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O75460

- ERN1_HUMAN

UniProt

O75460 - ERN1_HUMAN

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Protein
Serine/threonine-protein kinase/endoribonuclease IRE1
Gene
ERN1, IRE1
Organism
Homo sapiens (Human)
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 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.1 Publication

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 Publication
Active sitei688 – 6881Proton acceptor By similarityBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi577 – 5859ATP By similarityBy similarity

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. HAC1-type intron splice site recognition and cleavage Source: WormBase
  2. RNA phosphodiester bond hydrolysis, endonucleolytic Source: GOC
  3. activation of signaling protein activity involved in unfolded protein response Source: UniProtKB
  4. cell cycle arrest Source: UniProtKB
  5. cellular protein metabolic process Source: Reactome
  6. endoplasmic reticulum unfolded protein response Source: Reactome
  7. intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress Source: Ensembl
  8. positive regulation of endoplasmic reticulum unfolded protein response Source: UniProtKB
  9. protein autophosphorylation Source: Ensembl
  10. protein phosphorylation Source: UniProtKB
  11. regulation of transcription, DNA-templated Source: UniProtKB-KW
  12. transcription, DNA-templated Source: UniProtKB-KW
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_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:ERN1
Synonyms:IRE1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 17

Organism-specific databases

HGNCiHGNC:3449. ERN1.

Subcellular locationi

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

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini19 – 443425Lumenal Reviewed prediction
Add
BLAST
Transmembranei444 – 46421Helical; Reviewed prediction
Add
BLAST
Topological domaini465 – 977513Cytoplasmic Reviewed prediction
Add
BLAST

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
Complete GO annotation...

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 – 1818 Reviewed prediction
Add
BLAST
Chaini19 – 977959Serine/threonine-protein kinase/endoribonuclease IRE1
PRO_0000024327Add
BLAST

Amino acid modifications

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

Post-translational modificationi

Autophosphorylated.1 Publication
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 TRAF2.2 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
TRAF2Q129332EBI-371750,EBI-355744

Protein-protein interaction databases

BioGridi108391. 16 interactions.
DIPiDIP-31711N.
IntActiO75460. 10 interactions.
MINTiMINT-3001268.
STRINGi9606.ENSP00000401445.

Structurei

Secondary structure

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.

Miscellaneous databases

EvolutionaryTraceiO75460.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini571 – 832262Protein kinase
Add
BLAST
Domaini835 – 963129KEN
Add
BLAST

Sequence similaritiesi

Contains 1 KEN domain.

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

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.
VSP_034582Add
BLAST
Alternative sequencei71 – 977907Missing in isoform 2.
VSP_034583Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti190 – 1912DV → EG in AAC25991. 1 Publication
Sequence conflicti768 – 7681I → V in AAC25991. 1 Publication
Sequence conflicti816 – 8161D → G in BAF85092. 1 Publication
Sequence conflicti824 – 8252KH → ND in AAC25991. 1 Publication
Sequence conflicti880 – 8801V → D in AAC25991. 1 Publication
Sequence conflicti904 – 9041M → T in BAF85092. 1 Publication
Sequence conflicti924 – 9241S → T in AAC25991. 1 Publication

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. 10 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

« Hide 'large scale' publications
  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: Liver.
  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: September 3, 2014
This is version 140 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

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