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

Transcriptional repressor CTCF (11-zinc finger protein) (CCCTC-binding factor) (CTCFL paralog)

 CTCF_HUMAN              Reviewed;         727 AA.
P49711; B5MC38; Q53XI7; Q59EL8;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
01-OCT-1996, sequence version 1.
18-JUL-2018, entry version 186.
RecName: Full=Transcriptional repressor CTCF;
AltName: Full=11-zinc finger protein;
AltName: Full=CCCTC-binding factor;
AltName: Full=CTCFL paralog;
Name=CTCF;
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), FUNCTION, AND SUBCELLULAR
LOCATION.
PubMed=8649389; DOI=10.1128/MCB.16.6.2802;
Filippova G.N., Fagerlie S., Klenova E.M., Myers C., Dehner Y.,
Goodwin G., Neiman P.E., Collins S.J., Lobanenkov V.V.;
"An exceptionally conserved transcriptional repressor, CTCF, employs
different combinations of zinc fingers to bind diverged promoter
sequences of avian and mammalian c-myc oncogenes.";
Mol. Cell. Biol. 16:2802-2813(1996).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND TISSUE SPECIFICITY.
PubMed=9591631;
DOI=10.1002/(SICI)1098-2264(199805)22:1<26::AID-GCC4>3.3.CO;2-W;
Filippova G.N., Lindblom A., Meincke L.J., Klenova E.M., Neiman P.E.,
Collins S.J., Doggett N.A., Lobanenkov V.V.;
"A widely expressed transcription factor with multiple DNA sequence
specificity, CTCF, is localized at chromosome segment 16q22.1 within
one of the smallest regions of overlap for common deletions in breast
and prostate cancers.";
Genes Chromosomes Cancer 22:26-36(1998).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS WILMS TUMOR TRP-339 AND
GLN-448, VARIANT BREAST TUMOR GLU-344, AND VARIANT PROSTATE TUMOR
ARG-345.
PubMed=11782357;
Filippova G.N., Qi C.-F., Ulmer J.E., Moore J.M., Ward M.D., Hu Y.J.,
Loukinov D.I., Pugacheva E.M., Klenova E.M., Grundy P.E.,
Feinberg A.P., Cleton-Jansen A.-M., Moerland E.W., Cornelisse C.J.,
Suzuki H., Komiya A., Lindblom A., Dorion-Bonnet F., Neiman P.E.,
Morse H.C. III, Collins S.J., Lobanenkov V.V.;
"Tumor-associated zinc finger mutations in the CTCF transcription
factor selectively alter its DNA-binding specificity.";
Cancer Res. 62:48-52(2002).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Brain;
Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
Ohara O., Nagase T., Kikuno R.F.;
"Homo sapiens protein coding cDNA.";
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15616553; DOI=10.1038/nature03187;
Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X.,
Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A.,
Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.,
Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L.,
Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A.,
Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D.,
Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J.,
Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I.,
Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W.,
Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A.,
Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S.,
Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L.,
Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A.,
Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L.,
Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N.,
Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M.,
Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L.,
Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D.,
Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P.,
Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M.,
Rubin E.M., Pennacchio L.A.;
"The sequence and analysis of duplication-rich human chromosome 16.";
Nature 432:988-994(2004).
[7]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Placenta;
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).
[9]
PROTEIN SEQUENCE OF 471-479 AND 483-487, AND TRANSCRIPTIONAL
ACTIVATION OF APP.
PubMed=9407128; DOI=10.1074/jbc.272.52.33353;
Vostrov A.A., Quitschke W.W.;
"The zinc finger protein CTCF binds to the APBbeta domain of the
amyloid beta-protein precursor promoter. Evidence for a role in
transcriptional activation.";
J. Biol. Chem. 272:33353-33359(1997).
[10]
REVIEW.
PubMed=12191639; DOI=10.1016/S1044-579X(02)00060-3;
Klenova E.M., Morse H.C. III, Ohlsson R., Lobanenkov V.V.;
"The novel BORIS + CTCF gene family is uniquely involved in the
epigenetics of normal biology and cancer.";
Semin. Cancer Biol. 12:399-414(2002).
[11]
FUNCTION.
PubMed=11743158; DOI=10.1126/science.1065982;
Chao W., Huynh K.D., Spencer R.J., Davidow L.S., Lee J.T.;
"CTCF, a candidate trans-acting factor for X-inactivation choice.";
Science 295:345-347(2002).
[12]
SUBCELLULAR LOCATION, AND ASSOCIATION WITH H19 ICR.
