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P32361

- IRE1_YEAST

UniProt

P32361 - IRE1_YEAST

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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: 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)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 homodimerization activity Source: SGD
  6. protein serine/threonine kinase activity Source: SGD
  7. 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
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.
ReactomeiREACT_251918. 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
ProteomesiUP000002311: Chromosome VIII

Organism-specific databases

CYGDiYHR079c.
SGDiS000001121. IRE1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini19 – 526508LumenalSequence AnalysisAdd
BLAST
Transmembranei527 – 55529HelicalSequence AnalysisAdd
BLAST
Topological domaini556 – 1115560CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

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

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. 335 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 – 12712Combined sources
Beta strandi132 – 1365Combined sources
Turni137 – 1393Combined sources
Beta strandi142 – 1465Combined sources
Helixi148 – 1503Combined sources
Beta strandi154 – 1563Combined sources
Turni162 – 1643Combined sources
Beta strandi165 – 1717Combined sources
Turni175 – 1773Combined sources
Beta strandi178 – 1836Combined sources
Turni184 – 1863Combined sources
Beta strandi187 – 1948Combined sources
Helixi195 – 1995Combined sources
Beta strandi203 – 2075Combined sources
Beta strandi222 – 2265Combined sources
Beta strandi228 – 23710Combined sources
Turni238 – 2403Combined sources
Beta strandi243 – 2486Combined sources
Beta strandi277 – 28610Combined sources
Beta strandi300 – 3056Combined sources
Turni308 – 3103Combined sources
Helixi311 – 3144Combined sources
Beta strandi321 – 3233Combined sources
Beta strandi326 – 3294Combined sources
Turni330 – 3323Combined sources
Beta strandi333 – 3375Combined sources
Beta strandi344 – 3474Combined sources
Beta strandi355 – 36410Combined sources
Turni365 – 3684Combined sources
Beta strandi369 – 3746Combined sources
Beta strandi390 – 3945Combined sources
Beta strandi400 – 4045Combined sources
Turni405 – 4073Combined sources
Helixi409 – 4135Combined sources
Helixi419 – 4224Combined sources
Helixi424 – 4263Combined sources
Helixi429 – 4335Combined sources
Helixi435 – 4428Combined sources
Beta strandi444 – 4463Combined sources
Turni666 – 6694Combined sources
Beta strandi674 – 6829Combined sources
Turni684 – 6863Combined sources
Beta strandi688 – 70518Combined sources
Helixi706 – 7083Combined sources
Helixi709 – 72214Combined sources
Beta strandi731 – 7366Combined sources
Beta strandi738 – 7458Combined sources
Beta strandi749 – 7513Combined sources
Helixi752 – 7576Combined sources
Helixi765 – 7695Combined sources
Helixi774 – 79017Combined sources
Helixi800 – 8023Combined sources
Beta strandi803 – 8064Combined sources
Helixi809 – 8124Combined sources
Beta strandi823 – 8264Combined sources
Turni836 – 8383Combined sources
Helixi851 – 8555Combined sources
Helixi858 – 8614Combined sources
Helixi900 – 91415Combined sources
Turni924 – 9263Combined sources
Helixi927 – 9337Combined sources
Helixi947 – 96014Combined sources
Helixi965 – 9673Combined sources
Helixi971 – 9755Combined sources
Helixi978 – 9803Combined sources
Helixi983 – 99816Combined sources
Turni1002 – 10054Combined sources
Helixi1007 – 10137Combined sources
Helixi1016 – 10194Combined sources
Helixi1025 – 10284Combined sources
Helixi1031 – 10355Combined sources
Beta strandi1038 – 10414Combined sources
Helixi1048 – 106013Combined sources
Helixi1062 – 10643Combined sources
Helixi1067 – 10726Combined sources
Helixi1078 – 108710Combined sources
Helixi1091 – 110212Combined sources
Turni1107 – 11093Combined sources
Helixi1110 – 11145Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.

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.
InParanoidiP32361.
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

        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 AAB68894.1 differs from that shown. Reason: Erroneous initiation. Curated

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:
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 .
PIRi A47541.
RefSeqi NP_011946.1. NM_001179209.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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. 335 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.
InParanoidi P32361.
KOi K08852.
OMAi NILWFVE.
OrthoDBi EOG7X3R27.

Enzyme and pathway databases

BioCyci YEAST:G3O-31126-MONOMER.
BRENDAi 2.7.11.1. 984.
Reactomei REACT_251918. IRE1alpha activates chaperones.

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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 155 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