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PC4 and SFRS1-interacting protein (CLL-associated antigen KW-7) (Dense fine speckles 70 kDa protein) (DFS 70) (Lens epithelium-derived growth factor) (Transcriptional coactivator p75/p52)

 PSIP1_HUMAN             Reviewed;         530 AA.
O75475; D3DRI9; O00256; O95368; Q6P391; Q86YB9; Q9NZI3; Q9UER6;
05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
01-NOV-1998, sequence version 1.
25-OCT-2017, entry version 163.
RecName: Full=PC4 and SFRS1-interacting protein;
AltName: Full=CLL-associated antigen KW-7;
AltName: Full=Dense fine speckles 70 kDa protein;
Short=DFS 70;
AltName: Full=Lens epithelium-derived growth factor;
AltName: Full=Transcriptional coactivator p75/p52;
Name=PSIP1; Synonyms=DFS70, LEDGF, PSIP2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), PROTEIN SEQUENCE OF
4-39 AND 76-89, TISSUE SPECIFICITY, AND INTERACTION WITH PC4.
TISSUE=Cervix carcinoma;
PubMed=9822615; DOI=10.1093/emboj/17.22.6723;
Ge H., Si Y., Roeder R.G.;
"Isolation of cDNAs encoding novel transcription coactivators p52 and
p75 reveals an alternate regulatory mechanism of transcriptional
activation.";
EMBO J. 17:6723-6729(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Lens;
PubMed=10623627; DOI=10.1006/bbrc.1999.1979;
Singh D.P., Ohguro N., Kikuchi T., Sueno T., Reddy V.N., Yuge K.,
Chylack L.T. Jr., Shinohara T.;
"Lens epithelium-derived growth factor: effects on growth and survival
of lens epithelial cells, keratinocytes, and fibroblasts.";
Biochem. Biophys. Res. Commun. 267:373-381(2000).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1 AND 2).
PubMed=10721720; DOI=10.1016/S0378-1119(99)00506-5;
Singh D.P., Kimura A., Chylack L.T. Jr., Shinohara T.;
"Lens epithelium-derived growth factor (LEDGF/p75) and p52 are derived
from a single gene by alternative splicing.";
Gene 242:265-273(2000).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Leukemia;
PubMed=12200376; DOI=10.1182/blood-2002-02-0513;
Krackhardt A.M., Witzens M., Harig S., Hodi F.S., Zauls A.J.,
Chessia M., Barrett P., Gribben J.G.;
"Identification of tumor-associated antigens in chronic lymphocytic
leukemia by SEREX.";
Blood 100:2123-2131(2002).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164053; DOI=10.1038/nature02465;
Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E.,
Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
Kimberley A.M., King A., Knights A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S.,
Rogers J., Dunham I.;
"DNA sequence and analysis of human chromosome 9.";
Nature 429:369-374(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
TISSUE=Testis, 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).
[8]
NUCLEOTIDE SEQUENCE [MRNA] OF 180-530 (ISOFORM 1).
PubMed=10856157; DOI=10.1067/mai.2000.107039;
Ochs R.L., Muro Y., Si Y., Ge H., Chan E.K.L., Tan E.M.;
"Autoantibodies to DFS 70 kd/transcription coactivator p75 in atopic
dermatitis and other conditions.";
J. Allergy Clin. Immunol. 105:1211-1220(2000).
[9]
FUNCTION, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
PubMed=15642333; DOI=10.1016/j.exer.2004.08.022;
Chylack L.T. Jr., Fu L., Mancini R., Martin-Rehrmann M.D.,
Saunders A.J., Konopka G., Tian D., Hedley-Whyte E.T., Folkerth R.D.,
Goldstein L.E.;
"Lens epithelium-derived growth factor (LEDGF/p75) expression in fetal
and adult human brain.";
Exp. Eye Res. 79:941-948(2004).
[10]
INTERACTION WITH HUMAN HIV-1 INTEGRASE (ISOFORM 1).
