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X-box-binding protein 1 (XBP-1) (Tax-responsive element-binding protein 5) (TREB-5) [Cleaved into: X-box-binding protein 1, cytoplasmic form; X-box-binding protein 1, luminal form]

 XBP1_HUMAN              Reviewed;         261 AA.
P17861; Q8WYK6; Q969P1; Q96BD7;
01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
01-MAR-2005, sequence version 2.
07-JUN-2017, entry version 179.
RecName: Full=X-box-binding protein 1 {ECO:0000303|PubMed:2321018, ECO:0000312|HGNC:HGNC:12801};
Short=XBP-1 {ECO:0000303|PubMed:2321018};
AltName: Full=Tax-responsive element-binding protein 5 {ECO:0000303|PubMed:2196176};
Short=TREB-5 {ECO:0000303|PubMed:2196176};
Contains:
RecName: Full=X-box-binding protein 1, cytoplasmic form {ECO:0000303|PubMed:25239945};
Contains:
RecName: Full=X-box-binding protein 1, luminal form {ECO:0000303|PubMed:25239945};
Name=XBP1 {ECO:0000312|HGNC:HGNC:12801};
Synonyms=TREB5 {ECO:0000303|PubMed:2196176},
XBP2 {ECO:0000312|HGNC:HGNC:12801};
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), AND
DNA-BINDING (ISOFORM 1).
TISSUE=B-cell;
PubMed=2321018; DOI=10.1126/science.2321018;
Liou H.-C., Boothby M.R., Finn P.W., Davidon R., Nabavi N.,
Zeleznik-Le N.J., Ting J.P.-Y., Glimcher L.H.;
"A new member of the leucine zipper class of proteins that binds to
the HLA DR alpha promoter.";
Science 247:1581-1584(1990).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION (ISOFORM 1), AND
DNA-BINDING (ISOFORM 1).
PubMed=2196176;
Yoshimura T., Fujisawa J., Yoshida M.;
"Multiple cDNA clones encoding nuclear proteins that bind to the tax-
dependent enhancer of HTLV-1: all contain a leucine zipper structure
and basic amino acid domain.";
EMBO J. 9:2537-2542(1990).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND DNA-BINDING.
PubMed=8349596;
Ponath P.D., Fass D., Liou H.C., Glimcher L.H., Strominger J.L.;
"The regulatory gene, hXBP-1, and its target, HLA-DRA, utilize both
common and distinct regulatory elements and protein complexes.";
J. Biol. Chem. 268:17074-17082(1993).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION (ISOFORM 2),
ALTERNATIVE SPLICING (ISOFORM 2), DNA-BINDING (ISOFORMS 1 AND 2),
INDUCTION (ISOFORM 2), ER STRESS-MEDIATED DOWN-REGULATION (ISOFORM 1),
AND DOMAIN ((ISOFORMS 1 AND 2).
PubMed=11779464; DOI=10.1016/S0092-8674(01)00611-0;
Yoshida H., Matsui T., Yamamoto A., Okada T., Mori K.;
"XBP1 mRNA is induced by ATF6 and spliced by IRE1 in response to ER
stress to produce a highly active transcription factor.";
Cell 107:881-891(2001).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
Beare D.M., Dunham I.;
"A genome annotation-driven approach to cloning the human ORFeome.";
Genome Biol. 5:R84.1-R84.11(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=10591208; DOI=10.1038/990031;
Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M.,
Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K.,
Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P.,
Bird C.P., Blakey S.E., Bridgeman A.M., Buck D., Burgess J.,
Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G.,
Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R.,
Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E.,
Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G.,
Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S.,
Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A.,
Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M.,
Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T.,
Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J.,
Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T.,
Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T.,
Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L.,
Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M.,
Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J.,
Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S.,
Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T.,
Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I.,
Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H.,
Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L.,
Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z.,
Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P.,
Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S.,
Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J.,
Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T.,
Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J.,
Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S.,
Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E.,
Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P.,
Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E.,
O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X.,
Khan A.S., Lane L., Tilahun Y., Wright H.;
"The DNA sequence of human chromosome 22.";
Nature 402:489-495(1999).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Ovary, and 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).
[8]
FUNCTION (ISOFORM 1), DNA-BINDING (ISOFORM 1), AND INTERACTION WITH
FOS (ISOFORM 1).
PubMed=1903538; DOI=10.1073/pnas.88.10.4309;
Ono S.J., Liou H.C., Davidon R., Strominger J.L., Glimcher L.H.;
"Human X-box-binding protein 1 is required for the transcription of a
subset of human class II major histocompatibility genes and forms a
heterodimer with c-fos.";
Proc. Natl. Acad. Sci. U.S.A. 88:4309-4312(1991).
[9]
INDUCTION.
PubMed=8627152; DOI=10.1084/jem.183.2.393;
Reimold A.M., Ponath P.D., Li Y.S., Hardy R.R., David C.S.,
Strominger J.L., Glimcher L.H.;
"Transcription factor B cell lineage-specific activator protein
regulates the gene for human X-box binding protein 1.";
J. Exp. Med. 183:393-401(1996).
[10]
FUNCTION (ISOFORM 1), DNA-BINDING (ISOFORM 1), AND DOMAIN (ISOFORMS 1
AND 2).
PubMed=8657566; DOI=10.1093/nar/24.10.1855;
Clauss I.M., Chu M., Zhao J.-L., Glimcher L.H.;
"The basic domain/leucine zipper protein hXBP-1 preferentially binds
to and transactivates CRE-like sequences containing an ACGT core.";
Nucleic Acids Res. 24:1855-1864(1996).
[11]
INDUCTION.
PubMed=10375612;
Wen X.Y., Stewart A.K., Sooknanan R.R., Henderson G., Hawley T.S.,
Reimold A.M., Glimcher L.H., Baumann H., Malek L.T., Hawley R.G.;
"Identification of c-myc promoter-binding protein and X-box binding
protein 1 as interleukin-6 target genes in human multiple myeloma
cells.";
Int. J. Oncol. 15:173-178(1999).
[12]
FUNCTION, INDUCTION, AND TISSUE SPECIFICITY.
PubMed=11460154; DOI=10.1038/35085509;
Reimold A.M., Iwakoshi N.N., Manis J., Vallabhajosyula P.,
Szomolanyi-Tsuda E., Gravallese E.M., Friend D., Grusby M.J., Alt F.,
Glimcher L.H.;
"Plasma cell differentiation requires the transcription factor XBP-
1.";
Nature 412:300-307(2001).
[13]
INVOLVEMENT IN SUSCEPTIBILITY TO MAJOR AFFECTIVE DISORDER TYPE 7.
PubMed=12949534; DOI=10.1038/ng1235;
Kakiuchi C., Iwamoto K., Ishiwata M., Bundo M., Kasahara T.,
Kusumi I., Tsujita T., Okazaki Y., Nanko S., Kunugi H., Sasaki T.,
Kato T.;
"Impaired feedback regulation of XBP1 as a genetic risk factor for
bipolar disorder.";
Nat. Genet. 35:171-175(2003).
