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Cyclic AMP-responsive element-binding protein 3 (CREB-3) (cAMP-responsive element-binding protein 3) (Leucine zipper protein) (Luman) (Transcription factor LZIP-alpha) [Cleaved into: Processed cyclic AMP-responsive element-binding protein 3 (N-terminal Luman) (Transcriptionally active form)]

 CREB3_HUMAN             Reviewed;         371 AA.
O43889; D0PTW6; O14671; O14919; Q5TCV1; Q96GK8; Q9H2W3; Q9UE77;
09-NOV-2004, integrated into UniProtKB/Swiss-Prot.
28-MAR-2018, sequence version 2.
20-JUN-2018, entry version 173.
RecName: Full=Cyclic AMP-responsive element-binding protein 3;
Short=CREB-3;
Short=cAMP-responsive element-binding protein 3;
AltName: Full=Leucine zipper protein;
AltName: Full=Luman;
AltName: Full=Transcription factor LZIP-alpha;
Contains:
RecName: Full=Processed cyclic AMP-responsive element-binding protein 3;
Short=N-terminal Luman;
Short=Transcriptionally active form;
Name=CREB3; Synonyms=LZIP;
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 (ISOFORM 1),
DNA-BINDING (ISOFORM 1), INTERACTION WITH HCFC1 (ISOFORM 1), AND
TISSUE SPECIFICITY.
TISSUE=Cervix carcinoma;
PubMed=9271389; DOI=10.1128/MCB.17.9.5117;
Lu R., Yang P., O'Hare P., Misra V.;
"Luman, a new member of the CREB/ATF family, binds to herpes simplex
virus VP16-associated host cellular factor.";
Mol. Cell. Biol. 17:5117-5126(1997).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND INTERACTION WITH HCFC1
(ISOFORM 1).
TISSUE=Cervix carcinoma;
PubMed=9389645; DOI=10.1101/gad.11.23.3122;
Freiman R.N., Herr W.;
"Viral mimicry: common mode of association with HCF by VP16 and the
cellular protein LZIP.";
Genes Dev. 11:3122-3127(1997).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), FUNCTION IN CELL
PROLIFERATION (MICROBIAL INFECTION), HOMODIMERIZATION, INTERACTION
WITH HCV CORE PROTEIN (MICROBIAL INFECTION), DNA-BINDING, AND
SUBCELLULAR LOCATION.
TISSUE=Fetal liver;
PubMed=10675342; DOI=10.1093/emboj/19.4.729;
Jin D.-Y., Wang H.-L., Zhou Y., Chun A.C.S., Kibler K.V., Hou Y.-D.,
Kung H.-F., Jeang K.-T.;
"Hepatitis C virus core protein-induced loss of LZIP function
correlates with cellular transformation.";
EMBO J. 19:729-740(2000).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), ALTERNATIVE SPLICING (ISOFORM
1), FUNCTION IN LKN-1-STIMULATED CHEMOTAXIS SIGNALING (ISOFORM 1),
FUNCTION IN GLUCOCORTICOID-INDUCED TRANSCRIPTIONAL REPRESSION (ISOFORM
2), SUBCELLULAR LOCATION (ISOFORMS 1 AND 2), TISSUE SPECIFICITY
(ISOFORMS 1 AND 2), AND MUTAGENESIS OF 16-LEU-LEU-17 AND
57-LEU-LEU-58.
PubMed=19779205; DOI=10.1210/me.2009-0009;
Kang H., Kim Y.S., Ko J.;
"A novel isoform of human LZIP negatively regulates the
transactivation of the glucocorticoid receptor.";
Mol. Endocrinol. 23:1746-1757(2009).
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Brain;
Hayashi M., Tanaka T.;
"Novel activation and inhibitory domains of LZIP isoforms, retinoic
acid-inducible genes in P19 embryonal carcinoma cell, differentially
activate transcription in mouse development.";
Submitted (FEB-1997) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1).
Ben-Yosef T., Francomano C.A.;
"Complete nucleotide sequence and genomic structure of the human cAMP
responsive element binding protein 3 (Luman) gene (CREB3).";
Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164053; DOI=10.1038/nature02465;
Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E.,
Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
Kimberley A.M., King A., Knights A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S.,
Rogers J., Dunham I.;
"DNA sequence and analysis of human chromosome 9.";
Nature 429:369-374(2004).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Pancreas, and Skin;
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]
FUNCTION IN HSV-1 INFECTION (MICROBIAL INFECTION), MUTAGENESIS OF
TYR-81, AND SUBCELLULAR LOCATION (ISOFORM 1).
PubMed=10623756; DOI=10.1128/JVI.74.2.934-943.2000;
Lu R., Misra V.;
"Potential role for luman, the cellular homologue of herpes simplex
virus VP16 (alpha gene trans-inducing factor), in herpesvirus
latency.";
J. Virol. 74:934-943(2000).
[10]
INTERACTION WITH HCFC1.