PubMed=15475359; DOI=10.1074/jbc.M408508200;
Llano M., Delgado S., Vanegas M., Poeschla E.M.;
"Lens epithelium-derived growth factor/p75 prevents proteasomal
degradation of HIV-1 integrase.";
J. Biol. Chem. 279:55570-55577(2004).
[11]
INTERACTION WITH HUMAN HIV-1 AND HIV-2 INTEGRASE (ISOFORM 1).
PubMed=15749713; DOI=10.1074/jbc.M411681200;
Busschots K., Vercammen J., Emiliani S., Benarous R., Engelborghs Y.,
Christ F., Debyser Z.;
"The interaction of LEDGF/p75 with integrase is lentiviral-specific
and promotes DNA binding.";
J. Biol. Chem. 280:17841-17847(2005).
[12]
INTERACTION WITH HUMAN HIV-1 INTEGRASE (ISOFORM 1), AND NUCLEAR
LOCALIZATION SIGNAL.
PubMed=15797927; DOI=10.1242/jcs.02299;
Vanegas M., Llano M., Delgado S., Thompson D., Peretz M.,
Poeschla E.M.;
"Identification of the LEDGF/p75 HIV-1 integrase-interaction domain
and NLS reveals NLS-independent chromatin tethering.";
J. Cell Sci. 118:1733-1743(2005).
[13]
INTERACTION WITH SFRS1, AND SUBCELLULAR LOCATION.
PubMed=9885563; DOI=10.1016/S1097-2765(00)80290-7;
Ge H., Si Y., Wolffe A.P.;
"A novel transcriptional coactivator, p52, functionally interacts with
the essential splicing factor ASF/SF2.";
Mol. Cell 2:751-759(1998).
[14]
CHROMOSOMAL TRANSLOCATION WITH NUP98.
PubMed=15725483; DOI=10.1016/j.leukres.2004.09.002;
Morerio C., Acquila M., Rosanda C., Rapella A., Tassano E.,
Micalizzi C., Panarello C.;
"t(9;11)(p22;p15) with NUP98-LEDGF fusion gene in pediatric acute
myeloid leukemia.";
Leuk. Res. 29:467-470(2005).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-122, 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).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-437, 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).
[17]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=T-cell;
PubMed=19367720; DOI=10.1021/pr800500r;
Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.;
"Phosphorylation analysis of primary human T lymphocytes using
sequential IMAC and titanium oxide enrichment.";
J. Proteome Res. 7:5167-5176(2008).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106; THR-141; SER-273;
SER-275; SER-434; SER-443; SER-522 AND THR-527, 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).
[19]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=18318008; DOI=10.1002/pmic.200700884;
Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,
Zou H., Gu J.;
"Large-scale phosphoproteome analysis of human liver tissue by
enrichment and fractionation of phosphopeptides with strong anion
exchange chromatography.";
Proteomics 8:1346-1361(2008).
[20]
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).
[21]
INTERACTION WITH POGZ; HIV-1 INTEGRASE AND CDCA7L, AND MUTAGENESIS OF
LYS-360; ILE-365; ASP-366; VAL-370; PHE-406 AND VAL-408.
PubMed=19244240; DOI=10.1074/jbc.M807781200;
Bartholomeeusen K., Christ F., Hendrix J., Rain J.C., Emiliani S.,
Benarous R., Debyser Z., Gijsbers R., De Rijck J.;
"Lens epithelium-derived growth factor/p75 interacts with the
transposase-derived DDE domain of PogZ.";
J. Biol. Chem. 284:11467-11477(2009).
[22]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-141; THR-167; SER-177;
SER-273 AND SER-275, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[23]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106; THR-122; THR-141;
SER-206; SER-273; SER-275; SER-434 AND THR-527, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[24]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[25]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-129; THR-141; SER-177;
SER-206; SER-275 AND THR-527, AND IDENTIFICATION BY MASS SPECTROMETRY
[LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[26]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106; THR-122; SER-129;
SER-273; SER-275; SER-434 AND SER-514, 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).
