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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-Experimental evidence at protein leveli

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei194 – 1952Cleavage; by HM13/SPP1 Publication

GO - Molecular functioni

  1. chromatin DNA binding Source: UniProtKB
  2. core promoter binding Source: UniProtKB
  3. DNA binding Source: ProtInc
  4. enhancer sequence-specific DNA binding Source: UniProtKB
  5. estrogen receptor binding Source: ParkinsonsUK-UCL
  6. protease binding Source: UniProtKB
  7. protein heterodimerization activity Source: UniProtKB
  8. protein homodimerization activity Source: ParkinsonsUK-UCL
  9. protein kinase binding Source: UniProtKB
  10. RNA polymerase II regulatory region sequence-specific DNA binding Source: UniProtKB
  11. sequence-specific DNA binding RNA polymerase II transcription factor activity Source: Ensembl
  12. sequence-specific DNA binding transcription factor activity Source: UniProtKB
  13. transcription regulatory region DNA binding Source: UniProtKB
  14. ubiquitin protein ligase binding Source: UniProtKB

GO - Biological processi

  1. activation of signaling protein activity involved in unfolded protein response Source: Reactome
  2. adipose tissue development Source: UniProtKB
  3. angiogenesis Source: UniProtKB
  4. apoptotic process Source: UniProtKB-KW
  5. autophagy Source: UniProtKB-KW
  6. cell growth Source: UniProtKB
  7. cellular protein metabolic process Source: Reactome
  8. cellular response to amino acid stimulus Source: UniProtKB
  9. cellular response to antibiotic Source: Ensembl
  10. cellular response to fluid shear stress Source: UniProtKB
  11. cellular response to fructose stimulus Source: UniProtKB
  12. cellular response to glucose starvation Source: UniProtKB
  13. cellular response to glucose stimulus Source: UniProtKB
  14. cellular response to insulin stimulus Source: UniProtKB
  15. cellular response to interleukin-4 Source: UniProtKB
  16. cellular response to laminar fluid shear stress Source: UniProtKB
  17. cellular response to lipopolysaccharide Source: UniProtKB
  18. cellular response to nutrient Source: UniProtKB
  19. cellular response to oxidative stress Source: UniProtKB
  20. cellular response to peptide hormone stimulus Source: UniProtKB
  21. cellular response to vascular endothelial growth factor stimulus Source: UniProtKB
  22. cellular triglyceride homeostasis Source: UniProtKB
  23. cholesterol homeostasis Source: UniProtKB
  24. endoplasmic reticulum unfolded protein response Source: UniProtKB
  25. endothelial cell proliferation Source: UniProtKB
  26. epithelial cell maturation involved in salivary gland development Source: Ensembl
  27. exocrine pancreas development Source: Ensembl
  28. fatty acid biosynthetic process Source: ParkinsonsUK-UCL
  29. fatty acid homeostasis Source: UniProtKB
  30. immune response Source: ParkinsonsUK-UCL
  31. liver development Source: UniProtKB
  32. muscle organ development Source: UniProtKB-KW
  33. negative regulation of apoptotic process Source: UniProtKB
  34. negative regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway Source: ParkinsonsUK-UCL
  35. negative regulation of endoplasmic reticulum unfolded protein response Source: UniProtKB
  36. negative regulation of myotube differentiation Source: UniProtKB
  37. negative regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  38. neuron development Source: UniProtKB
  39. organelle organization Source: ParkinsonsUK-UCL
  40. phosphatidylinositol 3-kinase signaling Source: UniProtKB
  41. positive regulation of autophagy Source: UniProtKB
  42. positive regulation of B cell differentiation Source: UniProtKB
  43. positive regulation of endoplasmic reticulum unfolded protein response Source: UniProtKB
  44. positive regulation of endothelial cell apoptotic process Source: UniProtKB
  45. positive regulation of ER-associated ubiquitin-dependent protein catabolic process Source: ParkinsonsUK-UCL
  46. positive regulation of fat cell differentiation Source: UniProtKB
  47. positive regulation of hepatocyte proliferation Source: UniProtKB
  48. positive regulation of histone methylation Source: UniProtKB
  49. positive regulation of immunoglobulin production Source: UniProtKB
  50. positive regulation of immunoglobulin secretion Source: UniProtKB
  51. positive regulation of interleukin-6 secretion Source: UniProtKB
  52. positive regulation of lactation Source: UniProtKB
  53. positive regulation of MHC class II biosynthetic process Source: UniProtKB
  54. positive regulation of phospholipid biosynthetic process by positive regulation of transcription from RNA polymerase II promoter Source: ParkinsonsUK-UCL
  55. positive regulation of plasma cell differentiation Source: UniProtKB
  56. positive regulation of proteasomal protein catabolic process Source: Ensembl
  57. positive regulation of protein acetylation Source: UniProtKB
  58. positive regulation of protein phosphorylation Source: UniProtKB
  59. positive regulation of T cell differentiation Source: UniProtKB
  60. positive regulation of TOR signaling Source: UniProtKB
  61. positive regulation of transcription factor import into nucleus Source: UniProtKB
  62. positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  63. positive regulation of transcription from RNA polymerase II promoter in response to endoplasmic reticulum stress Source: ParkinsonsUK-UCL
  64. positive regulation of transcription from RNA polymerase II promoter involved in unfolded protein response Source: UniProtKB
  65. protein destabilization Source: UniProtKB
  66. protein transport Source: UniProtKB-KW
  67. regulation of protein stability Source: UniProtKB
  68. response to drug Source: Ensembl
  69. response to electrical stimulus Source: Ensembl
  70. response to endoplasmic reticulum stress Source: UniProtKB
  71. response to insulin-like growth factor stimulus Source: UniProtKB
  72. serotonin secretion, neurotransmission Source: Ensembl
  73. sterol homeostasis Source: UniProtKB
  74. transcription from RNA polymerase II promoter Source: UniProtKB
  75. ubiquitin-dependent protein catabolic process Source: UniProtKB
  76. vascular endothelial growth factor receptor signaling pathway Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Activator, Developmental protein

