Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P32361

- IRE1_YEAST

UniProt

P32361 - IRE1_YEAST

Protein

Serine/threonine-protein kinase/endoribonuclease IRE1

Gene

IRE1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 153 (01 Oct 2014)
      Sequence version 2 (01 Feb 1995)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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 HAC1 precursor mRNA to produce the mature form which then induces transcription of UPR target genes.3 Publications

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.

    Cofactori

    Magnesium.

    Enzyme regulationi

    The kinase domain is activated by trans-autophosphorylation. Kinase activity is required for activation of the endoribonuclease domain.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei702 – 7021ATP
    Active sitei797 – 7971Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi680 – 6889ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. endoribonuclease activity Source: SGD
    3. identical protein binding Source: IntAct
    4. metal ion binding Source: UniProtKB-KW
    5. protein binding Source: IntAct
    6. protein homodimerization activity Source: SGD
    7. protein serine/threonine kinase activity Source: SGD
    8. unfolded protein binding Source: SGD

    GO - Biological processi

    1. endoplasmic reticulum unfolded protein response Source: SGD
    2. fungal-type cell wall organization Source: SGD
    3. inositol metabolic process Source: SGD
    4. mRNA processing Source: InterPro
    5. protein homooligomerization Source: SGD
    6. protein phosphorylation Source: SGD
    7. protein trans-autophosphorylation Source: SGD
    8. regulation of transcription, DNA-templated Source: UniProtKB-KW
    9. RNA phosphodiester bond hydrolysis, endonucleolytic Source: GOC
    10. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

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

    Keywords - Biological processi

    Transcription, Transcription regulation, Unfolded protein response

    Keywords - Ligandi

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

    Enzyme and pathway databases

    BioCyciYEAST:G3O-31126-MONOMER.
    BRENDAi2.7.11.1. 984.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Serine/threonine-protein kinase/endoribonuclease IRE1
    Alternative name(s):
    Endoplasmic reticulum-to-nucleus signaling 1
    Including the following 2 domains:
    Gene namesi
    Name:IRE1
    Synonyms:ERN1
    Ordered Locus Names:YHR079C
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome VIII

    Organism-specific databases

    CYGDiYHR079c.
    SGDiS000001121. IRE1.

    Subcellular locationi

    GO - Cellular componenti

    1. endoplasmic reticulum membrane Source: Reactome
    2. integral component of endoplasmic reticulum membrane Source: SGD
    3. nucleus Source: SGD

    Keywords - Cellular componenti

    Endoplasmic reticulum, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi702 – 7021K → A: Loss of autophosphorylation. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1818Sequence AnalysisAdd
    BLAST
    Chaini19 – 11151097Serine/threonine-protein kinase/endoribonuclease IRE1PRO_0000024338Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi111 – 1111N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi213 – 2131N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi298 – 2981N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi397 – 3971N-linked (GlcNAc...)Sequence Analysis
    Modified residuei840 – 8401Phosphoserine; by autocatalysis1 Publication
    Modified residuei841 – 8411Phosphoserine; by autocatalysis1 Publication

    Post-translational modificationi

    Autophosphorylated mainly on serine residues.1 Publication

    Keywords - PTMi

    Glycoprotein, Phosphoprotein

    Proteomic databases

    MaxQBiP32361.
    PRIDEiP32361.

    Expressioni

    Gene expression databases

    GenevestigatoriP32361.

    Interactioni

    Subunit structurei

    Homodimer; in response to the accumulation of unfolded proteins.

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself2EBI-9364,EBI-9364
    DCR2Q059242EBI-9364,EBI-3669144

    Protein-protein interaction databases

    BioGridi36513. 334 interactions.
    DIPiDIP-233N.
    IntActiP32361. 4 interactions.
    MINTiMINT-408165.
    STRINGi4932.YHR079C.