[27]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106; THR-122; SER-129;
SER-271; THR-272; SER-273 AND SER-275, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[28]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-75, 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).
[29]
STRUCTURE BY NMR OF 347-471, SUBUNIT, AND MUTAGENESIS OF ILE-365;
ASP-366; PHE-406 AND VAL-408.
PubMed=15895093; DOI=10.1038/nsmb937;
Cherepanov P., Sun Z.-Y., Rahman S., Maertens G., Wagner G.,
Engelman A.;
"Solution structure of the HIV-1 integrase-binding domain in
LEDGF/p75.";
Nat. Struct. Mol. Biol. 12:526-532(2005).
[30]
X-RAY CRYSTALLOGRAPHY (2.02 ANGSTROMS) OF 347-442 IN COMPLEX WITH
HUMAN HIV-1 INTEGRASE.
PubMed=16260736; DOI=10.1073/pnas.0506924102;
Cherepanov P., Ambrosio A.L.B., Rahman S., Ellenberger T.,
Engelman A.;
"Structural basis for the recognition between HIV-1 integrase and
transcriptional coactivator p75.";
Proc. Natl. Acad. Sci. U.S.A. 102:17308-17313(2005).
-!- FUNCTION: Transcriptional coactivator involved in neuroepithelial
stem cell differentiation and neurogenesis. Involved in particular
in lens epithelial cell gene regulation and stress responses. May
play an important role in lens epithelial to fiber cell terminal
differentiation. May play a protective role during stress-induced
apoptosis. Isoform 2 is a more general and stronger
transcriptional coactivator. Isoform 2 may also act as an adapter
to coordinate pre-mRNA splicing. Cellular cofactor for lentiviral
integration. {ECO:0000269|PubMed:15642333}.
-!- SUBUNIT: Monomer. Interacts with IFRD1/PC4. Isoform 2 interacts
with SFRS1. Isoform 1 interacts POGZ and CDCA7L. Isoform 1
interacts with lentiviral integrase and acts as a chromatin
tethering factor to the chromosomal DNA. Isoform 1 interacts in
particular with the human HIV-1 integrase protein (HIV-1 IN),
determining its nuclear localization, its tight association with
chromatin and its protection from the proteasome. Isoform 1
interacts also with HIV-2 IN. Isoform 2 does not interact with
HIV-1 IN. {ECO:0000269|PubMed:15895093,
ECO:0000269|PubMed:16260736, ECO:0000269|PubMed:19244240,
ECO:0000269|PubMed:9822615, ECO:0000269|PubMed:9885563}.
-!- INTERACTION:
P04585:gag-pol (xeno); NbExp=21; IntAct=EBI-1801773, EBI-3989067;
P12497:gag-pol (xeno); NbExp=3; IntAct=EBI-5279836, EBI-10131955;
Q99708:RBBP8; NbExp=4; IntAct=EBI-1801773, EBI-745715;
P63165:SUMO1; NbExp=4; IntAct=EBI-1801773, EBI-80140;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15642333,
ECO:0000269|PubMed:9885563}. Note=Remains chromatin-associated
throughout the cell cycle.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1; Synonyms=p75, PSIP1;
IsoId=O75475-1; Sequence=Displayed;
Note=Less active than isoform 2 as transcriptional coactivator,
but more abundant in cells.;
Name=2; Synonyms=p52, PSIP2;
IsoId=O75475-2; Sequence=VSP_014297, VSP_014298;
Name=3;
IsoId=O75475-3; Sequence=VSP_044435;
-!- TISSUE SPECIFICITY: Widely expressed. Expressed at high level in
the thymus. Expressed in fetal and adult brain. Expressed in
neurons, but not astrocytes. Markedly elevated in fetal as
compared to adult brain. In the adult brain, expressed in the
subventricular zone (SVZ), in hippocampus, and undetectable
elsewhere. In the fetal brain, expressed in the germinal
neuroepithelium and cortical plate regions.
{ECO:0000269|PubMed:15642333, ECO:0000269|PubMed:9822615}.
