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

High mobility group protein HMG-I/HMG-Y (HMG-I(Y)) (High mobility group AT-hook protein 1) (High mobility group protein A1) (High mobility group protein R)

 HMGA1_HUMAN             Reviewed;         107 AA.
P17096; P10910; Q5T6U9; Q9UKB0;
01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
25-OCT-2017, entry version 203.
RecName: Full=High mobility group protein HMG-I/HMG-Y;
Short=HMG-I(Y);
AltName: Full=High mobility group AT-hook protein 1;
Short=High mobility group protein A1;
AltName: Full=High mobility group protein R;
Name=HMGA1; Synonyms=HMGIY;
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 HMG-I AND HMG-Y).
PubMed=2505228; DOI=10.1093/nar/17.15.5947;
Eckner R., Birnstiel M.L.;
"Cloning of cDNAs coding for human HMG I and HMG Y proteins: both are
capable of binding to the octamer sequence motif.";
Nucleic Acids Res. 17:5947-5959(1989).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS HMG-I AND HMG-Y).
PubMed=2701943; DOI=10.1128/MCB.9.5.2114;
Johnson K.R., Lehn D.A., Reeves R.;
"Alternative processing of mRNAs encoding mammalian chromosomal high-
mobility-group proteins HMG-I and HMG-Y.";
Mol. Cell. Biol. 9:2114-2123(1989).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
TISSUE=Placenta;
PubMed=8414980; DOI=10.1093/nar/21.18.4259;
Friedmann M., Holth L.T., Zoghbi H.Y., Reeves R.;
"Organization, inducible-expression and chromosome localization of the
human HMG-I(Y) nonhistone protein gene.";
Nucleic Acids Res. 21:4259-4267(1993).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM HMG-R).
PubMed=10428834; DOI=10.1074/jbc.274.32.22563;
Nagpal S., Ghosn C., DiSepio D., Molina Y., Sutter M., Klein E.S.,
Chandraratna R.A.S.;
"Retinoid-dependent recruitment of a histone H1 displacement activity
by retinoic acid receptor.";
J. Biol. Chem. 274:22563-22568(1999).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=14574404; DOI=10.1038/nature02055;
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
"The DNA sequence and analysis of human chromosome 6.";
Nature 425:805-811(2003).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS HMG-I AND HMG-Y).
TISSUE=B-cell, Mammary gland, Muscle, Pancreas, 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]
PROTEIN SEQUENCE OF 4-107 (HMG-I).
PubMed=3619901; DOI=10.1016/0006-291X(87)90589-4;
Lund T., Dahl K.H., Mork E., Holtlund J., Laland S.G.;
"The human chromosomal protein HMG I contains two identical palindrome
amino acid sequences.";
Biochem. Biophys. Res. Commun. 146:725-730(1987).
[8]
PROTEIN SEQUENCE OF 4-107 (HMG-Y).
PubMed=2920035; DOI=10.1016/0006-291X(89)92770-8;
Karlson J.R., Mork E., Holtlund J., Laland S.G., Lund T.;
"The amino acid sequence of the chromosomal protein HMG-Y, its
relation to HMG-I and possible domains for the preferential binding of
the proteins to stretches of A-T base pairs.";
Biochem. Biophys. Res. Commun. 158:646-651(1989).
[9]
DNA-BINDING DOMAINS.
PubMed=1692833;
Reeves R., Nissen M.S.;
"The A.T-DNA-binding domain of mammalian high mobility group I
chromosomal proteins. A novel peptide motif for recognizing DNA
structure.";
J. Biol. Chem. 265:8573-8582(1990).
[10]
CHROMOSOMAL TRANSLOCATION WITH RAD51B.
PubMed=11978964;
Blank C., Schoenmakers E.F.P.M., Rogalla P., Huys E.H., van Rijk A.A.,
Drieschner N., Bullerdiek J.;
"Intragenic breakpoint within RAD51L1 in a t(6;14)(p21.3;q24) of a
pulmonary chondroid hamartoma.";
Cytogenet. Cell Genet. 95:17-19(2001).
[11]
PHOSPHORYLATION, METHYLATION AT ARG-26, AND IDENTIFICATION BY MASS
SPECTROMETRY.
PubMed=12653562; DOI=10.1021/bi027338l;
Sgarra R., Diana F., Bellarosa C., Dekleva V., Rustighi A., Toller M.,
Manfioletti G., Giancotti V.;
"During apoptosis of tumor cells HMGA1a protein undergoes methylation:
identification of the modification site by mass spectrometry.";
Biochemistry 42:3575-3585(2003).
