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Protein

Serine/threonine-protein kinase/endoribonuclease IRE1

Gene

Ern1

Organism
Mus musculus (Mouse)
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 XBP1 mRNA to generate a new C-terminus, converting it into a potent unfolded-protein response transcriptional activator and triggering growth arrest and apoptosis.1 Publication

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.By similarity

Cofactori

Mg2+By similarity

Enzyme regulationi

The kinase domain is activated by trans-autophosphorylation. Kinase activity is required for activation of the endoribonuclease domain (By similarity).By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei599 – 5991ATPPROSITE-ProRule annotationBy similarity
Active sitei688 – 6881Proton acceptorPROSITE-ProRule annotationBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi577 – 5859ATPPROSITE-ProRule annotationBy similarity

GO - Molecular functioni

  1. ADP binding Source: MGI
  2. ATP binding Source: UniProtKB
  3. endonuclease activity Source: UniProtKB
  4. endoribonuclease activity Source: MGI
  5. enzyme binding Source: MGI
  6. identical protein binding Source: MGI
  7. magnesium ion binding Source: UniProtKB
  8. protein homodimerization activity Source: MGI
  9. 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 response to vascular endothelial growth factor stimulus Source: UniProtKB
  4. endoplasmic reticulum unfolded protein response Source: MGI
  5. endothelial cell proliferation Source: UniProtKB
  6. HAC1-type intron splice site recognition and cleavage Source: MGI
  7. intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress Source: ParkinsonsUK-UCL
  8. mRNA cleavage Source: MGI
  9. mRNA splicing, via endonucleolytic cleavage and ligation Source: UniProtKB
  10. peptidyl-serine trans-autophosphorylation Source: MGI
  11. positive regulation of endoplasmic reticulum unfolded protein response Source: MGI
  12. positive regulation of RNA splicing Source: UniProtKB
  13. protein autophosphorylation Source: MGI
  14. protein phosphorylation Source: UniProtKB
  15. regulation of transcription, DNA-templated Source: UniProtKB-KW
  16. RNA splicing Source: MGI
  17. transcription, DNA-templated Source: UniProtKB-KW
  18. UFP-specific transcription factor mRNA processing involved in endoplasmic reticulum unfolded protein response Source: MGI
Complete GO annotation...

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_320710. IRE1alpha activates chaperones.

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
Ire1-alpha
Short name:
IRE1a
Including the following 2 domains:
Gene namesi
Name:Ern1Imported
Synonyms:Ire1By similarity
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 11

Organism-specific databases

MGIiMGI:1930134. Ern1.

Subcellular locationi

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

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini21 – 445425LumenalSequence AnalysisAdd
BLAST
Transmembranei446 – 46621HelicalSequence AnalysisAdd
BLAST
Topological domaini467 – 977511CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. AIP1-IRE1 complex Source: ParkinsonsUK-UCL
  2. cytoplasm Source: MGI
  3. endoplasmic reticulum Source: MGI
  4. endoplasmic reticulum membrane Source: MGI
  5. integral component of endoplasmic reticulum membrane Source: MGI
  6. IRE1-TRAF2-ASK1 complex Source: MGI
  7. mitochondrion Source: MGI
  8. nuclear inner membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2020Sequence AnalysisAdd
BLAST
Chaini21 – 977957Serine/threonine-protein kinase/endoribonuclease IRE1PRO_0000024328Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi178 – 1781N-linked (GlcNAc...)Sequence Analysis

Post-translational modificationi

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

Keywords - PTMi

ADP-ribosylation, Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiQ9EQY0.
PaxDbiQ9EQY0.
PRIDEiQ9EQY0.

Expressioni

Tissue specificityi

Ubiquitously expressed. High levels in thymus, liver and lung. In the brain, preferentially expressed in cortical, hippocampal and olfactory neurons.1 Publication

Gene expression databases

BgeeiQ9EQY0.
ExpressionAtlasiQ9EQY0. baseline and differential.
GenevestigatoriQ9EQY0.

Interactioni

Subunit structurei

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 (By similarity). Interacts with TAOK3 (By similarity). 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. Interacts with TRAF2.By similarity1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
Tnfrsf1aP251182EBI-5480799,EBI-518014
Traf6P701966EBI-5480799,EBI-448028

Protein-protein interaction databases

BioGridi219724. 1 interaction.
IntActiQ9EQY0. 5 interactions.
MINTiMINT-2631281.