-!- DOMAIN: Residues 340-417 are necessary and sufficient for the
interaction with HIV-1 IN (IBD domain).
-!- PTM: Citrullinated by PADI4. {ECO:0000250}.
-!- DISEASE: Note=A chromosomal aberration involving PSIP1 is
associated with pediatric acute myeloid leukemia (AML) with
intermediate characteristics between M2-M3 French-American-British
(FAB) subtypes. Translocation t(9;11)(p22;p15) with NUP98. The
chimeric transcript is an in-frame fusion of NUP98 exon 8 to PSIP1
exon 4. {ECO:0000269|PubMed:15725483}.
-!- SIMILARITY: Belongs to the HDGF family. {ECO:0000305}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/PSIP1ID405ch9q22.html";
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EMBL; AF098483; AAC97946.1; -; mRNA.
EMBL; AF098482; AAC97945.1; -; mRNA.
EMBL; AF063020; AAC25167.1; -; mRNA.
EMBL; AF199339; AAF25870.1; -; Genomic_DNA.
EMBL; AF199339; AAF25871.1; -; Genomic_DNA.
EMBL; AF432220; AAL99926.1; -; mRNA.
EMBL; AL359998; CAH71355.1; -; Genomic_DNA.
EMBL; AL441925; CAH71355.1; JOINED; Genomic_DNA.
EMBL; AL513423; CAH71355.1; JOINED; Genomic_DNA.
EMBL; AL441925; CAI13287.1; -; Genomic_DNA.
EMBL; AL359998; CAI13287.1; JOINED; Genomic_DNA.
EMBL; AL513423; CAI13287.1; JOINED; Genomic_DNA.
EMBL; CH471071; EAW58677.1; -; Genomic_DNA.
EMBL; CH471071; EAW58678.1; -; Genomic_DNA.
EMBL; CH471071; EAW58679.1; -; Genomic_DNA.
EMBL; BC044568; AAH44568.2; -; mRNA.
EMBL; BC064135; AAH64135.1; -; mRNA.
EMBL; U94319; AAB52589.1; -; mRNA.
CCDS; CCDS6479.1; -. [O75475-1]
CCDS; CCDS6480.1; -. [O75475-2]
CCDS; CCDS83348.1; -. [O75475-3]
PIR; JC7168; JC7168.
RefSeq; NP_001121689.1; NM_001128217.2. [O75475-1]
RefSeq; NP_001304827.1; NM_001317898.1. [O75475-3]
RefSeq; NP_001304829.1; NM_001317900.1.
RefSeq; NP_066967.3; NM_021144.3. [O75475-2]
RefSeq; NP_150091.2; NM_033222.4. [O75475-1]
UniGene; Hs.658434; -.
PDB; 1Z9E; NMR; -; A=347-471.
PDB; 2B4J; X-ray; 2.02 A; C/D=347-442.
PDB; 2M16; NMR; -; A=1-93.
PDB; 2MSR; NMR; -; B=344-426.
PDB; 2MTN; NMR; -; A=337-442.
PDB; 2N3A; NMR; -; B=348-426.
PDB; 3F9K; X-ray; 3.20 A; C/G/K/O/S/W/a/e/i/m/q/u=347-435.
PDB; 3HPG; X-ray; 3.28 A; G/H/I/J/K/L=347-435.
PDB; 3HPH; X-ray; 2.64 A; E/F/G/H=348-435.
PDB; 3U88; X-ray; 3.00 A; C/D=347-435.
PDB; 3ZEH; NMR; -; A=3-100.
PDB; 4FU6; X-ray; 2.10 A; A=1-135.
PDBsum; 1Z9E; -.
PDBsum; 2B4J; -.
PDBsum; 2M16; -.
PDBsum; 2MSR; -.
PDBsum; 2MTN; -.
PDBsum; 2N3A; -.
PDBsum; 3F9K; -.
PDBsum; 3HPG; -.
PDBsum; 3HPH; -.
PDBsum; 3U88; -.