    Structurei

    Secondary structure

    1
    1115
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi116 – 12712
    Beta strandi132 – 1365
    Turni137 – 1393
    Beta strandi142 – 1465
    Helixi148 – 1503
    Beta strandi154 – 1563
    Turni162 – 1643
    Beta strandi165 – 1717
    Turni175 – 1773
    Beta strandi178 – 1836
    Turni184 – 1863
    Beta strandi187 – 1948
    Helixi195 – 1995
    Beta strandi203 – 2075
    Beta strandi222 – 2265
    Beta strandi228 – 23710
    Turni238 – 2403
    Beta strandi243 – 2486
    Beta strandi277 – 28610
    Beta strandi300 – 3056
    Turni308 – 3103
    Helixi311 – 3144
    Beta strandi321 – 3233
    Beta strandi326 – 3294
    Turni330 – 3323
    Beta strandi333 – 3375
    Beta strandi344 – 3474
    Beta strandi355 – 36410
    Turni365 – 3684
    Beta strandi369 – 3746
    Beta strandi390 – 3945
    Beta strandi400 – 4045
    Turni405 – 4073
    Helixi409 – 4135
    Helixi419 – 4224
    Helixi424 – 4263
    Helixi429 – 4335
    Helixi435 – 4428
    Beta strandi444 – 4463
    Turni666 – 6694
    Beta strandi674 – 6829
    Turni684 – 6863
    Beta strandi688 – 70518
    Helixi706 – 7083
    Helixi709 – 72214
    Beta strandi731 – 7366
    Beta strandi738 – 7458
    Beta strandi749 – 7513
    Helixi752 – 7576
    Helixi765 – 7695
    Helixi774 – 79017
    Helixi800 – 8023
    Beta strandi803 – 8064
    Helixi809 – 8124
    Beta strandi823 – 8264
    Turni836 – 8383
    Helixi851 – 8555
    Helixi858 – 8614
    Helixi900 – 91415
    Turni924 – 9263
    Helixi927 – 9337
    Helixi947 – 96014
    Helixi965 – 9673
    Helixi971 – 9755
    Helixi978 – 9803
    Helixi983 – 99816
    Turni1002 – 10054
    Helixi1007 – 10137
    Helixi1016 – 10194
    Helixi1025 – 10284
    Helixi1031 – 10355
    Beta strandi1038 – 10414
    Helixi1048 – 106013
    Helixi1062 – 10643
    Helixi1067 – 10726
    Helixi1078 – 108710
    Helixi1091 – 110212
    Turni1107 – 11093
    Helixi1110 – 11145

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2BE1X-ray2.98A/B111-449[»]
    2RIOX-ray2.40A/B658-1115[»]
    3FBVX-ray3.20A/B/C/D/E/F/G/H/I/J/K/L/M/N641-1115[»]
    3LJ0X-ray3.20A/B658-1115[»]
    3LJ1X-ray3.33A/B658-1115[»]
    3LJ2X-ray3.33A/B658-1115[»]
    3SDJX-ray3.65A/B/C/D/E/F/G/H/I/J/K/L/M/N641-1115[»]
    3SDMX-ray6.60A/B/C/D/E/F/G641-1115[»]
    ProteinModelPortaliP32361.
    SMRiP32361. Positions 111-449, 663-1115.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP32361.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini19 – 526508LumenalSequence AnalysisAdd
    BLAST
    Topological domaini556 – 1115560CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei527 – 55529HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini674 – 980307Protein kinasePROSITE-ProRule annotationAdd
    BLAST
    Domaini983 – 1115133KENPROSITE-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.
    HOGENOMiHOG000213215.
    KOiK08852.
    OMAiNILWFVE.
    OrthoDBiEOG7X3R27.

    Family and domain databases

    Gene3Di2.140.10.10. 1 hit.
    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. 3 hits.
    SM00580. PUG. 1 hit.
    [Graphical view]
    SUPFAMiSSF50998. SSF50998. 1 hit.
    SSF56112. SSF56112. 2 hits.
    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.