PubMed=10629049; DOI=10.1128/MCB.20.3.919-928.2000;
Mahajan S.S., Wilson A.C.;
"Mutations in host cell factor 1 separate its role in cell
proliferation from recruitment of VP16 and LZIP.";
Mol. Cell. Biol. 20:919-928(2000).
[11]
FUNCTION IN TRANSCRIPTIONAL REGULATION (ISOFORM 1), INTERACTION WITH
HCFC1, REGION, AND MUTAGENESIS OF 12-LEU-LEU-13; 16-LEU-LEU-17 AND
78-ASP--TYR-81.
PubMed=10984507; DOI=10.1073/pnas.190062797;
Luciano R.L., Wilson A.C.;
"N-terminal transcriptional activation domain of LZIP comprises two
LxxLL motifs and the host cell factor-1 binding motif.";
Proc. Natl. Acad. Sci. U.S.A. 97:10757-10762(2000).
[12]
GLYCOSYLATION, SUBCELLULAR LOCATION, TOPOLOGY, PROTEOLYTIC PROCESSING,
CLEAVAGE SITE, AND MUTAGENESIS OF ARG-252; ARG-264 AND ARG-267.
PubMed=12138176; DOI=10.1128/MCB.22.16.5639-5649.2002;
Raggo C., Rapin N., Stirling J., Gobeil P., Smith-Windsor E.,
O'Hare P., Misra V.;
"Luman, the cellular counterpart of herpes simplex virus VP16, is
processed by regulated intramembrane proteolysis.";
Mol. Cell. Biol. 22:5639-5649(2002).
[13]
FUNCTION IN LKN-1-STIMULATED CHEMOTAXIS SIGNALING, AND INTERACTION
WITH CCR1.
PubMed=15001559; DOI=10.1096/fj.03-0867fje;
Ko J., Jang S.W., Kim Y.S., Kim I.S., Sung H.J., Kim H.-H., Park J.Y.,
Lee Y.H., Kim J., Na D.S.;
"Human LZIP binds to CCR1 and differentially affects the chemotactic
activities of CCR1-dependent chemokines.";
FASEB J. 18:890-892(2004).
[14]
FUNCTION IN THE UNFOLDED PROTEIN RESPONSE, DNA-BINDING, AND INDUCTION.
PubMed=15845366; DOI=10.1016/j.bbrc.2005.03.141;
DenBoer L.M., Hardy-Smith P.W., Hogan M.R., Cockram G.P., Audas T.E.,
Lu R.;
"Luman is capable of binding and activating transcription from the
unfolded protein response element.";
Biochem. Biophys. Res. Commun. 331:113-119(2005).
[15]
FUNCTION (MICROBIAL INFECTION), INTERACTION WITH CREBZF AND HCFC1,
SUBCELLULAR LOCATION, AND MUTAGENESIS OF 78-ASP--TYR-81 AND ASN-160.
PubMed=15705566; DOI=10.1074/jbc.M500728200;
Misra V., Rapin N., Akhova O., Bainbridge M., Korchinski P.;
"Zhangfei is a potent and specific inhibitor of the host cell factor-
binding transcription factor Luman.";
J. Biol. Chem. 280:15257-15266(2005).
[16]
FUNCTION IN HIV-1 INFECTIVITY (MICROBIAL INFECTION), INTERACTION WITH
HIV-1 TAT (MICROBIAL INFECTION), INTERACTION WITH HIV-1 TMGP41
(MICROBIAL INFECTION), AND PROTEOLYTIC PROCESSING.
PubMed=17054986; DOI=10.1016/j.jmb.2006.09.080;
Blot G., Lopez-Verges S., Treand C., Kubat N.J., Delcroix-Genete D.,
Emiliani S., Benarous R., Berlioz-Torrent C.;
"Luman, a new partner of HIV-1 TMgp41, interferes with Tat-mediated
transcription of the HIV-1 LTR.";
J. Mol. Biol. 364:1034-1047(2006).
[17]
FUNCTION IN THE UNFOLDED PROTEIN RESPONSE, DNA-BINDING, GLYCOSYLATION,
PROTEOLYTIC PROCESSING, AND INDUCTION.
PubMed=16940180; DOI=10.1128/MCB.01046-06;
Liang G., Audas T.E., Li Y., Cockram G.P., Dean J.D., Martyn A.C.,
Kokame K., Lu R.;
"Luman/CREB3 induces transcription of the endoplasmic reticulum (ER)
stress response protein Herp through an ER stress response element.";
Mol. Cell. Biol. 26:7999-8010(2006).
[18]
FUNCTION IN LKN-1-STIMULATED CHEMOTAXIS SIGNALING, AND INDUCTION.
