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Entry version 195 (08 May 2019)
Sequence version 2 (01 Feb 1995)
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Protein

Serine/threonine-protein kinase/endoribonuclease IRE1

Gene

IRE1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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

Miscellaneous

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

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Mg2+

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity 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)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei702ATP1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei797Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi680 – 688ATPPROSITE-ProRule annotation9

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionHydrolase, Kinase, Multifunctional enzyme, Serine/threonine-protein kinase, Transferase
Biological processTranscription, Transcription regulation, Unfolded protein response
LigandATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
YEAST:G3O-31126-MONOMER

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
2.7.11.1 984

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-SCE-381070 IRE1alpha activates chaperones

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Serine/threonine-protein kinase/endoribonuclease IRE1
Alternative name(s):
Endoplasmic reticulum-to-nucleus signaling 1
Including the following 2 domains:
Serine/threonine-protein kinase (EC:2.7.11.1)
Endoribonuclease (EC:3.1.26.-)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:IRE1
Synonyms:ERN1
Ordered Locus Names:YHR079C
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri559292 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000002311 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome VIII

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...
EuPathDBi
FungiDB:YHR079C

Saccharomyces Genome Database

More...
SGDi
S000001121 IRE1

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini19 – 526LumenalSequence analysisAdd BLAST508
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei527 – 555HelicalSequence analysisAdd BLAST29
Topological domaini556 – 1115CytoplasmicSequence analysisAdd BLAST560

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi702K → A: Loss of autophosphorylation. 1 Publication1

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 18Sequence analysisAdd BLAST18
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000002433819 – 1115Serine/threonine-protein kinase/endoribonuclease IRE1Add BLAST1097

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi111N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi213N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi298N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi397N-linked (GlcNAc...) asparagineSequence analysis1
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei840Phosphoserine; by autocatalysis1 Publication1
Modified residuei841Phosphoserine; by autocatalysis1 Publication1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Autophosphorylated mainly on serine residues.1 Publication

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

MaxQB - The MaxQuant DataBase

More...
MaxQBi
P32361

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
P32361

PRoteomics IDEntifications database

More...
PRIDEi
P32361

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P32361

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homodimer; in response to the accumulation of unfolded proteins.

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
36513, 485 interactors

ComplexPortal: manually curated resource of macromolecular complexes

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ComplexPortali
CPX-2147 Ire1 complex

Database of interacting proteins

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DIPi
DIP-233N

Protein interaction database and analysis system

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IntActi
P32361, 5 interactors

Molecular INTeraction database

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MINTi
P32361

STRING: functional protein association networks

More...
STRINGi
4932.YHR079C

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

11115
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
P32361

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P32361

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini674 – 980Protein kinasePROSITE-ProRule annotationAdd BLAST307
Domaini983 – 1115KENPROSITE-ProRule annotationAdd BLAST133

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the protein kinase superfamily. Ser/Thr protein kinase family.PROSITE-ProRule annotation

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000167966

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000213215

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P32361

KEGG Orthology (KO)

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KOi
K08852

Identification of Orthologs from Complete Genome Data

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OMAi
GPGTENK

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
1.20.1440.180, 1 hit
2.130.10.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR010513 KEN_dom
IPR038357 KEN_sf
IPR011009 Kinase-like_dom_sf
IPR018391 PQQ_beta_propeller_repeat
IPR000719 Prot_kinase_dom
IPR018997 PUB_domain
IPR011047 Quinoprotein_ADH-like_supfam
IPR008271 Ser/Thr_kinase_AS
IPR015943 WD40/YVTN_repeat-like_dom_sf

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00069 Pkinase, 2 hits
PF06479 Ribonuc_2-5A, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00564 PQQ, 3 hits
SM00580 PUG, 1 hit
SM00220 S_TKc, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF50998 SSF50998, 1 hit
SSF56112 SSF56112, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS51392 KEN, 1 hit
PS50011 PROTEIN_KINASE_DOM, 1 hit
PS00108 PROTEIN_KINASE_ST, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

