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P17861

- XBP1_HUMAN

UniProt

P17861 - XBP1_HUMAN

Protein

X-box-binding protein 1

Gene

XBP1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 149 (01 Oct 2014)
      Sequence version 2 (01 Mar 2005)
      Previous versions | rss
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    Functioni

    Transcription factor essential for hepatocyte growth, the differentiation of plasma cells, the immunoglobulin secretion, and the unfolded protein response (UPR). Acts during endoplasmic reticulum stress (ER) by activating unfolded protein response (UPR) target genes via direct binding to the UPR element (UPRE). Binds DNA preferably to the CRE-like element 5'-GATGACGTG[TG]N3[AT]T-3', and also to some TPA response elements (TRE). Binds to the HLA DR-alpha promoter. Binds to the Tax-responsive element (TRE) of HTLV-I.5 Publications

    GO - Molecular functioni

    1. DNA binding Source: ProtInc
    2. sequence-specific DNA binding Source: Ensembl
    3. sequence-specific DNA binding transcription factor activity Source: ProtInc

    GO - Biological processi

    1. activation of signaling protein activity involved in unfolded protein response Source: Reactome
    2. cellular protein metabolic process Source: Reactome
    3. cellular response to antibiotic Source: Ensembl
    4. endoplasmic reticulum unfolded protein response Source: Reactome
    5. epithelial cell maturation involved in salivary gland development Source: Ensembl
    6. exocrine pancreas development Source: Ensembl
    7. immune response Source: ProtInc
    8. positive regulation of endoplasmic reticulum unfolded protein response Source: UniProtKB
    9. response to drug Source: Ensembl
    10. response to electrical stimulus Source: Ensembl
    11. serotonin secretion, neurotransmission Source: Ensembl
    12. transcription from RNA polymerase II promoter Source: Ensembl

    Keywords - Biological processi

    Transcription, Transcription regulation

    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 1
    Short name:
    XBP-1
    Alternative name(s):
    Tax-responsive element-binding protein 5
    Gene namesi
    Name:XBP1
    Synonyms:TREB5, XBP2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 22

    Organism-specific databases

    HGNCiHGNC:12801. XBP1.

    Subcellular locationi

    GO - Cellular componenti

    1. nucleoplasm Source: Reactome
    2. nucleus Source: LIFEdb

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    Major affective disorder 7 (MAFD7) [MIM:612371]: A major psychiatric disorder that is characterized by severe mood swings, with fluctuation between two abnormal mood states (manic or major depressive episode). Mania is accompanied by symptoms of euphoria, irritability, or excitation, whereas depression is associated with low mood and decreased motivation and energy.
    Note: Disease susceptibility may be associated with variations affecting the gene represented in this entry.

    Organism-specific databases

    MIMi612371. phenotype.
    PharmGKBiPA37400.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 261261X-box-binding protein 1PRO_0000076543Add
    BLAST

    Proteomic databases

    MaxQBiP17861.
    PaxDbiP17861.
    PRIDEiP17861.

    PTM databases

    PhosphoSiteiP17861.

    Expressioni

    Inductioni

    Up-regulated by ATF6 via direct binding to the ERSE in response to endoplasmic reticulum stress.1 Publication

    Gene expression databases

    ArrayExpressiP17861.
    BgeeiP17861.
    CleanExiHS_XBP1.
    GenevestigatoriP17861.

    Organism-specific databases

    HPAiHPA044305.