PubMed=17296613; DOI=10.1074/jbc.M607962200;
Jang S.W., Kim Y.S., Kim Y.R., Sung H.J., Ko J.;
"Regulation of human LZIP expression by NF-kappaB and its involvement
in monocyte cell migration induced by Lkn-1.";
J. Biol. Chem. 282:11092-11100(2007).
[19]
FUNCTION IN TRANSCRIPTIONAL ACTIVATION AND IN PROMOTING CHEMOTAXIS,
AND DNA-BINDING.
PubMed=18587271; DOI=10.3858/emm.2008.40.3.332;
Sung H.J., Kim Y.S., Kang H., Ko J.;
"Human LZIP induces monocyte CC chemokine receptor 2 expression
leading to enhancement of monocyte chemoattractant protein 1/CCL2-
induced cell migration.";
Exp. Mol. Med. 40:332-338(2008).
[20]
INTERACTION WITH CREBRF, PROTEOLYTIC PROCESSING, INDUCTION, AND
SUBCELLULAR LOCATION.
PubMed=18391022; DOI=10.1128/MCB.01439-07;
Audas T.E., Li Y., Liang G., Lu R.;
"A novel protein, Luman/CREB3 recruitment factor, inhibits Luman
activation of the unfolded protein response.";
Mol. Cell. Biol. 28:3952-3966(2008).
[21]
INTERACTION WITH DCSTAMP AND OS9, PROTEOLYTIC PROCESSING, INDUCTION,
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=20546900; DOI=10.1016/j.molimm.2010.04.019;
Eleveld-Trancikova D., Sanecka A., van Hout-Kuijer M.A., Looman M.W.,
Hendriks I.A., Jansen B.J., Adema G.J.;
"DC-STAMP interacts with ER-resident transcription factor LUMAN which
becomes activated during DC maturation.";
Mol. Immunol. 47:1963-1973(2010).
-!- FUNCTION: Endoplasmic reticulum (ER)-bound sequence-specific
transcription factor that directly binds DNA and activates
transcription (PubMed:9271389, PubMed:19779205, PubMed:10984507,
PubMed:15845366, PubMed:16940180). Plays a role in the unfolded
protein response (UPR), promoting cell survival versus ER stress-
induced apoptotic cell death (PubMed:15845366, PubMed:16940180).
Also involved in cell proliferation, migration and
differentiation, tumor suppression and inflammatory gene
expression. Acts as a positive regulator of LKN-1/CCL15-induced
chemotaxis signaling of leukocyte cell migration (PubMed:19779205,
PubMed:15001559, PubMed:17296613). Associates with chromatin to
the HERPUD1 promoter (PubMed:16940180). Also induces
transcriptional activation of chemokine receptors
(PubMed:18587271, PubMed:17296613). {ECO:0000269|PubMed:10984507,
ECO:0000269|PubMed:15001559, ECO:0000269|PubMed:15845366,
ECO:0000269|PubMed:16940180, ECO:0000269|PubMed:17296613,
ECO:0000269|PubMed:18587271, ECO:0000269|PubMed:19779205,
ECO:0000269|PubMed:9271389}.
-!- FUNCTION: Processed cyclic AMP-responsive element-binding protein
3: This is the transcriptionally active form that translocates to
the nucleus and activates unfolded protein response (UPR) target
genes during endoplasmic reticulum (ER) stress response. Binds the
cAMP response element (CRE) (consensus: 5'-GTGACGT[AG][AG]-3') and
C/EBP sequences present in many promoters to activate
transcription of the genes. Binds to the unfolded protein response
element (UPRE) consensus sequences sites. Binds DNA to the 5'-
CCAC[GA]-3'half of ERSE II (5'-ATTGG-N-CCACG-3').
{ECO:0000269|PubMed:16940180}.
-!- FUNCTION: Isoform 2: Functions as a negative transcriptional
regulator in ligand-induced transcriptional activation of the
glucocorticoid receptor NR3C1 by recruiting and activating histone
deacetylases (HDAC1, HDAC2 and HDAC6). Also decreases the
acetylation level of histone H4. Does not promote the chemotactic
activity of leukocyte cells. {ECO:0000269|PubMed:19779205}.
-!- FUNCTION: (Microbial infection) Plays a role in human
immunodeficiency virus type 1 (HIV-1) virus protein expression.
{ECO:0000269|PubMed:17054986}.
-!- FUNCTION: (Microbial infection) Isoform 1: Plays a role in herpes
simplex virus-1 (HSV-1) latent infection and reactivation from
latency. Represses the VP16-mediated transactivation of immediate
early genes of the HSV-1 virus by sequestering host cell factor-1
HCFC1 in the ER membrane of sensory neurons, thereby preventing
the initiation of the replicative cascade leading to latent
infection. {ECO:0000269|PubMed:10623756,
ECO:0000269|PubMed:15705566}.
-!- FUNCTION: (Microbial infection) Isoform 1: May play a role as a
cellular tumor suppressor that is targeted by the hepatitis C
virus (HCV) core protein. {ECO:0000269|PubMed:10675342}.