Keywords - Biological processi

Angiogenesis, Apoptosis, Autophagy, Differentiation, Lipid biosynthesis, Lipid metabolism, Myogenesis, Protein transport, Stress response, Transcription, Transcription regulation, Transport, Unfolded protein response

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiREACT_18273. XBP1(S) activates chaperone genes.
REACT_18368. IRE1alpha activates chaperones.
REACT_18423. ATF6-alpha activates chaperone genes.
SignaLinkiP17861.

Names & Taxonomyi

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
Gene namesi
Name:XBP1Imported
Synonyms:TREB51 Publication, XBP2Imported
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 22

Organism-specific databases

HGNCiHGNC:12801. XBP1.

Subcellular locationi

Endoplasmic reticulum 1 Publication
Note: Colocalizes with ERN1 and KDR in the endoplasmic reticulum in endothelial cells in a vascular endothelial growth factor (VEGF)-dependent manner (PubMed:23529610).1 Publication
Isoform 1 : Nucleus By similarity2 Publications. Cytoplasm By similarity4 Publications. Endoplasmic reticulum membrane 1 Publication; Single-pass type II membrane protein 1 Publication. Endoplasmic reticulum membrane 1 Publication; Peripheral membrane protein 1 Publication. Membrane 1 Publication; Peripheral membrane protein 1 Publication
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).By similarity3 Publications
Isoform 2 : Nucleus By similarity4 Publications. Cytoplasm By similarity
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).By similarity
Chain X-box-binding protein 1, cytoplasmic form : Cytoplasm 1 Publication. Nucleus 1 Publication
Note: Localizes in the cytoplasm and nucleus after HM13/SPP-mediated intramembranaire proteolytic cleavage of isoform 1 (PubMed:25239945).1 Publication

