NbExp=3; IntAct=EBI-358419, EBI-637818;
P06789:E1 (xeno); NbExp=5; IntAct=EBI-7015645, EBI-7015660;
P04585:gag-pol (xeno); NbExp=3; IntAct=EBI-358419, EBI-9872653;
P51532:SMARCA4; NbExp=22; IntAct=EBI-358419, EBI-302489;
Q8K1P7:Smarca4 (xeno); NbExp=2; IntAct=EBI-358419, EBI-689301;
-!- SUBCELLULAR LOCATION: Nucleus.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=A; Synonyms=INI1A;
IsoId=Q12824-1; Sequence=Displayed;
Name=B; Synonyms=INI1B;
IsoId=Q12824-2; Sequence=VSP_004399;
-!- DOMAIN: The N-terminal DNA-binding region is structurally similar
to winged helix domains. {ECO:0000305|PubMed:26073604}.
-!- DISEASE: Rhabdoid tumor predisposition syndrome 1 (RTPS1)
[MIM:609322]: A familial cancer syndrome predisposing to renal or
extrarenal malignant rhabdoid tumors and to a variety of tumors of
the central nervous system, including choroid plexus carcinoma,
medulloblastoma, and central primitive neuroectodermal tumors.
Rhabdoid tumors are the most aggressive and lethal malignancies
occurring in early childhood. {ECO:0000269|PubMed:9671307,
ECO:0000269|PubMed:9892189}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Schwannomatosis 1 (SWNTS1) [MIM:162091]: A cancer
syndrome in which patients develop multiple non-vestibular
schwannomas, benign neoplasms that arise from Schwann cells of the
cranial, peripheral, and autonomic nerves.
{ECO:0000269|PubMed:17357086, ECO:0000269|PubMed:18072270}.
Note=Disease susceptibility is associated with variations
affecting the gene represented in this entry.
-!- DISEASE: Coffin-Siris syndrome 3 (CSS3) [MIM:614608]: A form of
Coffin-Siris syndrome, a congenital multiple malformation syndrome
with broad phenotypic and genetic variability. Cardinal features
are intellectual disability, coarse facial features,
hypertrichosis, and hypoplastic or absent fifth digit nails or
phalanges. Additional features include malformations of the
cardiac, gastrointestinal, genitourinary, and/or central nervous
systems. Sucking/feeding difficulties, poor growth, ophthalmologic
abnormalities, hearing impairment, and spinal anomalies are common
findings. Both autosomal dominant and autosomal recessive
inheritance patterns have been reported.
{ECO:0000269|PubMed:22426308, ECO:0000269|PubMed:23906836}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- SIMILARITY: Belongs to the SNF5 family. {ECO:0000305}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/SMARCB1ID169.html";
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/smarcb1/";
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; U04847; AAA81905.1; -; mRNA.
EMBL; Y17118; CAA76639.1; ALT_SEQ; Genomic_DNA.
EMBL; Y17119; CAA76639.1; JOINED; Genomic_DNA.
EMBL; Y17120; CAA76639.1; JOINED; Genomic_DNA.
EMBL; Y17121; CAA76639.1; JOINED; Genomic_DNA.
EMBL; Y17122; CAA76639.1; JOINED; Genomic_DNA.
EMBL; Y17123; CAA76639.1; JOINED; Genomic_DNA.
EMBL; Y17124; CAA76639.1; JOINED; Genomic_DNA.
EMBL; Y17125; CAA76639.1; JOINED; Genomic_DNA.
EMBL; Y17126; CAA76639.1; JOINED; Genomic_DNA.
EMBL; AJ011738; CAA09759.1; -; mRNA.
EMBL; AJ011737; CAA09758.1; -; mRNA.
EMBL; AB017523; BAC77068.1; -; mRNA.
EMBL; CR456581; CAG30467.1; -; mRNA.
EMBL; AK021419; BAG51033.1; -; mRNA.