-!- FUNCTION: (Microbial infection) Processed cyclic AMP-responsive
element-binding protein 3: Activates transcription of genes
required for reactivation of the latent HSV-1 virus. It's
transcriptional activity is inhibited by CREBZF in a HCFC1-
dependent manner, by the viral transactivator protein VP16. Binds
DNA to the cAMP response element (CRE) (consensus: 5'-
GTGACGT[AG][AG]-3') and C/EBP sequences present in many viral
promoters. {ECO:0000269|PubMed:10623756}.
-!- FUNCTION: (Microbial infection) Processed cyclic AMP-responsive
element-binding protein 3: It's transcriptional activity is
inhibited by CREBZF in a HCFC1-dependent manner, by the viral
transactivator HCV core protein. {ECO:0000269|PubMed:10675342}.
-!- SUBUNIT: Homodimer (PubMed:10675342). Isoform 1 interacts with
HCFC1; the interaction is required to stimulate CREB3
transcriptional activity (PubMed:9271389, PubMed:9389645,
PubMed:10629049, PubMed:10984507). Isoform 1 interacts with
CREBZF; the interaction occurs only in combination with HCFC1
(PubMed:15705566). Isoform 1 interacts (via central part and
transmembrane region) with DCSTAMP (via C-terminus cytoplasmic
domain) (PubMed:20546900). Isoform 1 interacts with OS9
(PubMed:20546900). Isoform 1 interacts (via leucine-zipper domain)
with CREBRF (via leucine-zipper domain); the interaction occurs
only after CREB3 activation and promotes CREB3 degradation
(PubMed:18391022). Isoform 1 interacts (via C-terminal domain)
with CCR1 (PubMed:15001559). {ECO:0000269|PubMed:10629049,
ECO:0000269|PubMed:10675342, ECO:0000269|PubMed:10984507,
ECO:0000269|PubMed:15001559, ECO:0000269|PubMed:15705566,
ECO:0000269|PubMed:18391022, ECO:0000269|PubMed:20546900,
ECO:0000269|PubMed:9271389, ECO:0000269|PubMed:9389645}.
-!- SUBUNIT: (Microbial infection) Interacts with the HCV core
protein; homodimerization is prevented by the HCV core protein
(PubMed:10675342). Isoform 1 interacts (via leucine-zipper and
transmembrane domains) with HIV-1 TMgp41 (via cytoplasmic domain);
the interaction reduces CREB3 stability (PubMed:17054986).
Processed cyclic AMP-responsive element-binding protein 3
interacts with HIV-1 Tat (PubMed:17054986).
{ECO:0000269|PubMed:10675342, ECO:0000269|PubMed:17054986}.
-!- INTERACTION:
P29846:- (xeno); NbExp=8; IntAct=EBI-625022, EBI-909718;
Q15109:AGER; NbExp=3; IntAct=EBI-625022, EBI-1646426;
Q92685:ALG3; NbExp=3; IntAct=EBI-625022, EBI-2848814;
Q9BVK2:ALG8; NbExp=3; IntAct=EBI-625022, EBI-3921603;
P05090:APOD; NbExp=3; IntAct=EBI-625022, EBI-715495;
P29972:AQP1; NbExp=3; IntAct=EBI-625022, EBI-745213;
P41181:AQP2; NbExp=3; IntAct=EBI-625022, EBI-12701138;
P55087:AQP4; NbExp=3; IntAct=EBI-625022, EBI-10104898;
P09871:C1S; NbExp=3; IntAct=EBI-625022, EBI-2810045;
P06681:C2; NbExp=3; IntAct=EBI-625022, EBI-2835920;
P32246:CCR1; NbExp=7; IntAct=EBI-625022, EBI-608322;
Q9UJ71:CD207; NbExp=3; IntAct=EBI-625022, EBI-2873235;
Q9BXR6:CFHR5; NbExp=3; IntAct=EBI-625022, EBI-11579371;
Q8N6F1-2:CLDN19; NbExp=3; IntAct=EBI-625022, EBI-12256978;
Q68CJ9:CREB3L3; NbExp=2; IntAct=EBI-625002, EBI-852194;
Q8IUR6:CREBRF; NbExp=4; IntAct=EBI-625022, EBI-1042699;
P78329:CYP4F2; NbExp=3; IntAct=EBI-625022, EBI-1752413;
Q9H295:DCSTAMP; NbExp=6; IntAct=EBI-625022, EBI-6095316;
Q15125:EBP; NbExp=3; IntAct=EBI-625022, EBI-3915253;
P50402:EMD; NbExp=3; IntAct=EBI-625022, EBI-489887;
P37268:FDFT1; NbExp=3; IntAct=EBI-625022, EBI-714550;