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 185185Cytoplasmic1 PublicationAdd
BLAST
Transmembranei186 – 20318Helical; Signal-anchor for type II membrane protein1 PublicationSequence Analysis1 PublicationAdd
BLAST
Topological domaini204 – 26158Lumenal1 PublicationAdd
BLAST

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. cytosol Source: UniProtKB
  3. endoplasmic reticulum Source: UniProtKB
  4. endoplasmic reticulum membrane Source: UniProtKB-SubCell
  5. integral component of endoplasmic reticulum membrane Source: UniProtKB
  6. integral component of membrane Source: UniProtKB-KW
  7. nucleoplasm Source: Reactome
  8. nucleus Source: LIFEdb
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endoplasmic reticulum, Membrane, Nucleus

Pathology & Biotechi

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)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi189 – 1891W → E: Reduces endoplasmic reticulum localization of its own mRNA; when associated with E-193 and D-196. 1 Publication
Mutagenesisi193 – 1931V → E: Reduces endoplasmic reticulum localization of its own mRNA; when associated with E-189 and D-196. 1 Publication
Mutagenesisi194 – 1941L → E: Reduces endoplasmic reticulum localization of its own mRNA; when associated with D-198 and E-205. 1 Publication
Mutagenesisi196 – 1961L → D: Reduces endoplasmic reticulum localization of its own mRNA; when associated with E-189 and E-193. 1 Publication
Mutagenesisi197 – 1971Q → L: Inhibits HM13/SPP-mediated degradation of XBP1; when associated with L-199; L-200 and L-203. 1 Publication
Mutagenesisi198 – 1981I → D: Reduces endoplasmic reticulum localization of its own mRNA; when associated with E-194 and E-205. 1 Publication
Mutagenesisi199 – 1991Q → L: Inhibits HM13/SPP-mediated degradation of XBP1; when associated with L-197; L-200 and L-203. 1 Publication
Mutagenesisi200 – 2001S → L: Inhibits HM13/SPP-mediated degradation of XBP1; when associated with L-197; L-199 and L-203. 1 Publication
Mutagenesisi203 – 2031S → L: Inhibits HM13/SPP-mediated degradation of XBP1; when associated with L-197; L-199 and L-200. 1 Publication
Mutagenesisi205 – 2051W → E: Reduces endoplasmic reticulum localization of its own mRNA; when associated with E-194 and D-198. 1 Publication
Mutagenesisi212 – 2121T → N: Does not induce glycosylation. 1 Publication
Mutagenesisi215 – 2151C → N: Induces glycosylation. 1 Publication
Mutagenesisi232 – 2321R → N: Induces glycosylation. 1 Publication
Mutagenesisi246 – 2461L → A: Reduces translational pausing, membrane targeting and cytoplasmic splicing of its own mRNA. 1 Publication
Mutagenesisi255 – 2551S → A: Increases translational pausing of its own mRNA. 1 Publication
Mutagenesisi256 – 2561W → A: Reduces translational pausing, membrane targeting and cytoplasmic splicing of its own mRNA. 1 Publication

Keywords - Diseasei

Oncogene

Organism-specific databases

MIMi612371. phenotype.
PharmGKBiPA37400.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 261261X-box-binding protein 1PRO_0000076543Add
BLAST
Chaini1 – 193193X-box-binding protein 1, cytoplasmic form1 PublicationPRO_0000431891Add
BLAST
Chaini196 – 26166X-box-binding protein 1, luminal form1 PublicationPRO_0000431892Add
BLAST

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

Keywords - PTMi

Acetylation, Cleavage on pair of basic residues, Ubl conjugation

Proteomic databases

MaxQBiP17861.
PaxDbiP17861.
PRIDEiP17861.

PTM databases

PhosphoSiteiP17861.

