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Q9EQY0

- ERN1_MOUSE

UniProt

Q9EQY0 - ERN1_MOUSE

Protein

Serine/threonine-protein kinase/endoribonuclease IRE1

Gene

Ern1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 120 (01 Oct 2014)
      Sequence version 1 (01 Mar 2001)
      Previous versions | rss
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    Functioni

    Senses unfolded proteins in the lumen of the endoplasmic reticulum via its N-terminal domain which leads to enzyme auto-activation. The active endoribonuclease domain splices XBP1 mRNA to generate a new C-terminus, converting it into a potent unfolded-protein response transcriptional activator and triggering growth arrest and apoptosis.1 Publication

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.By similarity

    Cofactori

    Magnesium.By similarity

    Enzyme regulationi

    The kinase domain is activated by trans-autophosphorylation. Kinase activity is required for activation of the endoribonuclease domain By similarity.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei599 – 5991ATPBy similarityPROSITE-ProRule annotation
    Active sitei688 – 6881Proton acceptorBy similarityPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi577 – 5859ATPBy similarityPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB
    2. endonuclease activity Source: UniProtKB
    3. endoribonuclease activity Source: MGI
    4. magnesium ion binding Source: UniProtKB
    5. protein binding Source: IntAct
    6. protein serine/threonine kinase activity Source: UniProtKB

    GO - Biological processi

    1. activation of signaling protein activity involved in unfolded protein response Source: UniProtKB
    2. cell cycle arrest Source: UniProtKB
    3. endoplasmic reticulum unfolded protein response Source: MGI
    4. HAC1-type intron splice site recognition and cleavage Source: Ensembl
    5. intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress Source: MGI
    6. nucleic acid phosphodiester bond hydrolysis Source: GOC
    7. positive regulation of endoplasmic reticulum unfolded protein response Source: Ensembl
    8. protein autophosphorylation Source: MGI
    9. protein phosphorylation Source: UniProtKB
    10. regulation of transcription, DNA-templated Source: UniProtKB-KW
    11. RNA phosphodiester bond hydrolysis, endonucleolytic Source: GOC
    12. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Hydrolase, Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Biological processi

    Apoptosis, Transcription, Transcription regulation, Unfolded protein response

    Keywords - Ligandi

    ATP-binding, Magnesium, Metal-binding, Nucleotide-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Serine/threonine-protein kinase/endoribonuclease IRE1
    Alternative name(s):
    Endoplasmic reticulum-to-nucleus signaling 1
    Inositol-requiring protein 1
    Ire1-alpha
    Short name:
    IRE1a
    Including the following 2 domains:
    Gene namesi
    Name:Ern1Imported
    Synonyms:Ire1By similarity
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 11

    Organism-specific databases

    MGIiMGI:1930134. Ern1.

    Subcellular locationi

    Endoplasmic reticulum membrane 1 Publication; Single-pass type I membrane protein 1 Publication

    GO - Cellular componenti

    1. endoplasmic reticulum membrane Source: MGI
    2. integral component of endoplasmic reticulum membrane Source: Ensembl
    3. mitochondrion Source: MGI
    4. nuclear inner membrane Source: UniProtKB

    Keywords - Cellular componenti

    Endoplasmic reticulum, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2020Sequence AnalysisAdd
    BLAST
    Chaini21 – 977957Serine/threonine-protein kinase/endoribonuclease IRE1PRO_0000024328Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi178 – 1781N-linked (GlcNAc...)Sequence Analysis

    Post-translational modificationi

    Autophosphorylated.By similarity
    ADP-ribosylated by PARP16 upon ER stress, which increases both kinase and endonuclease activities.By similarity

    Keywords - PTMi

    ADP-ribosylation, Disulfide bond, Glycoprotein, Phosphoprotein

    Proteomic databases

    MaxQBiQ9EQY0.
    PaxDbiQ9EQY0.
    PRIDEiQ9EQY0.

    Expressioni

    Tissue specificityi

    Ubiquitously expressed. High levels in thymus, liver and lung. In the brain, preferentially expressed in cortical, hippocampal and olfactory neurons.1 Publication

    Gene expression databases

    ArrayExpressiQ9EQY0.
    BgeeiQ9EQY0.
    GenevestigatoriQ9EQY0.

