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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-Experimental evidence at protein leveli

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

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)DescriptionActionsGraphical viewLength
Binding sitei702ATP1
Active sitei797Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi680 – 688ATPPROSITE-ProRule annotation9

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • endoribonuclease activity Source: SGD
  • metal ion binding Source: UniProtKB-KW
  • protein homodimerization activity Source: SGD
  • protein serine/threonine kinase activity Source: SGD
  • unfolded protein binding Source: SGD

GO - Biological processi

  • endoplasmic reticulum unfolded protein response Source: SGD
  • fungal-type cell wall organization Source: SGD
  • inositol metabolic process Source: SGD
  • IRE1-mediated unfolded protein response Source: Reactome
  • mRNA processing Source: InterPro
  • protein homooligomerization Source: SGD
  • protein phosphorylation Source: SGD
  • protein targeting to Golgi Source: SGD
  • protein trans-autophosphorylation Source: SGD
  • regulation of transcription, DNA-templated Source: UniProtKB-KW
  • response to endoplasmic reticulum stress Source: SGD
  • transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

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.
ReactomeiR-SCE-381070. IRE1alpha activates chaperones.

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
Proteomesi
  • UP000002311 Componenti: Chromosome VIII

Organism-specific databases

EuPathDBiFungiDB:YHR079C.
SGDiS000001121. IRE1.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini19 – 526LumenalSequence analysisAdd BLAST508
Transmembranei527 – 555HelicalSequence analysisAdd BLAST29
Topological domaini556 – 1115CytoplasmicSequence analysisAdd BLAST560

GO - Cellular componenti

  • endoplasmic reticulum membrane Source: Reactome
  • integral component of endoplasmic reticulum membrane Source: SGD
  • nucleus Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi702K → A: Loss of autophosphorylation. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 18Sequence analysisAdd BLAST18
ChainiPRO_000002433819 – 1115Serine/threonine-protein kinase/endoribonuclease IRE1Add BLAST1097

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi111N-linked (GlcNAc...)Sequence analysis1
Glycosylationi213N-linked (GlcNAc...)Sequence analysis1
Glycosylationi298N-linked (GlcNAc...)Sequence analysis1
Glycosylationi397N-linked (GlcNAc...)Sequence analysis1
Modified residuei840Phosphoserine; by autocatalysis1 Publication1
Modified residuei841Phosphoserine; by autocatalysis1 Publication1

Post-translational modificationi

Autophosphorylated mainly on serine residues.1 Publication

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiP32361.
PRIDEiP32361.

PTM databases

iPTMnetiP32361.

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

GO - Molecular functioni

  • protein homodimerization activity Source: SGD
  • unfolded protein binding Source: SGD

Protein-protein interaction databases

BioGridi36513. 338 interactors.
DIPiDIP-233N.
IntActiP32361. 4 interactors.
MINTiMINT-408165.

