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Squamous cell carcinoma antigen recognized by T-cells 3 (SART-3) (Tat-interacting protein of 110 kDa) (Tip110) (p110 nuclear RNA-binding protein)

 SART3_HUMAN             Reviewed;         963 AA.
Q15020; A8K2E4; B7ZKM0; Q2M2H0; Q58F06; Q8IUS1; Q96J95;
07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
22-NOV-2017, entry version 163.
RecName: Full=Squamous cell carcinoma antigen recognized by T-cells 3 {ECO:0000305};
Short=SART-3 {ECO:0000312|EMBL:BAA78384.1};
AltName: Full=Tat-interacting protein of 110 kDa {ECO:0000303|PubMed:11959860};
Short=Tip110 {ECO:0000303|PubMed:11959860};
AltName: Full=p110 nuclear RNA-binding protein {ECO:0000303|PubMed:12032085};
Name=SART3 {ECO:0000312|HGNC:HGNC:16860};
Synonyms=KIAA0156 {ECO:0000312|EMBL:BAA09929.1},
TIP110 {ECO:0000303|PubMed:11959860};
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 SUBCELLULAR LOCATION.
PubMed=10463607;
Yang D., Nakao M., Shichijo S., Sasatomi T., Takasu H., Matsumoto H.,
Mori K., Hayashi A., Yamana H., Shirouzu K., Itoh K.;
"Identification of a gene coding for a protein possessing shared tumor
epitopes capable of inducing HLA-A24-restricted cytotoxic T
lymphocytes in cancer patients.";
Cancer Res. 59:4056-4063(1999).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY,
SUBCELLULAR LOCATION, FUNCTION, INTERACTION WITH TAT, AND REGION.
TISSUE=Fetal brain;
PubMed=11959860; DOI=10.1074/jbc.M200773200;
Liu Y., Li J., Kim B.O., Pace B.S., He J.J.;
"HIV-1 Tat protein-mediated transactivation of the HIV-1 long terminal
repeat promoter is potentiated by a novel nuclear Tat-interacting
protein of 110 kDa, Tip110.";
J. Biol. Chem. 277:23854-23863(2002).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Bone marrow;
PubMed=8590280; DOI=10.1093/dnares/2.4.167;
Nagase T., Seki N., Tanaka A., Ishikawa K., Nomura N.;
"Prediction of the coding sequences of unidentified human genes. IV.
The coding sequences of 40 new genes (KIAA0121-KIAA0160) deduced by
analysis of cDNA clones from human cell line KG-1.";
DNA Res. 2:167-174(1995).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
GLU-23.
TISSUE=Thalamus;
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).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16541075; DOI=10.1038/nature04569;
Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M.,
Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B.,
Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D.,
Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z.,
Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H.,
Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H.,
Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V.,
Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J.,
Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A.,
Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M.,
Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E.,
Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M.,
Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R.,
Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J.,
Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C.,
Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M.,
Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M.,
Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P.,
Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L.,
Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E.,
Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C.,
Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F.,
Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M.,
Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S.,
Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D.,
Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I.,
Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T.,
Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S.,
Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D.,
Kucherlapati R., Weinstock G., Gibbs R.A.;
"The finished DNA sequence of human chromosome 12.";
Nature 440:346-351(2006).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3 AND 4).
TISSUE=Brain, Eye, Skin, and Uterus;
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).
[7]
FUNCTION.
PubMed=12032085; DOI=10.1093/emboj/21.11.2724;
Bell M., Schreiner S., Damianov A., Reddy R., Bindereif A.;
"p110, a novel human U6 snRNP protein and U4/U6 snRNP recycling
factor.";
EMBO J. 21:2724-2735(2002).
[8]
SUBCELLULAR LOCATION.
PubMed=12578909; DOI=10.1083/jcb.200210087;
Stanek D., Rader S.D., Klingauf M., Neugebauer K.M.;
"Targeting of U4/U6 small nuclear RNP assembly factor SART3/p110 to
Cajal bodies.";
J. Cell Biol. 160:505-516(2003).
[9]
FUNCTION.