Q01740:FMO1; NbExp=3; IntAct=EBI-625022, EBI-12701460;
P31513:FMO3; NbExp=3; IntAct=EBI-625022, EBI-12361463;
P17302:GJA1; NbExp=3; IntAct=EBI-625022, EBI-1103439;
A0A0C4DFT7:GYPA; NbExp=3; IntAct=EBI-625022, EBI-12044847;
P51610:HCFC1; NbExp=5; IntAct=EBI-625002, EBI-396176;
P24593:IGFBP5; NbExp=3; IntAct=EBI-625022, EBI-720480;
P05412:JUN; NbExp=4; IntAct=EBI-625002, EBI-852823;
Q8TAF8:LHFPL5; NbExp=3; IntAct=EBI-625022, EBI-2820517;
Q6FG55:LTA; NbExp=3; IntAct=EBI-625022, EBI-11984863;
Q99735:MGST2; NbExp=3; IntAct=EBI-625022, EBI-11324706;
Q99519:NEU1; NbExp=3; IntAct=EBI-625022, EBI-721517;
P26678:PLN; NbExp=3; IntAct=EBI-625022, EBI-692836;
P60201-2:PLP1; NbExp=3; IntAct=EBI-625022, EBI-12188331;
Q01453:PMP22; NbExp=3; IntAct=EBI-625022, EBI-2845982;
P05155:SERPING1; NbExp=3; IntAct=EBI-625022, EBI-1223454;
P11686:SFTPC; NbExp=3; IntAct=EBI-625022, EBI-10197617;
Q9BZD2:SLC29A3; NbExp=3; IntAct=EBI-625022, EBI-12701374;
P11166:SLC2A1; NbExp=3; IntAct=EBI-625022, EBI-717153;
P14672:SLC2A4; NbExp=3; IntAct=EBI-625022, EBI-367146;
Q9BRI3:SLC30A2; NbExp=3; IntAct=EBI-625022, EBI-8644112;
P82251:SLC7A9; NbExp=3; IntAct=EBI-625022, EBI-3936589;
O43759-2:SYNGR1; NbExp=3; IntAct=EBI-625022, EBI-12187159;
O00268:TAF4; NbExp=2; IntAct=EBI-625002, EBI-1034261;
Q8TAA9:VANGL1; NbExp=3; IntAct=EBI-625022, EBI-682393;
Q9Y397:ZDHHC9; NbExp=3; IntAct=EBI-625022, EBI-12690113;
-!- SUBCELLULAR LOCATION: Isoform 1: Endoplasmic reticulum membrane
{ECO:0000269|PubMed:10623756, ECO:0000269|PubMed:12138176,
ECO:0000269|PubMed:18391022}; Single-pass type II membrane protein
{ECO:0000255, ECO:0000269|PubMed:12138176}. Golgi apparatus
{ECO:0000269|PubMed:10623756}. Note=Colocalizes with HCFC1 in
neuronal cell bodies of the trigeminal ganglia (PubMed:10623756).
Colocalizes with DCSTAMP in the ER membrane of immature dendritic
cell (DC) (PubMed:20546900). Colocalizes with CANX, CCR1, HCFC1 in
the ER membrane (PubMed:10623756). {ECO:0000269|PubMed:10623756,
ECO:0000269|PubMed:20546900}.
-!- SUBCELLULAR LOCATION: Isoform 2: Nucleus
{ECO:0000269|PubMed:19779205}. Cytoplasm
{ECO:0000269|PubMed:19779205}. Note=Predominantly in the nucleus
(PubMed:19779205). Not associated with membranes
(PubMed:19779205). {ECO:0000269|PubMed:19779205}.
-!- SUBCELLULAR LOCATION: Processed cyclic AMP-responsive element-
binding protein 3: Nucleus. Note=Upon RIP activation the
transcriptional active processed cyclic AMP-responsive element-
binding protein 3 form translocates into the nucleus. Detected in
the nucleus upon dendritic cell maturation and RIP activation.
Colocalizes with CREBRF in nuclear foci. Colocalizes with CREBZF
in promyelocytic leukemia protein nuclear bodies (PML-NB).
{ECO:0000269|PubMed:10675342, ECO:0000269|PubMed:15705566,
ECO:0000269|PubMed:18391022, ECO:0000269|PubMed:20546900}.
-!- SUBCELLULAR LOCATION: Isoform 1: Cytoplasm. Note=(Microbial
infection) Sequestered into the cytoplasm by the HCV core protein.
{ECO:0000269|PubMed:10675342}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1; Synonyms=LZIP;
IsoId=O43889-2; Sequence=Displayed;
Name=2; Synonyms=small LZIP, sLZIP;
IsoId=O43889-3; Sequence=VSP_059386;
Note=Does not contain a helical transmembrane domain.;
-!- TISSUE SPECIFICITY: Ubiquitously expressed (PubMed:9271389,
PubMed:19779205). Expressed in dendritic cells (DC). Weakly
expressed in monocytes (at protein level) (PubMed:20546900).