PDBsum; 3ZEH; -.
PDBsum; 4FU6; -.
ProteinModelPortal; O75475; -.
SMR; O75475; -.
BioGrid; 116339; 51.
CORUM; O75475; -.
DIP; DIP-46656N; -.
IntAct; O75475; 25.
MINT; MINT-4527154; -.
STRING; 9606.ENSP00000370109; -.
BindingDB; O75475; -.
Allergome; 2120; Hom s DSF70.
iPTMnet; O75475; -.
PhosphoSitePlus; O75475; -.
SwissPalm; O75475; -.
BioMuta; PSIP1; -.
EPD; O75475; -.
MaxQB; O75475; -.
PaxDb; O75475; -.
PeptideAtlas; O75475; -.
PRIDE; O75475; -.
TopDownProteomics; O75475-1; -. [O75475-1]
TopDownProteomics; O75475-2; -. [O75475-2]
DNASU; 11168; -.
Ensembl; ENST00000380715; ENSP00000370091; ENSG00000164985. [O75475-3]
Ensembl; ENST00000380716; ENSP00000370092; ENSG00000164985. [O75475-2]
Ensembl; ENST00000380733; ENSP00000370109; ENSG00000164985. [O75475-1]
Ensembl; ENST00000380738; ENSP00000370114; ENSG00000164985. [O75475-1]
Ensembl; ENST00000397519; ENSP00000380653; ENSG00000164985. [O75475-2]
GeneID; 11168; -.
KEGG; hsa:11168; -.
UCSC; uc003zlv.6; human. [O75475-1]
CTD; 11168; -.
DisGeNET; 11168; -.
EuPathDB; HostDB:ENSG00000164985.14; -.
GeneCards; PSIP1; -.
HGNC; HGNC:9527; PSIP1.
HPA; CAB013718; -.
HPA; HPA019697; -.
MIM; 603620; gene.
neXtProt; NX_O75475; -.
OpenTargets; ENSG00000164985; -.
PharmGKB; PA33872; -.
eggNOG; KOG1904; Eukaryota.
eggNOG; ENOG410Y5WD; LUCA.
GeneTree; ENSGT00530000063013; -.
HOVERGEN; HBG108300; -.
InParanoid; O75475; -.
OMA; GNLELWK; -.
OrthoDB; EOG091G045X; -.
PhylomeDB; O75475; -.
TreeFam; TF105385; -.
Reactome; R-HSA-162592; Integration of provirus.
Reactome; R-HSA-164843; 2-LTR circle formation.
Reactome; R-HSA-175567; Integration of viral DNA into host genomic DNA.
Reactome; R-HSA-177539; Autointegration results in viral DNA circles.
Reactome; R-HSA-180689; APOBEC3G mediated resistance to HIV-1 infection.
Reactome; R-HSA-180910; Vpr-mediated nuclear import of PICs.
SIGNOR; O75475; -.
ChiTaRS; PSIP1; human.
EvolutionaryTrace; O75475; -.
GeneWiki; PSIP1; -.
GenomeRNAi; 11168; -.
PMAP-CutDB; O75475; -.
PRO; PR:O75475; -.
Proteomes; UP000005640; Chromosome 9.
Bgee; ENSG00000164985; -.
CleanEx; HS_PSIP1; -.
ExpressionAtlas; O75475; baseline and differential.
Genevisible; O75475; HS.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005720; C:nuclear heterochromatin; IDA:UniProtKB.
GO; GO:0034399; C:nuclear periphery; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0035327; C:transcriptionally active chromatin; ISS:UniProtKB.
GO; GO:0033613; F:activating transcription factor binding; IDA:UniProtKB.
GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
GO; GO:0001105; F:RNA polymerase II transcription coactivator activity; IDA:UniProtKB.
GO; GO:0097100; F:supercoiled DNA binding; ISS:UniProtKB.
GO; GO:0075713; P:establishment of integrated proviral latency; TAS:Reactome.
GO; GO:0000395; P:mRNA 5'-splice site recognition; IDA:UniProtKB.