PubMed=14749385; DOI=10.1128/MCB.24.4.1700-1708.2004;
Damianov A., Schreiner S., Bindereif A.;
"Recycling of the U12-type spliceosome requires p110, a component of
the U6atac snRNP.";
Mol. Cell. Biol. 24:1700-1708(2004).
[10]
FUNCTION (ISOFORM 2), INTERACTION WITH PRPF3, AND REGION.
PubMed=15314151; DOI=10.1128/MCB.24.17.7392-7401.2004;
Medenbach J., Schreiner S., Liu S., Luhrmann R., Bindereif A.;
"Human U4/U6 snRNP recycling factor p110: mutational analysis reveals
the function of the tetratricopeptide repeat domain in recycling.";
Mol. Cell. Biol. 24:7392-7401(2004).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16, 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).
[12]
INTERACTION WITH AGO1 AND AGO2.
PubMed=17932509; DOI=10.1038/sj.embor.7401088;
Hoeck J., Weinmann L., Ender C., Ruedel S., Kremmer E., Raabe M.,
Urlaub H., Meister G.;
"Proteomic and functional analysis of Argonaute-containing mRNA-
protein complexes in human cells.";
EMBO Rep. 8:1052-1060(2007).
[13]
PROTEIN SEQUENCE OF 2-17; 121-130; 233-243; 295-322; 329-335; 350-356;
360-370; 452-463; 494-502; 555-568; 646-669; 758-768 AND 911-918,
CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, AND
IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Hepatoma;
Bienvenut W.V., Dhillon A.S., Kolch W.;
Submitted (FEB-2008) to UniProtKB.
[14]
IDENTIFICATION IN THE 7SK SNRNP COMPLEX.
PubMed=17643375; DOI=10.1016/j.molcel.2007.06.027;
Jeronimo C., Forget D., Bouchard A., Li Q., Chua G., Poitras C.,
Therien C., Bergeron D., Bourassa S., Greenblatt J., Chabot B.,
Poirier G.G., Hughes T.R., Blanchette M., Price D.H., Coulombe B.;
"Systematic analysis of the protein interaction network for the human
transcription machinery reveals the identity of the 7SK capping
enzyme.";
Mol. Cell 27:262-274(2007).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-852, 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).
[16]
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).
[17]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
Mann M., Daub H.;
"Large-scale proteomics analysis of the human kinome.";
Mol. Cell. Proteomics 8:1751-1764(2009).
[18]
FUNCTION, INTERACTION WITH PRPF3 AND USP4, AND REGION.
PubMed=20595234; DOI=10.1101/gad.1925010;
Song E.J., Werner S.L., Neubauer J., Stegmeier F., Aspden J., Rio D.,
Harper J.W., Elledge S.J., Kirschner M.W., Rape M.;
"The Prp19 complex and the Usp4Sart3 deubiquitinating enzyme control
reversible ubiquitination at the spliceosome.";
Genes Dev. 24:1434-1447(2010).
[19]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], 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).
[20]
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).
[21]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE
SCALE ANALYSIS] AT SER-10, 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).
[22]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[23]
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).
[24]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10; SER-215; SER-650;
THR-657; SER-769 AND SER-795, 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).
[25]
FUNCTION, AND INTERACTION WITH USP15.
PubMed=24526689; DOI=10.1074/jbc.M114.551754;
Long L., Thelen J.P., Furgason M., Haj-Yahya M., Brik A., Cheng D.,
Peng J., Yao T.;
"The U4/U6 recycling factor SART3 has histone chaperone activity and
associates with USP15 to regulate H2B deubiquitination.";
J. Biol. Chem. 289:8916-8930(2014).
[26]
METHYLATION [LARGE SCALE ANALYSIS] AT ARG-906, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Colon carcinoma;
PubMed=24129315; DOI=10.1074/mcp.O113.027870;
Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V.,
Aguiar M., Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C.,
Vemulapalli V., Bedford M.T., Comb M.J.;
"Immunoaffinity enrichment and mass spectrometry analysis of protein
methylation.";
Mol. Cell. Proteomics 13:372-387(2014).