PubMed=16107875; DOI=10.1038/sj.emboj.7600793;
Burke L.J., Zhang R., Bartkuhn M., Tiwari V.K., Tavoosidana G.,
Kurukuti S., Weth C., Leers J., Galjart N., Ohlsson R., Renkawitz R.;
"CTCF binding and higher order chromatin structure of the H19 locus
are maintained in mitotic chromatin.";
EMBO J. 24:3291-3300(2005).
[13]
SUBCELLULAR LOCATION.
PubMed=16595548; DOI=10.1242/jcs.02890;
Torrano V., Navascues J., Docquier F., Zhang R., Burke L.J.,
Chernukhin I., Farrar D., Leon J., Berciano M.T., Renkawitz R.,
Klenova E., Lafarga M., Delgado M.D.;
"Targeting of CTCF to the nucleolus inhibits nucleolar transcription
through a poly(ADP-ribosyl)ation-dependent mechanism.";
J. Cell Sci. 119:1746-1759(2006).
[14]
INTERACTION WITH CHD8.
PubMed=16949368; DOI=10.1016/j.molcel.2006.08.008;
Ishihara K., Oshimura M., Nakao M.;
"CTCF-dependent chromatin insulator is linked to epigenetic
remodeling.";
Mol. Cell 23:733-742(2006).
[15]
FUNCTION.
PubMed=16815976; DOI=10.1073/pnas.0600326103;
Kurukuti S., Tiwari V.K., Tavoosidana G., Pugacheva E., Murrell A.,
Zhao Z., Lobanenkov V., Reik W., Ohlsson R.;
"CTCF binding at the H19 imprinting control region mediates maternally
inherited higher-order chromatin conformation to restrict enhancer
access to Igf2.";
Proc. Natl. Acad. Sci. U.S.A. 103:10684-10689(2006).
[16]
FUNCTION.
PubMed=17827499; DOI=10.1074/jbc.M706213200;
Renda M., Baglivo I., Burgess-Beusse B., Esposito S., Fattorusso R.,
Felsenfeld G., Pedone P.V.;
"Critical DNA binding interactions of the insulator protein CTCF: a
small number of zinc fingers mediate strong binding, and a single
finger-DNA interaction controls binding at imprinted loci.";
J. Biol. Chem. 282:33336-33345(2007).
[17]
FUNCTION.
PubMed=18413740; DOI=10.1158/0008-5472.CAN-07-6654;
Sun L., Huang L., Nguyen P., Bisht K.S., Bar-Sela G., Ho A.S.,
Bradbury C.M., Yu W., Cui H., Lee S., Trepel J.B., Feinberg A.P.,
Gius D.;
"DNA methyltransferase 1 and 3B activate BAG-1 expression via
recruitment of CTCFL/BORIS and modulation of promoter histone
methylation.";
Cancer Res. 68:2726-2735(2008).
[18]
FUNCTION.
PubMed=18347100; DOI=10.1084/jem.20071843;
Majumder P., Gomez J.A., Chadwick B.P., Boss J.M.;
"The insulator factor CTCF controls MHC class II gene expression and
is required for the formation of long-distance chromatin
interactions.";
J. Exp. Med. 205:785-798(2008).
[19]
FUNCTION.
PubMed=18654629; DOI=10.1371/journal.pgen.1000138;
Fu Y., Sinha M., Peterson C.L., Weng Z.;
"The insulator binding protein CTCF positions 20 nucleosomes around
its binding sites across the human genome.";
PLoS Genet. 4:E1000138-E1000138(2008).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-374; SER-402; SER-609;
SER-610 AND SER-612, 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]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=18550811; DOI=10.1073/pnas.0801273105;
Rubio E.D., Reiss D.J., Welcsh P.L., Disteche C.M., Filippova G.N.,
Baliga N.S., Aebersold R., Ranish J.A., Krumm A.;
"CTCF physically links cohesin to chromatin.";
Proc. Natl. Acad. Sci. U.S.A. 105:8309-8314(2008).
[22]
FUNCTION.
PubMed=19322193; DOI=10.1038/emboj.2009.81;
Mishiro T., Ishihara K., Hino S., Tsutsumi S., Aburatani H.,
Shirahige K., Kinoshita Y., Nakao M.;
"Architectural roles of multiple chromatin insulators at the human
apolipoprotein gene cluster.";
EMBO J. 28:1234-1245(2009).
[23]
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]
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 THR-289; THR-317; SER-609;
SER-610 AND SER-612, 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-609; SER-610 AND
SER-612, 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]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[29]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-689, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25218447; DOI=10.1038/nsmb.2890;
Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
Vertegaal A.C.;
"Uncovering global SUMOylation signaling networks in a site-specific
manner.";
Nat. Struct. Mol. Biol. 21:927-936(2014).