    Interactioni

    Subunit structurei

    Homodimer; disulfide-linked. Dimer formation is driven by hydrophobic interactions within the N-terminal luminal domains and stabilized by disulfide bridges. Also binds HSPA5, a negative regulator of the unfolded protein response. This interaction may disrupt homodimerization and prevent activation of ERN1 By similarity. Interacts with TAOK3 By similarity. Interacts with DAB2IP (via PH domain); the interaction occurs in a ER stress-induced dependent manner and is required for subsequent recruitment of TRAF2 to ERN1. Interacts with TRAF2.By similarity1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Tnfrsf1aP251182EBI-5480799,EBI-518014

    Protein-protein interaction databases

    IntActiQ9EQY0. 4 interactions.
    MINTiMINT-2631281.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9EQY0.
    SMRiQ9EQY0. Positions 31-370, 561-964.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini21 – 445425LumenalSequence AnalysisAdd
    BLAST
    Topological domaini467 – 977511CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei446 – 46621HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini571 – 832262Protein kinasePROSITE-ProRule annotationAdd
    BLAST
    Domaini835 – 963129KENPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the protein kinase superfamily. Ser/Thr protein kinase family.PROSITE-ProRule annotation
    Contains 1 KEN domain.PROSITE-ProRule annotation
    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG0515.
    GeneTreeiENSGT00390000015684.
    HOGENOMiHOG000012929.
    HOVERGENiHBG051506.
    InParanoidiQ9EQY0.
    KOiK08852.
    OMAiGLRKVMH.
    OrthoDBiEOG7C2R0H.
    PhylomeDBiQ9EQY0.
    TreeFamiTF313986.

    Family and domain databases

    Gene3Di2.140.10.10. 2 hits.
    InterProiIPR010513. KEN_dom.
    IPR011009. Kinase-like_dom.
    IPR018391. PQQ_beta_propeller_repeat.
    IPR000719. Prot_kinase_dom.
    IPR006567. PUG-dom.
    IPR027295. Quinonprotein_ADH-like_fam.
    IPR011047. Quinonprotein_ADH-like_supfam.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view]
    PfamiPF00069. Pkinase. 1 hit.
    PF06479. Ribonuc_2-5A. 1 hit.
    [Graphical view]
    SMARTiSM00564. PQQ. 5 hits.
    SM00580. PUG. 1 hit.
    [Graphical view]
    SUPFAMiSSF50998. SSF50998. 1 hit.
    SSF56112. SSF56112. 1 hit.
    PROSITEiPS51392. KEN. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 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. Align

    Isoform 11 Publication (identifier: Q9EQY0-1) [UniParc]FASTAAdd to Basket

    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

    MPARWLLLLL ALLLPPPGPG SFGRTSTVTL PETLLFVSTL DGSLHAVSKR    50
    TGSIKWTLKE DPVLQVPTHV EEPAFLPDPN DGSLYTLGGK NNEGLTKLPF 100
    TIPELVQASP CRSSDGILYM GKKQDIWYVI DLLTGEKQQT LSSAFADSLC 150
    PSTSLLYLGR TEYTITMYDT KTRELRWNAT YFDYAASLPE DDVDYKMSHF 200
    VSNGDGLVVT VDSESGDVLW IQNYASPVVA FYVWQGEVLR KVVHINVAVE 250
    TLRYLTFMSG EVGRITKWKY PFPKETEAKS KLTPTLYVGK YSTSLYASPS 300
    MVHEGVAVVP RGSTLPLLEG PQTDGVTIGD KGECVITPST DLKFDPGLKG 350
    KSKLNYLRNY WLLIGHHETP LSASTKMLER FPNNLPKHRE NVIPADSEKR 400
    SFEEVINIVG QTSDNTPTTV SQDVEEKLAR APAKPEAPVD SMLKDMATII 450
    LSTFLLVGWV AFIITYPLSV HQQRQLQHQQ FQKELEKIQL LQQQQLPFHP 500
    HGDLTQDPEF LDSSGPFSES SGTSSPSPSP RASNHSLHPS SSASRAGTSP 550
    SLEQDDEDEE TRMVIVGKIS FCPKDVLGHG AEGTIVYKGM FDNRDVAVKR 600
    ILPECFSFAD REVQLLRESD EHPNVIRYFC TEKDRQFQYI AIELCAATLQ 650
    EYVEQKDFAH LGLEPITLLH QTTSGLAHLH SLNIVHRDLK PHNILLSMPN 700
    AHGRIKAMIS DFGLCKKLAV GRHSFSRRSG VPGTEGWIAP EMLSEDCKDN 750
    PTYTVDIFSA GCVFYYVISE GNHPFGKSLQ RQANILLGAC NLDCFHSDKH 800
    EDVIARELIE KMIAMDPQQR PSAKHVLKHP FFWSLEKQLQ FFQDVSDRIE 850
    KEALDGPIVR QLERGGRAVV KMDWRENITV PLQTDLRKFR TYKGGSVRDL 900
    LRAMRNKKHH YRELPVEVQE TLGSIPDDFV RYFTSRFPHL LSHTYQAMEL 950
    CRHERLFQTY YWHEPTEPQP PVIPYAL 977
    Length:977
    Mass (Da):110,185
    Last modified:March 1, 2001 - v1
    Checksum:i216E3E2FA2FF3F70
    GO
    Isoform 2Curated (identifier: Q9EQY0-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         406-408: INI → SGK
         409-977: Missing.