    Interactioni

    Protein-protein interaction databases

    BioGridi113331. 25 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
    Regioni98 – 13336Leucine-zipperPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiNOG285368.
    HOGENOMiHOG000007671.
    HOVERGENiHBG061457.
    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.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P17861-1) [UniParc]FASTAAdd to Basket

    Also known as: XBP-1U

    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

    MVVVAAAPNP ADGTPKVLLL SGQPASAAGA PAGQALPLMV PAQRGASPEA    50
    ASGGLPQARK RQRLTHLSPE EKALRRKLKN RVAAQTARDR KKARMSELEQ 100
    QVVDLEEENQ KLLLENQLLR EKTHGLVVEN QELRQRLGMD ALVAEEEAEA 150
    KGNEVRPVAG SAESAALRLR APLQQVQAQL SPLQNISPWI LAVLTLQIQS 200
    LISCWAFWTT WTQSCSSNAL PQSLPAWRSS QRSTQKDPVP YQPPFLCQWG 250
    RHQPSWKPLM N 261
    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: XBP-1S

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

    Note: Potent transcriptional activator. Induced by ERN1 in response to endoplasmic reticulum stress. ENR1 cleaves a 26-bp fragment causing a frameshift of the mRNA transcript.

    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:
    EMBL
    GenBank
    DDBJ
    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]
    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:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS13847.1. [P17861-1 ]
    PIRi A36299.
    RefSeqi NP_001073007.1. NM_001079539.1. [P17861-2 ]
    NP_005071.2. NM_005080.3. [P17861-1 ]
    UniGenei Hs.437638.

    3D structure databases

    ProteinModelPortali P17861.
    SMRi P17861. Positions 62-127.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 113331. 25 interactions.
    DIPi DIP-41692N.
    IntActi P17861. 4 interactions.
    MINTi MINT-268152.
    STRINGi 9606.ENSP00000216037.

    Chemistry

    BindingDBi P17861.
    ChEMBLi CHEMBL1741176.

    PTM databases

    PhosphoSitei P17861.

    Polymorphism databases

    DMDMi 60416406.

    Proteomic databases

    MaxQBi P17861.
    PaxDbi P17861.
    PRIDEi P17861.

    Protocols and materials databases

    DNASUi 7494.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000216037 ; ENSP00000216037 ; ENSG00000100219 . [P17861-1 ]
    ENST00000344347 ; ENSP00000343155 ; ENSG00000100219 . [P17861-2 ]
    GeneIDi 7494.
    KEGGi hsa:7494.
    UCSCi uc003aec.3. human. [P17861-2 ]

    Organism-specific databases

    CTDi 7494.
    GeneCardsi GC22M029190.
    HGNCi HGNC:12801. XBP1.
    HPAi HPA044305.
    MIMi 194355. gene.
    612371. phenotype.
    neXtProti NX_P17861.
    PharmGKBi PA37400.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG285368.
    HOGENOMi HOG000007671.
    HOVERGENi HBG061457.
    KOi K09027.
    OMAi FDHIYTK.
    OrthoDBi EOG74BJVQ.
    PhylomeDBi P17861.
    TreeFami TF319837.

    Enzyme and pathway databases

    Reactomei REACT_18273. XBP1(S) activates chaperone genes.
    REACT_18368. IRE1alpha activates chaperones.
    REACT_18423. ATF6-alpha activates chaperone genes.
    SignaLinki P17861.

    Miscellaneous databases

    GeneWikii XBP1.
    GenomeRNAii 7494.
    NextBioi 29352.
    PROi P17861.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P17861.
    Bgeei P17861.
    CleanExi HS_XBP1.
    Genevestigatori P17861.

    Family and domain databases

    InterProi IPR004827. bZIP.
    [Graphical view ]
    Pfami PF07716. bZIP_2. 1 hit.
    [Graphical view ]
    SMARTi SM00338. BRLZ. 1 hit.
    [Graphical view ]
    PROSITEi PS50217. BZIP. 1 hit.
    PS00036. BZIP_BASIC. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION.
    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(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION.
    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(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
    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(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), INDUCTION, FUNCTION.
    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(1999) [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(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Ovary and Placenta.
    8. "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(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    9. "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(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INVOLVEMENT IN SUSCEPTIBILITY TO MAJOR AFFECTIVE DISORDER TYPE 7.
    10. Cited for: VARIANT [LARGE SCALE ANALYSIS] VAL-12.
    11. "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(2007) [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: October 1, 2014
    This is version 149 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