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Telomeric repeat-binding factor 1 (NIMA-interacting protein 2) (TTAGGG repeat-binding factor 1) (Telomeric protein Pin2/TRF1)

 TERF1_HUMAN             Reviewed;         439 AA.
P54274; A7XP29; Q15553; Q8NHT6; Q93029;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
23-SEP-2008, sequence version 3.
20-JUN-2018, entry version 206.
RecName: Full=Telomeric repeat-binding factor 1;
AltName: Full=NIMA-interacting protein 2;
AltName: Full=TTAGGG repeat-binding factor 1;
AltName: Full=Telomeric protein Pin2/TRF1;
Name=TERF1; Synonyms=PIN2, TRBF1, TRF, TRF1;
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 PARTIAL PROTEIN SEQUENCE.
TISSUE=Cervix carcinoma;
PubMed=7502076; DOI=10.1126/science.270.5242.1663;
Chong L., van Steensel B., Broccoli D., Erdjument-Bromage H.,
Hanish J., Tempst P., de Lange T.;
"A human telomeric protein.";
Science 270:1663-1667(1995).
[2]
SEQUENCE REVISION TO 14.
de Lange T.;
Submitted (MAY-1997) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
[GENOMIC DNA] OF 1-138 (ISOFORMS 1 AND 2).
PubMed=9326950; DOI=10.1038/ng1097-231;
Broccoli D., Smogorzewska A., Chong L., de Lange T.;
"Human telomeres contain two distinct Myb-related proteins, TRF1 and
TRF2.";
Nat. Genet. 17:231-235(1997).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
TISSUE=Cervix carcinoma;
PubMed=9391075; DOI=10.1073/pnas.94.25.13618;
Shen M., Haggblom C., Vogt M., Hunter T., Lu K.P.;
"Characterization and cell cycle regulation of the related human
telomeric proteins Pin2 and TRF1 suggest a role in mitosis.";
Proc. Natl. Acad. Sci. U.S.A. 94:13618-13623(1997).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
NIEHS SNPs program;
Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16421571; DOI=10.1038/nature04406;
Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S.,
Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A.,
Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X.,
Allen N.R., Anderson S., Asakawa T., Blechschmidt K., Bloom T.,
Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K.,
DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G.,
Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B.,
Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C.,
O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K.,
Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R.,
Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K.,
Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q.,
Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N.,
Lander E.S.;
"DNA sequence and analysis of human chromosome 8.";
Nature 439:331-335(2006).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Liver;
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 329-439 (ISOFORMS 1/2).
TISSUE=Cervix carcinoma;
PubMed=8614633; DOI=10.1093/nar/24.7.1294;
Bilaud T., Koering C.E., Binet-Brasselet E., Ancelin K., Pollice A.,
Gasser S.M., Gilson E.;
"The telobox, a Myb-related telomeric DNA binding motif found in
proteins from yeast, plants and human.";
Nucleic Acids Res. 24:1294-1303(1996).
[9]
MUTAGENESIS OF SER-219, PHOSPHORYLATION AT SER-219, AND INTERACTION
WITH ATM.
PubMed=11375976; DOI=10.1074/jbc.M011534200;
Kishi S., Zhou X.Z., Ziv Y., Khoo C., Hill D.E., Shiloh Y., Lu K.P.;
"Telomeric protein Pin2/TRF1 as an important ATM target in response to
double strand DNA breaks.";
J. Biol. Chem. 276:29282-29291(2001).
[10]
INTERACTION WITH MAPRE1 AND WITH THE MITOTIC SPINDLE.
PubMed=11943150; DOI=10.1016/S0014-5793(02)02363-3;
Nakamura M., Zhen Zhou X., Kishi S., Ping Lu K.;
"Involvement of the telomeric protein Pin2/TRF1 in the regulation of
the mitotic spindle.";
FEBS Lett. 514:193-198(2002).
[11]
ADP-RIBOSYLATION.
PubMed=11739745; DOI=10.1128/MCB.22.1.332-342.2002;
Cook B.D., Dynek J.N., Chang W., Shostak G., Smith S.;
"Role for the related poly(ADP-Ribose) polymerases tankyrase 1 and 2
at human telomeres.";
Mol. Cell. Biol. 22:332-342(2002).
[12]
IDENTIFICATION IN A COMPLEX WITH POT1; TINF2 AND TNKS1.