GO; GO:0051169; P:nuclear transport; TAS:Reactome.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:UniProtKB.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0009408; P:response to heat; ISS:UniProtKB.
GO; GO:0006979; P:response to oxidative stress; ISS:UniProtKB.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
CDD; cd05834; HDGF_related; 1.
InterPro; IPR035496; HDGF-rel_PWWP.
InterPro; IPR036218; HIVI-bd_sf.
InterPro; IPR021567; LEDGF_IBD.
InterPro; IPR000313; PWWP_dom.
InterPro; IPR017859; Treacle-like_TCS.
Pfam; PF11467; LEDGF; 1.
Pfam; PF00855; PWWP; 1.
PRINTS; PR01503; TREACLE.
SMART; SM00293; PWWP; 1.
SUPFAM; SSF140576; SSF140576; 1.
PROSITE; PS50812; PWWP; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Chromosomal rearrangement;
Citrullination; Coiled coil; Complete proteome;
Direct protein sequencing; DNA-binding; Host-virus interaction;
Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome;
Transcription; Transcription regulation; Ubl conjugation.
CHAIN 1 530 PC4 and SFRS1-interacting protein.
/FTId=PRO_0000191708.
DOMAIN 1 64 PWWP. {ECO:0000255|PROSITE-
ProRule:PRU00162}.
COILED 306 334 {ECO:0000255}.
COILED 371 395 {ECO:0000255}.
MOTIF 146 156 Nuclear localization signal.
{ECO:0000269|PubMed:15797927}.
MOD_RES 102 102 Phosphoserine.
{ECO:0000250|UniProtKB:Q812D1}.
MOD_RES 105 105 Phosphoserine.
{ECO:0000250|UniProtKB:Q99JF8}.
MOD_RES 106 106 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 115 115 Phosphothreonine.
{ECO:0000250|UniProtKB:Q99JF8}.
MOD_RES 122 122 Phosphothreonine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 129 129 Phosphoserine.
{ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 141 141 Phosphothreonine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692}.
MOD_RES 167 167 Phosphothreonine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 177 177 Phosphoserine.
{ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:21406692}.
MOD_RES 206 206 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692}.
MOD_RES 271 271 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 272 272 Phosphothreonine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 273 273 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 275 275 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 434 434 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 437 437 Phosphothreonine.
{ECO:0000244|PubMed:17525332}.
MOD_RES 443 443 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 514 514 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 517 517 Citrulline. {ECO:0000250}.
MOD_RES 522 522 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 527 527 Phosphothreonine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692}.
CROSSLNK 75 75 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
VAR_SEQ 326 530 QQNKDEGKKPEVKKVEKKRETSMDSRLQRIHAEIKNSLKID
NLDVNRCIEALDELASLQVTMQQAQKHTEMITTLKKIRRFK
VSQVIMEKSTMLYNKFKNMFLVGEGDSVITQVLNKSLAEQR
QHEEANKTKDQGKKGPNKKLEKEQTGSKTLNGGSDAQDGNQ
PQHNGESNEDSKDNHEASTKKKPSSEERETEISLKDSTLDN
-> HFAL (in isoform 3).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_044435.
VAR_SEQ 326 333 QQNKDEGK -> HQTTCNLQ (in isoform 2).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:9822615}.
/FTId=VSP_014297.
VAR_SEQ 334 530 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:9822615}.
/FTId=VSP_014298.
MUTAGEN 360 360 K->A: Reduced interaction with POGZ,
CDCA7L and human HIV-1 integrase.
{ECO:0000269|PubMed:19244240}.
MUTAGEN 365 365 I->A: Loss of interaction with human HIV-
1 integrase; reduced interaction with
POGZ and CDCA7L.
{ECO:0000269|PubMed:15895093,
ECO:0000269|PubMed:19244240}.
MUTAGEN 366 366 D->A,N: Loss of interaction with human
HIV-1 integrase; no effect on interaction
with CDCA7L.