[14]
FUNCTION (ISOFORM 2).
PubMed=15466483; DOI=10.1083/jcb.200406136;
Sriburi R., Jackowski S., Mori K., Brewer J.W.;
"XBP1: a link between the unfolded protein response, lipid
biosynthesis, and biogenesis of the endoplasmic reticulum.";
J. Cell Biol. 167:35-41(2004).
[15]
INDUCTION (ISOFORM 2).
PubMed=17110785; DOI=10.1247/csf.06016;
Yoshida H., Nadanaka S., Sato R., Mori K.;
"XBP1 is critical to protect cells from endoplasmic reticulum stress:
evidence from Site-2 protease-deficient Chinese hamster ovary cells.";
Cell Struct. Funct. 31:117-125(2006).
[16]
FUNCTION (ISOFORMS 1 AND 2), INTERACTION WITH XBP1 ISOFORM 2 (ISOFORM
1), SUBCELLULAR LOCATION (ISOFORMS 1 AND 2), INDUCTION (ISOFORMS 1 AND
2), STRESS-MEDIATED DOWN-REGULATION (ISOFORM 1), AND DOMAIN (ISOFORMS
1 AND 2).
PubMed=16461360; DOI=10.1083/jcb.200508145;
Yoshida H., Oku M., Suzuki M., Mori K.;
"pXBP1(U) encoded in XBP1 pre-mRNA negatively regulates unfolded
protein response activator pXBP1(S) in mammalian ER stress response.";
J. Cell Biol. 172:565-575(2006).
[17]
INTERACTION WITH ATF6 (ISOFORM 2).
PubMed=17765680; DOI=10.1016/j.devcel.2007.07.018;
Yamamoto K., Sato T., Matsui T., Sato M., Okada T., Yoshida H.,
Harada A., Mori K.;
"Transcriptional induction of mammalian ER quality control proteins is
mediated by single or combined action of ATF6alpha and XBP1.";
Dev. Cell 13:365-376(2007).
[18]
UNCONVENTIONAL ALTERNATIVE SPLICING (ISOFORM 2).
PubMed=19622636; DOI=10.1242/jcs.040584;
Uemura A., Oku M., Mori K., Yoshida H.;
"Unconventional splicing of XBP1 mRNA occurs in the cytoplasm during
the mammalian unfolded protein response.";
J. Cell Sci. 122:2877-2886(2009).
[19]
FUNCTION (ISOFORM 1), SUBCELLULAR LOCATION (ISOFORMS 1 AND 2),
TOPOLOGY (ISOFORM 1), DOMAIN (ISOFORM 1), AND MUTAGENESIS OF TRP-189;
VAL-193; LEU-194; LEU-196; ILE-198 AND TRP-205.
PubMed=19394296; DOI=10.1016/j.molcel.2009.02.033;
Yanagitani K., Imagawa Y., Iwawaki T., Hosoda A., Saito M., Kimata Y.,
Kohno K.;
"Cotranslational targeting of XBP1 protein to the membrane promotes
cytoplasmic splicing of its own mRNA.";
Mol. Cell 34:191-200(2009).
[20]
FUNCTION (ISOFORM 2), DNA-BINDING (ISOFORMS 1 AND 2), INDUCTION
(ISOFORMS 1 AND 2), AND TISSUE SPECIFICITY (ISOFORMS 1 AND 2).
PubMed=19416856; DOI=10.1073/pnas.0903197106;
Zeng L., Zampetaki A., Margariti A., Pepe A.E., Alam S., Martin D.,
Xiao Q., Wang W., Jin Z.G., Cockerill G., Mori K., Li Y.S., Hu Y.,
Chien S., Xu Q.;
"Sustained activation of XBP1 splicing leads to endothelial apoptosis
and atherosclerosis development in response to disturbed flow.";
Proc. Natl. Acad. Sci. U.S.A. 106:8326-8331(2009).
[21]
FUNCTION, INTERACTION WITH PIK3R1 (ISOFORM 2), AND SUBCELLULAR
LOCATION (ISOFORMS 1 AND 2).
PubMed=20348923; DOI=10.1038/nm.2121;
Winnay J.N., Boucher J., Mori M.A., Ueki K., Kahn C.R.;
"A regulatory subunit of phosphoinositide 3-kinase increases the
nuclear accumulation of X-box-binding protein-1 to modulate the
unfolded protein response.";
Nat. Med. 16:438-445(2010).
[22]
ACETYLATION BY EP300 (ISOFORM 2), DEACETYLATION BY SIRT1 (ISOFORM 2),
AND SUBCELLULAR LOCATION (ISOFORM 2).
PubMed=20955178; DOI=10.1042/BJ20101293;
Wang F.M., Chen Y.J., Ouyang H.J.;
"Regulation of unfolded protein response modulator XBP1s by
acetylation and deacetylation.";
Biochem. J. 433:245-252(2011).
[23]
FUNCTION (ISOFORM 1), DOMAIN (ISOFORM 1), AND MUTAGENESIS OF LEU-246;
SER-255 AND TRP-256.
PubMed=21233347; DOI=10.1126/science.1197142;
Yanagitani K., Kimata Y., Kadokura H., Kohno K.;
"Translational pausing ensures membrane targeting and cytoplasmic
splicing of XBP1u mRNA.";
Science 331:586-589(2011).
[24]
FUNCTION (ISOFORMS 1 AND 2), SUBCELLULAR LOCATION, AND INDUCTION
(ISOFORM 2).
PubMed=23529610; DOI=10.1161/CIRCULATIONAHA.112.001337;
Zeng L., Xiao Q., Chen M., Margariti A., Martin D., Ivetic A., Xu H.,
Mason J., Wang W., Cockerill G., Mori K., Li J.Y., Chien S., Hu Y.,
Xu Q.;
"Vascular endothelial cell growth-activated XBP1 splicing in
endothelial cells is crucial for angiogenesis.";
Circulation 127:1712-1722(2013).
[25]
FUNCTION (ISOFORM 2), DNA-BINDING (ISOFORM 2), AND INDUCTION (ISOFORM
2).
PubMed=23184933; DOI=10.1074/jbc.M112.412783;
Margariti A., Li H., Chen T., Martin D., Vizcay-Barrena G., Alam S.,
Karamariti E., Xiao Q., Zampetaki A., Zhang Z., Wang W., Jiang Z.,
Gao C., Ma B., Chen Y.G., Cockerill G., Hu Y., Xu Q., Zeng L.;
"XBP1 mRNA splicing triggers an autophagic response in endothelial
cells through BECLIN-1 transcriptional activation.";
J. Biol. Chem. 288:859-872(2013).
[26]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-47 AND SER-68, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[27]
FUNCTION (ISOFORM 2), AND TISSUE SPECIFICITY.