PubMed=12768206; DOI=10.1038/nature01688;
Loayza D., De Lange T.;
"POT1 as a terminal transducer of TRF1 telomere length control.";
Nature 423:1013-1018(2003).
[13]
IDENTIFICATION IN THE SHELTERIN COMPLEX.
PubMed=15316005; DOI=10.1074/jbc.M409047200;
Ye J.Z.-S., Donigian J.R., van Overbeek M., Loayza D., Luo Y.,
Krutchinsky A.N., Chait B.T., de Lange T.;
"TIN2 binds TRF1 and TRF2 simultaneously and stabilizes the TRF2
complex on telomeres.";
J. Biol. Chem. 279:47264-47271(2004).
[14]
IDENTIFICATION IN THE SHELTERIN COMPLEX.
PubMed=15383534; DOI=10.1074/jbc.M409293200;
Liu D., O'Connor M.S., Qin J., Songyang Z.;
"Telosome, a mammalian telomere-associated complex formed by multiple
telomeric proteins.";
J. Biol. Chem. 279:51338-51342(2004).
[15]
FUNCTION OF THE SHELTERIN COMPLEX.
PubMed=16166375; DOI=10.1101/gad.1346005;
de Lange T.;
"Shelterin: the protein complex that shapes and safeguards human
telomeres.";
Genes Dev. 19:2100-2110(2005).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11, 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).
[17]
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).
[18]
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).
[19]
INTERACTION WITH RLIM, SUBCELLULAR LOCATION, AND UBIQUITINATION.
PubMed=19164295; DOI=10.1074/jbc.M806702200;
Her Y.R., Chung I.K.;
"Ubiquitin ligase RLIM modulates telomere length homeostasis through a
proteolysis of TRF1.";
J. Biol. Chem. 284:8557-8566(2009).
[20]
SUBCELLULAR LOCATION.
PubMed=19487455; DOI=10.1083/jcb.200812121;
Zhu Q., Meng L., Hsu J.K., Lin T., Teishima J., Tsai R.Y.;
"GNL3L stabilizes the TRF1 complex and promotes mitotic transition.";
J. Cell Biol. 185:827-839(2009).
[21]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE
SCALE ANALYSIS] AT SER-11, 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).
[22]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11, 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).
[23]
INTERACTION WITH RTEL1.
PubMed=23959892; DOI=10.1073/pnas.1300600110;
Deng Z., Glousker G., Molczan A., Fox A.J., Lamm N., Dheekollu J.,
Weizman O.E., Schertzer M., Wang Z., Vladimirova O., Schug J.,
Aker M., Londono-Vallejo A., Kaestner K.H., Lieberman P.M., Tzfati Y.;
"Inherited mutations in the helicase RTEL1 cause telomere dysfunction
and Hoyeraal-Hreidarsson syndrome.";
Proc. Natl. Acad. Sci. U.S.A. 110:E3408-E3416(2013).
[24]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-213; LYS-325 AND LYS-366,
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).
[25]
STRUCTURE BY NMR OF 378-430.
PubMed=9739097; DOI=10.1016/S0969-2126(98)00106-3;
Nishikawa T., Nagadoi A., Yoshimura S., Aimoto S., Nishimura Y.;
"Solution structure of the DNA-binding domain of human telomeric
protein, hTRF1.";
Structure 6:1057-1065(1998).
[26]
STRUCTURE BY NMR OF 371-439.
PubMed=11738049; DOI=10.1016/S0969-2126(01)00688-8;
Nishikawa T., Okamura H., Nagadoi A., Koenig P., Rhodes D.,
Nishimura Y.;
"Solution structure of a telomeric DNA complex of human TRF1.";
Structure 9:1237-1251(2001).
[27]
X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 48-268, AND MUTAGENESIS OF
ALA-74; ALA-75; TRP-77 AND PHE-81.
PubMed=11545737; DOI=10.1016/S1097-2765(01)00321-5;
Fairall L., Chapman L., Moss H., de Lange T., Rhodes D.;
"Structure of the TRFH dimerization domain of the human telomeric
proteins TRF1 and TRF2.";
Mol. Cell 8:351-361(2001).
[28]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 379-431 IN COMPLEX WITH
TELOMERIC DNA, AND SUBUNIT.
PubMed=15608617; DOI=10.1038/sj.embor.7400314;
Court R., Chapman L., Fairall L., Rhodes D.;
"How the human telomeric proteins TRF1 and TRF2 recognize telomeric
DNA: a view from high-resolution crystal structures.";
EMBO Rep. 6:39-45(2005).