Structurei

Secondary structure

11115
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi116 – 127Combined sources12
Beta strandi132 – 136Combined sources5
Turni137 – 139Combined sources3
Beta strandi142 – 146Combined sources5
Helixi148 – 150Combined sources3
Beta strandi154 – 156Combined sources3
Turni162 – 164Combined sources3
Beta strandi165 – 171Combined sources7
Turni175 – 177Combined sources3
Beta strandi178 – 183Combined sources6
Turni184 – 186Combined sources3
Beta strandi187 – 194Combined sources8
Helixi195 – 199Combined sources5
Beta strandi203 – 207Combined sources5
Beta strandi222 – 226Combined sources5
Beta strandi228 – 237Combined sources10
Turni238 – 240Combined sources3
Beta strandi243 – 248Combined sources6
Beta strandi277 – 286Combined sources10
Beta strandi300 – 305Combined sources6
Turni308 – 310Combined sources3
Helixi311 – 314Combined sources4
Beta strandi321 – 323Combined sources3
Beta strandi326 – 329Combined sources4
Turni330 – 332Combined sources3
Beta strandi333 – 337Combined sources5
Beta strandi344 – 347Combined sources4
Beta strandi355 – 364Combined sources10
Turni365 – 368Combined sources4
Beta strandi369 – 374Combined sources6
Beta strandi390 – 394Combined sources5
Beta strandi400 – 404Combined sources5
Turni405 – 407Combined sources3
Helixi409 – 413Combined sources5
Helixi419 – 422Combined sources4
Helixi424 – 426Combined sources3
Helixi429 – 433Combined sources5
Helixi435 – 442Combined sources8
Beta strandi444 – 446Combined sources3
Turni666 – 669Combined sources4
Beta strandi674 – 682Combined sources9
Turni684 – 686Combined sources3
Beta strandi688 – 705Combined sources18
Helixi706 – 708Combined sources3
Helixi709 – 722Combined sources14
Beta strandi731 – 736Combined sources6
Beta strandi738 – 745Combined sources8
Beta strandi749 – 751Combined sources3
Helixi752 – 757Combined sources6
Helixi765 – 769Combined sources5
Helixi774 – 790Combined sources17
Helixi800 – 802Combined sources3
Beta strandi803 – 806Combined sources4
Helixi809 – 812Combined sources4
Beta strandi823 – 826Combined sources4
Turni836 – 838Combined sources3
Helixi851 – 855Combined sources5
Helixi858 – 861Combined sources4
Helixi900 – 914Combined sources15
Turni924 – 926Combined sources3
Helixi927 – 933Combined sources7
Helixi947 – 960Combined sources14
Helixi965 – 967Combined sources3
Helixi971 – 975Combined sources5
Helixi978 – 980Combined sources3
Helixi983 – 998Combined sources16
Turni1002 – 1005Combined sources4
Helixi1007 – 1013Combined sources7
Helixi1016 – 1019Combined sources4
Helixi1025 – 1028Combined sources4
Helixi1031 – 1035Combined sources5
Beta strandi1038 – 1041Combined sources4
Helixi1048 – 1060Combined sources13
Helixi1062 – 1064Combined sources3
Helixi1067 – 1072Combined sources6
Helixi1078 – 1087Combined sources10
Helixi1091 – 1102Combined sources12
Turni1107 – 1109Combined sources3
Helixi1110 – 1114Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
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[»]
ProteinModelPortaliP32361.
SMRiP32361.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP32361.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini674 – 980Protein kinasePROSITE-ProRule annotationAdd BLAST307
Domaini983 – 1115KENPROSITE-ProRule annotationAdd BLAST133

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

GeneTreeiENSGT00390000015684.
HOGENOMiHOG000213215.
InParanoidiP32361.
KOiK08852.
OMAiNILWFVE.
OrthoDBiEOG092C0PG1.

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.
IPR018997. PUB_domain.
IPR027295. Quinoprotein_ADH-like_fam.
IPR011047. Quinoprotein_ADH-like_supfam.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00069. Pkinase. 2 hits.
PF06479. Ribonuc_2-5A. 1 hit.
[Graphical view]
SMARTiSM00564. PQQ. 3 hits.
SM00580. PUG. 1 hit.
SM00220. S_TKc. 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

        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
Checksum:iBD65D74E74365945
GO

Sequence cautioni

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

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti368N → S in CAA77763 (PubMed:1625574).Curated1
Sequence conflicti625 – 626ND → KH in CAA77763 (PubMed:1625574).Curated2

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.

Genome annotation databases

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

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:
PDBei
RCSB PDBi
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[»]
ProteinModelPortaliP32361.
SMRiP32361.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi36513. 338 interactors.
DIPiDIP-233N.
IntActiP32361. 4 interactors.
MINTiMINT-408165.

PTM databases

iPTMnetiP32361.

Proteomic databases

MaxQBiP32361.
PRIDEiP32361.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

EuPathDBiFungiDB:YHR079C.
SGDiS000001121. IRE1.

Phylogenomic databases

GeneTreeiENSGT00390000015684.
HOGENOMiHOG000213215.
InParanoidiP32361.
KOiK08852.
OMAiNILWFVE.
OrthoDBiEOG092C0PG1.

Enzyme and pathway databases

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

Miscellaneous databases

EvolutionaryTraceiP32361.
PROiP32361.

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.
IPR018997. PUB_domain.
IPR027295. Quinoprotein_ADH-like_fam.
IPR011047. Quinoprotein_ADH-like_supfam.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00069. Pkinase. 2 hits.
PF06479. Ribonuc_2-5A. 1 hit.
[Graphical view]
SMARTiSM00564. PQQ. 3 hits.
SM00580. PUG. 1 hit.
SM00220. S_TKc. 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]
ProtoNetiSearch...

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: November 2, 2016
This is version 172 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.