PubMed=25280941; DOI=10.1016/j.cellsig.2014.09.018;
Li H., Chen X., Gao Y., Wu J., Zeng F., Song F.;
"XBP1 induces snail expression to promote epithelial-to-mesenchymal
transition and invasion of breast cancer cells.";
Cell. Signal. 27:82-89(2015).
[28]
FUNCTION (ISOFORMS 1 AND 2), INTERACTION WITH DERL1; HM13; RNF139 AND
XBP1 ISOFORM 2 (ISOFORM 1), TOPOLOGY (ISOFORM 1), PROTEOLYTIC CLEAVAGE
(ISOFORM 1), SUBCELLULAR LOCATION (ISOFORM 1 AND CYTOPLASMIC FORM),
UBIQUITINATION (ISOFORM 1 AND LUMINAL FORM), STRESS-MEDIATED
DOWN-REGULATION (ISOFORM 2), AND MUTAGENESIS OF GLN-197; GLN-199;
SER-200; SER-203; THR-212; CYS-215 AND ARG-232.
PubMed=25239945; DOI=10.15252/embj.201488208;
Chen C.Y., Malchus N.S., Hehn B., Stelzer W., Avci D., Langosch D.,
Lemberg M.K.;
"Signal peptide peptidase functions in ERAD to cleave the unfolded
protein response regulator XBP1u.";
EMBO J. 33:2492-2506(2014).
[29]
FUNCTION (ISOFORM 1), DNA-BINDING (ISOFORMS 1 AND 2), INTERACTION WITH
HDAC3 AND AKT1 (ISOFORM 1), SUBCELLULAR LOCATION (ISOFORM 1), AND
INDUCTION (ISOFORMS 1 AND 2).
PubMed=25190803; DOI=10.1074/jbc.M114.571984;
Martin D., Li Y., Yang J., Wang G., Margariti A., Jiang Z., Yu H.,
Zampetaki A., Hu Y., Xu Q., Zeng L.;
"Unspliced X-box-binding protein 1 (XBP1) protects endothelial cells
from oxidative stress through interaction with histone deacetylase
3.";
J. Biol. Chem. 289:30625-30634(2014).
[30]
VARIANT [LARGE SCALE ANALYSIS] VAL-12.
PubMed=16959974; DOI=10.1126/science.1133427;
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal
cancers.";
Science 314:268-274(2006).
[31]
VARIANT LYS-232.
PubMed=17224074; DOI=10.1186/bcr1637;
Chanock S.J., Burdett L., Yeager M., Llaca V., Langeroed A.,
Presswalla S., Kaaresen R., Strausberg R.L., Gerhard D.S.,
Kristensen V., Perou C.M., Boerresen-Dale A.-L.;
"Somatic sequence alterations in twenty-one genes selected by
expression profile analysis of breast carcinomas.";
Breast Cancer Res. 9:R5-R5(2007).
-!- FUNCTION: Functions as a transcription factor during endoplasmic
reticulum (ER) stress by regulating the unfolded protein response
(UPR). Required for cardiac myogenesis and hepatogenesis during
embryonic development, and the development of secretory tissues
such as exocrine pancreas and salivary gland (By similarity).
Involved in terminal differentiation of B lymphocytes to plasma
cells and production of immunoglobulins (PubMed:11460154).
Modulates the cellular response to ER stress in a PIK3R-dependent
manner (PubMed:20348923). Binds to the cis-acting X box present in
the promoter regions of major histocompatibility complex class II
genes (PubMed:8349596). Involved in VEGF-induced endothelial cell
(EC) proliferation and retinal blood vessel formation during
embryonic development but also for angiogenesis in adult tissues
under ischemic conditions. Functions also as a major regulator of
the UPR in obesity-induced insulin resistance and type 2 diabetes
for the management of obesity and diabetes prevention (By
similarity). {ECO:0000250|UniProtKB:O35426,
ECO:0000269|PubMed:11460154, ECO:0000269|PubMed:20348923,
ECO:0000269|PubMed:8349596}.
-!- FUNCTION: Isoform 1: plays a role in the unconventional
cytoplasmic splicing processing of its own mRNA triggered by the
endoplasmic reticulum (ER) transmembrane endoribonuclease ENR1:
upon ER stress, the emerging XBP1 polypeptide chain, as part of a
mRNA-ribosome-nascent chain (R-RNC) complex, cotranslationally
recruits its own unprocessed mRNA through transient docking to the
ER membrane and translational pausing, therefore facilitating
efficient IRE1-mediated XBP1 mRNA isoform 2 production
(PubMed:19394296, PubMed:21233347). In endothelial cells (EC),
associated with KDR, promotes IRE1-mediated XBP1 mRNA isoform 2
productions in a vascular endothelial growth factor (VEGF)-
dependent manner, leading to EC proliferation and angiogenesis
(PubMed:23529610). Functions as a negative feed-back regulator of
the potent transcription factor XBP1 isoform 2 protein levels
through proteasome-mediated degradation, thus preventing the
constitutive activation of the ER stress response signaling
pathway (PubMed:16461360, PubMed:25239945). Inhibits the
transactivation activity of XBP1 isoform 2 in myeloma cells (By
similarity). Acts as a weak transcriptional factor
(PubMed:8657566). Together with HDAC3, contributes to the
activation of NFE2L2-mediated HMOX1 transcription factor gene
expression in a PI(3)K/mTORC2/Akt-dependent signaling pathway
leading to EC survival under disturbed flow/oxidative stress
(PubMed:25190803). Binds to the ER stress response element (ERSE)
upon ER stress (PubMed:11779464). Binds to the consensus 5'-
GATGACGTG[TG]N(3)[AT]T-3' sequence related to cAMP responsive
element (CRE)-like sequences (PubMed:8657566). Binds the Tax-
responsive element (TRE) present in the long terminal repeat (LTR)
of T-cell leukemia virus type 1 (HTLV-I) and to the TPA response
elements (TRE) (PubMed:2321018, PubMed:2196176, PubMed:1903538,
PubMed:8657566). Associates preferentially to the HDAC3 gene
promoter region in a static flow-dependent manner
(PubMed:25190803). Binds to the CDH5/VE-cadherin gene promoter
region (PubMed:19416856). {ECO:0000250|UniProtKB:O35426,
ECO:0000269|PubMed:11779464, ECO:0000269|PubMed:16461360,
ECO:0000269|PubMed:1903538, ECO:0000269|PubMed:19394296,
ECO:0000269|PubMed:19416856, ECO:0000269|PubMed:21233347,
ECO:0000269|PubMed:2196176, ECO:0000269|PubMed:2321018,
ECO:0000269|PubMed:23529610, ECO:0000269|PubMed:25190803,
ECO:0000269|PubMed:25239945, ECO:0000269|PubMed:8657566}.