[27]
STRUCTURE BY NMR OF 791-877.
RIKEN structural genomics initiative (RSGI);
"Solution structure of the RNA binding domain of squamous cell
carcinoma antigen recognized by T cells 3.";
Submitted (APR-2007) to the PDB data bank.
[28]
VARIANT MET-591.
PubMed=15840095; DOI=10.1111/j.1365-2133.2005.06443.x;
Zhang Z.H., Niu Z.M., Yuan W.T., Zhao J.J., Jiang F.X., Zhang J.,
Chai B., Cui F., Chen W., Lian C.H., Xiang L.H., Xu S.J., Liu W.D.,
Zheng Z.Z., Huang W.;
"A mutation in SART3 gene in a Chinese pedigree with disseminated
superficial actinic porokeratosis.";
Br. J. Dermatol. 152:658-663(2005).
-!- FUNCTION: U6 snRNP-binding protein that functions as a recycling
factor of the splicing machinery. Promotes the initial reassembly
of U4 and U6 snRNPs following their ejection from the spliceosome
during its maturation (PubMed:12032085). Also binds U6atac snRNPs
and may function as a recycling factor for U4atac/U6atac
spliceosomal snRNP, an initial step in the assembly of U12-type
spliceosomal complex. The U12-type spliceosomal complex plays a
role in the splicing of introns with non-canonical splice sites
(PubMed:14749385). May also function as a substrate-targeting
factor for deubiquitinases like USP4 and USP15. Recruits USP4 to
ubiquitinated PRPF3 within the U4/U5/U6 tri-snRNP complex,
promoting PRPF3 deubiquitination and thereby regulating the
spliceosome U4/U5/U6 tri-snRNP spliceosomal complex disassembly
(PubMed:20595234). May also recruit the deubiquitinase USP15 to
histone H2B and mediate histone deubiquitination, thereby
regulating gene expression and/or DNA repair (PubMed:24526689).
May play a role in hematopoiesis probably through transcription
regulation of specific genes including MYC (By similarity).
{ECO:0000250|UniProtKB:Q9JLI8, ECO:0000269|PubMed:12032085,
ECO:0000269|PubMed:14749385, ECO:0000269|PubMed:20595234,
ECO:0000269|PubMed:24526689}.
-!- FUNCTION: Regulates Tat transactivation activity through direct
interaction. May be a cellular factor for HIV-1 gene expression
and viral replication. {ECO:0000269|PubMed:11959860}.
-!- SUBUNIT: Component of the 7SK snRNP complex at least composed of
P-TEFb (composed of CDK9 and CCNT1/cyclin-T1), HEXIM1, HEXIM2,
BCDIN3, SART3 proteins and 7SK and U6 snRNAs (PubMed:17643375).
Interacts with AGO1 and AGO2 (PubMed:17932509). Interacts with
PRPF3 and USP4; the interaction with PRPF3 is direct and recruits
USP4 to its substrate PRPF3 (PubMed:15314151, PubMed:20595234).
Interacts with USP15; the interaction is direct (PubMed:24526689).
Interacts with HIV-1 Tat (PubMed:11959860).
{ECO:0000269|PubMed:11959860, ECO:0000269|PubMed:15314151,
ECO:0000269|PubMed:17643375, ECO:0000269|PubMed:17932509,
ECO:0000269|PubMed:20595234, ECO:0000269|PubMed:24526689}.
