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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;         395 AA.
O43889; D0PTW6; O14671; O14919; Q5TCV1; Q96GK8; Q9H2W3; Q9UE77;
09-NOV-2004, integrated into UniProtKB/Swiss-Prot.
01-JUN-1998, sequence version 1.
27-SEP-2017, entry version 165.
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 2), NUCLEAR FUNCTION IN
TRANSCRIPTIONAL REGULATION, DNA-BINDING, 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 2), INTERACTION WITH HCFC1, AND
TISSUE SPECIFICITY.
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 2), FUNCTION IN CELL
PROLIFERATION, HOMODIMERIZATION, INTERACTION WITH HCV CORE PROTEIN,
DNA-BINDING, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
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 3), ALTERNATIVE SPLICING (ISOFORM
2), FUNCTION IN LKN-1-STIMULATED CHEMOTAXIS SIGNALING (ISOFORM 2),
FUNCTION IN GLUCOCORTICOID-INDUCED TRANSCRIPTIONAL REPRESSION (ISOFORM
3), SUBCELLULAR LOCATION, TISSUE SPECIFICITY, 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 2).
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 2).
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 (ISOFORM 2), MUTAGENESIS OF TYR-81, AND
SUBCELLULAR LOCATION.
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 2), INTERACTION WITH
HCFC1, TRANSCRIPTIONAL ACTIVATION DOMAIN, 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, PROTEOLYTIC PROCESSING, CLEAVAGE
SITE, AND MUTAGENESIS OF ARG-276; ARG-288 AND ARG-291.
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 (ISOFORM 2),
INTERACTION WITH CCR1, AND SUBCELLULAR LOCATION.
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 (ISOFORM 2), DNA-BINDING,
ABSENCE OF PROTEOLYTIC CLEAVAGE, 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 (ISOFORM 2), INTERACTION WITH CREBZF AND HCFC1, SUBCELLULAR
LOCATION, AND MUTAGENESIS OF 78-ASP--TYR-81 AND ASN-184.
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 (ISOFORM 2), INTERACTION WITH HIV-1 ENV,
INTERACTION WITH HIV-1 TMGP41, SUBCELLULAR LOCATION, 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 (ISOFORM 2), 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 (ISOFORM 2), 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]
FUNCTION, INTERACTION WITH OS9 AND TM7SF4, 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 transcription factor
that plays a role in the unfolded protein response (UPR). Involved
in cell proliferation and migration, tumor suppression and
inflammatory gene expression. Plays also a role in the human
immunodeficiency virus type 1 (HIV-1) virus protein expression and
in the herpes simplex virus-1 (HSV-1) latent infection and
reactivation from latency. Isoform 2 plays a role in the unfolded
protein response (UPR). Isoform 2 acts as a positive regulator of
LKN-1/CCL15-induced chemotaxis signaling of leukocyte cell
migration. Isoform 2 may play a role as a cellular tumor
suppressor that is targeted by the hepatitis C virus (HSV) core
protein. Isoform 2 represses the VP16-mediated transactivation of
immediate early genes of the HSV-1 virus by sequestring host cell
factor-1 HCFC1 in the ER membrane of sensory neurons, thereby
preventing the initiation of the replicative cascade leading to
latent infection. Isoform 3 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). Isoform
3 decreases the acetylation level of histone H4. Isoform 3 does
not promote the chemotactic activity of leukocyte cells.
-!- FUNCTION: Processed cyclic AMP-responsive element-binding protein
3: acts as a transcription factor that activates unfolded protein
response (UPR) target genes during endoplasmic reticulum (ER)
stress response. Promotes cell survival against ER stress-induced
apoptotic cell death during UPR. Activates transcription from CRE
and C/EBP-containing reporter genes. Induces transcriptional
activation of chemokine receptors. Activates transcription of
genes required for reactivation of the latent HSV-1 virus. Down-
regulates Tat-dependent transcription of the HIV-1 LTR by
interacting with HIV-1 Tat. It's transcriptional activity is
inhibited by CREBZF in a HCFC1-dependent manner, by the viral
transactivator protein VP16 and by the HCV core protein. Binds DNA
to the cAMP response element (CRE) (consensus: 5'-GTGACGT[AG][AG]-
3') and C/EBP sequences present in many viral and cellular
promoters. Binds to the unfolded protein respons element (UPRE)
consensus sequences sites. Binds DNA to the 5'-CCAC[GA]-3'half of
ERSE II (5'-ATTGG-N-CCACG-3'). Associates with chromatin to the
HERPUD1 promoter.