[29]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 58-268 IN COMPLEX WITH TINF2,
INTERACTION WITH TINF2 AND PINX1, DOMAIN TRFH DIMERIZATION, AND
SUBUNIT.
PubMed=18202258; DOI=10.1126/science.1151804;
Chen Y., Yang Y., van Overbeek M., Donigian J.R., Baciu P.,
de Lange T., Lei M.;
"A shared docking motif in TRF1 and TRF2 used for differential
recruitment of telomeric proteins.";
Science 319:1092-1096(2008).
[30]
X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 58-268 IN COMPLEX WITH FBXO4,
MUTAGENESIS OF LEU-115 AND LEU-120, INTERACTION WITH TINF2, SUBUNIT,
AND UBIQUITINATION.
PubMed=20159592; DOI=10.1016/j.devcel.2010.01.007;
Zeng Z., Wang W., Yang Y., Chen Y., Yang X., Diehl J.A., Liu X.,
Lei M.;
"Structural basis of selective ubiquitination of TRF1 by SCFFbx4.";
Dev. Cell 18:214-225(2010).
-!- FUNCTION: Binds the telomeric double-stranded 5'-TTAGGG-3' repeat
and negatively regulates telomere length. Involved in the
regulation of the mitotic spindle. Component of the shelterin
complex (telosome) that is involved in the regulation of telomere
length and protection. Shelterin associates with arrays of double-
stranded 5'-TTAGGG-3' repeats added by telomerase and protects
chromosome ends; without its protective activity, telomeres are no
longer hidden from the DNA damage surveillance and chromosome ends
are inappropriately processed by DNA repair pathways.
{ECO:0000269|PubMed:16166375}.
-!- SUBUNIT: Homodimer; can contain both isoforms. Found in a complex
with POT1; TINF2 and TNKS1. Interacts with ATM, TINF2, TNKS1,
TNKS2, PINX1, NEK2 and MAPRE1. Component of the shelterin complex
(telosome) composed of TERF1, TERF2, TINF2, TERF2IP ACD and POT1.
Interacts with RLIM (via N-terminus). Interacts with FBXO4.
Interaction with TINF2 protects against interaction with FBXO4 and
subsequent polyubiquitination and proteasomal degradation.
Interacts with GNL3L; this interaction promotes homodimerization.
Interacts with TIN2. Interacts with RTEL1. Interactions with GNL3L
and TIN2 are mutually exclusive. Interacts with CCDC79/TERB1 (By
similarity). {ECO:0000250}.
-!- INTERACTION:
Q9BWD1:ACAT2; NbExp=2; IntAct=EBI-710997, EBI-1047273;
Q03154:ACY1; NbExp=2; IntAct=EBI-710997, EBI-742064;
Q01433:AMPD2; NbExp=2; IntAct=EBI-710997, EBI-8796759;
P49418:AMPH; NbExp=2; IntAct=EBI-710997, EBI-7121510;
Q13315:ATM; NbExp=5; IntAct=EBI-711018, EBI-495465;
P54132:BLM; NbExp=3; IntAct=EBI-710997, EBI-621372;
Q96C57:C12orf43; NbExp=2; IntAct=EBI-710997, EBI-11305571;
Q6P2H3:CEP85; NbExp=2; IntAct=EBI-710997, EBI-2808308;
Q9BR76:CORO1B; NbExp=2; IntAct=EBI-710997, EBI-351152;
P53674:CRYBB1; NbExp=2; IntAct=EBI-710997, EBI-7519424;
Q14894:CRYM; NbExp=2; IntAct=EBI-710997, EBI-7107048;
Q9UMR2:DDX19B; NbExp=2; IntAct=EBI-710997, EBI-719232;
Q9BUQ8:DDX23; NbExp=2; IntAct=EBI-710997, EBI-540096;
O00148:DDX39A; NbExp=2; IntAct=EBI-710997, EBI-348253;
P25685:DNAJB1; NbExp=2; IntAct=EBI-710997, EBI-357034;
O43598:DNPH1; NbExp=2; IntAct=EBI-710997, EBI-748674;