Expressioni

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

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

BgeeiP17861.
CleanExiHS_XBP1.
ExpressionAtlasiP17861. differential.
GenevestigatoriP17861.

Organism-specific databases

HPAiHPA044305.

Interactioni

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

Protein-protein interaction databases

BioGridi113331. 28 interactions.
DIPiDIP-41692N.
IntActiP17861. 4 interactions.
MINTiMINT-268152.
STRINGi9606.ENSP00000216037.

Structurei

3D structure databases

ProteinModelPortaliP17861.
SMRiP17861. Positions 62-127.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini70 – 13364bZIPPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni72 – 9423Basic motifPROSITE-ProRule annotationAdd
BLAST
Regioni75 – 9218Nuclear localization signal (NLS); in isoforms 1 and isoform 21 PublicationAdd
BLAST
Regioni98 – 13336Leucine-zipperPROSITE-ProRule annotationAdd
BLAST
Regioni235 – 26127Necessary for the translational pausing of its own mRNA1 PublicationAdd
BLAST

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

Sequence similaritiesi

Belongs to the bZIP family.Curated
Contains 1 bZIP (basic-leucine zipper) domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG285368.
GeneTreeiENSGT00390000017751.
HOGENOMiHOG000007671.
HOVERGENiHBG061457.
InParanoidiP17861.
KOiK09027.
OMAiFDHIYTK.
OrthoDBiEOG74BJVQ.
PhylomeDBiP17861.
TreeFamiTF319837.

Family and domain databases

InterProiIPR004827. bZIP.
[Graphical view]
PfamiPF07716. bZIP_2. 1 hit.
[Graphical view]
SMARTiSM00338. BRLZ. 1 hit.
[Graphical view]
PROSITEiPS50217. BZIP. 1 hit.
PS00036. BZIP_BASIC. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

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
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 (Ref.4, Ref.18, Ref.19). ENR1 cleaves a 26-bp fragment causing a frameshift of the mRNA transcript (Ref.4).3 Publications

Show »
Length:376
Mass (Da):40,148
Checksum:i4C1758D7BA055061
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti33 – 353GQA → AR in AAA36031 (PubMed:2321018).Curated
Sequence conflicti130 – 1301N → T in L13850 (PubMed:8349596).Curated
Sequence conflicti196 – 1961L → F in L13850 (PubMed:8349596).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti12 – 121D → V in a breast cancer sample; somatic mutation. 1 Publication
VAR_035998
Natural varianti232 – 2321R → K in a breast cancer sample; somatic mutation. 1 Publication
VAR_033023

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei167 – 26195LRLRA…KPLMN → GAGPVVTPPEHLPMDSGGID SSDSESDILLGILDNLDPVM FFKCPSPEPASLEELPEVYP EGPSSLPASLSLSVGTSSAK LEAINELIRFDHIYTKPLVL EIPSETESQANVVVKIEEAP LSPSENDHPEFIVSVKEEPV EDDLVPELGISNLLSSSHCP KPSSCLLDAYSDCGYGGSLS PFSDMSSLLGVNHSWEDTFA NELFPQLISV in isoform 2. 1 PublicationVSP_012936Add
BLAST

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. Translation: CAB45016.1.
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.

Genome annotation databases

EnsembliENST00000216037; ENSP00000216037; ENSG00000100219. [P17861-1]
ENST00000344347; ENSP00000343155; ENSG00000100219. [P17861-2]
ENST00000611155; ENSP00000481170; ENSG00000100219. [P17861-2]
GeneIDi7494.
KEGGihsa:7494.
UCSCiuc003aec.3. human. [P17861-2]

Polymorphism databases

DMDMi60416406.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

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. Translation: CAB45016.1.
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. Positions 62-127.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi113331. 28 interactions.
DIPiDIP-41692N.
IntActiP17861. 4 interactions.
MINTiMINT-268152.
STRINGi9606.ENSP00000216037.

Chemistry

BindingDBiP17861.
ChEMBLiCHEMBL1741176.