{ECO:0000269|PubMed:19779205, ECO:0000269|PubMed:20546900,
ECO:0000269|PubMed:9271389}.
-!- INDUCTION: Up-regulated upon differentiation of monocytes towards
immature dendritic cells (DC). Down-regulated upon DC maturation.
Up-regulated by endoplasmic reticulum stress triggered by
thapsigargin (Tg) or tunicamycin (Tm). Up-regulated by CCR1-
dependent chemokines in an immediate early response and biphasic
manner and by NF-kappa-B. {ECO:0000269|PubMed:15845366,
ECO:0000269|PubMed:16940180, ECO:0000269|PubMed:17296613,
ECO:0000269|PubMed:18391022, ECO:0000269|PubMed:20546900}.
-!- PTM: First proteolytically cleaved by site-1 protease (S1P) that
generates membrane-associated N-terminus and a luminal C-terminus
forms. The membrane-associated N-terminus form is further
proteolytically processed probably by the site-2 protease (S2P)
through a regulated intramembrane proteolysis (RIP), releasing the
transcriptional active processed cyclic AMP-responsive element-
binding protein 3 form, which is transported to the nucleus. The
proteolytic cleavage is strongly induced during dendritic cell
(DC) maturation and inhibited by DCSTAMP. That form is rapidly
degraded. {ECO:0000269|PubMed:12138176,
ECO:0000269|PubMed:16940180, ECO:0000269|PubMed:17054986,
ECO:0000269|PubMed:18391022, ECO:0000269|PubMed:20546900}.
-!- PTM: N-glycosylated. {ECO:0000269|PubMed:12138176,
ECO:0000269|PubMed:16940180}.
-!- SIMILARITY: Belongs to the bZIP family. ATF subfamily.
{ECO:0000305}.
-!- CAUTION: All experiments concerning the proteolytic cleavage are
done with isoform 1. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAC04325.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AF009368; AAB69652.1; -; mRNA.
EMBL; AF029674; AAB84166.1; -; mRNA.
EMBL; U59629; AAD09210.1; -; Genomic_DNA.
EMBL; FJ263669; ACN32251.1; -; mRNA.
EMBL; U88528; AAC04325.1; ALT_SEQ; mRNA.
EMBL; AF211847; AAG43527.1; -; Genomic_DNA.
EMBL; AF211848; AAG43528.1; -; mRNA.
EMBL; AL133410; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC009402; AAH09402.1; -; mRNA.
EMBL; BC010158; AAH10158.1; -; mRNA.
CCDS; CCDS6588.1; -. [O43889-2]
RefSeq; NP_006359.3; NM_006368.4. [O43889-2]
UniGene; Hs.522110; -.
ProteinModelPortal; O43889; -.
SMR; O43889; -.
BioGrid; 115751; 191.
DIP; DIP-33935N; -.
ELM; O43889; -.
IntAct; O43889; 169.
MINT; O43889; -.
iPTMnet; O43889; -.
PhosphoSitePlus; O43889; -.
BioMuta; CREB3; -.
PeptideAtlas; O43889; -.
PRIDE; O43889; -.
ProteomicsDB; 49216; -.
ProteomicsDB; 49217; -. [O43889-2]
ProteomicsDB; 49218; -. [O43889-3]
DNASU; 10488; -.
Ensembl; ENST00000353704; ENSP00000342136; ENSG00000107175. [O43889-2]
GeneID; 10488; -.
KEGG; hsa:10488; -.
UCSC; uc003zxv.4; human. [O43889-2]
CTD; 10488; -.
DisGeNET; 10488; -.
EuPathDB; HostDB:ENSG00000107175.10; -.
GeneCards; CREB3; -.
HGNC; HGNC:2347; CREB3.
HPA; HPA030978; -.
MIM; 606443; gene.
neXtProt; NX_O43889; -.
OpenTargets; ENSG00000107175; -.
PharmGKB; PA26865; -.
GeneTree; ENSGT00520000055538; -.
HOGENOM; HOG000133026; -.
HOVERGEN; HBG051114; -.
InParanoid; O43889; -.
KO; K09048; -.
OMA; HVSIDLD; -.
PhylomeDB; O43889; -.
TreeFam; TF316079; -.
Reactome; R-HSA-8874211; CREB3 factors activate genes.
SIGNOR; O43889; -.
ChiTaRS; CREB3; human.
GeneWiki; CREB3; -.
GenomeRNAi; 10488; -.
PRO; PR:O43889; -.
Proteomes; UP000005640; Chromosome 9.
Bgee; ENSG00000107175; -.
CleanEx; HS_CREB3; -.
Genevisible; O43889; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0005783; C:endoplasmic reticulum; IDA:ParkinsonsUK-UCL.
GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
GO; GO:0005794; C:Golgi apparatus; IMP:UniProtKB.