Q9H4G0:EPB41L1; NbExp=2; IntAct=EBI-710997, EBI-465536;
Q9UKT5-1:FBXO4; NbExp=3; IntAct=EBI-711018, EBI-960421;
P07332:FES; NbExp=2; IntAct=EBI-710997, EBI-1055635;
P48637:GSS; NbExp=2; IntAct=EBI-710997, EBI-2969145;
P14317:HCLS1; NbExp=2; IntAct=EBI-710997, EBI-750369;
Q96MH2:HEXIM2; NbExp=2; IntAct=EBI-710997, EBI-5460660;
Q93099:HGD; NbExp=2; IntAct=EBI-710997, EBI-3907760;
P17066:HSPA6; NbExp=2; IntAct=EBI-710997, EBI-355106;
Q14145:KEAP1; NbExp=2; IntAct=EBI-710997, EBI-751001;
Q8TBB5:KLHDC4; NbExp=2; IntAct=EBI-710997, EBI-8472352;
P07195:LDHB; NbExp=2; IntAct=EBI-710997, EBI-358748;
Q6UWE0:LRSAM1; NbExp=2; IntAct=EBI-710997, EBI-720984;
Q15691:MAPRE1; NbExp=2; IntAct=EBI-710997, EBI-1004115;
P40925:MDH1; NbExp=2; IntAct=EBI-710997, EBI-709625;
Q9BU76:MMTAG2; NbExp=2; IntAct=EBI-710997, EBI-742459;
P26038:MSN; NbExp=2; IntAct=EBI-710997, EBI-528768;
P55209:NAP1L1; NbExp=2; IntAct=EBI-710997, EBI-356392;
P07196:NEFL; NbExp=2; IntAct=EBI-710997, EBI-475646;
Q9UGY1:NOL12; NbExp=2; IntAct=EBI-710997, EBI-716098;
Q9Y5A7:NUB1; NbExp=8; IntAct=EBI-710997, EBI-3936907;
Q9UNF0:PACSIN2; NbExp=2; IntAct=EBI-710997, EBI-742503;
O96013:PAK4; NbExp=2; IntAct=EBI-710997, EBI-713738;
P12955:PEPD; NbExp=2; IntAct=EBI-710997, EBI-948765;
Q96BK5:PINX1; NbExp=3; IntAct=EBI-710997, EBI-721782;
O15355:PPM1G; NbExp=2; IntAct=EBI-710997, EBI-725702;
Q06830:PRDX1; NbExp=2; IntAct=EBI-710997, EBI-353193;
P30041:PRDX6; NbExp=2; IntAct=EBI-710997, EBI-2255129;
P54829:PTPN5; NbExp=2; IntAct=EBI-710997, EBI-1220572;
P0DJD3:RBMY1A1; NbExp=2; IntAct=EBI-710997, EBI-8638511;
O94761:RECQL4; NbExp=2; IntAct=EBI-710997, EBI-722861;
Q8N5U6:RNF10; NbExp=2; IntAct=EBI-710997, EBI-714023;
Q9H6T3:RPAP3; NbExp=2; IntAct=EBI-710997, EBI-356928;
P84098:RPL19; NbExp=2; IntAct=EBI-710997, EBI-916524;
O95197:RTN3; NbExp=2; IntAct=EBI-710997, EBI-740467;
Q9NUL5:RYDEN; NbExp=2; IntAct=EBI-710997, EBI-10313866;
Q9Y3L3:SH3BP1; NbExp=2; IntAct=EBI-710997, EBI-346869;
O76070:SNCG; NbExp=2; IntAct=EBI-710997, EBI-1053810;
P35610:SOAT1; NbExp=2; IntAct=EBI-710997, EBI-6621955;
P19623:SRM; NbExp=2; IntAct=EBI-710997, EBI-1056183;
Q8WVM7:STAG1; NbExp=4; IntAct=EBI-710997, EBI-1175097;
O00267:SUPT5H; NbExp=2; IntAct=EBI-710997, EBI-710464;
P43405:SYK; NbExp=2; IntAct=EBI-710997, EBI-78302;
Q9NWX6:THG1L; NbExp=2; IntAct=EBI-710997, EBI-746510;
Q9BSI4:TINF2; NbExp=11; IntAct=EBI-710997, EBI-717399;
Q9BSI4-3:TINF2; NbExp=2; IntAct=EBI-710997, EBI-717418;
P29401:TKT; NbExp=2; IntAct=EBI-710997, EBI-1050560;
O95271:TNKS; NbExp=4; IntAct=EBI-710997, EBI-1105254;
Q9H2K2:TNKS2; NbExp=2; IntAct=EBI-710997, EBI-4398527;
O14787:TNPO2; NbExp=2; IntAct=EBI-710997, EBI-431907;
P60174:TPI1; NbExp=2; IntAct=EBI-710997, EBI-717475;
Q9NXH9:TRMT1; NbExp=2; IntAct=EBI-710997, EBI-748900;
Q13509:TUBB3; NbExp=2; IntAct=EBI-710997, EBI-350989;
P23381:WARS; NbExp=2; IntAct=EBI-710997, EBI-721244;
O76024:WFS1; NbExp=2; IntAct=EBI-710997, EBI-720609;
-!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm, cytoskeleton, spindle.