PTM databases

PhosphoSiteiP17861.

Polymorphism databases

DMDMi60416406.

Proteomic databases

MaxQBiP17861.
PaxDbiP17861.
PRIDEiP17861.

Protocols and materials databases

DNASUi7494.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000216037; ENSP00000216037; ENSG00000100219. [P17861-1]
ENST00000344347; ENSP00000343155; ENSG00000100219. [P17861-2]
ENST00000611155; ENSP00000481170; ENSG00000100219. [P17861-2]
GeneIDi7494.
KEGGihsa:7494.
UCSCiuc003aec.3. human. [P17861-2]

Organism-specific databases

CTDi7494.
GeneCardsiGC22M029190.
HGNCiHGNC:12801. XBP1.
HPAiHPA044305.
MIMi194355. gene.
612371. phenotype.
neXtProtiNX_P17861.
PharmGKBiPA37400.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG285368.
GeneTreeiENSGT00390000017751.
HOGENOMiHOG000007671.
HOVERGENiHBG061457.
InParanoidiP17861.
KOiK09027.
OMAiFDHIYTK.
OrthoDBiEOG74BJVQ.
PhylomeDBiP17861.
TreeFamiTF319837.

Enzyme and pathway databases

ReactomeiREACT_18273. XBP1(S) activates chaperone genes.
REACT_18368. IRE1alpha activates chaperones.
REACT_18423. ATF6-alpha activates chaperone genes.
SignaLinkiP17861.

Miscellaneous databases

ChiTaRSiXBP1. human.
GeneWikiiXBP1.
GenomeRNAii7494.
NextBioi29352.
PROiP17861.
SOURCEiSearch...

Gene expression databases

BgeeiP17861.
CleanExiHS_XBP1.
ExpressionAtlasiP17861. differential.
GenevestigatoriP17861.