    P32361-1 [UniParc]FASTAAdd to Basket

    « Hide

    MRLLRRNMLV LTLLVCVFSS IISCSIPLSS RTSRRQIVED EVASTKKLNF     50
    NYGVDKNINS PIPAPRTTEG LPNMKLSSYP TPNLLNTADN RRANKKGRRA 100
    ANSISVPYLE NRSLNELSLS DILIAADVEG GLHAVDRRNG HIIWSIEPEN 150
    FQPLIEIQEP SRLETYETLI IEPFGDGNIY YFNAHQGLQK LPLSIRQLVS 200
    TSPLHLKTNI VVNDSGKIVE DEKVYTGSMR TIMYTINMLN GEIISAFGPG 250
    SKNGYFGSQS VDCSPEEKIK LQECENMIVI GKTIFELGIH SYDGASYNVT 300
    YSTWQQNVLD VPLALQNTFS KDGMCIAPFR DKSLLASDLD FRIARWVSPT 350
    FPGIIVGLFD VFNDLRTNEN ILVPHPFNPG DHESISSNKV YLDQTSNLSW 400
    FALSSQNFPS LVESAPISRY ASSDRWRVSS IFEDETLFKN AIMGVHQIYN 450
    NEYDHLYENY EKTNSLDTTH KYPPLMIDSS VDTTDLHQNN EMNSLKEYMS 500
    PEDLEAYRKK IHEQISRELD EKNQNSLLLK FGSLVYRIIE TGVFLLLFLI 550
    FCAILQRFKI LPPLYVLLSK IGFMPEKEIP IVESKSLNCP SSSENVTKPF 600
    DMKSGKQVVF EGAVNDGSLK SEKDNDDADE DDEKSLDLTT EKKKRKRGSR 650
    GGKKGRKSRI ANIPNFEQSL KNLVVSEKIL GYGSSGTVVF QGSFQGRPVA 700
    VKRMLIDFCD IALMEIKLLT ESDDHPNVIR YYCSETTDRF LYIALELCNL 750
    NLQDLVESKN VSDENLKLQK EYNPISLLRQ IASGVAHLHS LKIIHRDLKP 800
    QNILVSTSSR FTADQQTGAE NLRILISDFG LCKKLDSGQS SFRTNLNNPS 850
    GTSGWRAPEL LEESNNLQCQ VETEHSSSRH TVVSSDSFYD PFTKRRLTRS 900
    IDIFSMGCVF YYILSKGKHP FGDKYSRESN IIRGIFSLDE MKCLHDRSLI 950
    AEATDLISQM IDHDPLKRPT AMKVLRHPLF WPKSKKLEFL LKVSDRLEIE 1000
    NRDPPSALLM KFDAGSDFVI PSGDWTVKFD KTFMDNLERY RKYHSSKLMD 1050
    LLRALRNKYH HFMDLPEDIA ELMGPVPDGF YDYFTKRFPN LLIGVYMIVK 1100
    ENLSDDQILR EFLYS 1115
    Length:1,115
    Mass (Da):126,976
    Last modified:February 1, 1995 - v2
    Checksum:iBD65D74E74365945
    GO

    Sequence cautioni

    The sequence AAB68894.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti368 – 3681N → S in CAA77763. (PubMed:1625574)Curated
    Sequence conflicti625 – 6262ND → KH in CAA77763. (PubMed:1625574)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z11701 Genomic DNA. Translation: CAA77763.1.
    L19640 Genomic DNA. Translation: AAA34489.1.
    U10556 Genomic DNA. Translation: AAB68894.1. Different initiation.
    BK006934 Genomic DNA. Translation: DAA06773.1.
    PIRiA47541.
    RefSeqiNP_011946.1. NM_001179209.1.

