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Protein

X-box-binding protein 1

Gene

XBP1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

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).By similarity3 Publications
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 PI3K/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]N3[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).By similarity12 Publications
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).By similarity8 Publications

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionActivator, Developmental protein, DNA-binding
Biological processAngiogenesis, Apoptosis, Autophagy, Differentiation, Lipid biosynthesis, Lipid metabolism, Myogenesis, Protein transport, Stress response, Transcription, Transcription regulation, Transport, Unfolded protein response

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

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Reactomei
R-HSA-381038 XBP1(S) activates chaperone genes
R-HSA-381070 IRE1alpha activates chaperones
R-HSA-381183 ATF6 (ATF6-alpha) activates chaperone genes

SignaLink: a signaling pathway resource with multi-layered regulatory networks

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SignaLinki
P17861

SIGNOR Signaling Network Open Resource

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SIGNORi
P17861

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
X-box-binding protein 11 PublicationImported
Short name:
XBP-11 Publication
Alternative name(s):
Tax-responsive element-binding protein 51 Publication
Short name:
TREB-51 Publication
Cleaved into the following 2 chains:
X-box-binding protein 1, cytoplasmic form1 Publication
X-box-binding protein 1, luminal form1 Publication
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:XBP1Imported
Synonyms:TREB51 Publication, XBP2Imported
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 22

Organism-specific databases

Eukaryotic Pathogen Database Resources

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EuPathDBi
HostDB:ENSG00000100219.16

Human Gene Nomenclature Database

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HGNCi
HGNC:12801 XBP1

Online Mendelian Inheritance in Man (OMIM)

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MIMi
194355 gene

neXtProt; the human protein knowledge platform

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neXtProti
NX_P17861

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini1 – 185Cytoplasmic1 PublicationAdd BLAST185
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei186 – 203Helical; Signal-anchor for type II membrane protein1 PublicationSequence analysis1 PublicationAdd BLAST18
Topological domaini204 – 261Lumenal1 PublicationAdd BLAST58

Keywords - Cellular componenti

Cytoplasm, Endoplasmic reticulum, Membrane, Nucleus

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the ‘Pathology and Biotech’ section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei

Major affective disorder 7 (MAFD7)
Disease susceptibility may be associated with variations affecting the gene represented in this entry.
Disease descriptionA 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.
See also OMIM:612371

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi189W → E: Reduces endoplasmic reticulum localization of its own mRNA; when associated with E-193 and D-196. 1 Publication1
Mutagenesisi193V → E: Reduces endoplasmic reticulum localization of its own mRNA; when associated with E-189 and D-196. 1 Publication1
Mutagenesisi194L → E: Reduces endoplasmic reticulum localization of its own mRNA; when associated with D-198 and E-205. 1 Publication1
Mutagenesisi196L → D: Reduces endoplasmic reticulum localization of its own mRNA; when associated with E-189 and E-193. 1 Publication1
Mutagenesisi197Q → L: Inhibits HM13/SPP-mediated degradation of XBP1; when associated with L-199; L-200 and L-203. 1 Publication1
Mutagenesisi198I → D: Reduces endoplasmic reticulum localization of its own mRNA; when associated with E-194 and E-205. 1 Publication1
Mutagenesisi199Q → L: Inhibits HM13/SPP-mediated degradation of XBP1; when associated with L-197; L-200 and L-203. 1 Publication1
Mutagenesisi200S → L: Inhibits HM13/SPP-mediated degradation of XBP1; when associated with L-197; L-199 and L-203. 1 Publication1
Mutagenesisi203S → L: Inhibits HM13/SPP-mediated degradation of XBP1; when associated with L-197; L-199 and L-200. 1 Publication1
Mutagenesisi205W → E: Reduces endoplasmic reticulum localization of its own mRNA; when associated with E-194 and D-198. 1 Publication1
Mutagenesisi212T → N: Does not induce glycosylation. 1 Publication1
Mutagenesisi215C → N: Induces glycosylation. 1 Publication1
Mutagenesisi232R → N: Induces glycosylation. 1 Publication1
Mutagenesisi246L → A: Reduces translational pausing, membrane targeting and cytoplasmic splicing of its own mRNA. 1 Publication1
Mutagenesisi255S → A: Increases translational pausing of its own mRNA. 1 Publication1
Mutagenesisi256W → A: Reduces translational pausing, membrane targeting and cytoplasmic splicing of its own mRNA. 1 Publication1