-!- SUBUNIT: Homodimer; homodimerization is prevented by the HCV core
protein. Interacts with HCFC1; the interaction is required to
stimulate CREB3 transcriptional activity. Isoform 2 interacts with
CREBZF; the interaction occurs only in combination with HCFC1.
Isoform 2 interacts (via central part and transmembrane region)
with TM7SF4 (via C-terminus cytoplasmic domain). Isoform 2
interacts with OS9. Isoform 2 interacts (via leucine-zipper
domain) with CREBRF (via leucine-zipper domain); the interaction
occurs only after CREB3 activation and promotes CREB3 degradation.
Isoform 2 interacts (via C-terminal domain) with CCR1. Isoform 2
interacts (via leucine-zipper and transmembrane domains) with HIV-
1 ENV (via cytoplasmic domain). Isoform 2 interacts (via leucine-
zipper and transmembrane domains) with HIV-1 TMgp41 (via
cytoplasmic domain); the interaction reduces CREB3 stability.
Interacts with the HCV core protein. Processed cyclic AMP-
responsive element-binding protein 3 interacts with HIV-1 Tat.
{ECO:0000269|PubMed:10629049, ECO:0000269|PubMed:10675342,
ECO:0000269|PubMed:10984507, ECO:0000269|PubMed:15001559,
ECO:0000269|PubMed:15705566, ECO:0000269|PubMed:17054986,
ECO:0000269|PubMed:18391022, ECO:0000269|PubMed:20546900,
ECO:0000269|PubMed:9389645}.
-!- 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;
Q8TAA9:VANGL1; NbExp=3; IntAct=EBI-625022, EBI-682393;
Q9Y397:ZDHHC9; NbExp=3; IntAct=EBI-625022, EBI-12690113;
-!- SUBCELLULAR LOCATION: Isoform 2: Endoplasmic reticulum membrane;
Single-pass type II membrane protein. Membrane. Note=Colocalizes
with HCFC1 in neuronal cell bodies of the trigeminal ganglia (By
similarity). Colocalizes with TM7SF4 in the ER membrane of
immature dendritic cell (DC). Colocalizes with CANX, CCR1, HCFC1
in the ER membrane. Sequestred into the cytoplasm by the HCV core
protein. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Isoform 3: Nucleus. Cytoplasm.
Note=Predominantly in the nucleus.
-!- 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).
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=O43889-1; Sequence=Displayed;
Name=2; Synonyms=LZIP;
IsoId=O43889-2; Sequence=VSP_011838;
Name=3; Synonyms=smal LZIP, sLZIP;
IsoId=O43889-3; Sequence=VSP_011838, VSP_043805;
Note=Does not contain a helical transmembrane domain.;
-!- TISSUE SPECIFICITY: Expressed in dendritic cells (DC). Weakly
expressed in monocytes (at protein level). Ubiquitous.
{ECO:0000269|PubMed:10675342, ECO:0000269|PubMed:19779205,
ECO:0000269|PubMed:20546900, ECO:0000269|PubMed:9271389,
ECO:0000269|PubMed:9389645}.
-!- 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: The ER membrane embedded cyclic AMP-responsive element-
binding protein 3 form is 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 TM7SF4.
-!- PTM: The processed cyclic AMP-responsive element-binding protein 3
is rapidly degraded.
-!- 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 2. {ECO:0000305}.
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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; -; mRNA.
EMBL; AF211847; AAG43527.1; -; Genomic_DNA.
EMBL; AF211848; AAG43528.1; -; mRNA.
EMBL; AL133410; CAI10980.1; -; 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; 190.
DIP; DIP-33935N; -.
ELM; O43889; -.
IntAct; O43889; 168.
MINT; MINT-1446829; -.
iPTMnet; O43889; -.
PhosphoSitePlus; O43889; -.
BioMuta; CREB3; -.
PeptideAtlas; O43889; -.
PRIDE; O43889; -.
DNASU; 10488; -.
Ensembl; ENST00000353704; ENSP00000342136; ENSG00000107175. [O43889-2]
GeneID; 10488; -.
KEGG; hsa:10488; -.