-!- FUNCTION: Isoform 2: functions as a stress-inducible potent
transcriptional activator during endoplasmic reticulum (ER) stress
by inducing unfolded protein response (UPR) target genes via
binding to the UPR element (UPRE). Up-regulates target genes
encoding ER chaperones and ER-associated degradation (ERAD)
components to enhance the capacity of productive folding and
degradation mechanism, respectively, in order to maintain the
homeostasis of the ER under ER stress (PubMed:11779464,
PubMed:25239945). Plays a role in the production of
immunoglobulins and interleukin-6 in the presence of stimuli
required for plasma cell differentiation (By similarity). Induces
phospholipid biosynthesis and ER expansion (PubMed:15466483).
Contributes to the VEGF-induced endothelial cell (EC) growth and
proliferation in a Akt/GSK-dependent and/or -independent signaling
pathway, respectively, leading to beta-catenin nuclear
translocation and E2F2 gene expression (PubMed:23529610). Promotes
umbilical vein EC apoptosis and atherosclerotisis development in a
caspase-dependent signaling pathway, and contributes to VEGF-
induced EC proliferation and angiogenesis in adult tissues under
ischemic conditions (PubMed:19416856, PubMed:23529610). Involved
in the regulation of endostatin-induced autophagy in EC through
BECN1 transcriptional activation (PubMed:23184933). Plays a role
as an oncogene by promoting tumor progression: stimulates zinc
finger protein SNAI1 transcription to induce epithelial-to-
mesenchymal (EMT) transition, cell migration and invasion of
breast cancer cells (PubMed:25280941). Involved in adipocyte
differentiation by regulating lipogenic gene expression during
lactation. Plays a role in the survival of both dopaminergic
neurons of the substantia nigra pars compacta (SNpc), by
maintaining protein homeostasis and of myeloma cells. Increases
insulin sensitivity in the liver as a response to a high
carbohydrate diet, resulting in improved glucose tolerance.
Improves also glucose homeostasis in an ER stress- and/or insulin-
independent manner through both binding and proteasome-induced
degradation of the transcription factor FOXO1, hence resulting in
suppression of gluconeogenic genes expression and in a reduction
of blood glucose levels. Controls the induction of de novo fatty
acid synthesis in hepatocytes by regulating the expression of a
subset of lipogenic genes in an ER stress- and UPR-independent
manner (By similarity). Associates preferentially to the HDAC3
gene promoter region in a disturbed flow-dependent manner
(PubMed:25190803). Binds to the BECN1 gene promoter region
(PubMed:23184933). Binds to the CDH5/VE-cadherin gene promoter
region (PubMed:19416856). Binds to the ER stress response element
(ERSE) upon ER stress (PubMed:11779464). Binds to the 5'-CCACG-3'
motif in the PPARG promoter (By similarity).
{ECO:0000250|UniProtKB:O35426, ECO:0000269|PubMed:11779464,
ECO:0000269|PubMed:15466483, ECO:0000269|PubMed:19416856,
ECO:0000269|PubMed:23184933, ECO:0000269|PubMed:23529610,
ECO:0000269|PubMed:25190803, ECO:0000269|PubMed:25239945,
ECO:0000269|PubMed:25280941}.
-!- SUBUNIT: Isoform 2 interacts with SIRT1. Isoform 2 interacts with
PIK3R1 and PIK3R2; the interactions are direct and induce
translocation of XBP1 isoform 2 into the nucleus and the unfolded
protein response (UPR) XBP1-dependent target genes activation in a
ER stress- and/or insulin-dependent but PI3K-independent manner.
Isoform 2 interacts with FOXO1; the interaction is direct and
leads to FOXO1 ubiquitination and degradation via the proteasome
pathway in hepatocytes (By similarity). Isoform 1 interacts with
HM13 (PubMed:25239945). Isoform 1 interacts with RNF139; the
interaction induces ubiquitination and degradation of isoform 1
(PubMed:25239945). Isoform 1 interacts (via luminal domain) with
DERL1; the interaction obviates the need for ectodomain shedding
prior HM13/SPP-mediated XBP1 isoform 1 cleavage (PubMed:25239945).
Isoform 1 interacts with isoform 2; the interaction sequesters
isoform 2 from the nucleus and enhances isoform 2 degradation in
the cytoplasm (PubMed:16461360, PubMed:25239945). Isoform 1
interacts with HDAC3 and AKT1; the interactions occur in
endothelial cell (EC) under disturbed flow (PubMed:25190803).
Isoform 1 interacts with the oncoprotein FOS (PubMed:1903538).
Isoform 2 interacts with ATF6; the interaction occurs in a ER
stress-dependent manner and is required for DNA binding to the
unfolded protein response element (UPRE) (PubMed:17765680).
Isoform 2 interacts with PIK3R1; the interaction is direct and
induces translocation of XBP1 isoform 2 into the nucleus and the
unfolded protein response (UPR) XBP1-dependent target genes
activation in a ER stress- and/or insulin-dependent but PI3K-
independent manner (PubMed:20348923).
{ECO:0000250|UniProtKB:O35426, ECO:0000269|PubMed:16461360,
ECO:0000269|PubMed:17765680, ECO:0000269|PubMed:1903538,
ECO:0000269|PubMed:20348923, ECO:0000269|PubMed:25190803,
ECO:0000269|PubMed:25239945}.
-!- INTERACTION:
P18850:ATF6; NbExp=2; IntAct=EBI-6942961, EBI-852157;
Q9NS37:CREBZF; NbExp=2; IntAct=EBI-6942961, EBI-632965;
Q8TCT9:HM13; NbExp=2; IntAct=EBI-7631279, EBI-347472;
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum
{ECO:0000269|PubMed:23529610}. Note=Colocalizes with ERN1 and KDR
in the endoplasmic reticulum in endothelial cells in a vascular
endothelial growth factor (VEGF)-dependent manner
(PubMed:23529610). {ECO:0000269|PubMed:23529610}.
-!- SUBCELLULAR LOCATION: Isoform 1: Nucleus
{ECO:0000250|UniProtKB:O35426, ECO:0000269|PubMed:16461360,
ECO:0000269|PubMed:19394296}. Cytoplasm
{ECO:0000250|UniProtKB:O35426, ECO:0000269|PubMed:16461360,
ECO:0000269|PubMed:19394296, ECO:0000269|PubMed:20348923,
ECO:0000269|PubMed:25190803}. Endoplasmic reticulum membrane
{ECO:0000269|PubMed:25239945}; Single-pass type II membrane
protein {ECO:0000269|PubMed:25239945}. Endoplasmic reticulum
membrane {ECO:0000303|PubMed:25239945}; Peripheral membrane
protein {ECO:0000303|PubMed:25239945}. Membrane
{ECO:0000269|PubMed:19394296}; Peripheral membrane protein
{ECO:0000303|PubMed:19394296}. Note=Shows no preferential
localization to either the nucleus or the cytoplasm (By
similarity). Shuttles between the nucleus and the cytoplasm in a
CRM1-dependent manner (PubMed:16461360). Localizes predominantly
at the endoplasmic reticulum membrane as a membrane-spanning
protein; whereas may be only marginally localized on the cytosolic
side of the ER membrane as a peripheral membrane (PubMed:19394296,
PubMed:25190803). {ECO:0000250|UniProtKB:O35426,
ECO:0000269|PubMed:16461360, ECO:0000269|PubMed:19394296,
ECO:0000269|PubMed:25190803}.