[30]
FUNCTION, INTERACTION WITH CENPE, AND SUBCELLULAR LOCATION.
PubMed=26321640; DOI=10.1016/j.celrep.2015.08.005;
Xiao T., Wongtrakoongate P., Trainor C., Felsenfeld G.;
"CTCF recruits centromeric protein CENP-E to the
pericentromeric/centromeric regions of chromosomes through unusual
CTCF-binding sites.";
Cell Rep. 12:1704-1714(2015).
[31]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-18; LYS-219 AND LYS-689, 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).
[32]
STRUCTURE BY NMR OF 399-589.
RIKEN structural genomics initiative (RSGI);
"Solution structure of zinc finger domains of transcriptional
repressor CTCF protein.";
Submitted (NOV-2005) to the PDB data bank.
[33]
VARIANT MRD21 TRP-567.
PubMed=23746550; DOI=10.1016/j.ajhg.2013.05.007;
Gregor A., Oti M., Kouwenhoven E.N., Hoyer J., Sticht H., Ekici A.B.,
Kjaergaard S., Rauch A., Stunnenberg H.G., Uebe S., Vasileiou G.,
Reis A., Zhou H., Zweier C.;
"De novo mutations in the genome organizer CTCF cause intellectual
disability.";
Am. J. Hum. Genet. 93:124-131(2013).
[34]
VARIANTS 19-GLY--ARG-727 DEL; CYS-278; HIS-342 AND THR-365,
CHARACTERIZATION OF VARIANTS CYS-278; HIS-342 AND THR-365, AND
SUBCELLULAR LOCATION.
PubMed=28319062; DOI=10.1038/onc.2017.25;
Marshall A.D., Bailey C.G., Champ K., Vellozzi M., O'Young P.,
Metierre C., Feng Y., Thoeng A., Richards A.M., Schmitz U., Biro M.,
Jayasinghe R., Ding L., Anderson L., Mardis E.R., Rasko J.E.J.;
"CTCF genetic alterations in endometrial carcinoma are pro-
tumorigenic.";
Oncogene 36:4100-4110(2017).
-!- FUNCTION: Chromatin binding factor that binds to DNA sequence
specific sites. Involved in transcriptional regulation by binding
to chromatin insulators and preventing interaction between
promoter and nearby enhancers and silencers. Acts as
transcriptional repressor binding to promoters of vertebrate MYC
gene and BAG1 gene. Also binds to the PLK and PIM1 promoters. Acts
as a transcriptional activator of APP. Regulates APOA1/C3/A4/A5
gene cluster and controls MHC class II gene expression. Plays an
essential role in oocyte and preimplantation embryo development by
activating or repressing transcription. Seems to act as tumor
suppressor. Plays a critical role in the epigenetic regulation.
Participates in the allele-specific gene expression at the
imprinted IGF2/H19 gene locus. On the maternal allele, binding
within the H19 imprinting control region (ICR) mediates maternally
inherited higher-order chromatin conformation to restrict enhancer
access to IGF2. Plays a critical role in gene silencing over
considerable distances in the genome. Preferentially interacts
with unmethylated DNA, preventing spreading of CpG methylation and
maintaining methylation-free zones. Inversely, binding to target
sites is prevented by CpG methylation. Plays a important role in
chromatin remodeling. Can dimerize when it is bound to different
DNA sequences, mediating long-range chromatin looping. Mediates
interchromosomal association between IGF2/H19 and WSB1/NF1 and may
direct distant DNA segments to a common transcription factory.
Causes local loss of histone acetylation and gain of histone
methylation in the beta-globin locus, without affecting
transcription. When bound to chromatin, it provides an anchor
point for nucleosomes positioning. Seems to be essential for
homologous X-chromosome pairing. May participate with Tsix in
establishing a regulatable epigenetic switch for X chromosome
inactivation. May play a role in preventing the propagation of
stable methylation at the escape genes from X- inactivation.
Involved in sister chromatid cohesion. Associates with both
centromeres and chromosomal arms during metaphase and required for
cohesin localization to CTCF sites. Regulates asynchronous
replication of IGF2/H19. Plays a role in the recruitment of CENPE
to the pericentromeric/centromeric regions of the chromosome
during mitosis (PubMed:26321640). {ECO:0000269|PubMed:11743158,
ECO:0000269|PubMed:16815976, ECO:0000269|PubMed:17827499,
ECO:0000269|PubMed:18347100, ECO:0000269|PubMed:18413740,
ECO:0000269|PubMed:18550811, ECO:0000269|PubMed:18654629,
ECO:0000269|PubMed:19322193, ECO:0000269|PubMed:26321640,
ECO:0000269|PubMed:8649389, ECO:0000269|PubMed:9591631}.
