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Q9Z2E3

- ERN2_MOUSE

UniProt

Q9Z2E3 - ERN2_MOUSE

Protein

Serine/threonine-protein kinase/endoribonuclease IRE2

Gene

Ern2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 115 (01 Oct 2014)
      Sequence version 2 (27 Jul 2011)
      Previous versions | rss
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    Functioni

    Role in expression of the DDIT3 transcription factor, required for the unfolded-protein response, growth arrest and apoptosis. Has no effect on 28S ribosomal RNA cleavage, unlike the corresponding human protein.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 sitei536 – 5361ATPBy similarityPROSITE-ProRule annotation
    Active sitei625 – 6251Proton acceptorBy similarityPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi514 – 5229ATPBy similarityPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB
    2. endonuclease activity Source: Ensembl
    3. magnesium ion binding Source: UniProtKB
    4. protein serine/threonine kinase activity Source: UniProtKB
    5. ribonuclease activity Source: InterPro

    GO - Biological processi

    1. activation of signaling protein activity involved in unfolded protein response Source: UniProtKB
    2. apoptotic chromosome condensation Source: Ensembl
    3. cell cycle arrest Source: UniProtKB
    4. intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress Source: MGI
    5. mRNA processing Source: InterPro
    6. negative regulation of transcription, DNA-templated Source: Ensembl
    7. protein phosphorylation Source: UniProtKB
    8. regulation of transcription, DNA-templated Source: UniProtKB
    9. response to endoplasmic reticulum stress Source: MGI
    10. rRNA catabolic process Source: Ensembl
    11. 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 IRE2
    Alternative name(s):
    Endoplasmic reticulum-to-nucleus signaling 2
    Inositol-requiring protein 2
    Ire1-beta
    Short name:
    IRE1b
    Short name:
    mIre1
    Including the following 2 domains:
    Gene namesi
    Name:Ern2Imported
    Synonyms:Ire2By similarity
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 7

    Organism-specific databases

    MGIiMGI:1349436. Ern2.

    Subcellular locationi

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

    GO - Cellular componenti

    1. endoplasmic reticulum membrane Source: UniProtKB-SubCell
    2. integral component of membrane Source: UniProtKB-KW

    Keywords - Cellular componenti

    Endoplasmic reticulum, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 3333Sequence AnalysisAdd
    BLAST
    Chaini34 – 911878Serine/threonine-protein kinase/endoribonuclease IRE2PRO_0000024330Add
    BLAST

    Amino acid modifications

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

    Post-translational modificationi

    Autophosphorylated.By similarity

    Keywords - PTMi

    Glycoprotein, Phosphoprotein

    Proteomic databases

    MaxQBiQ9Z2E3.
    PRIDEiQ9Z2E3.

    PTM databases

    PhosphoSiteiQ9Z2E3.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9Z2E3.
    BgeeiQ9Z2E3.
    GenevestigatoriQ9Z2E3.

    Interactioni

    Protein-protein interaction databases

    BioGridi205062. 3 interactions.
    STRINGi10090.ENSMUSP00000033153.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9Z2E3.
    SMRiQ9Z2E3. Positions 36-310, 472-897.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini35 – 426392LumenalSequence AnalysisAdd
    BLAST
    Topological domaini448 – 911464CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei427 – 44721HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini508 – 768261Protein kinasePROSITE-ProRule annotationAdd
    BLAST
    Domaini771 – 899129KENPROSITE-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.
    InParanoidiQ3U5E3.
    KOiK11715.
    OMAiMLRVHPT.
    OrthoDBiEOG7C2R0H.
    TreeFamiTF313986.

    Family and domain databases

    Gene3Di2.140.10.10. 1 hit.
    InterProiIPR010513. KEN_dom.
    IPR011009. Kinase-like_dom.
    IPR018391. PQQ_beta_propeller_repeat.
    IPR002372. PQQ_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.
    PF01011. PQQ. 1 hit.
    PF06479. Ribonuc_2-5A. 1 hit.
    [Graphical view]
    SMARTiSM00564. PQQ. 4 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]

    Sequencei

    Sequence statusi: Complete.

