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O75460

- ERN1_HUMAN

UniProt

O75460 - ERN1_HUMAN

Protein

Serine/threonine-protein kinase/endoribonuclease IRE1

Gene

ERN1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 141 (01 Oct 2014)
      Sequence version 2 (01 Jul 2008)
      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.By similarity3 Publications

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.1 Publication

    Cofactori

    Magnesium.

    Enzyme regulationi

    The kinase domain is activated by trans-autophosphorylation. Kinase activity is required for activation of the endoribonuclease domain.2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei599 – 5991ATP1 PublicationPROSITE-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. endoribonuclease activity Source: UniProtKB
    3. enzyme binding Source: UniProt
    4. identical protein binding Source: IntAct
    5. magnesium ion binding Source: UniProtKB
    6. protein binding Source: IntAct
    7. 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. cellular protein metabolic process Source: Reactome
    4. endoplasmic reticulum unfolded protein response Source: Reactome
    5. HAC1-type intron splice site recognition and cleavage Source: WormBase
    6. intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress Source: Ensembl
    7. positive regulation of endoplasmic reticulum unfolded protein response Source: UniProtKB
    8. protein autophosphorylation Source: Ensembl
    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

    Enzyme and pathway databases

    ReactomeiREACT_18368. IRE1alpha activates chaperones.
    SignaLinkiO75460.

    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
    Short name:
    hIRE1p
    Ire1-alpha
    Short name:
    IRE1a
    Including the following 2 domains:
    Gene namesi
    Name:ERN1Imported
    Synonyms:IRE1Imported
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 17

    Organism-specific databases

    HGNCiHGNC:3449. ERN1.

    Subcellular locationi

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

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Endoplasmic reticulum, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi109 – 1091C → S: No effect on dimerization. 1 Publication
    Mutagenesisi148 – 1481C → S: No effect on dimerization. Weakens dimer; when associated with S-148. 1 Publication
    Mutagenesisi332 – 3321C → S: No effect on dimerization. Weakens dimer; when associated with S-332. 1 Publication
    Mutagenesisi599 – 5991K → A: Loss of autophosphorylation and of endoribonuclease activity. Inhibition of growth arrest. 2 Publications

    Organism-specific databases

    PharmGKBiPA27861.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1818Sequence AnalysisAdd
    BLAST
    Chaini19 – 977959Serine/threonine-protein kinase/endoribonuclease IRE1PRO_0000024327Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi176 – 1761N-linked (GlcNAc...)Sequence Analysis
    Modified residuei973 – 9731Phosphothreonine1 Publication

    Post-translational modificationi

    Autophosphorylated.2 Publications
    ADP-ribosylated by PARP16 upon ER stress, which increases both kinase and endonuclease activities.

    Keywords - PTMi

    ADP-ribosylation, Disulfide bond, Glycoprotein, Phosphoprotein

    Proteomic databases

    MaxQBiO75460.
    PaxDbiO75460.
    PRIDEiO75460.

    PTM databases

    PhosphoSiteiO75460.

    Expressioni

    Tissue specificityi

    Ubiquitously expressed. High levels observed in pancreatic tissue.1 Publication

    Gene expression databases

    BgeeiO75460.
    CleanExiHS_ERN1.
    GenevestigatoriO75460.

    Organism-specific databases

    HPAiCAB009495.
    HPA027730.

    Interactioni

    Subunit structurei

    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 By similarity. 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. Interacts with TAOK3 and TRAF2.By similarity2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself2EBI-371750,EBI-371750
    Bak1O087342EBI-371750,EBI-822441From a different organism.
    BAXQ078122EBI-371750,EBI-516580
    BaxQ078132EBI-371750,EBI-700711From a different organism.
    Hspa5P200292EBI-371750,EBI-772325From a different organism.
    SYVN1Q86TM62EBI-371750,EBI-947849
    TAOK3Q9H2K83EBI-371750,EBI-1384100
    TRAF2Q129333EBI-371750,EBI-355744

    Protein-protein interaction databases

    BioGridi108391. 16 interactions.
    DIPiDIP-31711N.
    IntActiO75460. 11 interactions.
    MINTiMINT-3001268.
    STRINGi9606.ENSP00000401445.