-!- SUBUNIT: Interacts with CHD8 (PubMed:16949368). Interacts with
LLPH (By similarity). Interacts with CENPE (PubMed:26321640).
{ECO:0000250|UniProtKB:Q61164, ECO:0000269|PubMed:16949368,
ECO:0000269|PubMed:26321640}.
-!- INTERACTION:
Q00341:HDLBP; NbExp=4; IntAct=EBI-932887, EBI-1049478;
Q9UGL1:KDM5B; NbExp=8; IntAct=EBI-932887, EBI-2514978;
Q01860:POU5F1; NbExp=2; IntAct=EBI-932887, EBI-475687;
Q5VZL5:ZMYM4; NbExp=3; IntAct=EBI-932887, EBI-2514659;
-!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm
{ECO:0000269|PubMed:28319062}. Chromosome
{ECO:0000269|PubMed:26321640}. Chromosome, centromere
{ECO:0000269|PubMed:26321640}. Note=May translocate to the
nucleolus upon cell differentiation. Associates with both
centromeres and chromosomal arms during metaphase. Associates with
the H19 ICR in mitotic chromosomes. May be preferentially excluded
from heterochromatin during interphase.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P49711-1; Sequence=Displayed;
Name=2;
IsoId=P49711-2; Sequence=VSP_045350;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Ubiquitous. Absent in primary spermatocytes.
{ECO:0000269|PubMed:9591631}.
-!- DOMAIN: The 11 zinc fingers are highly conserved among
vertebrates, exhibiting almost identical amino acid sequences.
Different subsets or combination of individual zinc fingers gives
the ability to CTCF to recognize multiple DNA target sites.
-!- PTM: Sumoylated on Lys-74 and Lys-689; sumoylation of CTCF
contributes to the repressive function of CTCF on the MYC P2
promoter. {ECO:0000250|UniProtKB:Q61164}.
-!- DISEASE: Mental retardation, autosomal dominant 21 (MRD21)
[MIM:615502]: A disorder characterized by significantly below
average general intellectual functioning associated with
impairments in adaptive behavior and manifested during the
developmental period. Additional MRD21 features include short
stature, microcephaly, and developmental delay.
{ECO:0000269|PubMed:23746550}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- MISCELLANEOUS: More than 13'00 CTCF-binding sites in potential
insulators were identified in the human genome.
-!- SIMILARITY: Belongs to the CTCF zinc-finger protein family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAD93030.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/CTCFID40187ch16q22.html";
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; U25435; AAB07788.1; -; mRNA.
EMBL; AF145477; AAF31318.1; -; Genomic_DNA.
EMBL; AF145468; AAF31318.1; JOINED; Genomic_DNA.
EMBL; AF145469; AAF31318.1; JOINED; Genomic_DNA.
EMBL; AF145470; AAF31318.1; JOINED; Genomic_DNA.
EMBL; AF145471; AAF31318.1; JOINED; Genomic_DNA.
EMBL; AF145472; AAF31318.1; JOINED; Genomic_DNA.
EMBL; AF145473; AAF31318.1; JOINED; Genomic_DNA.
EMBL; AF145474; AAF31318.1; JOINED; Genomic_DNA.
EMBL; AF145475; AAF31318.1; JOINED; Genomic_DNA.
EMBL; AF145476; AAF31318.1; JOINED; Genomic_DNA.
EMBL; BT009915; AAP88917.1; -; mRNA.
EMBL; AB209793; BAD93030.1; ALT_INIT; mRNA.
EMBL; AC009095; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC027682; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471092; EAW83142.1; -; Genomic_DNA.
EMBL; BC014267; AAH14267.1; -; mRNA.
CCDS; CCDS10841.1; -. [P49711-1]
CCDS; CCDS54029.1; -. [P49711-2]
PIR; G01792; G01792.
RefSeq; NP_001177951.1; NM_001191022.1. [P49711-2]
RefSeq; NP_006556.1; NM_006565.3. [P49711-1]
RefSeq; XP_016878357.1; XM_017022868.1. [P49711-1]
UniGene; Hs.368367; -.
PDB; 1X6H; NMR; -; A=515-587.
PDB; 2CT1; NMR; -; A=399-462.
PDB; 5K5H; X-ray; 3.11 A; A=348-464.
PDB; 5K5I; X-ray; 2.19 A; A=378-489.
PDB; 5K5J; X-ray; 2.29 A; A=378-489.
PDB; 5K5L; X-ray; 3.12 A; E/F/G=405-492.
PDB; 5KKQ; X-ray; 1.74 A; A/D=321-465.
PDB; 5T00; X-ray; 2.19 A; A/D=321-465.