EMBL; DQ230988; ABB02184.1; -; Genomic_DNA.
EMBL; CH471095; EAW59606.1; -; Genomic_DNA.
EMBL; BC117114; AAI17115.1; -; mRNA.
EMBL; BC143667; AAI43668.1; -; mRNA.
CCDS; CCDS13817.1; -. [Q12824-1]
CCDS; CCDS46671.1; -. [Q12824-2]
PIR; S54705; S54705.
RefSeq; NP_001007469.1; NM_001007468.2. [Q12824-2]
RefSeq; NP_003064.2; NM_003073.4. [Q12824-1]
UniGene; Hs.534350; -.
PDB; 5AJ1; NMR; -; A=2-113.
PDB; 5GJK; X-ray; 2.05 A; B=183-249.
PDB; 5L7A; X-ray; 2.10 A; A/B/C/D=184-252.
PDB; 5L7B; NMR; -; A=184-258.
PDBsum; 5AJ1; -.
PDBsum; 5GJK; -.
PDBsum; 5L7A; -.
PDBsum; 5L7B; -.
ProteinModelPortal; Q12824; -.
SMR; Q12824; -.
BioGrid; 112482; 129.
CORUM; Q12824; -.
DIP; DIP-27550N; -.
IntAct; Q12824; 51.
MINT; MINT-94943; -.
STRING; 9606.ENSP00000263121; -.
iPTMnet; Q12824; -.
PhosphoSitePlus; Q12824; -.
BioMuta; SMARCB1; -.
DMDM; 51338799; -.
EPD; Q12824; -.
MaxQB; Q12824; -.
PaxDb; Q12824; -.
PeptideAtlas; Q12824; -.
PRIDE; Q12824; -.
DNASU; 6598; -.
Ensembl; ENST00000263121; ENSP00000263121; ENSG00000099956. [Q12824-1]
Ensembl; ENST00000407422; ENSP00000383984; ENSG00000099956. [Q12824-2]
Ensembl; ENST00000618915; ENSP00000479330; ENSG00000275837. [Q12824-1]
Ensembl; ENST00000631333; ENSP00000486870; ENSG00000275837. [Q12824-2]
GeneID; 6598; -.
KEGG; hsa:6598; -.
UCSC; uc002zyb.4; human. [Q12824-1]
CTD; 6598; -.
DisGeNET; 6598; -.
EuPathDB; HostDB:ENSG00000099956.18; -.
GeneCards; SMARCB1; -.
GeneReviews; SMARCB1; -.
HGNC; HGNC:11103; SMARCB1.
HPA; CAB009196; -.
HPA; HPA018248; -.
HPA; HPA019127; -.
MalaCards; SMARCB1; -.
MIM; 162091; phenotype.
MIM; 601607; gene.
MIM; 609322; phenotype.
MIM; 614608; phenotype.
neXtProt; NX_Q12824; -.
OpenTargets; ENSG00000099956; -.
Orphanet; 99966; Atypical teratoid rhabdoid tumor.
Orphanet; 1465; Coffin-Siris syndrome.
Orphanet; 263662; Familial multiple meningioma.
Orphanet; 231108; Familial rhabdoid tumor.
Orphanet; 93921; Neurofibromatosis type 3.
PharmGKB; PA35953; -.
eggNOG; KOG1649; Eukaryota.
eggNOG; ENOG410XSZD; LUCA.
GeneTree; ENSGT00440000038585; -.
HOGENOM; HOG000015760; -.
HOVERGEN; HBG011709; -.
InParanoid; Q12824; -.
KO; K11648; -.
PhylomeDB; Q12824; -.
TreeFam; TF105993; -.
Reactome; R-HSA-3214858; RMTs methylate histone arginines.
Reactome; R-HSA-8939243; RUNX1 interacts with co-factors whose precise effect on RUNX1 targets is not known.
SIGNOR; Q12824; -.