    Structurei

    Secondary structure

    1
    977
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi32 – 376
    Beta strandi40 – 467
    Turni47 – 493
    Beta strandi52 – 576
    Beta strandi73 – 753
    Turni77 – 793
    Beta strandi82 – 843
    Beta strandi93 – 953
    Helixi100 – 1045
    Beta strandi120 – 1289
    Beta strandi154 – 16411
    Beta strandi168 – 1725
    Beta strandi176 – 1827
    Beta strandi197 – 2015
    Beta strandi205 – 2095
    Turni211 – 2133
    Beta strandi216 – 2216
    Beta strandi226 – 2316
    Beta strandi238 – 2403
    Beta strandi243 – 2464
    Helixi247 – 26418
    Helixi273 – 2797
    Beta strandi280 – 2845
    Beta strandi286 – 2883
    Beta strandi297 – 3004
    Turni359 – 3613
    Beta strandi564 – 5663
    Beta strandi569 – 57911
    Helixi581 – 5833
    Beta strandi585 – 60117
    Turni603 – 6053
    Beta strandi606 – 6083
    Helixi610 – 6189
    Beta strandi628 – 6347
    Beta strandi637 – 6437
    Beta strandi646 – 6483
    Helixi649 – 6546
    Beta strandi655 – 6573
    Helixi665 – 68117
    Beta strandi693 – 6964
    Beta strandi707 – 7093
    Beta strandi714 – 7163
    Helixi740 – 7423
    Helixi754 – 76815
    Turni778 – 7803
    Helixi781 – 7866
    Helixi800 – 81213
    Helixi817 – 8193
    Helixi823 – 8275
    Turni830 – 8323
    Helixi835 – 84814
    Helixi857 – 8648
    Turni868 – 8714
    Helixi874 – 8763
    Helixi880 – 8856
    Helixi897 – 90913
    Turni910 – 9134
    Helixi916 – 9227
    Helixi927 – 9348
    Helixi940 – 9478
    Helixi948 – 9514
    Beta strandi952 – 9543
    Helixi955 – 9573
    Turni958 – 9603

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2HZ6X-ray3.10A24-390[»]
    3P23X-ray2.70A/B/C/D547-977[»]
    ProteinModelPortaliO75460.
    SMRiO75460. Positions 29-368, 561-964.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO75460.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini19 – 443425LumenalSequence AnalysisAdd
    BLAST
    Topological domaini465 – 977513CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei444 – 46421HelicalSequence 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.
    HOGENOMiHOG000012929.
    HOVERGENiHBG051506.
    InParanoidiO75460.
    KOiK08852.
    OMAiGLRKVMH.
    OrthoDBiEOG7C2R0H.
    PhylomeDBiO75460.
    TreeFamiTF313986.

    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. 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 1 (identifier: O75460-1) [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

    MPARRLLLLL TLLLPGLGIF GSTSTVTLPE TLLFVSTLDG SLHAVSKRTG    50
    SIKWTLKEDP VLQVPTHVEE PAFLPDPNDG SLYTLGSKNN EGLTKLPFTI 100
    PELVQASPCR SSDGILYMGK KQDIWYVIDL LTGEKQQTLS SAFADSLCPS 150
    TSLLYLGRTE YTITMYDTKT RELRWNATYF DYAASLPEDD VDYKMSHFVS 200
    NGDGLVVTVD SESGDVLWIQ NYASPVVAFY VWQREGLRKV MHINVAVETL 250
    RYLTFMSGEV GRITKWKYPF PKETEAKSKL TPTLYVGKYS TSLYASPSMV 300
    HEGVAVVPRG STLPLLEGPQ TDGVTIGDKG ECVITPSTDV KFDPGLKSKN 350
    KLNYLRNYWL LIGHHETPLS ASTKMLERFP NNLPKHRENV IPADSEKKSF 400
    EEVINLVDQT SENAPTTVSR DVEEKPAHAP ARPEAPVDSM LKDMATIILS 450
    TFLLIGWVAF IITYPLSMHQ QQQLQHQQFQ KELEKIQLLQ QQQQQLPFHP 500
    PGDTAQDGEL LDTSGPYSES SGTSSPSTSP RASNHSLCSG SSASKAGSSP 550
    SLEQDDGDEE TSVVIVGKIS FCPKDVLGHG AEGTIVYRGM FDNRDVAVKR 600
    ILPECFSFAD REVQLLRESD EHPNVIRYFC TEKDRQFQYI AIELCAATLQ 650
    EYVEQKDFAH LGLEPITLLQ QTTSGLAHLH SLNIVHRDLK PHNILISMPN 700
    AHGKIKAMIS DFGLCKKLAV GRHSFSRRSG VPGTEGWIAP EMLSEDCKEN 750
    PTYTVDIFSA GCVFYYVISE GSHPFGKSLQ RQANILLGAC SLDCLHPEKH 800
    EDVIARELIE KMIAMDPQKR PSAKHVLKHP FFWSLEKQLQ FFQDVSDRIE 850
    KESLDGPIVK QLERGGRAVV KMDWRENITV PLQTDLRKFR TYKGGSVRDL 900
    LRAMRNKKHH YRELPAEVRE TLGSLPDDFV CYFTSRFPHL LAHTYRAMEL 950
    CSHERLFQPY YFHEPPEPQP PVTPDAL 977
    Length:977
    Mass (Da):109,735
    Last modified:July 1, 2008 - v2
    Checksum:iA2DF808CCE015536
    GO
    Isoform 2 (identifier: O75460-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         19-70: IFGSTSTVTL...VLQVPTHVEE → VSDRGAWGGG...SPAVGGSGRA
         71-977: Missing.