Chromosome, telomere. Note=Colocalizes with telomeric DNA in
interphase and prophase cells. Telomeric localization decreases in
metaphase, anaphase and telophase. Associates with the mitotic
spindle.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1; Synonyms=TRF1;
IsoId=P54274-1; Sequence=Displayed;
Name=2; Synonyms=Pin2;
IsoId=P54274-2; Sequence=VSP_003303;
-!- TISSUE SPECIFICITY: Highly expressed and ubiquitous. Isoform Pin2
predominates.
-!- INDUCTION: Expression is tightly regulated during the cell cycle;
levels are low in G1 and S phase and increase during G2 phase and
mitosis.
-!- DOMAIN: The acidic N-terminal domain binds to the ankyrin repeats
of TNKS1 and TNKS2. The C-terminal domain binds microtubules.
{ECO:0000269|PubMed:18202258}.
-!- DOMAIN: The TRFH dimerization region mediates the interaction with
TINF2. {ECO:0000269|PubMed:18202258}.
-!- DOMAIN: The HTH domain is an independent structural unit and
mediates binding to telomeric DNA. {ECO:0000269|PubMed:18202258}.
-!- PTM: Phosphorylated preferentially on Ser-219 in an ATM-dependent
manner in response to ionizing DNA damage.
{ECO:0000269|PubMed:11375976}.
-!- PTM: ADP-ribosylation by TNKS1 or TNKS2 diminishes its ability to
bind to telomeric DNA.
-!- PTM: Ubiquitinated by RLIM/RNF12, leading to its degradation by
the proteasome. Ubiquitinated by a SCF (SKP1-CUL1-F-box protein)
ubiquitin-protein ligase complex, leading to its degradation by
the proteasome. {ECO:0000269|PubMed:19164295,
ECO:0000269|PubMed:20159592}.
-!- WEB RESOURCE: Name=NIEHS SNPs;
URL="http://egp.gs.washington.edu/data/terf1/";
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EMBL; U40705; AAB54036.1; -; mRNA.
EMBL; AF003001; AAB81137.1; -; mRNA.
EMBL; AH003684; AAB17975.1; -; Genomic_DNA.
EMBL; U74382; AAB53363.1; -; mRNA.
EMBL; EU088287; ABV02580.1; -; Genomic_DNA.
EMBL; AC022893; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC029378; AAH29378.1; -; mRNA.
EMBL; X93511; CAA63768.1; -; mRNA.
CCDS; CCDS6210.1; -. [P54274-2]
CCDS; CCDS6211.1; -. [P54274-1]
PIR; A57573; A57573.
RefSeq; NP_003209.2; NM_003218.3. [P54274-2]
RefSeq; NP_059523.2; NM_017489.2. [P54274-1]
UniGene; Hs.442707; -.
PDB; 1BA5; NMR; -; A=378-430.
PDB; 1H6O; X-ray; 2.90 A; A=62-265.
PDB; 1ITY; NMR; -; A=371-439.
PDB; 1IV6; NMR; -; A=371-439.
PDB; 1W0T; X-ray; 2.00 A; A/B=379-431.
PDB; 3BQO; X-ray; 2.00 A; A=58-268.
PDB; 3L82; X-ray; 2.40 A; A=58-268.
PDB; 5HKP; X-ray; 2.20 A; C/D=1-55.
PDB; 5WIR; X-ray; 2.10 A; A/B=62-265.
PDB; 5XUP; X-ray; 2.10 A; A/B=65-266.
PDBsum; 1BA5; -.
PDBsum; 1H6O; -.
PDBsum; 1ITY; -.
PDBsum; 1IV6; -.
PDBsum; 1W0T; -.
PDBsum; 3BQO; -.
PDBsum; 3L82; -.
PDBsum; 5HKP; -.
PDBsum; 5WIR; -.
PDBsum; 5XUP; -.
ProteinModelPortal; P54274; -.