GO; GO:0000139; C:Golgi membrane; IDA:UniProtKB.
GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IDA:UniProtKB.
GO; GO:0016021; C:integral component of membrane; IDA:UniProtKB.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0043025; C:neuronal cell body; IDA:UniProtKB.
GO; GO:0016604; C:nuclear body; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0035497; F:cAMP response element binding; IEA:InterPro.
GO; GO:0008140; F:cAMP response element binding protein binding; IDA:UniProtKB.
GO; GO:0031726; F:CCR1 chemokine receptor binding; IDA:UniProtKB.
GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
GO; GO:0003700; F:DNA binding transcription factor activity; IDA:UniProtKB.
GO; GO:0046983; F:protein dimerization activity; TAS:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
GO; GO:0000978; F:RNA polymerase II proximal promoter sequence-specific DNA binding; IDA:NTNU_SB.
GO; GO:0000977; F:RNA polymerase II regulatory region sequence-specific DNA binding; IDA:ParkinsonsUK-UCL.
GO; GO:0000981; F:RNA polymerase II transcription factor activity, sequence-specific DNA binding; ISA:NTNU_SB.
GO; GO:0000982; F:transcription factor activity, RNA polymerase II proximal promoter sequence-specific DNA binding; IDA:NTNU_SB.
GO; GO:0001077; F:transcriptional activator activity, RNA polymerase II proximal promoter sequence-specific DNA binding; IMP:NTNU_SB.
GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-KW.
GO; GO:0042994; P:cytoplasmic sequestering of transcription factor; IDA:UniProtKB.
GO; GO:0030968; P:endoplasmic reticulum unfolded protein response; TAS:Reactome.
GO; GO:0019043; P:establishment of viral latency; IDA:UniProtKB.
GO; GO:0050930; P:induction of positive chemotaxis; IDA:UniProtKB.
GO; GO:0045786; P:negative regulation of cell cycle; NAS:UniProtKB.
GO; GO:1902236; P:negative regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway; IDA:ParkinsonsUK-UCL.
GO; GO:2000326; P:negative regulation of ligand-dependent nuclear receptor transcription coactivator activity; IDA:UniProtKB.
GO; GO:0051928; P:positive regulation of calcium ion transport; IMP:UniProtKB.
GO; GO:0030335; P:positive regulation of cell migration; IMP:UniProtKB.
GO; GO:0090045; P:positive regulation of deacetylase activity; IDA:UniProtKB.
GO; GO:0002230; P:positive regulation of defense response to virus by host; IDA:UniProtKB.
GO; GO:0090026; P:positive regulation of monocyte chemotaxis; IDA:UniProtKB.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB.
GO; GO:0006990; P:positive regulation of transcription from RNA polymerase II promoter involved in unfolded protein response; IDA:ParkinsonsUK-UCL.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0042981; P:regulation of apoptotic process; IDA:UniProtKB.
GO; GO:0001558; P:regulation of cell growth; IDA:UniProtKB.
GO; GO:0042127; P:regulation of cell proliferation; IMP:UniProtKB.
GO; GO:0019046; P:release from viral latency; IDA:UniProtKB.
GO; GO:0034976; P:response to endoplasmic reticulum stress; IDA:UniProtKB.
GO; GO:0006351; P:transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
InterPro; IPR004827; bZIP.
InterPro; IPR029808; Luman.
PANTHER; PTHR22952:SF100; PTHR22952:SF100; 1.
Pfam; PF00170; bZIP_1; 1.
SMART; SM00338; BRLZ; 1.
PROSITE; PS50217; BZIP; 1.
PROSITE; PS00036; BZIP_BASIC; 1.
1: Evidence at protein level;
Activator; Alternative splicing; Chemotaxis; Complete proteome;
Cytoplasm; DNA-binding; Endoplasmic reticulum; Glycoprotein;
Golgi apparatus; Host-virus interaction; Membrane; Nucleus;
Reference proteome; Repeat; Repressor; Signal-anchor; Transcription;
Transcription regulation; Transmembrane; Transmembrane helix;
Unfolded protein response.
CHAIN 1 371 Cyclic AMP-responsive element-binding
protein 3.
/FTId=PRO_0000076602.
CHAIN 1 ? Processed cyclic AMP-responsive element-
binding protein 3.
/FTId=PRO_0000296204.
TOPO_DOM 1 230 Cytoplasmic.
{ECO:0000269|PubMed:12138176}.
TRANSMEM 231 247 Helical; Signal-anchor for type II
membrane protein. {ECO:0000255}.
TOPO_DOM 248 371 Lumenal. {ECO:0000269|PubMed:12138176}.
DOMAIN 150 213 bZIP. {ECO:0000255|PROSITE-
ProRule:PRU00978}.
REGION 1 92 Transcription activation (acidic).
{ECO:0000269|PubMed:10984507}.
REGION 152 184 Basic motif. {ECO:0000255|PROSITE-
ProRule:PRU00978}.