[12]
METHYLATION BY PRMT6.
PubMed=16157300; DOI=10.1016/j.bbrc.2005.08.179;
Miranda T.B., Webb K.J., Edberg D.D., Reeves R., Clarke S.;
"Protein arginine methyltransferase 6 specifically methylates the
nonhistone chromatin protein HMGA1a.";
Biochem. Biophys. Res. Commun. 336:831-835(2005).
[13]
PHOSPHORYLATION AT SER-99; SER-102 AND SER-103, METHYLATION AT ARG-26,
AND MASS SPECTROMETRY.
PubMed=15835918; DOI=10.1021/bi0475525;
Zou Y., Wang Y.;
"Tandem mass spectrometry for the examination of the posttranslational
modifications of high-mobility group A1 proteins: symmetric and
asymmetric dimethylation of Arg25 in HMGA1a protein.";
Biochemistry 44:6293-6301(2005).
[14]
METHYLATION AT ARG-58 AND ARG-60 BY PRMT6, AND MUTAGENESIS OF ARG-26;
ARG-58 AND ARG-60.
PubMed=16159886; DOI=10.1074/jbc.M502458200;
Herrmann F., Lee J., Bedford M.T., Fackelmayer F.O.;
"Dynamics of human protein arginine methyltransferase 1(PRMT1) in
vivo.";
J. Biol. Chem. 280:38005-38010(2005).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36; SER-99; SER-102 AND
SER-103, 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 SER-36 AND THR-53,
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-42 (ISOFORM HMG-Y), AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17924679; DOI=10.1021/pr070152u;
Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
"Improved titanium dioxide enrichment of phosphopeptides from HeLa
cells and high confident phosphopeptide identification by cross-
validation of MS/MS and MS/MS/MS spectra.";
J. Proteome Res. 6:4150-4162(2007).
[17]
PHOSPHORYLATION AT SER-36; THR-53 AND THR-78 BY HIPK2 AND CDK1/CDC2
(ISOFORM HMG-I), AND PHOSPHORYLATION AT THR-42 AND THR-67 BY HIPK2 AND
CDK1/CDC2 (ISOFORM HMG-Y).
PubMed=17960875; DOI=10.1021/pr700571d;
Zhang Q., Wang Y.;
"Homeodomain-interacting protein kinase-2 (HIPK2) phosphorylates
HMGA1a at Ser-35, Thr-52, and Thr-77 and modulates its DNA binding
affinity.";
J. Proteome Res. 6:4711-4719(2007).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-99; SER-102 AND SER-103,
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).
[19]
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).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36; THR-39; SER-44;
SER-49 AND THR-53, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[21]
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).
[22]
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).
[23]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-99; SER-102 AND SER-103,
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).
[24]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-15, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[25]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36; THR-53; SER-99;
SER-102 AND SER-103, 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).
[26]
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).
[27]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36; THR-53; SER-99 AND
SER-102, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-42 (ISOFORM
HMG-Y), 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).
[28]
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).
[29]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9; SER-36; SER-44;
THR-53; SER-99; SER-102 AND SER-103, 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).
[30]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36; THR-39; SER-44 AND
SER-49, 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).
[31]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[32]
ADP-RIBOSYLATION AT SER-8 AND SER-9.
PubMed=28190768; DOI=10.1016/j.molcel.2017.01.003;
Bonfiglio J.J., Fontana P., Zhang Q., Colby T., Gibbs-Seymour I.,
Atanassov I., Bartlett E., Zaja R., Ahel I., Matic I.;
"Serine ADP-ribosylation depends on HPF1.";
Mol. Cell 0:0-0(2017).
[33]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-15, 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).
[34]
STRUCTURE BY NMR OF 51-75 AND 80-89.
PubMed=9253416; DOI=10.1038/nsb0897-657;
Huth J.R., Bewley C.A., Nissen M.S., Evans J.N., Reeves R.,
Gronenborn A.M., Clore G.M.;
"The solution structure of an HMG-I(Y)-DNA complex defines a new
architectural minor groove binding motif.";
Nat. Struct. Biol. 4:657-665(1997).