Keywords - Diseasei

Oncogene

Organism-specific databases

DisGeNET

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DisGeNETi
7494

MalaCards human disease database

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MalaCardsi
XBP1
MIMi612371 phenotype

Open Targets

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OpenTargetsi
ENSG00000100219

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA37400

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

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ChEMBLi
CHEMBL1741176

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

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BioMutai
XBP1

Domain mapping of disease mutations (DMDM)

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DMDMi
60416406

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000765431 – 261X-box-binding protein 1Add BLAST261
ChainiPRO_00004318911 – 193X-box-binding protein 1, cytoplasmic form1 PublicationAdd BLAST193
ChainiPRO_0000431892196 – 261X-box-binding protein 1, luminal form1 PublicationAdd BLAST66

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei47PhosphoserineCombined sources1
Modified residuei68PhosphoserineCombined sources1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

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).1 Publication1 Publication
Isoform 1 is ubiquitinated, leading to proteasome-mediated degradation in response to ER stress (PubMed:11779464, PubMed:16461360, PubMed:25239945).By similarity3 Publications
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).1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei194 – 195Cleavage; by HM13/SPP1 Publication2

Keywords - PTMi

Acetylation, Cleavage on pair of basic residues, Phosphoprotein, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
P17861

MaxQB - The MaxQuant DataBase

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MaxQBi
P17861

PaxDb, a database of protein abundance averages across all three domains of life

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PaxDbi
P17861

PeptideAtlas

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PeptideAtlasi
P17861

PRoteomics IDEntifications database

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PRIDEi
P17861

ProteomicsDB human proteome resource

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ProteomicsDBi
53522
53523 [P17861-2]

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
P17861

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

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PhosphoSitePlusi
P17861

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

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).3 Publications

<p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

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).10 Publications

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000100219 Expressed in 121 organ(s), highest expression level in body of pancreas

CleanEx database of gene expression profiles

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CleanExi
HS_XBP1

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
P17861 baseline and differential

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

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).By similarity6 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
113331, 32 interactors

Database of interacting proteins

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DIPi
DIP-41692N

Protein interaction database and analysis system

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IntActi
P17861, 14 interactors

Molecular INTeraction database

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MINTi
P17861

STRING: functional protein association networks

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STRINGi
9606.ENSP00000216037

Chemistry databases

BindingDB database of measured binding affinities

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BindingDBi
P17861

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
P17861

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
P17861

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini70 – 133bZIPPROSITE-ProRule annotationAdd BLAST64

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni72 – 94Basic motifPROSITE-ProRule annotationAdd BLAST23
Regioni75 – 92Nuclear localization signal (NLS); in isoforms 1 and isoform 21 PublicationAdd BLAST18
Regioni98 – 133Leucine-zipperPROSITE-ProRule annotationAdd BLAST36
Regioni235 – 261Necessary for the translational pausing of its own mRNA1 PublicationAdd BLAST27

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

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).By similarity5 Publications

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the bZIP family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG4005 Eukaryota
ENOG410XSJI LUCA

Ensembl GeneTree

More...
GeneTreei
ENSGT00390000017751

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000007671

The HOVERGEN Database of Homologous Vertebrate Genes

More...
HOVERGENi
HBG061457

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P17861

KEGG Orthology (KO)

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KOi
K09027

Identification of Orthologs from Complete Genome Data

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OMAi
LIHFDHI

Database of Orthologous Groups

More...
OrthoDBi
EOG091G0T4E

Database for complete collections of gene phylogenies

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PhylomeDBi
P17861

TreeFam database of animal gene trees

More...
TreeFami
TF319837

Family and domain databases

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR004827 bZIP

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF07716 bZIP_2, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00338 BRLZ, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS50217 BZIP, 1 hit
PS00036 BZIP_BASIC, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (2+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 2 described isoforms and 2 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: P17861-1) [UniParc]FASTAAdd to basket
Also known as: Unprocessed XBP-1Curated, XBP-1U1 Publication, XBP1u1 Publication