REGION 192 213 Leucine-zipper. {ECO:0000255|PROSITE-
ProRule:PRU00978}.
MOTIF 13 17 LXXLL motif 1.
MOTIF 54 58 LXXLL motif 2.
MOTIF 78 81 HCFC1-binding-motif (HBM).
COMPBIAS 316 361 Pro-rich.
SITE 263 264 Cleavage; by PS1.
{ECO:0000269|PubMed:12138176}.
SITE 266 267 Cleavage; by PS1.
{ECO:0000269|PubMed:12138176}.
CARBOHYD 307 307 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 348 348 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
VAR_SEQ 229 245 Missing (in isoform 2).
/FTId=VSP_059386.
MUTAGEN 12 13 LL->AA: Does not inhibit interaction with
HCFC1. Reduces transcriptional
activation. Inhibits strongly
transcriptional activation; when
associated with 56-A-A-57 and 78-A--A-81
(isoform 1).
{ECO:0000269|PubMed:10984507}.
MUTAGEN 16 17 LL->AA: Does not affect the
transcriptional activation of the
glucocorticoid receptor NR3C1; when
associated with 57-A-A-58 (isoform 2).
{ECO:0000269|PubMed:10984507,
ECO:0000269|PubMed:19779205}.
MUTAGEN 57 58 LL->AA: Does not affect the
transcriptional activation of the
glucocorticoid receptor NR3C1; when
associated with 16-A-A-17 (isoform 2).
{ECO:0000269|PubMed:19779205}.
MUTAGEN 57 58 LL->AA: Does not inhibit interaction with
HCFC1. Reduces transcriptional
activation. Inhibits strongly
transcriptional activation; when
associated with 12-A-A-13 and 78-A--A-81
(isoform 1).
{ECO:0000269|PubMed:19779205}.
MUTAGEN 78 81 DHTY->AAAA: Inhibits interaction with
HCFC1. Reduces transcriptional
activation. Inhibits strongly
transcriptional activation; when
associated with 12-A-A-13 and 56-A-A-57.
Colocalizes with HCFC1 in the nucleus
(isoform 1).
{ECO:0000269|PubMed:10984507,
ECO:0000269|PubMed:15705566}.
MUTAGEN 81 81 Y->A: Does not retain HCFC1 in the
cytoplasm, does not interact with HCFC1,
does not activate promoter and fail to
protect cells from a productive infection
by HSV-1. {ECO:0000269|PubMed:10623756}.
MUTAGEN 160 160 N->G: Does not bind to DNA but retains
its ability to interact with HCFC1.
Reduces transcriptional activation of
unfolded protein response elements
(UPRE)-containing promoter. Colocalizes
with HCFC1 in the ER membrane.
{ECO:0000269|PubMed:15705566}.
MUTAGEN 252 252 R->A: Does not inhibit proteolytic
cleavage and transcriptional activation.
{ECO:0000269|PubMed:12138176}.
MUTAGEN 264 264 R->G: Inhibits proteolytic cleavage and
transcriptional activation.
{ECO:0000269|PubMed:12138176}.
MUTAGEN 267 267 R->G: Inhibits proteolytic cleavage and
transcriptional activation.
{ECO:0000269|PubMed:12138176}.
CONFLICT 21 21 G -> E (in Ref. 6; AAG43527).
{ECO:0000305}.
CONFLICT 230 230 C -> G (in Ref. 3; AAD09210).
{ECO:0000305}.
CONFLICT 246 246 M -> I (in Ref. 8; AAH09402).
{ECO:0000305}.
CONFLICT 262 262 L -> C (in Ref. 3; AAD09210).
{ECO:0000305}.
CONFLICT 333 333 F -> S (in Ref. 1; AAB69652).
{ECO:0000305}.
CONFLICT 338 338 C -> V (in Ref. 3; AAD09210).
{ECO:0000305}.
SEQUENCE 371 AA; 41379 MW; 82152E496B924EEC CRC64;
MELELDAGDQ DLLAFLLEES GDLGTAPDEA VRAPLDWALP LSEVPSDWEV DDLLCSLLSP
PASLNILSSS NPCLVHHDHT YSLPRETVSM DLESESCRKE GTQMTPQHME ELAEQEIARL
VLTDEEKSLL EKEGLILPET LPLTKTEEQI LKRVRRKIRN KRSAQESRRK KKVYVGGLES
RVLKYTAQNM ELQNKVQLLE EQNLSLLDQL RKLQAMVIEI SNKTSSSSTC ILVLLVSFCL
LLVPAMYSSD TRGSLPAEHG VLSRQLRALP SEDPYQLELP ALQSEVPKDS THQWLDGSDC
VLQAPGNTSC LLHYMPQAPS AEPPLEWPFP DLFSEPLCRG PILPLQANLT RKGGWLPTGS
PSVILQDRYS G


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