    Show »
    Length:70
    Mass (Da):6,649
    Checksum:iC93BA0CB092E6204
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti190 – 1912DV → EG in AAC25991. (PubMed:9637683)Curated
    Sequence conflicti768 – 7681I → V in AAC25991. (PubMed:9637683)Curated
    Sequence conflicti816 – 8161D → G in BAF85092. (PubMed:14702039)Curated
    Sequence conflicti824 – 8252KH → ND in AAC25991. (PubMed:9637683)Curated
    Sequence conflicti880 – 8801V → D in AAC25991. (PubMed:9637683)Curated
    Sequence conflicti904 – 9041M → T in BAF85092. (PubMed:14702039)Curated
    Sequence conflicti924 – 9241S → T in AAC25991. (PubMed:9637683)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti244 – 2441N → S in a renal clear cell carcinoma sample; somatic mutation. 1 Publication
    VAR_040488
    Natural varianti418 – 4181V → M.1 Publication
    Corresponds to variant rs55869215 [ dbSNP | Ensembl ].
    VAR_040489
    Natural varianti474 – 4741L → R in a lung adenocarcinoma sample; somatic mutation. 1 Publication
    Corresponds to variant rs186305118 [ dbSNP | Ensembl ].
    VAR_040490
    Natural varianti635 – 6351R → W in a gastric adenocarcinoma sample; somatic mutation. 1 Publication
    VAR_040491
    Natural varianti700 – 7001N → S.1 Publication
    VAR_040492
    Natural varianti769 – 7691S → F in a glioblastoma multiforme sample; somatic mutation. 1 Publication
    VAR_040493
    Natural varianti830 – 8301P → L in an ovarian serous carcinoma sample; somatic mutation. 1 Publication
    VAR_040494

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei19 – 7052IFGST…THVEE → VSDRGAWGGGQLATAGSGPG QRRGAGAGVRAGSATAAARC PVSPAVGGSGRA in isoform 2. 2 PublicationsVSP_034582Add
    BLAST
    Alternative sequencei71 – 977907Missing in isoform 2. 2 PublicationsVSP_034583Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF059198 mRNA. Translation: AAC25991.1.
    AK292403 mRNA. Translation: BAF85092.1.
    DA254477 mRNA. No translation available.
    AB209869 mRNA. Translation: BAD93106.1.
    AC005803 Genomic DNA. No translation available.
    AC025362 Genomic DNA. No translation available.
    CH471109 Genomic DNA. Translation: EAW94214.1.
    BC130405 mRNA. Translation: AAI30406.1.
    BC130407 mRNA. Translation: AAI30408.1.
    BI912495 mRNA. No translation available.
    CCDSiCCDS45762.1. [O75460-1]
    RefSeqiNP_001424.3. NM_001433.3. [O75460-1]
    UniGeneiHs.133982.
    Hs.700027.
    Hs.744953.

    Genome annotation databases

    EnsembliENST00000433197; ENSP00000401445; ENSG00000178607. [O75460-1]
    ENST00000606895; ENSP00000475519; ENSG00000178607. [O75460-2]
    GeneIDi2081.
    KEGGihsa:2081.
    UCSCiuc002jdz.2. human. [O75460-1]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF059198 mRNA. Translation: AAC25991.1 .
    AK292403 mRNA. Translation: BAF85092.1 .
    DA254477 mRNA. No translation available.
    AB209869 mRNA. Translation: BAD93106.1 .
    AC005803 Genomic DNA. No translation available.
    AC025362 Genomic DNA. No translation available.
    CH471109 Genomic DNA. Translation: EAW94214.1 .
    BC130405 mRNA. Translation: AAI30406.1 .
    BC130407 mRNA. Translation: AAI30408.1 .
    BI912495 mRNA. No translation available.
    CCDSi CCDS45762.1. [O75460-1 ]
    RefSeqi NP_001424.3. NM_001433.3. [O75460-1 ]
    UniGenei Hs.133982.
    Hs.700027.
    Hs.744953.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2HZ6 X-ray 3.10 A 24-390 [» ]
    3P23 X-ray 2.70 A/B/C/D 547-977 [» ]
    ProteinModelPortali O75460.
    SMRi O75460. Positions 29-368, 561-964.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108391. 16 interactions.
    DIPi DIP-31711N.
    IntActi O75460. 11 interactions.
    MINTi MINT-3001268.
    STRINGi 9606.ENSP00000401445.

    Chemistry

    BindingDBi O75460.
    ChEMBLi CHEMBL1163101.
    GuidetoPHARMACOLOGYi 2020.