-!- SUBCELLULAR LOCATION: Isoform 2: Nucleus
{ECO:0000250|UniProtKB:O35426, ECO:0000269|PubMed:16461360,
ECO:0000269|PubMed:19394296, ECO:0000269|PubMed:20348923,
ECO:0000269|PubMed:20955178}. Cytoplasm
{ECO:0000250|UniProtKB:O35426}. Note=Localizes predominantly in
the nucleus. Colocalizes in the nucleus with SIRT1. Translocates
into the nucleus in a PIK3R-, ER stress-induced- and/or insulin-
dependent manner (By similarity). {ECO:0000250|UniProtKB:O35426}.
-!- SUBCELLULAR LOCATION: X-box-binding protein 1, cytoplasmic form:
Cytoplasm {ECO:0000269|PubMed:25239945}. Nucleus
{ECO:0000269|PubMed:25239945}. Note=Localizes in the cytoplasm and
nucleus after HM13/SPP-mediated intramembranaire proteolytic
cleavage of isoform 1 (PubMed:25239945).
{ECO:0000269|PubMed:25239945}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1; Synonyms=Unprocessed XBP-1 {ECO:0000305}, XBP-1U
{ECO:0000303|PubMed:11779464}, XBP1u
{ECO:0000303|PubMed:19394296};
IsoId=P17861-1; Sequence=Displayed;
Name=2; Synonyms=Processed XBP-1 {ECO:0000305}, XBP-1S
{ECO:0000303|PubMed:11779464}, XBP1s
{ECO:0000303|PubMed:19394296};
IsoId=P17861-2; Sequence=VSP_012936;
Note=Potent transcriptional activator. Induced by unconventional
ERN1-dependent splicing in response to endoplasmic reticulum
stress (Ref.4, Ref.18, Ref.19). ENR1 cleaves a 26-bp fragment
causing a frameshift of the mRNA transcript (Ref.4).
{ECO:0000269|PubMed:11779464, ECO:0000269|PubMed:19394296,
ECO:0000269|PubMed:19622636};
-!- TISSUE SPECIFICITY: Expressed in plasma cells in rheumatoid
synovium (PubMed:11460154). Over-expressed in primary breast
cancer and metastatic breast cancer cells (PubMed:25280941).
Isoform 1 and isoform 2 are expressed at higher level in
proliferating as compared to confluent quiescent endothelial cells
(PubMed:19416856). {ECO:0000269|PubMed:11460154,
ECO:0000269|PubMed:19416856, ECO:0000269|PubMed:25280941}.
-!- INDUCTION: Isoform 1 is up-regulated at the recovery phase of the
endoplasmic reticulum (ER) stress response and isoform 2 is up-
regulated early during the ER stress response and gradually
decreased at later phase of ER stress (PubMed:16461360). Isoform 1
and isoform 2 are down-regulated by laminar flow but up-regulated
by disturbed flow in umbilical vein endothelial cells in vitro (at
protein level) (PubMed:19416856). Down-regulated by the B-cell-
specific transcription factor PAX5 (PubMed:8627152). Up-regulated
by interleukin IL-6 in myeloma cells (PubMed:10375612). Up-
regulated during plasma-cell differentiation, either through the
CD40 receptor signaling pathway or mitogens such as
lipopolysaccharide (LPS) (PubMed:11460154). Isoform 1 and isoform
2 are down-regulated by laminar flow but up-regulated by disturbed
flow in umbilical vein endothelial cells in vitro
(PubMed:25190803). Isoform 2 is up-regulated early during the ER
stress response in a ATF6-dependent manner (PubMed:11779464,
PubMed:17110785, PubMed:16461360). Isoform 2 is up-regulated by
endostatin in a ERN1-dependent manner (PubMed:23184933). Isoform 2
is transiently up-regulated by the mitogenic vascular endothelial
growth factor (VEGF) in endothelial cells (PubMed:23529610).
{ECO:0000269|PubMed:10375612, ECO:0000269|PubMed:11460154,
ECO:0000269|PubMed:11779464, ECO:0000269|PubMed:16461360,
ECO:0000269|PubMed:17110785, ECO:0000269|PubMed:19416856,
ECO:0000269|PubMed:23184933, ECO:0000269|PubMed:23529610,
ECO:0000269|PubMed:25190803, ECO:0000269|PubMed:8627152}.
-!- DOMAIN: Isoform 1 and isoform 2 N-terminus domains are necessary
for nuclear localization targeting. Isoform 1 C-terminus domain
confers localization to the cytoplasm and is sufficient to impose
rapid degradation (By similarity). Isoform 1 transmembrane signal-
anchor domain is necessary for its own mRNA to be recruited to the
endoplasmic reticulum (ER) which will undergo unconventional ERN1-
dependent splicing in response to ER stress (PubMed:19394296,
PubMed:21233347). Isoform 1 N-terminus and C-terminus regions are
necessary for DNA-binding and weak transcriptional activity,
respectively. Isoform 2 N-terminus and C-terminus regions are
necessary for DNA-binding and strong transcriptional activity upon
ER stress, respectively (PubMed:11779464, PubMed:8657566). Isoform
2 C-terminus region contains a nuclear exclusion signal (NES) at
positions 186 through 208. Isoform 2 C-terminus region contains a
degradation domain at positions 209 through 261 (PubMed:16461360).
{ECO:0000250|UniProtKB:O35426, ECO:0000269|PubMed:11779464,
ECO:0000269|PubMed:16461360, ECO:0000269|PubMed:19394296,
ECO:0000269|PubMed:21233347, ECO:0000269|PubMed:8657566}.
-!- PTM: Isoform 2 is acetylated by EP300; acetylation positively
regulates the transcriptional activity of XBP1 isoform 2
(PubMed:20955178). Isoform 2 is deacetylated by SIRT1;
deacetylation negatively regulates the transcriptional activity of
XBP1 isoform 2 (PubMed:20955178). {ECO:0000269|PubMed:20955178,
ECO:0000305|PubMed:20955178}.
-!- PTM: Isoform 1 is ubiquitinated, leading to proteasome-mediated
degradation in response to ER stress (PubMed:11779464,
PubMed:16461360, PubMed:25239945). {ECO:0000250|UniProtKB:O35426,
ECO:0000269|PubMed:11779464, ECO:0000269|PubMed:16461360,
ECO:0000269|PubMed:25239945}.