PDB; 5T0U; X-ray; 3.20 A; A/D=294-465.
PDB; 5UND; X-ray; 2.55 A; A/B=348-547.
PDB; 5YEF; X-ray; 2.81 A; A/B/G/J=292-490.
PDB; 5YEG; X-ray; 2.00 A; A=349-490, B=349-489.
PDB; 5YEH; X-ray; 2.33 A; A/B=349-490.
PDB; 5YEL; X-ray; 2.96 A; A/B=405-580.
PDBsum; 1X6H; -.
PDBsum; 2CT1; -.
PDBsum; 5K5H; -.
PDBsum; 5K5I; -.
PDBsum; 5K5J; -.
PDBsum; 5K5L; -.
PDBsum; 5KKQ; -.
PDBsum; 5T00; -.
PDBsum; 5T0U; -.
PDBsum; 5UND; -.
PDBsum; 5YEF; -.
PDBsum; 5YEG; -.
PDBsum; 5YEH; -.
PDBsum; 5YEL; -.
ProteinModelPortal; P49711; -.
SMR; P49711; -.
BioGrid; 115906; 56.
CORUM; P49711; -.
DIP; DIP-35252N; -.
IntAct; P49711; 32.
MINT; P49711; -.
STRING; 9606.ENSP00000264010; -.
iPTMnet; P49711; -.
PhosphoSitePlus; P49711; -.
BioMuta; CTCF; -.
DMDM; 1706179; -.
EPD; P49711; -.
MaxQB; P49711; -.
PaxDb; P49711; -.
PeptideAtlas; P49711; -.
PRIDE; P49711; -.
ProteomicsDB; 56053; -.
DNASU; 10664; -.
Ensembl; ENST00000264010; ENSP00000264010; ENSG00000102974. [P49711-1]
Ensembl; ENST00000401394; ENSP00000384707; ENSG00000102974. [P49711-2]
Ensembl; ENST00000642819; ENSP00000494408; ENSG00000102974. [P49711-1]
Ensembl; ENST00000644753; ENSP00000493495; ENSG00000102974. [P49711-1]
Ensembl; ENST00000645699; ENSP00000495348; ENSG00000102974. [P49711-1]
Ensembl; ENST00000646076; ENSP00000494538; ENSG00000102974. [P49711-1]
GeneID; 10664; -.
KEGG; hsa:10664; -.
UCSC; uc002etl.4; human. [P49711-1]
CTD; 10664; -.
DisGeNET; 10664; -.
EuPathDB; HostDB:ENSG00000102974.14; -.
GeneCards; CTCF; -.
HGNC; HGNC:13723; CTCF.
HPA; CAB062550; -.
HPA; CAB068181; -.
HPA; CAB068182; -.
HPA; HPA004122; -.
MalaCards; CTCF; -.
MIM; 604167; gene.
MIM; 615502; phenotype.
neXtProt; NX_P49711; -.
OpenTargets; ENSG00000102974; -.
Orphanet; 363611; Intellectual disability-feeding difficulties-developmental delay-microcephaly syndrome.
PharmGKB; PA26998; -.
eggNOG; KOG1721; Eukaryota.
eggNOG; COG5048; LUCA.
GeneTree; ENSGT00890000139371; -.
HOGENOM; HOG000276534; -.
HOVERGEN; HBG000350; -.
InParanoid; P49711; -.
OMA; EGEPMIC; -.
OrthoDB; EOG091G06B4; -.
PhylomeDB; P49711; -.
TreeFam; TF106430; -.
Reactome; R-HSA-5617472; Activation of anterior HOX genes in hindbrain development during early embryogenesis.
SignaLink; P49711; -.
SIGNOR; P49711; -.
ChiTaRS; CTCF; human.
EvolutionaryTrace; P49711; -.
GeneWiki; CTCF; -.
GenomeRNAi; 10664; -.
PRO; PR:P49711; -.
Proteomes; UP000005640; Chromosome 16.
Bgee; ENSG00000102974; -.
CleanEx; HS_CTCF; -.
Genevisible; P49711; HS.
GO; GO:0000775; C:chromosome, centromeric region; IDA:UniProtKB.
GO; GO:0000793; C:condensed chromosome; IDA:UniProtKB.
GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0043035; F:chromatin insulator sequence binding; IDA:UniProtKB.
GO; GO:0003700; F:DNA binding transcription factor activity; IDA:UniProtKB.
GO; GO:0000978; F:RNA polymerase II proximal promoter sequence-specific DNA binding; IDA:NTNU_SB.
GO; GO:0000981; F:RNA polymerase II transcription factor activity, sequence-specific DNA binding; ISA:NTNU_SB.