P32361-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MRLLRRNMLV LTLLVCVFSS IISCSIPLSS RTSRRQIVED EVASTKKLNF
60 70 80 90 100
NYGVDKNINS PIPAPRTTEG LPNMKLSSYP TPNLLNTADN RRANKKGRRA
110 120 130 140 150
ANSISVPYLE NRSLNELSLS DILIAADVEG GLHAVDRRNG HIIWSIEPEN
160 170 180 190 200
FQPLIEIQEP SRLETYETLI IEPFGDGNIY YFNAHQGLQK LPLSIRQLVS
210 220 230 240 250
TSPLHLKTNI VVNDSGKIVE DEKVYTGSMR TIMYTINMLN GEIISAFGPG
260 270 280 290 300
SKNGYFGSQS VDCSPEEKIK LQECENMIVI GKTIFELGIH SYDGASYNVT
310 320 330 340 350
YSTWQQNVLD VPLALQNTFS KDGMCIAPFR DKSLLASDLD FRIARWVSPT
360 370 380 390 400
FPGIIVGLFD VFNDLRTNEN ILVPHPFNPG DHESISSNKV YLDQTSNLSW
410 420 430 440 450
FALSSQNFPS LVESAPISRY ASSDRWRVSS IFEDETLFKN AIMGVHQIYN
460 470 480 490 500
NEYDHLYENY EKTNSLDTTH KYPPLMIDSS VDTTDLHQNN EMNSLKEYMS
510 520 530 540 550
PEDLEAYRKK IHEQISRELD EKNQNSLLLK FGSLVYRIIE TGVFLLLFLI
560 570 580 590 600
FCAILQRFKI LPPLYVLLSK IGFMPEKEIP IVESKSLNCP SSSENVTKPF
610 620 630 640 650
DMKSGKQVVF EGAVNDGSLK SEKDNDDADE DDEKSLDLTT EKKKRKRGSR
660 670 680 690 700
GGKKGRKSRI ANIPNFEQSL KNLVVSEKIL GYGSSGTVVF QGSFQGRPVA
710 720 730 740 750
VKRMLIDFCD IALMEIKLLT ESDDHPNVIR YYCSETTDRF LYIALELCNL
760 770 780 790 800
NLQDLVESKN VSDENLKLQK EYNPISLLRQ IASGVAHLHS LKIIHRDLKP
810 820 830 840 850
QNILVSTSSR FTADQQTGAE NLRILISDFG LCKKLDSGQS SFRTNLNNPS
860 870 880 890 900
GTSGWRAPEL LEESNNLQCQ VETEHSSSRH TVVSSDSFYD PFTKRRLTRS
910 920 930 940 950
IDIFSMGCVF YYILSKGKHP FGDKYSRESN IIRGIFSLDE MKCLHDRSLI
960 970 980 990 1000
AEATDLISQM IDHDPLKRPT AMKVLRHPLF WPKSKKLEFL LKVSDRLEIE
1010 1020 1030 1040 1050
NRDPPSALLM KFDAGSDFVI PSGDWTVKFD KTFMDNLERY RKYHSSKLMD
1060 1070 1080 1090 1100
LLRALRNKYH HFMDLPEDIA ELMGPVPDGF YDYFTKRFPN LLIGVYMIVK
1110
ENLSDDQILR EFLYS
Length:1,115
Mass (Da):126,976
Last modified:February 1, 1995 - v2
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iBD65D74E74365945
GO

<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

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

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti368N → S in CAA77763 (PubMed:1625574).Curated1
Sequence conflicti625 – 626ND → KH in CAA77763 (PubMed:1625574).Curated2

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
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

Protein sequence database of the Protein Information Resource

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PIRi
A47541

NCBI Reference Sequences

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RefSeqi
NP_011946.1, NM_001179209.1

Genome annotation databases

Ensembl fungal genome annotation project

More...
EnsemblFungii
YHR079C_mRNA; YHR079C_mRNA; YHR079C

Database of genes from NCBI RefSeq genomes

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GeneIDi
856478

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
sce:YHR079C

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB 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[»]
SMRiP32361
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi36513, 485 interactors
ComplexPortaliCPX-2147 Ire1 complex
DIPiDIP-233N
IntActiP32361, 5 interactors
MINTiP32361
STRINGi4932.YHR079C

PTM databases

iPTMnetiP32361

Proteomic databases

MaxQBiP32361
PaxDbiP32361
PRIDEiP32361

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYHR079C_mRNA; YHR079C_mRNA; YHR079C
GeneIDi856478
KEGGisce:YHR079C

Organism-specific databases

EuPathDBiFungiDB:YHR079C
SGDiS000001121 IRE1

Phylogenomic databases

GeneTreeiENSGT00940000167966
HOGENOMiHOG000213215
InParanoidiP32361
KOiK08852
OMAiGPGTENK

Enzyme and pathway databases

BioCyciYEAST:G3O-31126-MONOMER
BRENDAi2.7.11.1 984
ReactomeiR-SCE-381070 IRE1alpha activates chaperones

Miscellaneous databases

EvolutionaryTraceiP32361

Protein Ontology

More...
PROi
PR:P32361

Family and domain databases

Gene3Di1.20.1440.180, 1 hit
2.130.10.10, 1 hit
InterProiView protein in InterPro
IPR010513 KEN_dom
IPR038357 KEN_sf
IPR011009 Kinase-like_dom_sf
IPR018391 PQQ_beta_propeller_repeat
IPR000719 Prot_kinase_dom
IPR018997 PUB_domain
IPR011047 Quinoprotein_ADH-like_supfam
IPR008271 Ser/Thr_kinase_AS
IPR015943 WD40/YVTN_repeat-like_dom_sf
PfamiView protein in Pfam
PF00069 Pkinase, 2 hits
PF06479 Ribonuc_2-5A, 1 hit
SMARTiView protein in SMART
SM00564 PQQ, 3 hits
SM00580 PUG, 1 hit
SM00220 S_TKc, 1 hit
SUPFAMiSSF50998 SSF50998, 1 hit
SSF56112 SSF56112, 1 hit
PROSITEiView protein in PROSITE
PS51392 KEN, 1 hit
PS50011 PROTEIN_KINASE_DOM, 1 hit
PS00108 PROTEIN_KINASE_ST, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiIRE1_YEAST
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P32361
Secondary accession number(s): D3DL29
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: February 1, 1995
Last modified: May 8, 2019
This is version 195 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

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