-!- PTM: X-box-binding protein 1, cytoplasmic form and luminal form
are produced by intramembrane proteolytic cleavage of ER membrane-
anchored isoform 1 triggered by HM13/SPP in a DERL1-RNF139-
dependent and VCP/p97-independent manner. X-box-binding protein 1,
luminal form is ubiquitinated leading to proteasomal degradation
(PubMed:25239945). {ECO:0000269|PubMed:25239945}.
-!- DISEASE: Major affective disorder 7 (MAFD7) [MIM:612371]: A major
psychiatric disorder that is characterized by severe mood swings,
with fluctuation between two abnormal mood states (manic or major
depressive episode). Mania is accompanied by symptoms of euphoria,
irritability, or excitation, whereas depression is associated with
low mood and decreased motivation and energy. Note=Disease
susceptibility may be associated with variations affecting the
gene represented in this entry.
-!- SIMILARITY: Belongs to the bZIP family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; M31627; AAA36031.1; -; mRNA.
EMBL; X55543; CAA39149.1; -; Genomic_DNA.
EMBL; L13850; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AB076383; BAB82981.1; -; mRNA.
EMBL; AB076384; BAB82982.1; -; mRNA.
EMBL; CR456611; CAG30497.1; -; mRNA.
EMBL; Z93930; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC000938; AAH00938.1; -; mRNA.
EMBL; BC012841; AAH12841.1; -; mRNA.
EMBL; BC015709; AAH15709.1; -; mRNA.
CCDS; CCDS13847.1; -. [P17861-1]
PIR; A36299; A36299.
RefSeq; NP_001073007.1; NM_001079539.1. [P17861-2]
RefSeq; NP_005071.2; NM_005080.3. [P17861-1]
UniGene; Hs.437638; -.
ProteinModelPortal; P17861; -.
BioGrid; 113331; 31.
DIP; DIP-41692N; -.
IntAct; P17861; 11.
MINT; MINT-268152; -.
STRING; 9606.ENSP00000216037; -.
BindingDB; P17861; -.
ChEMBL; CHEMBL1741176; -.
iPTMnet; P17861; -.
PhosphoSitePlus; P17861; -.
BioMuta; XBP1; -.
DMDM; 60416406; -.
EPD; P17861; -.
MaxQB; P17861; -.
PaxDb; P17861; -.
PeptideAtlas; P17861; -.
PRIDE; P17861; -.
DNASU; 7494; -.
Ensembl; ENST00000216037; ENSP00000216037; ENSG00000100219. [P17861-1]
Ensembl; ENST00000344347; ENSP00000343155; ENSG00000100219. [P17861-2]
Ensembl; ENST00000611155; ENSP00000481170; ENSG00000100219. [P17861-2]
GeneID; 7494; -.
KEGG; hsa:7494; -.
UCSC; uc062cvg.1; human. [P17861-1]
CTD; 7494; -.
DisGeNET; 7494; -.
GeneCards; XBP1; -.
HGNC; HGNC:12801; XBP1.
MalaCards; XBP1; -.
MIM; 194355; gene.
MIM; 612371; phenotype.
neXtProt; NX_P17861; -.
OpenTargets; ENSG00000100219; -.
PharmGKB; PA37400; -.
eggNOG; KOG4005; Eukaryota.
eggNOG; ENOG410XSJI; LUCA.
GeneTree; ENSGT00390000017751; -.
HOGENOM; HOG000007671; -.
HOVERGEN; HBG061457; -.
InParanoid; P17861; -.
KO; K09027; -.
OMA; TFANELF; -.
OrthoDB; EOG091G0T4E; -.
PhylomeDB; P17861; -.
TreeFam; TF319837; -.
Reactome; R-HSA-381038; XBP1(S) activates chaperone genes.
Reactome; R-HSA-381070; IRE1alpha activates chaperones.
Reactome; R-HSA-381183; ATF6 (ATF6-alpha) activates chaperone genes.
SignaLink; P17861; -.
SIGNOR; P17861; -.
ChiTaRS; XBP1; human.
GeneWiki; XBP1; -.
GenomeRNAi; 7494; -.
PRO; PR:P17861; -.
Proteomes; UP000005640; Chromosome 22.
Bgee; ENSG00000100219; -.
CleanEx; HS_XBP1; -.
ExpressionAtlas; P17861; baseline and differential.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IDA:UniProtKB.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:LIFEdb.
GO; GO:0031490; F:chromatin DNA binding; IDA:UniProtKB.
GO; GO:0001047; F:core promoter binding; ISS:UniProtKB.
GO; GO:0003677; F:DNA binding; TAS:ProtInc.
GO; GO:0001158; F:enhancer sequence-specific DNA binding; IDA:UniProtKB.
GO; GO:0030331; F:estrogen receptor binding; TAS:ParkinsonsUK-UCL.
GO; GO:0002020; F:protease binding; IPI:UniProtKB.
GO; GO:0046982; F:protein heterodimerization activity; IDA:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; TAS:ParkinsonsUK-UCL.
GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
GO; GO:0000977; F:RNA polymerase II regulatory region sequence-specific DNA binding; IDA:UniProtKB.
GO; GO:0000981; F:RNA polymerase II transcription factor activity, sequence-specific DNA binding; IEA:Ensembl.
GO; GO:0001085; F:RNA polymerase II transcription factor binding; IEA:Ensembl.
GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IDA:UniProtKB.
GO; GO:0044212; F:transcription regulatory region DNA binding; IDA:UniProtKB.
GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:UniProtKB.
GO; GO:0060612; P:adipose tissue development; ISS:UniProtKB.
GO; GO:0001525; P:angiogenesis; ISS:UniProtKB.
GO; GO:0036500; P:ATF6-mediated unfolded protein response; TAS:Reactome.
GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
GO; GO:0016049; P:cell growth; IDA:UniProtKB.
GO; GO:0071230; P:cellular response to amino acid stimulus; ISS:UniProtKB.
GO; GO:0071498; P:cellular response to fluid shear stress; IDA:UniProtKB.
GO; GO:0071332; P:cellular response to fructose stimulus; ISS:UniProtKB.
GO; GO:0042149; P:cellular response to glucose starvation; ISS:UniProtKB.
GO; GO:0071333; P:cellular response to glucose stimulus; ISS:UniProtKB.
GO; GO:0032869; P:cellular response to insulin stimulus; ISS:UniProtKB.
GO; GO:0071353; P:cellular response to interleukin-4; ISS:UniProtKB.
GO; GO:0071499; P:cellular response to laminar fluid shear stress; IDA:UniProtKB.
GO; GO:0071222; P:cellular response to lipopolysaccharide; IDA:UniProtKB.
GO; GO:0031670; P:cellular response to nutrient; ISS:UniProtKB.
GO; GO:0034599; P:cellular response to oxidative stress; IDA:UniProtKB.
GO; GO:0071375; P:cellular response to peptide hormone stimulus; ISS:UniProtKB.