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide
        10         20         30         40         50
MVVVAAAPNP ADGTPKVLLL SGQPASAAGA PAGQALPLMV PAQRGASPEA
60 70 80 90 100
ASGGLPQARK RQRLTHLSPE EKALRRKLKN RVAAQTARDR KKARMSELEQ
110 120 130 140 150
QVVDLEEENQ KLLLENQLLR EKTHGLVVEN QELRQRLGMD ALVAEEEAEA
160 170 180 190 200
KGNEVRPVAG SAESAALRLR APLQQVQAQL SPLQNISPWI LAVLTLQIQS
210 220 230 240 250
LISCWAFWTT WTQSCSSNAL PQSLPAWRSS QRSTQKDPVP YQPPFLCQWG
260
RHQPSWKPLM N
Length:261
Mass (Da):28,695
Last modified:March 1, 2005 - v2
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iA4EF69EEE0D344A6
GO
Isoform 2 (identifier: P17861-2) [UniParc]FASTAAdd to basket
Also known as: Processed XBP-1Curated, XBP-1S1 Publication, XBP1s1 Publication

The sequence of this isoform differs from the canonical sequence as follows:
     167-261: LRLRAPLQQV...HQPSWKPLMN → GAGPVVTPPE...NELFPQLISV

Note: Potent transcriptional activator. Induced by unconventional ERN1-dependent splicing in response to endoplasmic reticulum stress (PubMed:11779464, PubMed:19622636, PubMed:19394296). ENR1 cleaves a 26-bp fragment causing a frameshift of the mRNA transcript (PubMed:11779464).3 Publications
Show »
Length:376
Mass (Da):40,148
Checksum:i4C1758D7BA055061
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
B1AHH1B1AHH1_HUMAN
X-box-binding protein 1
XBP1
211Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
B1AHH2B1AHH2_HUMAN
X-box-binding protein 1
XBP1
266Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti33 – 35GQA → AR in AAA36031 (PubMed:2321018).Curated3
Sequence conflicti130N → T in L13850 (PubMed:8349596).Curated1
Sequence conflicti196L → F in L13850 (PubMed:8349596).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_03599812D → V in a breast cancer sample; somatic mutation. 1 Publication1
Natural variantiVAR_033023232R → K in a breast cancer sample; somatic mutation. 1 Publication1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_012936167 – 261LRLRA…KPLMN → GAGPVVTPPEHLPMDSGGID SSDSESDILLGILDNLDPVM FFKCPSPEPASLEELPEVYP EGPSSLPASLSLSVGTSSAK LEAINELIRFDHIYTKPLVL EIPSETESQANVVVKIEEAP LSPSENDHPEFIVSVKEEPV EDDLVPELGISNLLSSSHCP KPSSCLLDAYSDCGYGGSLS PFSDMSSLLGVNHSWEDTFA NELFPQLISV in isoform 2. 1 PublicationAdd BLAST95

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
M31627 mRNA Translation: AAA36031.1
X55543 Genomic DNA Translation: CAA39149.1
L13850 Genomic DNA No translation available.
AB076383 mRNA Translation: BAB82981.1
AB076384 mRNA Translation: BAB82982.1
CR456611 mRNA Translation: CAG30497.1
Z93930 Genomic DNA No translation available.
BC000938 mRNA Translation: AAH00938.1
BC012841 mRNA Translation: AAH12841.1
BC015709 mRNA Translation: AAH15709.1

The Consensus CDS (CCDS) project

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CCDSi
CCDS13847.1 [P17861-1]

Protein sequence database of the Protein Information Resource

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PIRi
A36299

NCBI Reference Sequences

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RefSeqi
NP_001073007.1, NM_001079539.1 [P17861-2]
NP_005071.2, NM_005080.3 [P17861-1]

UniGene gene-oriented nucleotide sequence clusters

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UniGenei
Hs.437638

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000216037; ENSP00000216037; ENSG00000100219 [P17861-1]
ENST00000344347; ENSP00000343155; ENSG00000100219 [P17861-2]
ENST00000611155; ENSP00000481170; ENSG00000100219 [P17861-2]