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

    Q9Z2E3-1 [UniParc]FASTAAdd to Basket

    « Hide

    MARPVQRFQL WSPLGFLLQL VTLLGKLGPQ VQSVRPESLL FVSTLDGSLH    50
    ALNKQTGDLK WTVKDDPIIQ GPMYVTEMAF LSDPADGSLY VLGTQKQQGL 100
    MKLPFTIPEL VHASPCRSSD GVFYTGRKQD AWFVVDPESG ETQMTLTTEG 150
    LSTPQLFIGR TQYTVSMHDL RTPALRWNTT YRRYSAPLLN GSPGKYMSHL 200
    TSCGMGLLLT VDPGSGIVLW TQDLGVPVTG IYTWHQDGLH QLPHLTLARD 250
    TLHFLVLRWG HIRLPASSYQ DTATQFSSLD TQLLMTLYVG KEEAGFYVSK 300
    ALVHAGVALV PRGLTLAPMD GPTTDEVTLQ VSGEREGSPS TAVRYPSGSV 350
    ALPSQWLLIG YHEPPPVLHT TMLRVHPIPG KVSAETRASE DLHAPPVFFE 400
    LLNLRREDPE LHPEEKASDS YPGLGSQDLL AATFTAILLG AWVLYLMRQQ 450
    QQSPSAPAGP PDLSQDAQGQ LSRDILQDQR RFQSPSEPAQ PPHDPEAGQP 500
    TVVGKISFNP KDVLGRGAGG TFVFRGQFEG RAVAVKRLLR ECFGLVRREV 550
    QLLQESDRHP NVLRYFCTEH GPQFHYIALE LCQASLQEYV ESPDLDRWGL 600
    EPTTVLQQMM SGLAHLHSLH IVHRDLKPAN ILMAGPDSQG QGRVVISDFG 650
    LCKKLPVGRC SFSLHSGIPG TEGWMAPELL QLPPDSPTSA VDIFSAGCVF 700
    YYVLSGGSHP FGESLYRQAN ILSGDPCLAQ LQEETHDKVV ALDLVRAMLS 750
    LLPQDRPSAG WVLAHPLFWS RAKELQFFQD VSDWLEKEPD QGPLVSALEA 800
    GSYKVVREDW HKHISAPLQA DLKRFRSYKG TSVRDLLRAM RNKKHHYREL 850
    PAEVRQTLGQ LPAGFIQYFT QRFPRLLLHT HRAMRTCASE SLFLPYYPPA 900
    LEARRPDATK S 911
    Length:911
    Mass (Da):101,262
    Last modified:July 27, 2011 - v2
    Checksum:i77E210F1D8D15737
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti45 – 451L → W in AAC64400. (PubMed:9755171)Curated
    Sequence conflicti95 – 951Q → H in AAC64400. (PubMed:9755171)Curated
    Sequence conflicti97 – 971Q → L in AAC64400. (PubMed:9755171)Curated
    Sequence conflicti689 – 6891S → N in AAC64400. (PubMed:9755171)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF071777 mRNA. Translation: AAC64400.1.
    AK153659 mRNA. Translation: BAE32136.1.
    CH466531 Genomic DNA. Translation: EDL17275.1.
    CCDSiCCDS21813.1.
    RefSeqiNP_036146.2. NM_012016.2.
    UniGeneiMm.20452.

    Genome annotation databases

    EnsembliENSMUST00000033153; ENSMUSP00000033153; ENSMUSG00000030866.
    GeneIDi26918.
    KEGGimmu:26918.
    UCSCiuc009joq.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF071777 mRNA. Translation: AAC64400.1 .
    AK153659 mRNA. Translation: BAE32136.1 .
    CH466531 Genomic DNA. Translation: EDL17275.1 .
    CCDSi CCDS21813.1.
    RefSeqi NP_036146.2. NM_012016.2.
    UniGenei Mm.20452.

    3D structure databases

    ProteinModelPortali Q9Z2E3.
    SMRi Q9Z2E3. Positions 36-310, 472-897.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 205062. 3 interactions.
    STRINGi 10090.ENSMUSP00000033153.

    PTM databases

    PhosphoSitei Q9Z2E3.

    Proteomic databases

    MaxQBi Q9Z2E3.
    PRIDEi Q9Z2E3.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000033153 ; ENSMUSP00000033153 ; ENSMUSG00000030866 .
    GeneIDi 26918.
    KEGGi mmu:26918.
    UCSCi uc009joq.1. mouse.

    Organism-specific databases

    CTDi 10595.
    MGIi MGI:1349436. Ern2.

    Phylogenomic databases

    eggNOGi COG0515.
    GeneTreei ENSGT00390000015684.
    HOGENOMi HOG000012929.
    HOVERGENi HBG051506.
    InParanoidi Q3U5E3.
    KOi K11715.
    OMAi MLRVHPT.
    OrthoDBi EOG7C2R0H.
    TreeFami TF313986.

    Miscellaneous databases

    NextBioi 304797.
    PROi Q9Z2E3.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9Z2E3.
    Bgeei Q9Z2E3.
    Genevestigatori Q9Z2E3.

    Family and domain databases

    Gene3Di 2.140.10.10. 1 hit.
    InterProi IPR010513. KEN_dom.
    IPR011009. Kinase-like_dom.
    IPR018391. PQQ_beta_propeller_repeat.
    IPR002372. PQQ_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.
    PF01011. PQQ. 1 hit.
    PF06479. Ribonuc_2-5A. 1 hit.
    [Graphical view ]
    SMARTi SM00564. PQQ. 4 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. "Cloning of mammalian Ire1 reveals a diversity in the ER stress responses."
      Wang X.-Z., Harding H.P., Zhang Y., Jolicoeur E.M., Kuroda M., Ron D.
      EMBO J. 17:5708-5717(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION.
    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].
      Strain: C57BL/6J.
      Tissue: Thymus.
    3. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
      Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

    Entry informationi

    Entry nameiERN2_MOUSE
    AccessioniPrimary (citable) accession number: Q9Z2E3
    Secondary accession number(s): Q3U5E3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 16, 2004
    Last sequence update: July 27, 2011
    Last modified: October 1, 2014
    This is version 115 of the entry and version 2 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