-!- FUNCTION: HMG-I/Y bind preferentially to the minor groove of A+T
rich regions in double-stranded DNA. It is suggested that these
proteins could function in nucleosome phasing and in the 3'-end
processing of mRNA transcripts. They are also involved in the
transcription regulation of genes containing, or in close
proximity to A+T-rich regions.
-!- SUBUNIT: Interacts with HIPK2 (By similarity). Interacts with HIV-
1 pre-integration complex. {ECO:0000250}.
-!- INTERACTION:
Q9Y5N6:ORC6; NbExp=4; IntAct=EBI-746843, EBI-374840;
Q96LA8:PRMT6; NbExp=4; IntAct=EBI-746854, EBI-912440;
-!- SUBCELLULAR LOCATION: Nucleus. Chromosome.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=HMG-I; Synonyms=HMGA1a;
IsoId=P17096-1; Sequence=Displayed;
Name=HMG-Y; Synonyms=HMGA1b;
IsoId=P17096-2; Sequence=VSP_002182;
Note=Contains a phosphothreonine at position 67. Contains a
phosphothreonine at position 42. {ECO:0000244|PubMed:17924679,
ECO:0000244|PubMed:21406692};
Name=HMG-R; Synonyms=HMGA1c;
IsoId=P17096-3; Sequence=VSP_018084;
-!- PTM: Constitutively phosphorylated on two or three sites.
Hyperphosphorylated at early stages of apoptosis, followed by
dephosphorylation and methylation, which coincides with chromatin
condensation. Isoforms HMG-I and HMG-Y can be phosphorylated by
HIPK2. Phosphorylation of HMG-I at Ser-36, Thr-53 and Thr-78 and
of HMG-Y at Thr-42 and Thr-67 by HIPK2 modulates DNA-binding
affinity. {ECO:0000269|PubMed:12653562,
ECO:0000269|PubMed:15835918}.
-!- PTM: HMG-Y is not methylated.
-!- PTM: Methylation at Arg-58 is mutually exclusive with methylation
at Arg-60. {ECO:0000269|PubMed:16159886}.
-!- MASS SPECTROMETRY: Mass=11750; Mass_error=12; Method=MALDI;
Range=2-107 (P17096-1); Note=With 1 acetyl and 2 phosphate
groups.; Evidence={ECO:0000269|PubMed:15835918};
-!- MASS SPECTROMETRY: Mass=11828; Mass_error=12; Method=MALDI;
Range=2-107 (P17096-1); Note=With 1 acetyl and 3 phosphate
groups.; Evidence={ECO:0000269|PubMed:15835918};
-!- MASS SPECTROMETRY: Mass=11765; Mass_error=12; Method=MALDI;
Range=2-107 (P17096-1); Note=With 1 acetyl, 1 methyl and 2
phosphate groups.; Evidence={ECO:0000269|PubMed:15835918};
-!- MASS SPECTROMETRY: Mass=11844; Mass_error=12; Method=MALDI;
Range=2-107 (P17096-1); Note=With 1 acetyl, 1 methyl and 3
phosphate groups.; Evidence={ECO:0000269|PubMed:15835918};
-!- MASS SPECTROMETRY: Mass=11780; Mass_error=12; Method=MALDI;
Range=2-107 (P17096-1); Note=With 1 acetyl, 2 methyl and 2
phosphate groups.; Evidence={ECO:0000269|PubMed:15835918};
-!- MASS SPECTROMETRY: Mass=11858; Mass_error=12; Method=MALDI;
Range=2-107 (P17096-1); Note=With 1 acetyl, 2 methyl and 3
phosphate groups.; Evidence={ECO:0000269|PubMed:15835918};
-!- DISEASE: Note=A chromosomal aberration involving HMGA1 is found in
pulmonary chondroid hamartoma. Translocation t(6;14)(p21;q23-24)
with RAD51B. {ECO:0000269|PubMed:11978964}.
-!- SIMILARITY: Belongs to the HMGA family. {ECO:0000305}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/HMGIYID221.html";
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; X14957; CAA33080.1; -; mRNA.
EMBL; X14958; CAA33081.1; -; mRNA.
EMBL; M23614; AAA88072.1; -; mRNA.
EMBL; M23615; AAA88073.1; -; mRNA.
EMBL; M23616; AAA88074.1; -; mRNA.
EMBL; M23617; AAA88075.1; -; mRNA.
EMBL; M23618; AAA88076.1; -; mRNA.
EMBL; M23619; AAA35998.1; -; mRNA.
EMBL; L17131; AAB00145.1; -; Genomic_DNA.