GO; GO:0043565; F:sequence-specific DNA binding; IDA:UniProtKB.
GO; GO:0003714; F:transcription corepressor activity; TAS:ProtInc.
GO; GO:0044212; F:transcription regulatory region DNA binding; IDA:UniProtKB.
GO; GO:0001078; F:transcriptional repressor activity, RNA polymerase II proximal promoter sequence-specific DNA binding; IDA:NTNU_SB.
GO; GO:0008270; F:zinc ion binding; TAS:UniProtKB.
GO; GO:0007059; P:chromosome segregation; IEA:UniProtKB-KW.
GO; GO:0008285; P:negative regulation of cell proliferation; IMP:UniProtKB.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0016584; P:nucleosome positioning; IDA:UniProtKB.
GO; GO:0010628; P:positive regulation of gene expression; IMP:UniProtKB.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0071459; P:protein localization to chromosome, centromeric region; IMP:UniProtKB.
GO; GO:0070602; P:regulation of centromeric sister chromatid cohesion; NAS:UniProtKB.
GO; GO:0040029; P:regulation of gene expression, epigenetic; IMP:UniProtKB.
GO; GO:0040030; P:regulation of molecular function, epigenetic; IMP:UniProtKB.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
InterPro; IPR036236; Znf_C2H2_sf.
InterPro; IPR013087; Znf_C2H2_type.
SMART; SM00355; ZnF_C2H2; 11.
SUPFAM; SSF57667; SSF57667; 7.
PROSITE; PS00028; ZINC_FINGER_C2H2_1; 8.
PROSITE; PS50157; ZINC_FINGER_C2H2_2; 11.
1: Evidence at protein level;
3D-structure; Acetylation; Activator; Alternative splicing;
Centromere; Chromatin regulator; Chromosome; Chromosome partition;
Complete proteome; Direct protein sequencing; Disease mutation;
DNA-binding; Isopeptide bond; Mental retardation; Metal-binding;
Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Repeat;
Repressor; Transcription; Transcription regulation; Tumor suppressor;
Ubl conjugation; Zinc; Zinc-finger.
CHAIN 1 727 Transcriptional repressor CTCF.
/FTId=PRO_0000047228.
ZN_FING 266 288 C2H2-type 1. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 294 316 C2H2-type 2. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 322 345 C2H2-type 3. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 351 373 C2H2-type 4. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 379 401 C2H2-type 5. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 407 430 C2H2-type 6. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 437 460 C2H2-type 7. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 467 489 C2H2-type 8. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 495 517 C2H2-type 9. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 523 546 C2H2-type 10. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 555 577 C2H2-type 11; atypical.
{ECO:0000255|PROSITE-ProRule:PRU00042}.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000244|PubMed:22814378}.
MOD_RES 289 289 Phosphothreonine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 317 317 Phosphothreonine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 374 374 Phosphothreonine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 402 402 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 609 609 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692}.
MOD_RES 610 610 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692}.
MOD_RES 612 612 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692}.
CROSSLNK 18 18 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 74 74 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO).
{ECO:0000250}.
CROSSLNK 219 219 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 689 689 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:28112733}.
VAR_SEQ 1 328 Missing (in isoform 2).
{ECO:0000303|Ref.5}.
/FTId=VSP_045350.
VARIANT 19 727 Missing (found in an endometrial
carcinoma sample; unknown pathological
significance).
{ECO:0000269|PubMed:28319062}.
/FTId=VAR_079374.
VARIANT 278 278 R -> C (found in an endometrial carcinoma
sample; no effect on its nuclear
localization; loss of its ability to
inhibit cell proliferation; unknown
pathological significance).
{ECO:0000269|PubMed:28319062}.
/FTId=VAR_079375.
VARIANT 339 339 R -> W (in a Wilms' tumor).
{ECO:0000269|PubMed:11782357}.
/FTId=VAR_013141.
VARIANT 342 342 R -> H (found in an endometrial carcinoma
sample; no effect on its nuclear
localization; loss of its ability to
inhibit cell proliferation; unknown
pathological significance).
{ECO:0000269|PubMed:28319062}.
/FTId=VAR_079376.
VARIANT 344 344 K -> E (in a breast tumor).
{ECO:0000269|PubMed:11782357}.
/FTId=VAR_013142.
VARIANT 345 345 H -> R (in a prostate tumor).
{ECO:0000269|PubMed:11782357}.
/FTId=VAR_013143.
VARIANT 365 365 K -> T (found in an endometrial carcinoma
sample; no effect on its nuclear
localization; no loss of its ability to
inhibit cell proliferation; unknown
pathological significance).
{ECO:0000269|PubMed:28319062}.