GO; GO:0035924; P:cellular response to vascular endothelial growth factor stimulus; IDA:UniProtKB.
GO; GO:0035356; P:cellular triglyceride homeostasis; ISS:UniProtKB.
GO; GO:0042632; P:cholesterol homeostasis; ISS:UniProtKB.
GO; GO:0030968; P:endoplasmic reticulum unfolded protein response; ISS:UniProtKB.
GO; GO:0001935; P:endothelial cell proliferation; IDA:UniProtKB.
GO; GO:0060691; P:epithelial cell maturation involved in salivary gland development; IEA:Ensembl.
GO; GO:0031017; P:exocrine pancreas development; IEA:Ensembl.
GO; GO:0006633; P:fatty acid biosynthetic process; TAS:ParkinsonsUK-UCL.
GO; GO:0055089; P:fatty acid homeostasis; ISS:UniProtKB.
GO; GO:0006955; P:immune response; TAS:ParkinsonsUK-UCL.
GO; GO:0070059; P:intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress; IEA:Ensembl.
GO; GO:0036498; P:IRE1-mediated unfolded protein response; TAS:ParkinsonsUK-UCL.
GO; GO:0001889; P:liver development; ISS:UniProtKB.
GO; GO:0007517; P:muscle organ development; IEA:UniProtKB-KW.
GO; GO:0043066; P:negative regulation of apoptotic process; ISS:UniProtKB.
GO; GO:1902236; P:negative regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway; IDA:ParkinsonsUK-UCL.
GO; GO:1900102; P:negative regulation of endoplasmic reticulum unfolded protein response; IDA:UniProtKB.
GO; GO:0070373; P:negative regulation of ERK1 and ERK2 cascade; IDA:BHF-UCL.
GO; GO:0010832; P:negative regulation of myotube differentiation; ISS:UniProtKB.
GO; GO:0060394; P:negative regulation of pathway-restricted SMAD protein phosphorylation; IDA:BHF-UCL.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:UniProtKB.
GO; GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; IDA:BHF-UCL.
GO; GO:0048666; P:neuron development; ISS:UniProtKB.
GO; GO:0006996; P:organelle organization; TAS:ParkinsonsUK-UCL.
GO; GO:0014065; P:phosphatidylinositol 3-kinase signaling; IDA:UniProtKB.
GO; GO:0045766; P:positive regulation of angiogenesis; IMP:BHF-UCL.
GO; GO:0010508; P:positive regulation of autophagy; IDA:UniProtKB.
GO; GO:0045579; P:positive regulation of B cell differentiation; IDA:UniProtKB.
GO; GO:0030335; P:positive regulation of cell migration; IDA:BHF-UCL.
GO; GO:0008284; P:positive regulation of cell proliferation; IDA:BHF-UCL.
GO; GO:1900103; P:positive regulation of endoplasmic reticulum unfolded protein response; IMP:UniProtKB.
GO; GO:2000353; P:positive regulation of endothelial cell apoptotic process; IDA:UniProtKB.
GO; GO:1903071; P:positive regulation of ER-associated ubiquitin-dependent protein catabolic process; TAS:ParkinsonsUK-UCL.
GO; GO:0045600; P:positive regulation of fat cell differentiation; ISS:UniProtKB.
GO; GO:2000347; P:positive regulation of hepatocyte proliferation; ISS:UniProtKB.
GO; GO:0031062; P:positive regulation of histone methylation; IDA:UniProtKB.
GO; GO:0002639; P:positive regulation of immunoglobulin production; IDA:UniProtKB.
GO; GO:0051024; P:positive regulation of immunoglobulin secretion; ISS:UniProtKB.
GO; GO:2000778; P:positive regulation of interleukin-6 secretion; ISS:UniProtKB.
GO; GO:1903489; P:positive regulation of lactation; ISS:UniProtKB.
GO; GO:0045348; P:positive regulation of MHC class II biosynthetic process; IMP:UniProtKB.
GO; GO:1900413; P:positive regulation of phospholipid biosynthetic process by positive regulation of transcription from RNA polymerase II promoter; TAS:ParkinsonsUK-UCL.
GO; GO:1900100; P:positive regulation of plasma cell differentiation; IDA:UniProtKB.
GO; GO:1901800; P:positive regulation of proteasomal protein catabolic process; IEA:Ensembl.
GO; GO:1901985; P:positive regulation of protein acetylation; IDA:UniProtKB.
GO; GO:0051897; P:positive regulation of protein kinase B signaling; IDA:BHF-UCL.
GO; GO:0001934; P:positive regulation of protein phosphorylation; IDA:BHF-UCL.
GO; GO:0045582; P:positive regulation of T cell differentiation; IDA:UniProtKB.
GO; GO:0032008; P:positive regulation of TOR signaling; IMP:UniProtKB.
GO; GO:0042993; P:positive regulation of transcription factor import into nucleus; IDA:UniProtKB.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:ParkinsonsUK-UCL.
GO; GO:1990440; P:positive regulation of transcription from RNA polymerase II promoter in response to endoplasmic reticulum stress; TAS:ParkinsonsUK-UCL.
GO; GO:0006990; P:positive regulation of transcription from RNA polymerase II promoter involved in unfolded protein response; IDA:UniProtKB.
GO; GO:1904754; P:positive regulation of vascular associated smooth muscle cell migration; IDA:BHF-UCL.
GO; GO:1904707; P:positive regulation of vascular smooth muscle cell proliferation; IDA:BHF-UCL.
GO; GO:0035470; P:positive regulation of vascular wound healing; IDA:BHF-UCL.
GO; GO:0031648; P:protein destabilization; IDA:UniProtKB.
GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
GO; GO:0010506; P:regulation of autophagy; IEA:Ensembl.
GO; GO:0031647; P:regulation of protein stability; IDA:UniProtKB.
GO; GO:0034976; P:response to endoplasmic reticulum stress; IDA:UniProtKB.
GO; GO:1990418; P:response to insulin-like growth factor stimulus; ISS:UniProtKB.
GO; GO:0055092; P:sterol homeostasis; ISS:UniProtKB.
GO; GO:0006366; P:transcription from RNA polymerase II promoter; ISS:UniProtKB.
GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
GO; GO:0048010; P:vascular endothelial growth factor receptor signaling pathway; IDA:UniProtKB.
InterPro; IPR004827; bZIP.
Pfam; PF07716; bZIP_2; 1.
SMART; SM00338; BRLZ; 1.
PROSITE; PS50217; BZIP; 1.
PROSITE; PS00036; BZIP_BASIC; 1.