EMBL; AF176039; AAD53889.1; -; mRNA.
EMBL; AL354740; CAI14991.1; -; Genomic_DNA.
EMBL; BC004924; AAH04924.1; -; mRNA.
EMBL; BC008832; AAH08832.1; -; mRNA.
EMBL; BC063434; AAH63434.1; -; mRNA.
EMBL; BC067083; AAH67083.1; -; mRNA.
EMBL; BC071864; AAH71864.1; -; mRNA.
CCDS; CCDS4788.1; -. [P17096-2]
CCDS; CCDS4789.1; -. [P17096-1]
PIR; A32794; A32794.
RefSeq; NP_001306006.1; NM_001319077.1. [P17096-2]
RefSeq; NP_001306007.1; NM_001319078.1. [P17096-1]
RefSeq; NP_001306008.1; NM_001319079.1. [P17096-1]
RefSeq; NP_001306009.1; NM_001319080.1.
RefSeq; NP_001306010.1; NM_001319081.1. [P17096-1]
RefSeq; NP_001306011.1; NM_001319082.1. [P17096-1]
RefSeq; NP_002122.1; NM_002131.3. [P17096-2]
RefSeq; NP_665906.1; NM_145899.2. [P17096-1]
RefSeq; NP_665908.1; NM_145901.2. [P17096-1]
RefSeq; NP_665909.1; NM_145902.2. [P17096-2]
RefSeq; NP_665910.1; NM_145903.2. [P17096-2]
RefSeq; NP_665912.1; NM_145905.2. [P17096-2]
UniGene; Hs.518805; -.
UniGene; Hs.696527; -.
UniGene; Hs.703764; -.
PDB; 2EZD; NMR; -; A=51-71.
PDB; 2EZE; NMR; -; A=51-75.
PDB; 2EZF; NMR; -; A=80-89.
PDB; 2EZG; NMR; -; A=80-89.
PDBsum; 2EZD; -.
PDBsum; 2EZE; -.
PDBsum; 2EZF; -.
PDBsum; 2EZG; -.
DisProt; DP00040; -.
ProteinModelPortal; P17096; -.
SMR; P17096; -.
BioGrid; 109402; 107.
DIP; DIP-29687N; -.
IntAct; P17096; 54.
MINT; MINT-262941; -.
STRING; 9606.ENSP00000308227; -.
iPTMnet; P17096; -.
PhosphoSitePlus; P17096; -.
BioMuta; HMGA1; -.
DMDM; 123377; -.
EPD; P17096; -.
MaxQB; P17096; -.
PaxDb; P17096; -.
PeptideAtlas; P17096; -.
PRIDE; P17096; -.
TopDownProteomics; P17096-1; -. [P17096-1]
TopDownProteomics; P17096-2; -. [P17096-2]
TopDownProteomics; P17096-3; -. [P17096-3]
DNASU; 3159; -.
Ensembl; ENST00000311487; ENSP00000308227; ENSG00000137309. [P17096-1]
Ensembl; ENST00000347617; ENSP00000288245; ENSG00000137309. [P17096-2]
Ensembl; ENST00000374116; ENSP00000363230; ENSG00000137309. [P17096-2]
Ensembl; ENST00000401473; ENSP00000385693; ENSG00000137309. [P17096-2]
Ensembl; ENST00000447654; ENSP00000399888; ENSG00000137309. [P17096-1]
GeneID; 3159; -.
KEGG; hsa:3159; -.
UCSC; uc003oit.4; human. [P17096-1]
CTD; 3159; -.
DisGeNET; 3159; -.
EuPathDB; HostDB:ENSG00000137309.19; -.
GeneCards; HMGA1; -.
HGNC; HGNC:5010; HMGA1.
HPA; CAB032200; -.
MalaCards; HMGA1; -.
MIM; 600701; gene.
neXtProt; NX_P17096; -.
OpenTargets; ENSG00000137309; -.
PharmGKB; PA35094; -.
eggNOG; ENOG410J4ZT; Eukaryota.
eggNOG; ENOG410Z566; LUCA.
GeneTree; ENSGT00730000111329; -.
HOGENOM; HOG000076308; -.
HOVERGEN; HBG063451; -.
InParanoid; P17096; -.
KO; K09282; -.
OMA; NMSDKGT; -.
TreeFam; TF351623; -.
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.