{ECO:0000269|PubMed:15895093,
ECO:0000269|PubMed:19244240}.
MUTAGEN 366 366 D->A: No effect on interaction with POGZ.
{ECO:0000269|PubMed:15895093,
ECO:0000269|PubMed:19244240}.
MUTAGEN 370 370 V->A: Reduced interaction with POGZ,
CDCA7L and human HIV-1 integrase.
{ECO:0000269|PubMed:19244240}.
MUTAGEN 406 406 F->A: Loss of interaction with human HIV-
1 integrase and POGZ; reduced interaction
with CDCA7L.
{ECO:0000269|PubMed:15895093,
ECO:0000269|PubMed:19244240}.
MUTAGEN 408 408 V->A: Reduced interaction with human HIV-
1 integrase; no effect on interaction
with POGZ and CDCA7L.
{ECO:0000269|PubMed:15895093,
ECO:0000269|PubMed:19244240}.
CONFLICT 153 161 Missing (in Ref. 7; AAH64135).
{ECO:0000305}.
CONFLICT 224 224 E -> G (in Ref. 1; AAC97946/AAC97945).
{ECO:0000305}.
CONFLICT 272 272 T -> P (in Ref. 8; AAB52589).
{ECO:0000305}.
CONFLICT 420 420 Y -> F (in Ref. 1; AAC97946 and 8;
AAB52589). {ECO:0000305}.
HELIX 2 4 {ECO:0000244|PDB:4FU6}.
STRAND 10 13 {ECO:0000244|PDB:4FU6}.
STRAND 21 25 {ECO:0000244|PDB:4FU6}.
STRAND 30 33 {ECO:0000244|PDB:2M16}.
STRAND 40 44 {ECO:0000244|PDB:4FU6}.
TURN 45 47 {ECO:0000244|PDB:4FU6}.
STRAND 50 53 {ECO:0000244|PDB:4FU6}.
HELIX 55 57 {ECO:0000244|PDB:4FU6}.
STRAND 58 60 {ECO:0000244|PDB:4FU6}.
HELIX 61 68 {ECO:0000244|PDB:4FU6}.
HELIX 77 86 {ECO:0000244|PDB:4FU6}.
HELIX 347 362 {ECO:0000244|PDB:2B4J}.
HELIX 365 367 {ECO:0000244|PDB:3HPH}.
HELIX 370 381 {ECO:0000244|PDB:2B4J}.
HELIX 387 391 {ECO:0000244|PDB:2B4J}.
HELIX 394 403 {ECO:0000244|PDB:2B4J}.
HELIX 410 425 {ECO:0000244|PDB:2B4J}.
SEQUENCE 530 AA; 60103 MW; 4B653D02B1D0E174 CRC64;
MTRDFKPGDL IFAKMKGYPH WPARVDEVPD GAVKPPTNKL PIFFFGTHET AFLGPKDIFP
YSENKEKYGK PNKRKGFNEG LWEIDNNPKV KFSSQQAATK QSNASSDVEV EEKETSVSKE
DTDHEEKASN EDVTKAVDIT TPKAARRGRK RKAEKQVETE EAGVVTTATA SVNLKVSPKR
GRPAATEVKI PKPRGRPKMV KQPCPSESDI ITEEDKSKKK GQEEKQPKKQ PKKDEEGQKE
EDKPRKEPDK KEGKKEVESK RKNLAKTGVT STSDSEEEGD DQEGEKKRKG GRNFQTAHRR
NMLKGQHEKE AADRKRKQEE QMETEQQNKD EGKKPEVKKV EKKRETSMDS RLQRIHAEIK
NSLKIDNLDV NRCIEALDEL ASLQVTMQQA QKHTEMITTL KKIRRFKVSQ VIMEKSTMLY
NKFKNMFLVG EGDSVITQVL NKSLAEQRQH EEANKTKDQG KKGPNKKLEK EQTGSKTLNG
GSDAQDGNQP QHNGESNEDS KDNHEASTKK KPSSEERETE ISLKDSTLDN


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