    Genome annotation databases

    EnsemblFungiiYHR079C; YHR079C; YHR079C.
    GeneIDi856478.
    KEGGisce:YHR079C.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z11701 Genomic DNA. Translation: CAA77763.1 .
    L19640 Genomic DNA. Translation: AAA34489.1 .
    U10556 Genomic DNA. Translation: AAB68894.1 . Different initiation.
    BK006934 Genomic DNA. Translation: DAA06773.1 .
    PIRi A47541.
    RefSeqi NP_011946.1. NM_001179209.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2BE1 X-ray 2.98 A/B 111-449 [» ]
    2RIO X-ray 2.40 A/B 658-1115 [» ]
    3FBV X-ray 3.20 A/B/C/D/E/F/G/H/I/J/K/L/M/N 641-1115 [» ]
    3LJ0 X-ray 3.20 A/B 658-1115 [» ]
    3LJ1 X-ray 3.33 A/B 658-1115 [» ]
    3LJ2 X-ray 3.33 A/B 658-1115 [» ]
    3SDJ X-ray 3.65 A/B/C/D/E/F/G/H/I/J/K/L/M/N 641-1115 [» ]
    3SDM X-ray 6.60 A/B/C/D/E/F/G 641-1115 [» ]
    ProteinModelPortali P32361.
    SMRi P32361. Positions 111-449, 663-1115.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 36513. 334 interactions.
    DIPi DIP-233N.
    IntActi P32361. 4 interactions.
    MINTi MINT-408165.
    STRINGi 4932.YHR079C.

    Proteomic databases

    MaxQBi P32361.
    PRIDEi P32361.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YHR079C ; YHR079C ; YHR079C .
    GeneIDi 856478.
    KEGGi sce:YHR079C.

    Organism-specific databases

    CYGDi YHR079c.
    SGDi S000001121. IRE1.

    Phylogenomic databases

    eggNOGi COG0515.
    GeneTreei ENSGT00390000015684.
    HOGENOMi HOG000213215.
    KOi K08852.
    OMAi NILWFVE.
    OrthoDBi EOG7X3R27.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-31126-MONOMER.
    BRENDAi 2.7.11.1. 984.

    Miscellaneous databases

    EvolutionaryTracei P32361.
    NextBioi 982158.
    PROi P32361.

    Gene expression databases

    Genevestigatori P32361.

    Family and domain databases

    Gene3Di 2.140.10.10. 1 hit.
    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. 3 hits.
    SM00580. PUG. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50998. SSF50998. 1 hit.
    SSF56112. SSF56112. 2 hits.
    PROSITEi PS51392. KEN. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "IRE1 encodes a putative protein kinase containing a membrane-spanning domain and is required for inositol phototrophy in Saccharomyces cerevisiae."
      Nikawa J., Yamashita S.
      Mol. Microbiol. 6:1441-1446(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "A transmembrane protein with a cdc2+/CDC28-related kinase activity is required for signaling from the ER to the nucleus."
      Mori K., Ma W., Gething M.J., Sambrook J.
      Cell 74:743-756(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    4. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    5. "The unfolded protein response pathway in Saccharomyces cerevisiae. Oligomerization and trans-phosphorylation of Ire1p (Ern1p) are required for kinase activation."
      Welihinda A.A., Kaufman R.J.
      J. Biol. Chem. 271:18181-18187(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, ENZYME REGULATION, HOMODIMERIZATION, MUTAGENESIS OF LYS-702.
    6. "Oligomerization and phosphorylation of the Ire1p kinase during intracellular signaling from the endoplasmic reticulum to the nucleus."
      Shamu C.E., Walter P.
      EMBO J. 15:3028-3039(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, OLIGOMERIZATION, PHOSPHORYLATION.
    7. "The transmembrane kinase Ire1p is a site-specific endonuclease that initiates mRNA splicing in the unfolded protein response."
      Sidrauski C., Walter P.
      Cell 90:1031-1039(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    8. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    9. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
      Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
      Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiIRE1_YEAST
    AccessioniPrimary (citable) accession number: P32361
    Secondary accession number(s): D3DL29
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1993
    Last sequence update: February 1, 1995
    Last modified: October 1, 2014
    This is version 153 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Present with 259 molecules/cell in log phase SD medium.1 Publication

    Keywords - Technical termi

    3D-structure, Complete proteome, Multifunctional enzyme, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families
    3. Yeast
      Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
    4. Yeast chromosome VIII
      Yeast (Saccharomyces cerevisiae) chromosome VIII: entries and gene names

    External Data

    Dasty 3