1: Evidence at protein level;
Acetylation; Activator; Alternative splicing; Angiogenesis; Apoptosis;
Autophagy; Cleavage on pair of basic residues; Complete proteome;
Cytoplasm; Developmental protein; Differentiation; DNA-binding;
Endoplasmic reticulum; Lipid biosynthesis; Lipid metabolism; Membrane;
Myogenesis; Nucleus; Oncogene; Phosphoprotein; Polymorphism;
Protein transport; Reference proteome; Signal-anchor; Stress response;
Transcription; Transcription regulation; Transmembrane;
Transmembrane helix; Transport; Ubl conjugation;
Unfolded protein response.
CHAIN 1 261 X-box-binding protein 1.
/FTId=PRO_0000076543.
CHAIN 1 193 X-box-binding protein 1, cytoplasmic
form. {ECO:0000303|PubMed:25239945}.
/FTId=PRO_0000431891.
CHAIN 196 261 X-box-binding protein 1, luminal form.
{ECO:0000303|PubMed:25239945}.
/FTId=PRO_0000431892.
TOPO_DOM 1 185 Cytoplasmic.
{ECO:0000269|PubMed:25239945}.
TRANSMEM 186 203 Helical; Signal-anchor for type II
membrane protein. {ECO:0000255,
ECO:0000269|PubMed:25239945,
ECO:0000303|PubMed:25239945}.
TOPO_DOM 204 261 Lumenal. {ECO:0000269|PubMed:25239945}.
DOMAIN 70 133 bZIP. {ECO:0000255|PROSITE-
ProRule:PRU00978}.
REGION 72 94 Basic motif. {ECO:0000255|PROSITE-
ProRule:PRU00978}.
REGION 75 92 Nuclear localization signal (NLS); in
isoforms 1 and isoform 2.
{ECO:0000269|PubMed:16461360}.
REGION 98 133 Leucine-zipper. {ECO:0000255|PROSITE-
ProRule:PRU00978}.
REGION 235 261 Necessary for the translational pausing
of its own mRNA.
{ECO:0000269|PubMed:21233347}.
SITE 194 195 Cleavage; by HM13/SPP.
{ECO:0000303|PubMed:25239945}.
MOD_RES 47 47 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 68 68 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
VAR_SEQ 167 261 LRLRAPLQQVQAQLSPLQNISPWILAVLTLQIQSLISCWAF
WTTWTQSCSSNALPQSLPAWRSSQRSTQKDPVPYQPPFLCQ
WGRHQPSWKPLMN -> GAGPVVTPPEHLPMDSGGIDSSDS
ESDILLGILDNLDPVMFFKCPSPEPASLEELPEVYPEGPSS
LPASLSLSVGTSSAKLEAINELIRFDHIYTKPLVLEIPSET
ESQANVVVKIEEAPLSPSENDHPEFIVSVKEEPVEDDLVPE
LGISNLLSSSHCPKPSSCLLDAYSDCGYGGSLSPFSDMSSL
LGVNHSWEDTFANELFPQLISV (in isoform 2).
{ECO:0000303|PubMed:11779464}.
/FTId=VSP_012936.
VARIANT 12 12 D -> V (in a breast cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_035998.
VARIANT 232 232 R -> K (in a breast cancer sample;
somatic mutation).
{ECO:0000269|PubMed:17224074}.
/FTId=VAR_033023.
MUTAGEN 189 189 W->E: Reduces endoplasmic reticulum
localization of its own mRNA; when
associated with E-193 and D-196.
{ECO:0000269|PubMed:19394296}.
MUTAGEN 193 193 V->E: Reduces endoplasmic reticulum
localization of its own mRNA; when
associated with E-189 and D-196.
{ECO:0000269|PubMed:19394296}.
MUTAGEN 194 194 L->E: Reduces endoplasmic reticulum
localization of its own mRNA; when
associated with D-198 and E-205.
{ECO:0000269|PubMed:19394296}.
MUTAGEN 196 196 L->D: Reduces endoplasmic reticulum
localization of its own mRNA; when
associated with E-189 and E-193.
{ECO:0000269|PubMed:19394296}.
MUTAGEN 197 197 Q->L: Inhibits HM13/SPP-mediated
degradation of XBP1; when associated with
L-199; L-200 and L-203.
{ECO:0000269|PubMed:25239945}.
MUTAGEN 198 198 I->D: Reduces endoplasmic reticulum
localization of its own mRNA; when
associated with E-194 and E-205.
{ECO:0000269|PubMed:19394296}.
MUTAGEN 199 199 Q->L: Inhibits HM13/SPP-mediated
degradation of XBP1; when associated with
L-197; L-200 and L-203.
{ECO:0000269|PubMed:25239945}.
MUTAGEN 200 200 S->L: Inhibits HM13/SPP-mediated
degradation of XBP1; when associated with
L-197; L-199 and L-203.
{ECO:0000269|PubMed:25239945}.
MUTAGEN 203 203 S->L: Inhibits HM13/SPP-mediated
degradation of XBP1; when associated with
L-197; L-199 and L-200.
{ECO:0000269|PubMed:25239945}.
MUTAGEN 205 205 W->E: Reduces endoplasmic reticulum
localization of its own mRNA; when
associated with E-194 and D-198.
{ECO:0000269|PubMed:19394296}.
MUTAGEN 212 212 T->N: Does not induce glycosylation.
{ECO:0000269|PubMed:25239945}.
MUTAGEN 215 215 C->N: Induces glycosylation.
{ECO:0000269|PubMed:25239945}.
MUTAGEN 232 232 R->N: Induces glycosylation.
{ECO:0000269|PubMed:25239945}.
MUTAGEN 246 246 L->A: Reduces translational pausing,
membrane targeting and cytoplasmic
splicing of its own mRNA.
{ECO:0000269|PubMed:21233347}.
MUTAGEN 255 255 S->A: Increases translational pausing of
its own mRNA.
{ECO:0000269|PubMed:21233347}.
MUTAGEN 256 256 W->A: Reduces translational pausing,
membrane targeting and cytoplasmic
splicing of its own mRNA.
{ECO:0000269|PubMed:21233347}.
CONFLICT 33 35 GQA -> AR (in Ref. 1; AAA36031).
{ECO:0000305}.
CONFLICT 130 130 N -> T (in Ref. 3; L13850).
{ECO:0000305}.
CONFLICT 196 196 L -> F (in Ref. 3; L13850).
{ECO:0000305}.
SEQUENCE 261 AA; 28695 MW; A4EF69EEE0D344A6 CRC64;
MVVVAAAPNP ADGTPKVLLL SGQPASAAGA PAGQALPLMV PAQRGASPEA ASGGLPQARK
RQRLTHLSPE EKALRRKLKN RVAAQTARDR KKARMSELEQ QVVDLEEENQ KLLLENQLLR
EKTHGLVVEN QELRQRLGMD ALVAEEEAEA KGNEVRPVAG SAESAALRLR APLQQVQAQL
SPLQNISPWI LAVLTLQIQS LISCWAFWTT WTQSCSSNAL PQSLPAWRSS QRSTQKDPVP
YQPPFLCQWG RHQPSWKPLM N


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