Reactome; R-HSA-2559584; Formation of Senescence-Associated Heterochromatin Foci (SAHF).
SignaLink; P17096; -.
SIGNOR; P17096; -.
ChiTaRS; HMGA1; human.
GeneWiki; HMGA1; -.
GenomeRNAi; 3159; -.
PRO; PR:P17096; -.
Proteomes; UP000005640; Chromosome 6.
Bgee; ENSG00000137309; -.
CleanEx; HS_HMGA1; -.
ExpressionAtlas; P17096; baseline and differential.
Genevisible; P17096; HS.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005925; C:focal adhesion; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0090575; C:RNA polymerase II transcription factor complex; ISS:BHF-UCL.
GO; GO:0035985; C:senescence-associated heterochromatin focus; IDA:UniProtKB.
GO; GO:0005667; C:transcription factor complex; TAS:UniProtKB.
GO; GO:0051575; F:5'-deoxyribose-5-phosphate lyase activity; IDA:UniProtKB.
GO; GO:0003680; F:AT DNA binding; IDA:CAFA.
GO; GO:0003682; F:chromatin binding; ISS:BHF-UCL.
GO; GO:0003677; F:DNA binding; TAS:ProtInc.
GO; GO:0003906; F:DNA-(apurinic or apyrimidinic site) lyase activity; IDA:UniProtKB.
GO; GO:0001158; F:enhancer sequence-specific DNA binding; IDA:CAFA.
GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
GO; GO:0030374; F:ligand-dependent nuclear receptor transcription coactivator activity; IMP:UniProtKB.
GO; GO:0042975; F:peroxisome proliferator activated receptor binding; IDA:UniProtKB.
GO; GO:0042974; F:retinoic acid receptor binding; IDA:UniProtKB.
GO; GO:0046965; F:retinoid X receptor binding; IDA:UniProtKB.
GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IBA:GO_Central.
GO; GO:0008134; F:transcription factor binding; IDA:UniProtKB.
GO; GO:0001205; F:transcriptional activator activity, RNA polymerase II distal enhancer sequence-specific binding; ISS:BHF-UCL.
GO; GO:0006284; P:base-excision repair; IDA:UniProtKB.
GO; GO:0006268; P:DNA unwinding involved in DNA replication; NAS:UniProtKB.
GO; GO:0075713; P:establishment of integrated proviral latency; TAS:Reactome.
GO; GO:0008285; P:negative regulation of cell proliferation; IMP:UniProtKB.
GO; GO:0031936; P:negative regulation of chromatin silencing; TAS:UniProtKB.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IMP:UniProtKB.
GO; GO:0051169; P:nuclear transport; TAS:Reactome.
GO; GO:0006337; P:nucleosome disassembly; TAS:UniProtKB.
GO; GO:0090402; P:oncogene-induced cell senescence; IDA:UniProtKB.
GO; GO:2000774; P:positive regulation of cellular senescence; IMP:UniProtKB.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; ISS:BHF-UCL.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:UniProtKB.
GO; GO:0006461; P:protein complex assembly; TAS:UniProtKB.
GO; GO:0006355; P:regulation of transcription, DNA-templated; TAS:ProtInc.
GO; GO:0009615; P:response to virus; IEP:UniProtKB.
GO; GO:0035986; P:senescence-associated heterochromatin focus assembly; IDA:UniProtKB.
InterPro; IPR017956; AT_hook_DNA-bd_motif.
InterPro; IPR000116; HMGA.
InterPro; IPR031079; HMGA1_mammal.
InterPro; IPR000637; HMGI/Y_DNA-bd_CS.
PANTHER; PTHR23341:SF1; PTHR23341:SF1; 1.
PRINTS; PR00929; ATHOOK.
PRINTS; PR00930; HIGHMOBLTYIY.
SMART; SM00384; AT_hook; 3.
PROSITE; PS00354; HMGI_Y; 3.
1: Evidence at protein level;
3D-structure; Acetylation; ADP-ribosylation; Alternative splicing;
Chromosomal rearrangement; Chromosome; Complete proteome;
Direct protein sequencing; DNA-binding; Host-virus interaction;
Isopeptide bond; Methylation; Nucleus; Phosphoprotein;
Reference proteome; Repeat; Transcription; Transcription regulation;
Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:P17095}.
CHAIN 2 107 High mobility group protein HMG-I/HMG-Y.
/FTId=PRO_0000206708.
DNA_BIND 21 31 A.T hook 1.