-!- INTERACTION:
F5HFL9:K4 (xeno); NbExp=2; IntAct=EBI-308619, EBI-14032776;
Q15287:RNPS1; NbExp=5; IntAct=EBI-308619, EBI-395959;
-!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm
{ECO:0000269|PubMed:10463607, ECO:0000269|PubMed:11959860,
ECO:0000269|PubMed:12578909}. Nucleus, Cajal body
{ECO:0000269|PubMed:12578909}. Nucleus speckle
{ECO:0000269|PubMed:11959860}. Cytoplasm
{ECO:0000269|PubMed:10463607, ECO:0000269|PubMed:11959860}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1;
IsoId=Q15020-1; Sequence=Displayed;
Name=2;
IsoId=Q15020-2; Sequence=VSP_017250, VSP_017251;
Note=May be produced at very low levels due to a premature stop
codon in the mRNA, leading to nonsense-mediated mRNA decay.
Inactive in U4/U6 snRNP recycling.
{ECO:0000269|PubMed:15314151};
Name=3;
IsoId=Q15020-3; Sequence=VSP_017248, VSP_017249;
Note=No experimental confirmation available.;
Name=4;
IsoId=Q15020-4; Sequence=VSP_057284;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Ubiquitously expressed.
{ECO:0000269|PubMed:11959860}.
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EMBL; AB020880; BAA78384.1; -; mRNA.
EMBL; AF387506; AAK69347.1; -; mRNA.
EMBL; D63879; BAA09929.1; -; mRNA.
EMBL; AK290209; BAF82898.1; -; mRNA.
EMBL; AC008119; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC010206; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; KF455716; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; KF511170; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC032601; AAH32601.1; -; mRNA.
EMBL; BC041638; AAH41638.1; -; mRNA.
EMBL; BC093784; AAH93784.1; -; mRNA.
EMBL; BC103706; AAI03707.1; -; mRNA.
EMBL; BC111983; AAI11984.1; -; mRNA.
EMBL; BC143253; AAI43254.1; -; mRNA.
CCDS; CCDS9117.1; -. [Q15020-1]
RefSeq; NP_055521.1; NM_014706.3. [Q15020-1]
UniGene; Hs.584842; -.
PDB; 2DO4; NMR; -; A=791-877.
PDB; 5CTQ; X-ray; 2.60 A; A/B/C/D=94-611.
PDB; 5CTR; X-ray; 3.01 A; A/B=278-611.
PDB; 5CTT; X-ray; 1.70 A; B=601-649.
PDB; 5JJW; X-ray; 3.01 A; A=280-578.
PDB; 5JJX; X-ray; 2.00 A; A=81-393.
PDB; 5JPZ; X-ray; 3.04 A; A/B=96-574.
PDBsum; 2DO4; -.
PDBsum; 5CTQ; -.
PDBsum; 5CTR; -.
PDBsum; 5CTT; -.
PDBsum; 5JJW; -.
PDBsum; 5JJX; -.
PDBsum; 5JPZ; -.
ProteinModelPortal; Q15020; -.
SMR; Q15020; -.
BioGrid; 115082; 172.
IntAct; Q15020; 45.
MINT; MINT-2867335; -.
STRING; 9606.ENSP00000228284; -.
iPTMnet; Q15020; -.
PhosphoSitePlus; Q15020; -.
BioMuta; SART3; -.
DMDM; 74762140; -.
EPD; Q15020; -.
MaxQB; Q15020; -.
PaxDb; Q15020; -.
PeptideAtlas; Q15020; -.
PRIDE; Q15020; -.
Ensembl; ENST00000228284; ENSP00000228284; ENSG00000075856. [Q15020-1]
Ensembl; ENST00000431469; ENSP00000414453; ENSG00000075856. [Q15020-4]
Ensembl; ENST00000546611; ENSP00000448554; ENSG00000075856. [Q15020-3]
Ensembl; ENST00000546728; ENSP00000449743; ENSG00000075856. [Q15020-2]
GeneID; 9733; -.
KEGG; hsa:9733; -.
UCSC; uc001tmz.2; human. [Q15020-1]
CTD; 9733; -.
DisGeNET; 9733; -.
EuPathDB; HostDB:ENSG00000075856.11; -.
GeneCards; SART3; -.
HGNC; HGNC:16860; SART3.
HPA; HPA044322; -.
MIM; 611684; gene.
neXtProt; NX_Q15020; -.