SMR; P54274; -.
BioGrid; 112872; 314.
ComplexPortal; CPX-152; Shelterin complex.
CORUM; P54274; -.
DIP; DIP-29412N; -.
ELM; P54274; -.
IntAct; P54274; 209.
MINT; P54274; -.
STRING; 9606.ENSP00000276603; -.
iPTMnet; P54274; -.
PhosphoSitePlus; P54274; -.
BioMuta; TERF1; -.
DMDM; 206729904; -.
EPD; P54274; -.
MaxQB; P54274; -.
PaxDb; P54274; -.
PeptideAtlas; P54274; -.
PRIDE; P54274; -.
ProteomicsDB; 56664; -.
ProteomicsDB; 56665; -. [P54274-2]
DNASU; 7013; -.
Ensembl; ENST00000276602; ENSP00000276602; ENSG00000147601. [P54274-2]
Ensembl; ENST00000276603; ENSP00000276603; ENSG00000147601. [P54274-1]
GeneID; 7013; -.
KEGG; hsa:7013; -.
UCSC; uc003xzd.3; human. [P54274-1]
CTD; 7013; -.
DisGeNET; 7013; -.
EuPathDB; HostDB:ENSG00000147601.13; -.
GeneCards; TERF1; -.
H-InvDB; HIX0007582; -.
HGNC; HGNC:11728; TERF1.
HPA; HPA048379; -.
MIM; 600951; gene.
neXtProt; NX_P54274; -.
OpenTargets; ENSG00000147601; -.
PharmGKB; PA36445; -.
eggNOG; ENOG410IIKA; Eukaryota.
eggNOG; ENOG4111QH9; LUCA.
GeneTree; ENSGT00530000063796; -.
HOGENOM; HOG000132847; -.
HOVERGEN; HBG054097; -.
InParanoid; P54274; -.
KO; K11110; -.
OMA; LRTVYIC; -.
OrthoDB; EOG091G04CC; -.
PhylomeDB; P54274; -.
TreeFam; TF333209; -.
Reactome; R-HSA-1221632; Meiotic synapsis.
Reactome; R-HSA-171306; Packaging Of Telomere Ends.
Reactome; R-HSA-2559586; DNA Damage/Telomere Stress Induced Senescence.
SIGNOR; P54274; -.
ChiTaRS; TERF1; human.
EvolutionaryTrace; P54274; -.
GeneWiki; TERF1; -.
GenomeRNAi; 7013; -.
PRO; PR:P54274; -.
Proteomes; UP000005640; Chromosome 8.
Bgee; ENSG00000147601; -.
CleanEx; HS_TERF1; -.
ExpressionAtlas; P54274; baseline and differential.
Genevisible; P54274; HS.
GO; GO:0000781; C:chromosome, telomeric region; IDA:UniProtKB.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
GO; GO:0001650; C:fibrillar center; IDA:HPA.
GO; GO:0016604; C:nuclear body; IDA:HPA.
GO; GO:0000784; C:nuclear chromosome, telomeric region; IDA:BHF-UCL.
GO; GO:0000783; C:nuclear telomere cap complex; IDA:BHF-UCL.
GO; GO:0005730; C:nucleolus; IDA:BHF-UCL.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0070187; C:shelterin complex; IDA:BHF-UCL.
GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
GO; GO:0071532; F:ankyrin repeat binding; IPI:BHF-UCL.
GO; GO:0003677; F:DNA binding; NAS:UniProtKB.
GO; GO:0008301; F:DNA binding, bending; IDA:BHF-UCL.
GO; GO:0003691; F:double-stranded telomeric DNA binding; IDA:UniProtKB.
GO; GO:0098505; F:G-rich strand telomeric DNA binding; IDA:BHF-UCL.
GO; GO:0008017; F:microtubule binding; IDA:UniProtKB.
GO; GO:0008022; F:protein C-terminus binding; IPI:BHF-UCL.
GO; GO:0046982; F:protein heterodimerization activity; IDA:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; IMP:BHF-UCL.
GO; GO:0000981; F:RNA polymerase II transcription factor activity, sequence-specific DNA binding; ISM:NTNU_SB.
GO; GO:0042162; F:telomeric DNA binding; IDA:BHF-UCL.
GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
GO; GO:0000086; P:G2/M transition of mitotic cell cycle; IEP:UniProtKB.
GO; GO:0045141; P:meiotic telomere clustering; IEA:Ensembl.