/FTId=VAR_079377.
VARIANT 448 448 R -> Q (in a Wilms' tumor).
{ECO:0000269|PubMed:11782357}.
/FTId=VAR_013144.
VARIANT 567 567 R -> W (in MRD21; dbSNP:rs879255516).
{ECO:0000269|PubMed:23746550}.
/FTId=VAR_070776.
STRAND 297 300 {ECO:0000244|PDB:5T0U}.
STRAND 302 305 {ECO:0000244|PDB:5T0U}.
HELIX 306 316 {ECO:0000244|PDB:5T0U}.
STRAND 325 327 {ECO:0000244|PDB:5YEF}.
STRAND 330 333 {ECO:0000244|PDB:5KKQ}.
HELIX 334 344 {ECO:0000244|PDB:5KKQ}.
STRAND 354 357 {ECO:0000244|PDB:5KKQ}.
STRAND 359 362 {ECO:0000244|PDB:5KKQ}.
HELIX 363 374 {ECO:0000244|PDB:5KKQ}.
STRAND 382 385 {ECO:0000244|PDB:5KKQ}.
STRAND 387 390 {ECO:0000244|PDB:5KKQ}.
HELIX 391 402 {ECO:0000244|PDB:5KKQ}.
STRAND 406 408 {ECO:0000244|PDB:2CT1}.
TURN 410 412 {ECO:0000244|PDB:5KKQ}.
STRAND 415 418 {ECO:0000244|PDB:5KKQ}.
HELIX 419 429 {ECO:0000244|PDB:5KKQ}.
HELIX 431 433 {ECO:0000244|PDB:5K5L}.
STRAND 437 439 {ECO:0000244|PDB:5KKQ}.
TURN 440 443 {ECO:0000244|PDB:5KKQ}.
STRAND 444 448 {ECO:0000244|PDB:5KKQ}.
HELIX 449 459 {ECO:0000244|PDB:5KKQ}.
STRAND 460 468 {ECO:0000244|PDB:5YEF}.
STRAND 470 473 {ECO:0000244|PDB:5YEG}.
STRAND 475 478 {ECO:0000244|PDB:5YEG}.
HELIX 479 486 {ECO:0000244|PDB:5YEG}.
TURN 489 493 {ECO:0000244|PDB:5UND}.
STRAND 498 500 {ECO:0000244|PDB:5UND}.
STRAND 503 506 {ECO:0000244|PDB:5YEL}.
HELIX 507 514 {ECO:0000244|PDB:5UND}.
STRAND 526 529 {ECO:0000244|PDB:5YEL}.
STRAND 531 535 {ECO:0000244|PDB:5YEL}.
HELIX 536 540 {ECO:0000244|PDB:5YEL}.
HELIX 541 545 {ECO:0000244|PDB:5YEL}.
STRAND 558 560 {ECO:0000244|PDB:5YEL}.
STRAND 563 565 {ECO:0000244|PDB:1X6H}.
HELIX 567 575 {ECO:0000244|PDB:5YEL}.
SEQUENCE 727 AA; 82785 MW; 2110538B65DC5706 CRC64;
MEGDAVEAIV EESETFIKGK ERKTYQRRRE GGQEEDACHL PQNQTDGGEV VQDVNSSVQM
VMMEQLDPTL LQMKTEVMEG TVAPEAEAAV DDTQIITLQV VNMEEQPINI GELQLVQVPV
PVTVPVATTS VEELQGAYEN EVSKEGLAES EPMICHTLPL PEGFQVVKVG ANGEVETLEQ
GELPPQEDPS WQKDPDYQPP AKKTKKTKKS KLRYTEEGKD VDVSVYDFEE EQQEGLLSEV
NAEKVVGNMK PPKPTKIKKK GVKKTFQCEL CSYTCPRRSN LDRHMKSHTD ERPHKCHLCG
RAFRTVTLLR NHLNTHTGTR PHKCPDCDMA FVTSGELVRH RRYKHTHEKP FKCSMCDYAS
VEVSKLKRHI RSHTGERPFQ CSLCSYASRD TYKLKRHMRT HSGEKPYECY ICHARFTQSG
TMKMHILQKH TENVAKFHCP HCDTVIARKS DLGVHLRKQH SYIEQGKKCR YCDAVFHERY
ALIQHQKSHK NEKRFKCDQC DYACRQERHM IMHKRTHTGE KPYACSHCDK TFRQKQLLDM
HFKRYHDPNF VPAAFVCSKC GKTFTRRNTM ARHADNCAGP DGVEGENGGE TKKSKRGRKR
KMRSKKEDSS DSENAEPDLD DNEDEEEPAV EIEPEPEPQP VTPAPPPAKK RRGRPPGRTN
QPKQNQPTAI IQVEDQNTGA IENIIVEVKK EPDAEPAEGE EEEAQPAATD APNGDLTPEM
ILSMMDR


Related products :

Catalog number Product name Quantity
EIAAB09772 11-zinc finger protein,CCCTC-binding factor,Ctcf,CTCFL paralog,Rat,Rattus norvegicus,Transcriptional repressor CTCF
EIAAB09770 11-zinc finger protein,CCCTC-binding factor,Ctcf,CTCFL paralog,Mouse,Mus musculus,Transcriptional repressor CTCF
EIAAB09771 11-zinc finger protein,CCCTC-binding factor,CTCF,CTCFL paralog,Homo sapiens,Human,Transcriptional repressor CTCF