UCSC; uc003zxv.4; human. [O43889-1]
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:0046983; F:protein dimerization activity; TAS:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
GO; GO:0000978; F:RNA polymerase II core promoter proximal region 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:0000982; F:transcription factor activity, RNA polymerase II core promoter proximal region sequence-specific binding; IDA:NTNU_SB.
GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IDA:UniProtKB.
GO; GO:0001077; F:transcriptional activator activity, RNA polymerase II core promoter proximal region sequence-specific 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 from RNA polymerase II promoter; 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:SF263; PTHR22952:SF263; 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;
Host-virus interaction; Membrane; Nucleus; Reference proteome; Repeat;
Repressor; Signal-anchor; Transcription; Transcription regulation;
Transmembrane; Transmembrane helix; Unfolded protein response.
CHAIN 1 395 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 1 254 Cytoplasmic. {ECO:0000255}.
TRANSMEM 255 271 Helical; Signal-anchor for type II
membrane protein. {ECO:0000255}.
TOPO_DOM 272 395 Lumenal. {ECO:0000255}.
DOMAIN 174 237 bZIP. {ECO:0000255|PROSITE-
ProRule:PRU00978}.
REGION 1 92 Transcription activation (acidic).
REGION 176 208 Basic motif. {ECO:0000255|PROSITE-
ProRule:PRU00978}.
REGION 216 237 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 340 385 Pro-rich.
SITE 287 288 Cleavage; by PS1. {ECO:0000305}.
SITE 290 291 Cleavage; by PS1. {ECO:0000305}.
CARBOHYD 331 331 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 372 372 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
VAR_SEQ 93 116 Missing (in isoform 2 and isoform 3).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:19779205,
ECO:0000303|PubMed:9271389,
ECO:0000303|PubMed:9389645,
ECO:0000303|Ref.6}.
/FTId=VSP_011838.
VAR_SEQ 253 269 Missing (in isoform 3).
{ECO:0000303|PubMed:19779205}.
/FTId=VSP_043805.
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 2).
{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 3).
{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 3).
{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 2).
{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 2).
{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 184 184 N->G: Does not bind to DNA but retains
its ability to interact with HCFC1.
Reduces transcriptional activation of
unfolded protein respons elements (UPRE)-
containing promoter. Colocalizes with
HCFC1 in the ER membrane.
{ECO:0000269|PubMed:15705566}.
MUTAGEN 276 276 R->A: Does not inhibit proteolytic
cleavage and transcriptional activation.
{ECO:0000269|PubMed:12138176}.
MUTAGEN 288 288 R->G: Inhibits proteolytic cleavage and
transcriptional activation.
{ECO:0000269|PubMed:12138176}.
MUTAGEN 291 291 R->G: Inhibits proteolytic cleavage and
transcriptional activation.
{ECO:0000269|PubMed:12138176}.
CONFLICT 21 21 G -> E (in Ref. 6; AAG43527).
{ECO:0000305}.
CONFLICT 254 254 C -> G (in Ref. 3; AAD09210).
{ECO:0000305}.
CONFLICT 270 270 M -> I (in Ref. 8; AAH09402).
{ECO:0000305}.
CONFLICT 286 286 L -> C (in Ref. 3; AAD09210).
{ECO:0000305}.
CONFLICT 357 357 F -> S (in Ref. 1; AAB69652).
{ECO:0000305}.
CONFLICT 362 362 C -> V (in Ref. 3; AAD09210).
{ECO:0000305}.
SEQUENCE 395 AA; 43917 MW; 1C412AA0D51CB7B2 CRC64;
MELELDAGDQ DLLAFLLEES GDLGTAPDEA VRAPLDWALP LSEVPSDWEV DDLLCSLLSP
PASLNILSSS NPCLVHHDHT YSLPRETVSM DLGECEISLT GRTGFMGLAI HTFPFAESES
CRKEGTQMTP QHMEELAEQE IARLVLTDEE KSLLEKEGLI LPETLPLTKT EEQILKRVRR
KIRNKRSAQE SRRKKKVYVG GLESRVLKYT AQNMELQNKV QLLEEQNLSL LDQLRKLQAM
VIEISNKTSS SSTCILVLLV SFCLLLVPAM YSSDTRGSLP AEHGVLSRQL RALPSEDPYQ
LELPALQSEV PKDSTHQWLD GSDCVLQAPG NTSCLLHYMP QAPSAEPPLE WPFPDLFSEP
LCRGPILPLQ ANLTRKGGWL PTGSPSVILQ DRYSG


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