DNA_BIND 53 63 A.T hook 2.
DNA_BIND 78 89 A.T hook 3.
REGION 53 77 Interaction with HIPK2. {ECO:0000250}.
COMPBIAS 91 106 Glu-rich (acidic).
MOD_RES 2 2 N-acetylserine.
{ECO:0000250|UniProtKB:P17095}.
MOD_RES 7 7 N6-acetyllysine.
{ECO:0000250|UniProtKB:P17095}.
MOD_RES 8 8 ADP-ribosylserine.
{ECO:0000269|PubMed:28190768}.
MOD_RES 9 9 ADP-ribosylserine; alternate.
{ECO:0000269|PubMed:28190768}.
MOD_RES 9 9 Phosphoserine; alternate.
{ECO:0000244|PubMed:23186163}.
MOD_RES 15 15 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:19608861}.
MOD_RES 26 26 Asymmetric dimethylarginine; alternate.
{ECO:0000269|PubMed:12653562,
ECO:0000269|PubMed:15835918}.
MOD_RES 26 26 Omega-N-methylarginine; alternate.
{ECO:0000269|PubMed:12653562,
ECO:0000269|PubMed:15835918}.
MOD_RES 26 26 Symmetric dimethylarginine; alternate.
{ECO:0000269|PubMed:12653562,
ECO:0000269|PubMed:15835918}.
MOD_RES 36 36 Phosphoserine; by HIPK2 and CDC2.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:17924679,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 39 39 Phosphothreonine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:24275569}.
MOD_RES 44 44 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 49 49 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:24275569}.
MOD_RES 53 53 Phosphothreonine; by HIPK2 and CDC2.
{ECO:0000244|PubMed:17924679,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 58 58 Asymmetric dimethylarginine; by PRMT6;
alternate. {ECO:0000269|PubMed:16159886}.
MOD_RES 58 58 Omega-N-methylarginine; by PRMT6;
alternate. {ECO:0000269|PubMed:16159886}.
MOD_RES 60 60 Asymmetric dimethylarginine; by PRMT6;
alternate. {ECO:0000269|PubMed:16159886}.
MOD_RES 60 60 Omega-N-methylarginine; by PRMT6;
alternate. {ECO:0000269|PubMed:16159886}.
MOD_RES 78 78 Phosphothreonine; by HIPK2 and CDC2.
{ECO:0000269|PubMed:12653562}.
MOD_RES 99 99 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:17525332,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:15835918}.
MOD_RES 102 102 Phosphoserine; by CK.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:17525332,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:15835918}.
MOD_RES 103 103 Phosphoserine; by CK.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:17525332,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:15835918}.
CROSSLNK 15 15 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate. {ECO:0000244|PubMed:28112733}.
VAR_SEQ 35 45 Missing (in isoform HMG-Y).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:2505228,
ECO:0000303|PubMed:2701943}.
/FTId=VSP_002182.
VAR_SEQ 66 107 NKGAAKTRKTTTTPGRKPRGRPKKLEKEEEEGISQESSEEE
Q -> KNWRRRKRRASRRSPRRRSSDPCVPPAPHWRSSFLL
GLDSFAPLPPPPPLPQAHHHHRLWPPPPSSTCALTTTLHST
PAAAGLPWAEWGAVFPWPQFPAPPAHPRIHTCPPGQG (in
isoform HMG-R).
{ECO:0000303|PubMed:10428834}.
/FTId=VSP_018084.
MUTAGEN 26 26 R->A: Does not affect methylation by
PRMT6. {ECO:0000269|PubMed:16159886}.
MUTAGEN 58 58 R->A: Decreases methylation by PRMT6.
Abolishes methylation by PRMT6; when
associated with A-60.
{ECO:0000269|PubMed:16159886}.
MUTAGEN 60 60 R->A: Decreases methylation by PRMT6.
Abolishes methylation by PRMT6; when
associated with A-58.
{ECO:0000269|PubMed:16159886}.
CONFLICT 107 107 Q -> QQQ (in Ref. 8; AA sequence).
{ECO:0000305}.
STRAND 53 55 {ECO:0000244|PDB:2EZE}.