OpenTargets; ENSG00000075856; -.
PharmGKB; PA34948; -.
eggNOG; KOG0128; Eukaryota.
eggNOG; ENOG410XP88; LUCA.
GeneTree; ENSGT00900000141107; -.
HOGENOM; HOG000063708; -.
HOVERGEN; HBG053888; -.
InParanoid; Q15020; -.
OMA; AFDYNCH; -.
OrthoDB; EOG091G041L; -.
PhylomeDB; Q15020; -.
TreeFam; TF317554; -.
ChiTaRS; SART3; human.
EvolutionaryTrace; Q15020; -.
GeneWiki; SART3; -.
GenomeRNAi; 9733; -.
PRO; PR:Q15020; -.
Proteomes; UP000005640; Chromosome 12.
Bgee; ENSG00000075856; -.
CleanEx; HS_SART3; -.
ExpressionAtlas; Q15020; baseline and differential.
Genevisible; Q15020; HS.
GO; GO:0015030; C:Cajal body; IDA:UniProtKB.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0042393; F:histone binding; IDA:UniProtKB.
GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
GO; GO:0030621; F:U4 snRNA binding; IDA:UniProtKB.
GO; GO:0017070; F:U6 snRNA binding; IDA:UniProtKB.
GO; GO:0030624; F:U6atac snRNA binding; IDA:UniProtKB.
GO; GO:1990381; F:ubiquitin-specific protease binding; IPI:UniProtKB.
GO; GO:0000902; P:cell morphogenesis; IEA:Ensembl.
GO; GO:0071425; P:hematopoietic stem cell proliferation; IEA:Ensembl.
GO; GO:0048872; P:homeostasis of number of cells; IEA:Ensembl.
GO; GO:0000398; P:mRNA splicing, via spliceosome; IDA:UniProtKB.
GO; GO:0006334; P:nucleosome assembly; IDA:UniProtKB.
GO; GO:1903586; P:positive regulation of histone deubiquitination; IDA:UniProtKB.
GO; GO:0010468; P:regulation of gene expression; IDA:MGI.
GO; GO:0000387; P:spliceosomal snRNP assembly; IDA:UniProtKB.
GO; GO:0000244; P:spliceosomal tri-snRNP complex assembly; IDA:UniProtKB.
CDD; cd12391; RRM1_SART3; 1.
CDD; cd12392; RRM2_SART3; 1.
Gene3D; 1.25.40.10; -; 3.
InterPro; IPR003107; HAT.
InterPro; IPR008669; LSM_interact.
InterPro; IPR035979; RBD_domain_sf.
InterPro; IPR000504; RRM_dom.
InterPro; IPR034217; SART3_RRM1.
InterPro; IPR034218; SART3_RRM2.
InterPro; IPR011990; TPR-like_helical_dom_sf.
Pfam; PF05391; Lsm_interact; 1.
Pfam; PF00076; RRM_1; 2.
SMART; SM00386; HAT; 7.
SMART; SM00360; RRM; 2.
SUPFAM; SSF48452; SSF48452; 1.
SUPFAM; SSF54928; SSF54928; 1.
PROSITE; PS50102; RRM; 2.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Coiled coil;
Complete proteome; Cytoplasm; Direct protein sequencing; Methylation;
mRNA processing; mRNA splicing; Nucleus; Phosphoprotein; Polymorphism;
Reference proteome; Repeat; RNA-binding.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:19369195,
ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:22814378,
ECO:0000269|Ref.13}.
CHAIN 2 963 Squamous cell carcinoma antigen
recognized by T-cells 3.
/FTId=PRO_0000223313.
REPEAT 126 158 HAT 1.
REPEAT 164 195 HAT 2.
REPEAT 201 237 HAT 3.
REPEAT 242 275 HAT 4.
REPEAT 324 356 HAT 5.
REPEAT 359 391 HAT 6.
REPEAT 394 430 HAT 7.
REPEAT 487 520 HAT 8.