Family and domain databases

InterProiIPR004827. bZIP.
[Graphical view]
PfamiPF07716. bZIP_2. 1 hit.
[Graphical view]
SMARTiSM00338. BRLZ. 1 hit.
[Graphical view]
PROSITEiPS50217. BZIP. 1 hit.
PS00036. BZIP_BASIC. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A new member of the leucine zipper class of proteins that binds to the HLA DR alpha promoter."
    Liou H.-C., Boothby M.R., Finn P.W., Davidon R., Nabavi N., Zeleznik-Le N.J., Ting J.P.-Y., Glimcher L.H.
    Science 247:1581-1584(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION (ISOFORM 1), DNA-BINDING (ISOFORM 1).
    Tissue: B-cell.
  2. "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."
    Yoshimura T., Fujisawa J., Yoshida M.
    EMBO J. 9:2537-2542(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION (ISOFORM 1), DNA-BINDING (ISOFORM 1).
  3. "The regulatory gene, hXBP-1, and its target, HLA-DRA, utilize both common and distinct regulatory elements and protein complexes."
    Ponath P.D., Fass D., Liou H.C., Glimcher L.H., Strominger J.L.
    J. Biol. Chem. 268:17074-17082(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, DNA-BINDING.
  4. "XBP1 mRNA is induced by ATF6 and spliced by IRE1 in response to ER stress to produce a highly active transcription factor."
    Yoshida H., Matsui T., Yamamoto A., Okada T., Mori K.
    Cell 107:881-891(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: 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), DOMAIN ((ISOFORMS 1 AND 2).
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  6. "The DNA sequence of human chromosome 22."
    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.
    Nature 402:489-495(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Ovary and Placenta.
  8. "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."
    Ono S.J., Liou H.C., Davidon R., Strominger J.L., Glimcher L.H.
    Proc. Natl. Acad. Sci. U.S.A. 88:4309-4312(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION (ISOFORM 1), DNA-BINDING (ISOFORM 1), INTERACTION WITH FOS (ISOFORM 1).
  9. "Transcription factor B cell lineage-specific activator protein regulates the gene for human X-box binding protein 1."
    Reimold A.M., Ponath P.D., Li Y.S., Hardy R.R., David C.S., Strominger J.L., Glimcher L.H.
    J. Exp. Med. 183:393-401(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  10. "The basic domain/leucine zipper protein hXBP-1 preferentially binds to and transactivates CRE-like sequences containing an ACGT core."
    Clauss I.M., Chu M., Zhao J.-L., Glimcher L.H.
    Nucleic Acids Res. 24:1855-1864(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION (ISOFORM 1), DNA-BINDING (ISOFORM 1), DOMAIN (ISOFORMS 1 AND 2).
  11. "Identification of c-myc promoter-binding protein and X-box binding protein 1 as interleukin-6 target genes in human multiple myeloma cells."
    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.
    Int. J. Oncol. 15:173-178(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  12. Cited for: FUNCTION, INDUCTION, TISSUE SPECIFICITY.
  13. "Impaired feedback regulation of XBP1 as a genetic risk factor for bipolar disorder."
    Kakiuchi C., Iwamoto K., Ishiwata M., Bundo M., Kasahara T., Kusumi I., Tsujita T., Okazaki Y., Nanko S., Kunugi H., Sasaki T., Kato T.
    Nat. Genet. 35:171-175(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN SUSCEPTIBILITY TO MAJOR AFFECTIVE DISORDER TYPE 7.
  14. "XBP1: a link between the unfolded protein response, lipid biosynthesis, and biogenesis of the endoplasmic reticulum."
    Sriburi R., Jackowski S., Mori K., Brewer J.W.
    J. Cell Biol. 167:35-41(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION (ISOFORM 2).
  15. "XBP1 is critical to protect cells from endoplasmic reticulum stress: evidence from Site-2 protease-deficient Chinese hamster ovary cells."
    Yoshida H., Nadanaka S., Sato R., Mori K.
    Cell Struct. Funct. 31:117-125(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION (ISOFORM 2).
  16. "pXBP1(U) encoded in XBP1 pre-mRNA negatively regulates unfolded protein response activator pXBP1(S) in mammalian ER stress response."
    Yoshida H., Oku M., Suzuki M., Mori K.
    J. Cell Biol. 172:565-575(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: 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), DOMAIN (ISOFORMS 1 AND 2).
  17. "Transcriptional induction of mammalian ER quality control proteins is mediated by single or combined action of ATF6alpha and XBP1."
    Yamamoto K., Sato T., Matsui T., Sato M., Okada T., Yoshida H., Harada A., Mori K.
    Dev. Cell 13:365-376(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ATF6 (ISOFORM 2).
  18. "Unconventional splicing of XBP1 mRNA occurs in the cytoplasm during the mammalian unfolded protein response."