Structurei

Secondary structure

1
977
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi570 – 57910Combined sources
Beta strandi581 – 5833Combined sources
Beta strandi585 – 59410Combined sources
Beta strandi597 – 6015Combined sources
Turni603 – 6053Combined sources
Beta strandi606 – 6083Combined sources
Helixi610 – 6178Combined sources
Beta strandi628 – 6347Combined sources
Beta strandi637 – 6426Combined sources
Beta strandi646 – 6483Combined sources
Helixi649 – 6546Combined sources
Helixi665 – 68016Combined sources
Turni681 – 6833Combined sources
Helixi691 – 6933Combined sources
Beta strandi694 – 6963Combined sources
Beta strandi707 – 7093Combined sources
Beta strandi713 – 7164Combined sources
Turni735 – 7373Combined sources
Helixi740 – 7423Combined sources
Helixi753 – 76816Combined sources
Turni769 – 7713Combined sources
Turni778 – 7803Combined sources
Helixi781 – 7877Combined sources
Beta strandi797 – 7993Combined sources
Helixi800 – 81213Combined sources
Helixi817 – 8193Combined sources
Helixi823 – 8286Combined sources
Helixi830 – 8323Combined sources
Helixi835 – 84915Combined sources
Beta strandi854 – 8563Combined sources
Helixi857 – 8626Combined sources
Helixi867 – 8704Combined sources
Helixi874 – 8774Combined sources
Helixi880 – 8878Combined sources
Helixi897 – 90913Combined sources
Helixi911 – 9133Combined sources
Helixi916 – 9216Combined sources
Beta strandi924 – 9263Combined sources
Helixi927 – 93610Combined sources
Helixi938 – 94710Combined sources
Helixi948 – 9514Combined sources
Turni954 – 9563Combined sources
Helixi957 – 9593Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4PL3X-ray2.90A/B550-977[»]
4PL4X-ray3.00A/B/C/D550-977[»]
4PL5X-ray3.40A/B/C/D550-977[»]
ProteinModelPortaliQ9EQY0.
SMRiQ9EQY0. Positions 31-370, 560-964.
ModBaseiSearch...
MobiDBiSearch...

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.
GeneTreeiENSGT00390000015684.
HOGENOMiHOG000012929.
HOVERGENiHBG051506.
InParanoidiQ9EQY0.
KOiK08852.
OMAiYVWQREG.
OrthoDBiEOG7C2R0H.
PhylomeDBiQ9EQY0.
TreeFamiTF313986.

Family and domain databases

Gene3Di2.140.10.10. 2 hits.
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. AlignAdd to basket

Isoform 11 Publication (identifier: Q9EQY0-1) [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

        10         20         30         40         50
MPARWLLLLL ALLLPPPGPG SFGRTSTVTL PETLLFVSTL DGSLHAVSKR
60 70 80 90 100
TGSIKWTLKE DPVLQVPTHV EEPAFLPDPN DGSLYTLGGK NNEGLTKLPF
110 120 130 140 150
TIPELVQASP CRSSDGILYM GKKQDIWYVI DLLTGEKQQT LSSAFADSLC
160 170 180 190 200
PSTSLLYLGR TEYTITMYDT KTRELRWNAT YFDYAASLPE DDVDYKMSHF
210 220 230 240 250
VSNGDGLVVT VDSESGDVLW IQNYASPVVA FYVWQGEVLR KVVHINVAVE
260 270 280 290 300
TLRYLTFMSG EVGRITKWKY PFPKETEAKS KLTPTLYVGK YSTSLYASPS
310 320 330 340 350
MVHEGVAVVP RGSTLPLLEG PQTDGVTIGD KGECVITPST DLKFDPGLKG
360 370 380 390 400
KSKLNYLRNY WLLIGHHETP LSASTKMLER FPNNLPKHRE NVIPADSEKR
410 420 430 440 450
SFEEVINIVG QTSDNTPTTV SQDVEEKLAR APAKPEAPVD SMLKDMATII
460 470 480 490 500
LSTFLLVGWV AFIITYPLSV HQQRQLQHQQ FQKELEKIQL LQQQQLPFHP
510 520 530 540 550
HGDLTQDPEF LDSSGPFSES SGTSSPSPSP RASNHSLHPS SSASRAGTSP
560 570 580 590 600
SLEQDDEDEE TRMVIVGKIS FCPKDVLGHG AEGTIVYKGM FDNRDVAVKR
610 620 630 640 650
ILPECFSFAD REVQLLRESD EHPNVIRYFC TEKDRQFQYI AIELCAATLQ
660 670 680 690 700
EYVEQKDFAH LGLEPITLLH QTTSGLAHLH SLNIVHRDLK PHNILLSMPN
710 720 730 740 750
AHGRIKAMIS DFGLCKKLAV GRHSFSRRSG VPGTEGWIAP EMLSEDCKDN
760 770 780 790 800
PTYTVDIFSA GCVFYYVISE GNHPFGKSLQ RQANILLGAC NLDCFHSDKH
810 820 830 840 850
EDVIARELIE KMIAMDPQQR PSAKHVLKHP FFWSLEKQLQ FFQDVSDRIE
860 870 880 890 900
KEALDGPIVR QLERGGRAVV KMDWRENITV PLQTDLRKFR TYKGGSVRDL
910 920 930 940 950
LRAMRNKKHH YRELPVEVQE TLGSIPDDFV RYFTSRFPHL LSHTYQAMEL
960 970
CRHERLFQTY YWHEPTEPQP PVIPYAL
Length:977
Mass (Da):110,185
Last modified:March 1, 2001 - v1
Checksum:i216E3E2FA2FF3F70
GO
Isoform 2Curated (identifier: Q9EQY0-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     406-408: INI → SGK
     409-977: Missing.