DOMAIN 704 782 RRM 1. {ECO:0000255|PROSITE-
ProRule:PRU00176}.
DOMAIN 801 878 RRM 2. {ECO:0000255|PROSITE-
ProRule:PRU00176}.
REGION 2 351 Mediates interaction with PRPF3.
{ECO:0000269|PubMed:15314151}.
REGION 487 520 Required for interaction with USP4.
{ECO:0000269|PubMed:20595234}.
REGION 537 953 Necessary and sufficient for U6 snRNA
binding. {ECO:0000269|PubMed:15314151}.
REGION 600 670 Required for nuclear localization.
{ECO:0000269|PubMed:11959860}.
COILED 21 46 {ECO:0000255}.
COILED 82 110 {ECO:0000255}.
COILED 559 619 {ECO:0000255}.
MOTIF 601 617 Nuclear localization signal.
{ECO:0000255}.
COMPBIAS 89 92 Poly-Glu.
COMPBIAS 612 616 Poly-Lys.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:19369195,
ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:22814378,
ECO:0000269|Ref.13}.
MOD_RES 10 10 Phosphoserine.
{ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 16 16 Phosphoserine.
{ECO:0000244|PubMed:17081983}.
MOD_RES 215 215 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 650 650 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 657 657 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 769 769 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 795 795 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 852 852 Phosphoserine.
{ECO:0000244|PubMed:17525332}.
MOD_RES 906 906 Omega-N-methylarginine.
{ECO:0000244|PubMed:24129315}.
VAR_SEQ 105 129 LSINVYDYNCHVDLIRLLRLEGELT -> VGPGVGSGHLPV
FQVLGSPCPGPPP (in isoform 3).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_017248.
VAR_SEQ 130 963 Missing (in isoform 3).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_017249.
VAR_SEQ 351 364 SQYLDRQLKVKDLV -> RSTTESKGFGFICT (in
isoform 2).
{ECO:0000303|PubMed:11959860}.
/FTId=VSP_017250.
VAR_SEQ 365 963 Missing (in isoform 2).
{ECO:0000303|PubMed:11959860}.
/FTId=VSP_017251.
VAR_SEQ 401 436 Missing (in isoform 4).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_057284.
VARIANT 23 23 D -> E (in dbSNP:rs2072579).
{ECO:0000269|PubMed:14702039}.
/FTId=VAR_038802.
VARIANT 591 591 V -> M (found in a patient with
disseminated superficial actinic
porokeratosis; unknown pathological
significance; dbSNP:rs118203954).
{ECO:0000269|PubMed:15840095}.
/FTId=VAR_038683.
VARIANT 621 621 E -> D (in dbSNP:rs2287546).
/FTId=VAR_038684.
HELIX 91 107 {ECO:0000244|PDB:5JJX}.
HELIX 112 124 {ECO:0000244|PDB:5JJX}.
HELIX 128 141 {ECO:0000244|PDB:5JJX}.
HELIX 146 159 {ECO:0000244|PDB:5JJX}.
HELIX 163 176 {ECO:0000244|PDB:5JJX}.
HELIX 183 195 {ECO:0000244|PDB:5JJX}.
TURN 196 198 {ECO:0000244|PDB:5JJX}.
HELIX 202 217 {ECO:0000244|PDB:5JJX}.
TURN 221 223 {ECO:0000244|PDB:5JJX}.
HELIX 225 236 {ECO:0000244|PDB:5JJX}.
STRAND 240 242 {ECO:0000244|PDB:5CTQ}.
HELIX 245 255 {ECO:0000244|PDB:5JJX}.
HELIX 262 272 {ECO:0000244|PDB:5JJX}.
HELIX 279 304 {ECO:0000244|PDB:5JJX}.
HELIX 310 323 {ECO:0000244|PDB:5JJX}.
HELIX 326 339 {ECO:0000244|PDB:5JJX}.
HELIX 344 354 {ECO:0000244|PDB:5JJX}.
HELIX 361 374 {ECO:0000244|PDB:5JJX}.