EIAAB09774 BORIS,Brother of the regulator of imprinted sites,Cancer_testis antigen 27,CCCTC-binding factor,CT27,CTCF paralog,CTCFL,CTCF-like protein,Homo sapiens,Human,Transcriptional repressor CTCFL,Zinc finger
18-003-43402 Transcriptional repressor CTCF - CCCTC-binding factor; CTCFL paralog; 11-zinc finger protein Polyclonal 0.05 mg Aff Pur
18-003-43348 Transcriptional repressor CTCF - CCCTC-binding factor; CTCFL paralog; 11-zinc finger protein Polyclonal 0.05 mg Aff Pur
18-003-43144 Transcriptional repressor CTCFL - CCCTC-binding factor; Brother of the regulator of imprinted sites; Zinc finger protein CTCF-T; CTCF paralog Polyclonal 0.05 mg Aff Pur
EIAAB09773 11-zinc finger protein,CCCTC-binding factor,Chicken,CTCF,CTCFL paralog,Gallus gallus,Transcriptional repressor CTCF
EIAAB09775 Boris,Brother of the regulator of imprinted sites,CCCTC-binding factor,CTCF paralog,Ctcfl,CTCF-like protein,Mouse,Mus musculus,Transcriptional repressor CTCFL
CTDP1 CTCFL Gene CCCTC-binding factor (zinc finger protein)-like
GWB-B6A293 Anti- CTCFL (CCCTC-binding factor (zinc finger protein)-like) Antibody
CTD CTCF Gene CCCTC-binding factor (zinc finger protein)
GWB-BB043A Anti- CTCF (CCCTC-binding factor (zinc finger protein)) Antibody
GWB-D27C66 Anti- CTCF (CCCTC-binding factor (zinc finger protein)) Antibody
CSB-EL006138RA Rat CCCTC-binding factor (zinc finger protein) (CTCF) ELISA kit, Species Rat, Sample Type serum, plasma 96T
CSB-EL006139MO Mouse CCCTC-binding factor (zinc finger protein)-like (CTCFL) ELISA kit, Species Mouse, Sample Type serum, plasma 96T
CSB-EL006139HU Human CCCTC-binding factor (zinc finger protein)-like (CTCFL) ELISA kit, Species Human, Sample Type serum, plasma 96T
CSB-EL006138CH Chicken CCCTC-binding factor (zinc finger protein) (CTCF) ELISA kit, Species Chicken, Sample Type serum, plasma 96T
CSB-EL006138MO Mouse CCCTC-binding factor (zinc finger protein) (CTCF) ELISA kit, Species Mouse, Sample Type serum, plasma 96T
CSB-EL006138HU Human CCCTC-binding factor (zinc finger protein) (CTCF) ELISA kit, Species Human, Sample Type serum, plasma 96T
EIAAB47328 58 kDa repressor protein,Homo sapiens,Human,RP58,TAZ1,TAZ-1,Transcriptional repressor RP58,Translin-associated zinc finger protein 1,ZBTB18,Zinc finger and BTB domain-containing protein 18,Zinc finger
28-436 CTCFL is a paralog of CTCF and appears to be expressed primarily in the cytoplasm of spermatocytes. CTCFL is normally expressed in a mutually exclusive pattern that correlates with resetting of methyl 0.05 mg
EIAAB47268 Beta enolase repressor factor 1,G-rich box-binding protein,Mouse,Mus musculus,Transcription factor BFCOL1,Transcription factor ZBP-89,Zbp89,Zfp148,Zinc finger DNA-binding protein 89,Zinc finger protei
abx111451 Polyclonal Rabbit Ccctc-Binding Factor (Zinc Finger Protein)-Like Antibody 50 μl
abx111450 Polyclonal Rabbit Ccctc-Binding Factor (Zinc Finger Protein) Antibody 50 μl


 

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