Note: No experimental confirmation available.Curated

Show »
Length:408
Mass (Da):45,303
Checksum:i4FF98C4A4EC4D1F3
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei406 – 4083INI → SGK in isoform 2. 1 PublicationVSP_050794
Alternative sequencei409 – 977569Missing in isoform 2. 1 PublicationVSP_050795Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB031332 mRNA. Translation: BAB20901.1.
AK018505 mRNA. Translation: BAB31243.1.
CCDSiCCDS25556.1. [Q9EQY0-1]
RefSeqiNP_076402.1. NM_023913.2. [Q9EQY0-1]
UniGeneiMm.340943.

Genome annotation databases

EnsembliENSMUST00000001059; ENSMUSP00000001059; ENSMUSG00000020715. [Q9EQY0-1]
ENSMUST00000106801; ENSMUSP00000102413; ENSMUSG00000020715. [Q9EQY0-2]
GeneIDi78943.
KEGGimmu:78943.
UCSCiuc007lyy.1. mouse. [Q9EQY0-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB031332 mRNA. Translation: BAB20901.1.
AK018505 mRNA. Translation: BAB31243.1.
CCDSiCCDS25556.1. [Q9EQY0-1]
RefSeqiNP_076402.1. NM_023913.2. [Q9EQY0-1]
UniGeneiMm.340943.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4PL3X-ray2.90A/B550-977[»]
4PL4X-ray3.00A/B/C/D550-977[»]
4PL5X-ray3.40A/B/C/D550-977[»]
ProteinModelPortaliQ9EQY0.
SMRiQ9EQY0. Positions 31-370, 560-964.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi219724. 1 interaction.
IntActiQ9EQY0. 5 interactions.
MINTiMINT-2631281.

Proteomic databases

MaxQBiQ9EQY0.
PaxDbiQ9EQY0.
PRIDEiQ9EQY0.

Protocols and materials databases

DNASUi78943.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000001059; ENSMUSP00000001059; ENSMUSG00000020715. [Q9EQY0-1]
ENSMUST00000106801; ENSMUSP00000102413; ENSMUSG00000020715. [Q9EQY0-2]
GeneIDi78943.
KEGGimmu:78943.
UCSCiuc007lyy.1. mouse. [Q9EQY0-1]

Organism-specific databases

CTDi2081.
MGIiMGI:1930134. Ern1.

Phylogenomic databases

eggNOGiCOG0515.
GeneTreeiENSGT00390000015684.
HOGENOMiHOG000012929.
HOVERGENiHBG051506.
InParanoidiQ9EQY0.
KOiK08852.
OMAiYVWQREG.
OrthoDBiEOG7C2R0H.
PhylomeDBiQ9EQY0.
TreeFamiTF313986.

Enzyme and pathway databases

ReactomeiREACT_320710. IRE1alpha activates chaperones.

Miscellaneous databases

NextBioi349824.
PROiQ9EQY0.
SOURCEiSearch...

Gene expression databases

BgeeiQ9EQY0.
ExpressionAtlasiQ9EQY0. baseline and differential.
GenevestigatoriQ9EQY0.

Family and domain databases

Gene3Di2.140.10.10. 2 hits.
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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Characterization of mouse Ire1alpha: cloning, mRNA localization in the brain and functional analysis in a neural cell line."
    Miyoshi K., Katayama T., Imaizumi K., Taniguchi M., Mori Y., Hitomi J., Yui D., Manabe T., Gomi F., Yoneda T., Tohyama M.
    Brain Res. Mol. Brain Res. 85:68-76(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
    Strain: C57BL/61 Publication.
    Tissue: Brain1 Publication.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Strain: C57BL/6J.
    Tissue: Colon.
  3. "IRE1-mediated unconventional mRNA splicing and S2P-mediated ATF6 cleavage merge to regulate XBP1 in signaling the unfolded protein response."
    Lee K., Tirasophon W., Shen X., Michalak M., Prywes R., Okada T., Yoshida H., Mori K., Kaufman R.J.
    Genes Dev. 16:452-466(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  4. "AIP1 is critical in transducing IRE1-mediated endoplasmic reticulum stress response."
    Luo D., He Y., Zhang H., Yu L., Chen H., Xu Z., Tang S., Urano F., Min W.
    J. Biol. Chem. 283:11905-11912(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DAB2IP AND TRAF2.

Entry informationi

Entry nameiERN1_MOUSE
AccessioniPrimary (citable) accession number: Q9EQY0
Secondary accession number(s): Q9D340
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: March 1, 2001
Last modified: April 29, 2015
This is version 127 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

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

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.