    Note: No experimental confirmation available.Curated

    Show »
    Length:408
    Mass (Da):45,303
    Checksum:i4FF98C4A4EC4D1F3
    GO

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei406 – 4083INI → SGK in isoform 2. 1 PublicationVSP_050794
    Alternative sequencei409 – 977569Missing in isoform 2. 1 PublicationVSP_050795Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB031332 mRNA. Translation: BAB20901.1.
    AK018505 mRNA. Translation: BAB31243.1.
    CCDSiCCDS25556.1. [Q9EQY0-1]
    RefSeqiNP_076402.1. NM_023913.2. [Q9EQY0-1]
    UniGeneiMm.340943.

    Genome annotation databases

    EnsembliENSMUST00000001059; ENSMUSP00000001059; ENSMUSG00000020715. [Q9EQY0-1]
    ENSMUST00000106801; ENSMUSP00000102413; ENSMUSG00000020715. [Q9EQY0-2]
    GeneIDi78943.
    KEGGimmu:78943.
    UCSCiuc007lyy.1. mouse. [Q9EQY0-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB031332 mRNA. Translation: BAB20901.1 .
    AK018505 mRNA. Translation: BAB31243.1 .
    CCDSi CCDS25556.1. [Q9EQY0-1 ]
    RefSeqi NP_076402.1. NM_023913.2. [Q9EQY0-1 ]
    UniGenei Mm.340943.

    3D structure databases

    ProteinModelPortali Q9EQY0.
    SMRi Q9EQY0. Positions 31-370, 561-964.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q9EQY0. 4 interactions.
    MINTi MINT-2631281.

    Proteomic databases

    MaxQBi Q9EQY0.
    PaxDbi Q9EQY0.
    PRIDEi Q9EQY0.

    Protocols and materials databases

    DNASUi 78943.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000001059 ; ENSMUSP00000001059 ; ENSMUSG00000020715 . [Q9EQY0-1 ]
    ENSMUST00000106801 ; ENSMUSP00000102413 ; ENSMUSG00000020715 . [Q9EQY0-2 ]
    GeneIDi 78943.
    KEGGi mmu:78943.
    UCSCi uc007lyy.1. mouse. [Q9EQY0-1 ]

    Organism-specific databases

    CTDi 2081.
    MGIi MGI:1930134. Ern1.

    Phylogenomic databases

    eggNOGi COG0515.
    GeneTreei ENSGT00390000015684.
    HOGENOMi HOG000012929.
    HOVERGENi HBG051506.
    InParanoidi Q9EQY0.
    KOi K08852.
    OMAi GLRKVMH.
    OrthoDBi EOG7C2R0H.
    PhylomeDBi Q9EQY0.
    TreeFami TF313986.

    Miscellaneous databases

    NextBioi 349824.
    PROi Q9EQY0.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9EQY0.
    Bgeei Q9EQY0.
    Genevestigatori Q9EQY0.

    Family and domain databases

    Gene3Di 2.140.10.10. 2 hits.
    InterProi IPR010513. KEN_dom.
    IPR011009. Kinase-like_dom.
    IPR018391. PQQ_beta_propeller_repeat.
    IPR000719. Prot_kinase_dom.
    IPR006567. PUG-dom.
    IPR027295. Quinonprotein_ADH-like_fam.
    IPR011047. Quinonprotein_ADH-like_supfam.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view ]
    Pfami PF00069. Pkinase. 1 hit.
    PF06479. Ribonuc_2-5A. 1 hit.
    [Graphical view ]
    SMARTi SM00564. PQQ. 5 hits.
    SM00580. PUG. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50998. SSF50998. 1 hit.
    SSF56112. SSF56112. 1 hit.
    PROSITEi PS51392. KEN. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Characterization of mouse Ire1alpha: cloning, mRNA localization in the brain and functional analysis in a neural cell line."
      Miyoshi K., Katayama T., Imaizumi K., Taniguchi M., Mori Y., Hitomi J., Yui D., Manabe T., Gomi F., Yoneda T., Tohyama M.
      Brain Res. Mol. Brain Res. 85:68-76(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
      Strain: C57BL/61 Publication.
      Tissue: Brain1 Publication.
    2. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Strain: C57BL/6J.
      Tissue: Colon.
    3. "IRE1-mediated unconventional mRNA splicing and S2P-mediated ATF6 cleavage merge to regulate XBP1 in signaling the unfolded protein response."
      Lee K., Tirasophon W., Shen X., Michalak M., Prywes R., Okada T., Yoshida H., Mori K., Kaufman R.J.
      Genes Dev. 16:452-466(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    4. "AIP1 is critical in transducing IRE1-mediated endoplasmic reticulum stress response."
      Luo D., He Y., Zhang H., Yu L., Chen H., Xu Z., Tang S., Urano F., Min W.
      J. Biol. Chem. 283:11905-11912(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH DAB2IP AND TRAF2.

    Entry informationi

    Entry nameiERN1_MOUSE
    AccessioniPrimary (citable) accession number: Q9EQY0
    Secondary accession number(s): Q9D340
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 16, 2004
    Last sequence update: March 1, 2001
    Last modified: October 1, 2014
    This is version 120 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Multifunctional enzyme, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3