GO; GO:0007094; P:mitotic spindle assembly checkpoint; IMP:UniProtKB.
GO; GO:0008156; P:negative regulation of DNA replication; IDA:BHF-UCL.
GO; GO:1904850; P:negative regulation of establishment of protein localization to telomere; IMP:BHF-UCL.
GO; GO:1904914; P:negative regulation of establishment of protein-containing complex localization to telomere; IC:BHF-UCL.
GO; GO:1904911; P:negative regulation of establishment of RNA localization to telomere; IMP:BHF-UCL.
GO; GO:1905778; P:negative regulation of exonuclease activity; IDA:BHF-UCL.
GO; GO:0051974; P:negative regulation of telomerase activity; IGI:BHF-UCL.
GO; GO:0032214; P:negative regulation of telomere maintenance via semi-conservative replication; NAS:BHF-UCL.
GO; GO:0032211; P:negative regulation of telomere maintenance via telomerase; IGI:BHF-UCL.
GO; GO:1904357; P:negative regulation of telomere maintenance via telomere lengthening; TAS:BHF-UCL.
GO; GO:1905839; P:negative regulation of telomeric D-loop disassembly; IDA:BHF-UCL.
GO; GO:0043065; P:positive regulation of apoptotic process; IDA:UniProtKB.
GO; GO:0031116; P:positive regulation of microtubule polymerization; IDA:UniProtKB.
GO; GO:0045931; P:positive regulation of mitotic cell cycle; IMP:UniProtKB.
GO; GO:0045840; P:positive regulation of mitotic nuclear division; IMP:UniProtKB.
GO; GO:1904792; P:positive regulation of shelterin complex assembly; IMP:BHF-UCL.
GO; GO:0051260; P:protein homooligomerization; IDA:UniProtKB.
GO; GO:0042493; P:response to drug; IEA:Ensembl.
GO; GO:0090656; P:t-circle formation; TAS:BHF-UCL.
GO; GO:0016233; P:telomere capping; TAS:Reactome.
GO; GO:0000723; P:telomere maintenance; IMP:BHF-UCL.
GO; GO:0007004; P:telomere maintenance via telomerase; IDA:BHF-UCL.
GO; GO:0061820; P:telomeric D-loop disassembly; IGI:BHF-UCL.
GO; GO:0031627; P:telomeric loop formation; IBA:GO_Central.
Gene3D; 1.25.40.210; -; 1.
InterPro; IPR009057; Homeobox-like_sf.
InterPro; IPR017930; Myb_dom.
InterPro; IPR001005; SANT/Myb.
InterPro; IPR013867; Telomere_rpt-bd_fac_dimer_dom.
InterPro; IPR036507; Telomere_rpt-bd_fac_dimer_sf.
InterPro; IPR017357; TERF1/2.
Pfam; PF00249; Myb_DNA-binding; 1.
Pfam; PF08558; TRF; 1.
PIRSF; PIRSF038016; Telomere_bd-1_Pin2; 1.
ProDom; PD014243; Telomere_repeat-bd_fac_dimer; 1.
SMART; SM00717; SANT; 1.
SUPFAM; SSF46689; SSF46689; 1.
SUPFAM; SSF63600; SSF63600; 1.
PROSITE; PS51294; HTH_MYB; 1.
1: Evidence at protein level;
3D-structure; Acetylation; ADP-ribosylation; Alternative splicing;
Cell cycle; Cell division; Chromosome; Complete proteome; Cytoplasm;
Cytoskeleton; Direct protein sequencing; DNA-binding; Isopeptide bond;
Mitosis; Nucleus; Phosphoprotein; Reference proteome; Telomere;
Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:20068231}.
CHAIN 2 439 Telomeric repeat-binding factor 1.
/FTId=PRO_0000197129.
DOMAIN 375 432 HTH myb-type. {ECO:0000255|PROSITE-
ProRule:PRU00625}.
DNA_BIND 403 428 H-T-H motif. {ECO:0000255|PROSITE-
ProRule:PRU00625}.
REGION 58 268 TRFH dimerization.
REGION 265 378 Interaction with RLIM.
{ECO:0000269|PubMed:19164295}.
MOTIF 337 356 Nuclear localization signal.
{ECO:0000255}.
COMPBIAS 2 71 Asp/Glu-rich (acidic).
COMPBIAS 55 62 Poly-Glu.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:20068231}.
MOD_RES 11 11 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 219 219 Phosphoserine; by ATM.