ChiTaRS; SMARCB1; human.
GeneWiki; SMARCB1; -.
GenomeRNAi; 6598; -.
PRO; PR:Q12824; -.
Proteomes; UP000005640; Chromosome 22.
Bgee; ENSG00000099956; -.
CleanEx; HS_SMARCB1; -.
ExpressionAtlas; Q12824; baseline and differential.
Genevisible; Q12824; HS.
GO; GO:0001650; C:fibrillar center; IDA:HPA.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
GO; GO:0071565; C:nBAF complex; ISS:UniProtKB.
GO; GO:0071564; C:npBAF complex; ISS:UniProtKB.
GO; GO:0000790; C:nuclear chromatin; IDA:UniProtKB.
GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0043234; C:protein complex; IDA:UniProtKB.
GO; GO:0016514; C:SWI/SNF complex; IDA:UniProtKB.
GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
GO; GO:0002039; F:p53 binding; IPI:BHF-UCL.
GO; GO:0001164; F:RNA polymerase I CORE element sequence-specific DNA binding; IMP:UniProtKB.
GO; GO:0030957; F:Tat protein binding; IPI:BHF-UCL.
GO; GO:0003713; F:transcription coactivator activity; IMP:BHF-UCL.
GO; GO:0043044; P:ATP-dependent chromatin remodeling; IDA:UniProtKB.
GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
GO; GO:0006338; P:chromatin remodeling; IDA:BHF-UCL.
GO; GO:0016569; P:covalent chromatin modification; IEA:UniProtKB-KW.
GO; GO:0015074; P:DNA integration; TAS:ProtInc.
GO; GO:0006281; P:DNA repair; IBA:GO_Central.
GO; GO:0008285; P:negative regulation of cell proliferation; IBA:GO_Central.
GO; GO:1900110; P:negative regulation of histone H3-K9 dimethylation; IMP:UniProtKB.
GO; GO:1900113; P:negative regulation of histone H3-K9 trimethylation; IMP:UniProtKB.
GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
GO; GO:0006337; P:nucleosome disassembly; IDA:BHF-UCL.
GO; GO:0043923; P:positive regulation by host of viral transcription; IMP:BHF-UCL.
GO; GO:1902661; P:positive regulation of glucose mediated signaling pathway; IDA:UniProtKB.
GO; GO:2000617; P:positive regulation of histone H3-K9 acetylation; IMP:UniProtKB.
GO; GO:0090240; P:positive regulation of histone H4 acetylation; IMP:UniProtKB.
GO; GO:0051091; P:positive regulation of sequence-specific DNA binding transcription factor activity; IDA:BHF-UCL.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:BHF-UCL.
GO; GO:1901838; P:positive regulation of transcription of nuclear large rRNA transcript from RNA polymerase I promoter; IMP:UniProtKB.
GO; GO:0006357; P:regulation of transcription from RNA polymerase II promoter; TAS:ProtInc.
GO; GO:0039692; P:single stranded viral RNA replication via double stranded DNA intermediate; IDA:MGI.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
InterPro; IPR017393; Sfh1/SNF5.
InterPro; IPR006939; SNF5.
PANTHER; PTHR10019; PTHR10019; 1.
Pfam; PF04855; SNF5; 2.
PIRSF; PIRSF038126; SWI_SNF; 1.
1: Evidence at protein level;
3D-structure; Activator; Alternative splicing; Cell cycle;
Chromatin regulator; Complete proteome; Disease mutation; DNA-binding;
Host-virus interaction; Hypotrichosis; Isopeptide bond;
Mental retardation; Neurogenesis; Nucleus; Phosphoprotein;
Reference proteome; Repeat; Transcription; Transcription regulation;
Tumor suppressor; Ubl conjugation.
CHAIN 1 385 SWI/SNF-related matrix-associated actin-
dependent regulator of chromatin
subfamily B member 1.