Database of genes from NCBI RefSeq genomes

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GeneIDi
7494

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
hsa:7494

UCSC genome browser

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UCSCi
uc062cvg.1 human [P17861-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M31627 mRNA Translation: AAA36031.1
X55543 Genomic DNA Translation: CAA39149.1
L13850 Genomic DNA No translation available.
AB076383 mRNA Translation: BAB82981.1
AB076384 mRNA Translation: BAB82982.1
CR456611 mRNA Translation: CAG30497.1
Z93930 Genomic DNA No translation available.
BC000938 mRNA Translation: AAH00938.1
BC012841 mRNA Translation: AAH12841.1
BC015709 mRNA Translation: AAH15709.1
CCDSiCCDS13847.1 [P17861-1]
PIRiA36299
RefSeqiNP_001073007.1, NM_001079539.1 [P17861-2]
NP_005071.2, NM_005080.3 [P17861-1]
UniGeneiHs.437638

3D structure databases

ProteinModelPortaliP17861
SMRiP17861
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi113331, 32 interactors
DIPiDIP-41692N
IntActiP17861, 14 interactors
MINTiP17861
STRINGi9606.ENSP00000216037

Chemistry databases

BindingDBiP17861
ChEMBLiCHEMBL1741176

PTM databases

iPTMnetiP17861
PhosphoSitePlusiP17861

Polymorphism and mutation databases

BioMutaiXBP1
DMDMi60416406

Proteomic databases

EPDiP17861
MaxQBiP17861
PaxDbiP17861
PeptideAtlasiP17861
PRIDEiP17861
ProteomicsDBi53522
53523 [P17861-2]

Protocols and materials databases

The DNASU plasmid repository

More...
DNASUi
7494
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000216037; ENSP00000216037; ENSG00000100219 [P17861-1]
ENST00000344347; ENSP00000343155; ENSG00000100219 [P17861-2]
ENST00000611155; ENSP00000481170; ENSG00000100219 [P17861-2]
GeneIDi7494
KEGGihsa:7494
UCSCiuc062cvg.1 human [P17861-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
7494
DisGeNETi7494
EuPathDBiHostDB:ENSG00000100219.16

GeneCards: human genes, protein and diseases

More...
GeneCardsi
XBP1
HGNCiHGNC:12801 XBP1
MalaCardsiXBP1
MIMi194355 gene
612371 phenotype
neXtProtiNX_P17861
OpenTargetsiENSG00000100219
PharmGKBiPA37400

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG4005 Eukaryota
ENOG410XSJI LUCA
GeneTreeiENSGT00390000017751
HOGENOMiHOG000007671
HOVERGENiHBG061457
InParanoidiP17861
KOiK09027
OMAiLIHFDHI
OrthoDBiEOG091G0T4E
PhylomeDBiP17861
TreeFamiTF319837

Enzyme and pathway databases

ReactomeiR-HSA-381038 XBP1(S) activates chaperone genes
R-HSA-381070 IRE1alpha activates chaperones
R-HSA-381183 ATF6 (ATF6-alpha) activates chaperone genes
SignaLinkiP17861
SIGNORiP17861

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...
ChiTaRSi
XBP1 human

The Gene Wiki collection of pages on human genes and proteins

More...
GeneWikii
XBP1

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...
GenomeRNAii
7494

Protein Ontology

More...
PROi
PR:P17861

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000100219 Expressed in 121 organ(s), highest expression level in body of pancreas
CleanExiHS_XBP1
ExpressionAtlasiP17861 baseline and differential

Family and domain databases

InterProiView protein in InterPro
IPR004827 bZIP
PfamiView protein in Pfam
PF07716 bZIP_2, 1 hit
SMARTiView protein in SMART
SM00338 BRLZ, 1 hit
PROSITEiView protein in PROSITE
PS50217 BZIP, 1 hit
PS00036 BZIP_BASIC, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiXBP1_HUMAN
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P17861
Secondary accession number(s): Q8WYK6, Q969P1, Q96BD7
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: March 1, 2005
Last modified: November 7, 2018
This is version 191 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Human chromosome 22
    Human chromosome 22: entries, gene names and cross-references to MIM
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
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