{ECO:0000269|PubMed:11375976}.
CROSSLNK 213 213 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 325 325 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 366 366 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
VAR_SEQ 296 315 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:9326950,
ECO:0000303|PubMed:9391075}.
/FTId=VSP_003303.
MUTAGEN 74 74 A->D: Abolishes dimerization and telomere
binding; when associated with P-75.
{ECO:0000269|PubMed:11545737}.
MUTAGEN 75 75 A->P: Abolishes dimerization and telomere
binding; when associated with D-74.
{ECO:0000269|PubMed:11545737}.
MUTAGEN 77 77 W->P: Abolishes telomere binding.
{ECO:0000269|PubMed:11545737}.
MUTAGEN 81 81 F->P: Abolishes telomere binding.
{ECO:0000269|PubMed:11545737}.
MUTAGEN 90 90 F->P: Diminishes telomere binding.
MUTAGEN 115 115 L->R: Loss of interaction with FBXO4.
{ECO:0000269|PubMed:20159592}.
MUTAGEN 120 120 L->R: Loss of interaction with FBXO4.
{ECO:0000269|PubMed:20159592}.
MUTAGEN 219 219 S->A: Loss of phosphorylation; induction
of mitotic entry and apoptosis and
increased radiation hypersensitivity of
ataxia-telangiectasia cells.
{ECO:0000269|PubMed:11375976}.
MUTAGEN 219 219 S->D,E: Fails to induce apoptosis and
decreases radiation hypersensitivity of
ataxia-telangiectasia cells (phospho-
mimicking mutants).
{ECO:0000269|PubMed:11375976}.
CONFLICT 14 14 G -> R (in Ref. 1; AAB54036, 3; AAB17975/
AAB81137 and 4; AAB53363). {ECO:0000305}.
CONFLICT 338 338 K -> E (in Ref. 8; CAA63768).
{ECO:0000305}.
HELIX 63 92 {ECO:0000244|PDB:3BQO}.
HELIX 95 110 {ECO:0000244|PDB:3BQO}.
STRAND 113 115 {ECO:0000244|PDB:3L82}.
HELIX 117 133 {ECO:0000244|PDB:3BQO}.
TURN 134 136 {ECO:0000244|PDB:3BQO}.
STRAND 143 145 {ECO:0000244|PDB:3BQO}.
HELIX 150 158 {ECO:0000244|PDB:3BQO}.
HELIX 167 186 {ECO:0000244|PDB:3BQO}.
HELIX 190 200 {ECO:0000244|PDB:3BQO}.
STRAND 203 205 {ECO:0000244|PDB:3L82}.
HELIX 211 219 {ECO:0000244|PDB:3BQO}.
HELIX 226 230 {ECO:0000244|PDB:3BQO}.
HELIX 233 251 {ECO:0000244|PDB:3BQO}.
STRAND 252 254 {ECO:0000244|PDB:1H6O}.
HELIX 255 265 {ECO:0000244|PDB:3BQO}.
STRAND 377 379 {ECO:0000244|PDB:1ITY}.
HELIX 385 398 {ECO:0000244|PDB:1W0T}.
HELIX 403 409 {ECO:0000244|PDB:1W0T}.
HELIX 417 428 {ECO:0000244|PDB:1W0T}.
SEQUENCE 439 AA; 50246 MW; AB548E7D3124A211 CRC64;
MAEDVSSAAP SPRGCADGRD ADPTEEQMAE TERNDEEQFE CQELLECQVQ VGAPEEEEEE
EEDAGLVAEA EAVAAGWMLD FLCLSLCRAF RDGRSEDFRR TRNSAEAIIH GLSSLTACQL
RTIYICQFLT RIAAGKTLDA QFENDERITP LESALMIWGS IEKEHDKLHE EIQNLIKIQA
IAVCMENGNF KEAEEVFERI FGDPNSHMPF KSKLLMIISQ KDTFHSFFQH FSYNHMMEKI
KSYVNYVLSE KSSTFLMKAA AKVVESKRTR TITSQDKPSG NDVEMETEAN LDTRKSVSDK
QSAVTESSEG TVSLLRSHKN LFLSKLQHGT QQQDLNKKER RVGTPQSTKK KKESRRATES
RIPVSKSQPV TPEKHRARKR QAWLWEEDKN LRSGVRKYGE GNWSKILLHY KFNNRTSVML
KDRWRTMKKL KLISSDSED


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