SEQUENCE 107 AA; 11676 MW; E9C4E3F2200914B8 CRC64;
MSESSSKSSQ PLASKQEKDG TEKRGRGRPR KQPPVSPGTA LVGSQKEPSE VPTPKRPRGR
PKGSKNKGAA KTRKTTTTPG RKPRGRPKKL EKEEEEGISQ ESSEEEQ


Related products :

Catalog number Product name Quantity
18-003-43339 High mobility group protein HMGI-C - High mobility group AT-hook protein 2 Polyclonal 0.1 mg Protein A
E0399r ELISA kit Amphoterin,Heparin-binding protein p30,High mobility group protein 1,High mobility group protein B1,Hmg1,HMG-1,Hmg-1,Hmgb1,Rat,Rattus norvegicus 96T
U0399r CLIA Amphoterin,Heparin-binding protein p30,High mobility group protein 1,High mobility group protein B1,Hmg1,HMG-1,Hmg-1,Hmgb1,Rat,Rattus norvegicus 96T
E0399r ELISA Amphoterin,Heparin-binding protein p30,High mobility group protein 1,High mobility group protein B1,Hmg1,HMG-1,Hmg-1,Hmgb1,Rat,Rattus norvegicus 96T
EIAAB43466 Homo sapiens,Human,KIAA0808,Thymocyte selection-associated high mobility group box protein TOX,Thymus high mobility group box protein TOX,TOX
E0399h ELISA kit High mobility group protein 1,High mobility group protein B1,HMG1,HMG-1,HMGB1,Homo sapiens,Human 96T
U0399h CLIA High mobility group protein 1,High mobility group protein B1,HMG1,HMG-1,HMGB1,Homo sapiens,Human 96T
E0399h ELISA High mobility group protein 1,High mobility group protein B1,HMG1,HMG-1,HMGB1,Homo sapiens,Human 96T
E0399m ELISA kit High mobility group protein 1,High mobility group protein B1,Hmg1,HMG-1,Hmg-1,Hmgb1,Mouse,Mus musculus 96T
U0399m CLIA High mobility group protein 1,High mobility group protein B1,Hmg1,HMG-1,Hmg-1,Hmgb1,Mouse,Mus musculus 96T
E0399m ELISA High mobility group protein 1,High mobility group protein B1,Hmg1,HMG-1,Hmg-1,Hmgb1,Mouse,Mus musculus 96T
E0399b ELISA kit Bos taurus,Bovine,High mobility group protein 1,High mobility group protein B1,HMG1,HMG-1,HMGB1 96T
U0399b CLIA Bos taurus,Bovine,High mobility group protein 1,High mobility group protein B1,HMG1,HMG-1,HMGB1 96T
EIAAB43465 Mouse,Mus musculus,Thymocyte selection-associated high mobility group box protein TOX,Thymus high mobility group box protein TOX,Tox
E0399b ELISA Bos taurus,Bovine,High mobility group protein 1,High mobility group protein B1,HMG1,HMG-1,HMGB1 96T
U0399p CLIA High mobility group protein 1,High mobility group protein B1,HMG1,HMG-1,HMGB1,Pig,Sus scrofa 96T
E0399p ELISA High mobility group protein 1,High mobility group protein B1,HMG1,HMG-1,HMGB1,Pig,Sus scrofa 96T
E0399p ELISA kit High mobility group protein 1,High mobility group protein B1,HMG1,HMG-1,HMGB1,Pig,Sus scrofa 96T
orb82706 Human HMG His tag protein Human High-mobility group box 1 protein (HMGB1), previously known as HMG-1 oramphoterin, is a member of the high mobility group box family of non-histonechromosomal proteins. 1 mg
18-003-42695 High mobility group protein B3 - High mobility group protein 4; HMG-4; High mobility group protein 2a; HMG-2a Polyclonal 0.1 mg Protein A
18-003-42696 High mobility group protein B3 - High mobility group protein 4; HMG-4; High mobility group protein 2a; HMG-2a Polyclonal 0.1 mg Protein A
126-10094 Goat Anti-High-Mobility Group Box 3 (HMGB3) + High-Mobility Group Box 4 (HMG4), with HRP-conjugated secondary antibody 100
E0399c ELISA kit Chicken,Gallus gallus,High mobility group protein 1,High mobility group protein B1,HMG1,HMG-1,HMGB1 96T
U0399c CLIA Chicken,Gallus gallus,High mobility group protein 1,High mobility group protein B1,HMG1,HMG-1,HMGB1 96T
E0399c ELISA Chicken,Gallus gallus,High mobility group protein 1,High mobility group protein B1,HMG1,HMG-1,HMGB1 96T


 

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