    PTM databases

    PhosphoSitei O75460.

    Proteomic databases

    MaxQBi O75460.
    PaxDbi O75460.
    PRIDEi O75460.

    Protocols and materials databases

    DNASUi 2081.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000433197 ; ENSP00000401445 ; ENSG00000178607 . [O75460-1 ]
    ENST00000606895 ; ENSP00000475519 ; ENSG00000178607 . [O75460-2 ]
    GeneIDi 2081.
    KEGGi hsa:2081.
    UCSCi uc002jdz.2. human. [O75460-1 ]

    Organism-specific databases

    CTDi 2081.
    GeneCardsi GC17M062120.
    H-InvDB HIX0014084.
    HGNCi HGNC:3449. ERN1.
    HPAi CAB009495.
    HPA027730.
    MIMi 604033. gene.
    neXtProti NX_O75460.
    PharmGKBi PA27861.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0515.
    HOGENOMi HOG000012929.
    HOVERGENi HBG051506.
    InParanoidi O75460.
    KOi K08852.
    OMAi GLRKVMH.
    OrthoDBi EOG7C2R0H.
    PhylomeDBi O75460.
    TreeFami TF313986.

    Enzyme and pathway databases

    Reactomei REACT_18368. IRE1alpha activates chaperones.
    SignaLinki O75460.

    Miscellaneous databases

    ChiTaRSi ERN1. human.
    EvolutionaryTracei O75460.
    GeneWikii ERN1.
    GenomeRNAii 2081.
    NextBioi 8459.
    PROi O75460.
    SOURCEi Search...

    Gene expression databases

    Bgeei O75460.
    CleanExi HS_ERN1.
    Genevestigatori O75460.

    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. 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. "A stress response pathway from the endoplasmic reticulum to the nucleus requires a novel bifunctional protein kinase/endoribonuclease (Ire1p) in mammalian cells."
      Tirasophon W., Welihinda A.A., Kaufman R.J.
      Genes Dev. 12:1812-1824(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, ENZYME REGULATION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AUTOPHOSPHORYLATION, GLYCOSYLATION, MUTAGENESIS OF LYS-599.
      Tissue: LiverImported.
    2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
      Tissue: Testis.
    3. Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
      Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Endothelial cell.
    4. "DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
      Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L.
      , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
      Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2-977 (ISOFORM 2).
      Tissue: Brain and Leukocyte.
    7. "Activation of caspase-12, an endoplastic reticulum (ER) resident caspase, through tumor necrosis factor receptor-associated factor 2-dependent mechanism in response to the ER stress."
      Yoneda T., Imaizumi K., Oono K., Yui D., Gomi F., Katayama T., Tohyama M.
      J. Biol. Chem. 276:13935-13940(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TAOK3 AND TRAF2.
    8. "Translational control by the ER transmembrane kinase/ribonuclease IRE1 under ER stress."
      Iwawaki T., Hosoda A., Okuda T., Kamigori Y., Nomura-Furuwatari C., Kimata Y., Tsuru A., Kohno K.
      Nat. Cell Biol. 3:158-164(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF LYS-599.
    9. "Structure and intermolecular interactions of the luminal dimerization domain of human IRE1alpha."
      Liu C.Y., Xu Z., Kaufman R.J.
      J. Biol. Chem. 278:17680-17687(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, HOMODIMERIZATION, ENZYME REGULATION, INTERACTION WITH HSPA5, MUTAGENESIS OF CYS-109; CYS-148 AND CYS-332.
    10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-973, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. "PARP16 is a tail-anchored endoplasmic reticulum protein required for the PERK-and IRE1alpha-mediated unfolded protein response."
      Jwa M., Chang P.
      Nat. Cell Biol. 14:1223-1230(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: ADP-RIBOSYLATION BY PARP16.
    13. "The crystal structure of human IRE1 luminal domain reveals a conserved dimerization interface required for activation of the unfolded protein response."
      Zhou J., Liu C.Y., Back S.H., Clark R.L., Peisach D., Xu Z., Kaufman R.J.
      Proc. Natl. Acad. Sci. U.S.A. 103:14343-14348(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF 24-390.
    14. "Patterns of somatic mutation in human cancer genomes."
      Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.
      , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
      Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS [LARGE SCALE ANALYSIS] SER-244; MET-418; ARG-474; TRP-635; SER-700; PHE-769 AND LEU-830.

    Entry informationi

    Entry nameiERN1_HUMAN
    AccessioniPrimary (citable) accession number: O75460
    Secondary accession number(s): A1L457
    , A8K8N8, A8MXS7, Q59EE2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 16, 2004
    Last sequence update: July 1, 2008
    Last modified: October 1, 2014
    This is version 141 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

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

    Documents

    1. Human chromosome 17
      Human chromosome 17: 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3