HELIX 379 392 {ECO:0000244|PDB:5JJX}.
HELIX 396 409 {ECO:0000244|PDB:5CTQ}.
HELIX 414 429 {ECO:0000244|PDB:5CTQ}.
STRAND 436 438 {ECO:0000244|PDB:5JJW}.
HELIX 440 457 {ECO:0000244|PDB:5CTQ}.
HELIX 459 464 {ECO:0000244|PDB:5CTQ}.
HELIX 473 484 {ECO:0000244|PDB:5CTQ}.
HELIX 489 501 {ECO:0000244|PDB:5CTQ}.
TURN 502 506 {ECO:0000244|PDB:5CTQ}.
HELIX 508 521 {ECO:0000244|PDB:5CTQ}.
HELIX 524 537 {ECO:0000244|PDB:5CTQ}.
HELIX 542 556 {ECO:0000244|PDB:5CTQ}.
HELIX 559 603 {ECO:0000244|PDB:5CTQ}.
STRAND 803 807 {ECO:0000244|PDB:2DO4}.
HELIX 814 821 {ECO:0000244|PDB:2DO4}.
TURN 822 824 {ECO:0000244|PDB:2DO4}.
STRAND 827 834 {ECO:0000244|PDB:2DO4}.
STRAND 840 850 {ECO:0000244|PDB:2DO4}.
HELIX 851 861 {ECO:0000244|PDB:2DO4}.
STRAND 864 868 {ECO:0000244|PDB:2DO4}.
STRAND 870 875 {ECO:0000244|PDB:2DO4}.
SEQUENCE 963 AA; 109935 MW; 06B26CEB8B19102A CRC64;
MATAAETSAS EPEAESKAGP KADGEEDEVK AARTRRKVLS RAVAAATYKT MGPAWDQQEE
GVSESDGDEY AMASSAESSP GEYEWEYDEE EEKNQLEIER LEEQLSINVY DYNCHVDLIR
LLRLEGELTK VRMARQKMSE IFPLTEELWL EWLHDEISMA QDGLDREHVY DLFEKAVKDY
ICPNIWLEYG QYSVGGIGQK GGLEKVRSVF ERALSSVGLH MTKGLALWEA YREFESAIVE
AARLEKVHSL FRRQLAIPLY DMEATFAEYE EWSEDPIPES VIQNYNKALQ QLEKYKPYEE
ALLQAEAPRL AEYQAYIDFE MKIGDPARIQ LIFERALVEN CLVPDLWIRY SQYLDRQLKV
KDLVLSVHNR AIRNCPWTVA LWSRYLLAME RHGVDHQVIS VTFEKALNAG FIQATDYVEI
WQAYLDYLRR RVDFKQDSSK ELEELRAAFT RALEYLKQEV EERFNESGDP SCVIMQNWAR
IEARLCNNMQ KARELWDSIM TRGNAKYANM WLEYYNLERA HGDTQHCRKA LHRAVQCTSD
YPEHVCEVLL TMERTEGSLE DWDIAVQKTE TRLARVNEQR MKAAEKEAAL VQQEEEKAEQ
RKRARAEKKA LKKKKKIRGP EKRGADEDDE KEWGDDEEEQ PSKRRRVENS IPAAGETQNV
EVAAGPAGKC AAVDVEPPSK QKEKAASLKR DMPKVLHDSS KDSITVFVSN LPYSMQEPDT
KLRPLFEACG EVVQIRPIFS NRGDFRGYCY VEFKEEKSAL QALEMDRKSV EGRPMFVSPC
VDKSKNPDFK VFRYSTSLEK HKLFISGLPF SCTKEELEEI CKAHGTVKDL RLVTNRAGKP
KGLAYVEYEN ESQASQAVMK MDGMTIKENI IKVAISNPPQ RKVPEKPETR KAPGGPMLLP
QTYGARGKGR TQLSLLPRAL QRPSAAAPQA ENGPAAAPAV AAPAATEAPK MSNADFAKLF
LRK


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