    Uemura A., Oku M., Mori K., Yoshida H.
    J. Cell Sci. 122:2877-2886(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: UNCONVENTIONAL ALTERNATIVE SPLICING (ISOFORM 2).
  19. "Cotranslational targeting of XBP1 protein to the membrane promotes cytoplasmic splicing of its own mRNA."
    Yanagitani K., Imagawa Y., Iwawaki T., Hosoda A., Saito M., Kimata Y., Kohno K.
    Mol. Cell 34:191-200(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION (ISOFORM 1), SUBCELLULAR LOCATION (ISOFORMS 1 AND 2), TOPOLOGY (ISOFORM 1), DOMAIN (ISOFORM 1), MUTAGENESIS OF TRP-189; VAL-193; LEU-194; LEU-196; ILE-198 AND TRP-205.
  20. "Sustained activation of XBP1 splicing leads to endothelial apoptosis and atherosclerosis development in response to disturbed flow."
    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.
    Proc. Natl. Acad. Sci. U.S.A. 106:8326-8331(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION (ISOFORM 2), DNA-BINDING (ISOFORMS 1 AND 2), INDUCTION (ISOFORMS 1 AND 2), TISSUE SPECIFICITY (ISOFORMS 1 AND 2).
  21. "A regulatory subunit of phosphoinositide 3-kinase increases the nuclear accumulation of X-box-binding protein-1 to modulate the unfolded protein response."
    Winnay J.N., Boucher J., Mori M.A., Ueki K., Kahn C.R.
    Nat. Med. 16:438-445(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH PIK3R1 (ISOFORM 2), SUBCELLULAR LOCATION (ISOFORMS 1 AND 2).
  22. "Regulation of unfolded protein response modulator XBP1s by acetylation and deacetylation."
    Wang F.M., Chen Y.J., Ouyang H.J.
    Biochem. J. 433:245-252(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION BY EP300 (ISOFORM 2), DEACETYLATION BY SIRT1 (ISOFORM 2), SUBCELLULAR LOCATION (ISOFORM 2).
  23. "Translational pausing ensures membrane targeting and cytoplasmic splicing of XBP1u mRNA."
    Yanagitani K., Kimata Y., Kadokura H., Kohno K.
    Science 331:586-589(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION (ISOFORM 1), DOMAIN (ISOFORM 1), MUTAGENESIS OF LEU-246; SER-255 AND TRP-256.
  24. "Vascular endothelial cell growth-activated XBP1 splicing in endothelial cells is crucial for angiogenesis."
    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.
    Circulation 127:1712-1722(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION (ISOFORMS 1 AND 2), SUBCELLULAR LOCATION, INDUCTION (ISOFORM 2).
  25. "XBP1 mRNA splicing triggers an autophagic response in endothelial cells through BECLIN-1 transcriptional activation."
    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.
    J. Biol. Chem. 288:859-872(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION (ISOFORM 2), DNA-BINDING (ISOFORM 2), INDUCTION (ISOFORM 2).
  26. "XBP1 induces snail expression to promote epithelial-to-mesenchymal transition and invasion of breast cancer cells."
    Li H., Chen X., Gao Y., Wu J., Zeng F., Song F.
    Cell. Signal. 27:82-89(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION (ISOFORM 2), TISSUE SPECIFICITY.
  27. "Signal peptide peptidase functions in ERAD to cleave the unfolded protein response regulator XBP1u."
    Chen C.Y., Malchus N.S., Hehn B., Stelzer W., Avci D., Langosch D., Lemberg M.K.
    EMBO J. 33:2492-2506(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: 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), MUTAGENESIS OF GLN-197; GLN-199; SER-200; SER-203; THR-212; CYS-215 AND ARG-232.
  28. "Unspliced X-box-binding protein 1 (XBP1) protects endothelial cells from oxidative stress through interaction with histone deacetylase 3."
    Martin D., Li Y., Yang J., Wang G., Margariti A., Jiang Z., Yu H., Zampetaki A., Hu Y., Xu Q., Zeng L.
    J. Biol. Chem. 289:30625-30634(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION (ISOFORM 1), DNA-BINDING (ISOFORMS 1 AND 2), INTERACTION WITH HDAC3 AND AKT1 (ISOFORM 1), SUBCELLULAR LOCATION (ISOFORM 1), INDUCTION (ISOFORMS 1 AND 2).
  29. Cited for: VARIANT [LARGE SCALE ANALYSIS] VAL-12.
  30. "Somatic sequence alterations in twenty-one genes selected by expression profile analysis of breast carcinomas."
    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.
    Breast Cancer Res. 9:R5-R5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT LYS-232.

Entry informationi

Entry nameiXBP1_HUMAN
AccessioniPrimary (citable) accession number: P17861
Secondary accession number(s): Q8WYK6, Q969P1, Q96BD7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: March 1, 2005
Last modified: April 1, 2015
This is version 155 of the entry and version 2 of the sequence. [Complete history]
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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

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

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.