/FTId=PRO_0000205948.
REPEAT 186 245 1.
REPEAT 259 319 2.
REGION 1 113 DNA-binding.
{ECO:0000269|PubMed:26073604}.
REGION 183 243 HIV-1 integrase-binding.
REGION 186 319 2 X approximate tandem repeats.
REGION 186 245 MYC-binding.
{ECO:0000269|PubMed:10208879}.
REGION 304 318 Interaction with PPP1R15A.
{ECO:0000269|PubMed:12016208}.
MOD_RES 129 129 Phosphoserine.
{ECO:0000244|PubMed:17525332}.
CROSSLNK 106 106 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 108 108 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 124 124 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 161 161 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
VAR_SEQ 69 77 Missing (in isoform B).
{ECO:0000303|PubMed:10208879,
ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334,
ECO:0000303|Ref.4}.
/FTId=VSP_004399.
VARIANT 364 364 Missing (in CSS3).
{ECO:0000269|PubMed:22426308}.
/FTId=VAR_068178.
VARIANT 366 366 R -> C (in CSS3).
{ECO:0000269|PubMed:23906836}.
/FTId=VAR_076934.
VARIANT 374 374 R -> Q (in CSS3).
{ECO:0000269|PubMed:23906836}.
/FTId=VAR_076935.
VARIANT 377 377 R -> H (in CSS3; dbSNP:rs387906812).
{ECO:0000269|PubMed:22426308}.
/FTId=VAR_068179.
CONFLICT 136 136 P -> S (in Ref. 1 and 2; CAA76639).
{ECO:0000305}.
CONFLICT 378 378 L -> E (in Ref. 2; CAA76639).
{ECO:0000305}.
CONFLICT 382 382 A -> G (in Ref. 1 and 2; CAA76639).
{ECO:0000305}.
STRAND 16 18 {ECO:0000244|PDB:5AJ1}.
STRAND 25 28 {ECO:0000244|PDB:5AJ1}.
HELIX 29 36 {ECO:0000244|PDB:5AJ1}.
HELIX 42 46 {ECO:0000244|PDB:5AJ1}.
STRAND 52 54 {ECO:0000244|PDB:5AJ1}.
HELIX 57 66 {ECO:0000244|PDB:5AJ1}.
STRAND 72 74 {ECO:0000244|PDB:5AJ1}.
STRAND 89 92 {ECO:0000244|PDB:5AJ1}.
HELIX 93 101 {ECO:0000244|PDB:5AJ1}.
HELIX 105 108 {ECO:0000244|PDB:5AJ1}.
STRAND 186 195 {ECO:0000244|PDB:5GJK}.
STRAND 198 207 {ECO:0000244|PDB:5GJK}.
HELIX 215 226 {ECO:0000244|PDB:5GJK}.
HELIX 230 247 {ECO:0000244|PDB:5GJK}.
SEQUENCE 385 AA; 44141 MW; B7BCA26875BD943D CRC64;
MMMMALSKTF GQKPVKFQLE DDGEFYMIGS EVGNYLRMFR GSLYKRYPSL WRRLATVEER
KKIVASSHGK KTKPNTKDHG YTTLATSVTL LKASEVEEIL DGNDEKYKAV SISTEPPTYL
REQKAKRNSQ WVPTLPNSSH HLDAVPCSTT INRNRMGRDK KRTFPLCFDD HDPAVIHENA
SQPEVLVPIR LDMEIDGQKL RDAFTWNMNE KLMTPEMFSE ILCDDLDLNP LTFVPAIASA
IRQQIESYPT DSILEDQSDQ RVIIKLNIHV GNISLVDQFE WDMSEKENSP EKFALKLCSE
LGLGGEFVTT IAYSIRGQLS WHQKTYAFSE NPLPTVEIAI RNTGDADQWC PLLETLTDAE
MEKKIRDQDR NTRRMRRLAN TAPAW


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