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Protein

Serine/threonine-protein kinase/endoribonuclease IRE1

Gene

ERN1

Organism
Homo sapiens (Human)
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.By similarity3 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.1 Publication

Cofactori

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)DescriptionActionsGraphical viewLength
Binding sitei599ATPPROSITE-ProRule annotation1 Publication1
Active sitei688Proton acceptorPROSITE-ProRule annotationBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi577 – 585ATPPROSITE-ProRule annotationBy similarity9

GO - Molecular functioni

  • ADP binding Source: ParkinsonsUK-UCL
  • ATP binding Source: UniProtKB
  • endoribonuclease activity Source: UniProtKB
  • enzyme binding Source: UniProtKB
  • Hsp70 protein binding Source: ParkinsonsUK-UCL
  • Hsp90 protein binding Source: ParkinsonsUK-UCL
  • magnesium ion binding Source: UniProtKB
  • platelet-derived growth factor receptor binding Source: BHF-UCL
  • protein homodimerization activity Source: ParkinsonsUK-UCL
  • protein serine/threonine kinase activity Source: UniProtKB

GO - Biological processi

  • activation of JUN kinase activity Source: ParkinsonsUK-UCL
  • activation of signaling protein activity involved in unfolded protein response Source: UniProtKB
  • cell cycle arrest Source: UniProtKB
  • cellular response to glucose stimulus Source: ParkinsonsUK-UCL
  • cellular response to vascular endothelial growth factor stimulus Source: UniProtKB
  • endothelial cell proliferation Source: UniProtKB
  • insulin metabolic process Source: ParkinsonsUK-UCL
  • intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress Source: Ensembl
  • IRE1-mediated unfolded protein response Source: ParkinsonsUK-UCL
  • mRNA catabolic process Source: ParkinsonsUK-UCL
  • mRNA cleavage Source: ParkinsonsUK-UCL
  • mRNA endonucleolytic cleavage involved in unfolded protein response Source: WormBase
  • mRNA splicing, via endonucleolytic cleavage and ligation Source: UniProtKB
  • peptidyl-serine autophosphorylation Source: ParkinsonsUK-UCL
  • peptidyl-serine trans-autophosphorylation Source: ParkinsonsUK-UCL
  • positive regulation of endoplasmic reticulum unfolded protein response Source: UniProtKB
  • positive regulation of RNA splicing Source: UniProtKB
  • positive regulation of vascular smooth muscle cell proliferation Source: BHF-UCL
  • protein autophosphorylation Source: ParkinsonsUK-UCL
  • protein phosphorylation Source: UniProtKB
  • regulation of macroautophagy Source: ParkinsonsUK-UCL
  • regulation of transcription, DNA-templated Source: UniProtKB-KW
  • response to endoplasmic reticulum stress Source: ParkinsonsUK-UCL
  • 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

BioCyciZFISH:HS17093-MONOMER.
ReactomeiR-HSA-381070. 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:ERN1Imported
Synonyms:IRE1Imported
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 17

Organism-specific databases

HGNCiHGNC:3449. ERN1.

Subcellular locationi

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

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini19 – 443LumenalSequence analysisAdd BLAST425
Transmembranei444 – 464HelicalSequence analysisAdd BLAST21
Topological domaini465 – 977CytoplasmicSequence analysisAdd BLAST513

GO - Cellular componenti

  • AIP1-IRE1 complex Source: Ensembl
  • cytoplasm Source: UniProtKB
  • endoplasmic reticulum Source: UniProtKB
  • endoplasmic reticulum membrane Source: Reactome
  • integral component of endoplasmic reticulum membrane Source: UniProtKB
  • Ire1 complex Source: ParkinsonsUK-UCL
  • IRE1-RACK1-PP2A complex Source: ParkinsonsUK-UCL
  • IRE1-TRAF2-ASK1 complex Source: ParkinsonsUK-UCL
  • mitochondrion Source: Ensembl
  • nuclear inner membrane Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi109C → S: No effect on dimerization. 1 Publication1
Mutagenesisi148C → S: No effect on dimerization. Weakens dimer; when associated with S-148. 1 Publication1
Mutagenesisi332C → S: No effect on dimerization. Weakens dimer; when associated with S-332. 1 Publication1
Mutagenesisi599K → A: Loss of autophosphorylation and of endoribonuclease activity. Inhibition of growth arrest. 2 Publications1

Organism-specific databases

DisGeNETi2081.
OpenTargetsiENSG00000178607.
PharmGKBiPA27861.

Chemistry databases

ChEMBLiCHEMBL1163101.
GuidetoPHARMACOLOGYi2020.

Polymorphism and mutation databases

BioMutaiERN1.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 18Sequence analysisAdd BLAST18
ChainiPRO_000002432719 – 977Serine/threonine-protein kinase/endoribonuclease IRE1Add BLAST959

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi176N-linked (GlcNAc...)Sequence analysis1
Modified residuei973PhosphothreonineCombined sources1

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.
PeptideAtlasiO75460.
PRIDEiO75460.

PTM databases

iPTMnetiO75460.
PhosphoSitePlusiO75460.

Expressioni

Tissue specificityi

Ubiquitously expressed. High levels observed in pancreatic tissue.1 Publication

Gene expression databases

BgeeiENSG00000178607.
CleanExiHS_ERN1.
GenevisibleiO75460. HS.

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.By similarity2 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.
HSPA5P110213EBI-371750,EBI-354921
Hspa5P200292EBI-371750,EBI-772325From a different organism.
SYVN1Q86TM62EBI-371750,EBI-947849
TAOK3Q9H2K83EBI-371750,EBI-1384100
TRAF2Q129333EBI-371750,EBI-355744
YIPF5Q969M33EBI-371750,EBI-2124787

GO - Molecular functioni

  • enzyme binding Source: UniProtKB
  • Hsp70 protein binding Source: ParkinsonsUK-UCL
  • Hsp90 protein binding Source: ParkinsonsUK-UCL
  • platelet-derived growth factor receptor binding Source: BHF-UCL
  • protein homodimerization activity Source: ParkinsonsUK-UCL

Protein-protein interaction databases

BioGridi108391. 28 interactors.
DIPiDIP-31711N.
IntActiO75460. 17 interactors.
MINTiMINT-3001268.
STRINGi9606.ENSP00000401445.

Chemistry databases

BindingDBiO75460.

Structurei

Secondary structure

1977
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi32 – 37Combined sources6
Beta strandi40 – 46Combined sources7
Turni47 – 49Combined sources3
Beta strandi52 – 57Combined sources6
Beta strandi73 – 75Combined sources3
Turni77 – 79Combined sources3
Beta strandi82 – 84Combined sources3
Beta strandi93 – 95Combined sources3
Helixi100 – 104Combined sources5
Beta strandi120 – 128Combined sources9
Beta strandi154 – 164Combined sources11
Beta strandi168 – 172Combined sources5
Beta strandi176 – 182Combined sources7
Beta strandi197 – 201Combined sources5
Beta strandi205 – 209Combined sources5
Turni211 – 213Combined sources3
Beta strandi216 – 221Combined sources6
Beta strandi226 – 231Combined sources6
Beta strandi238 – 240Combined sources3
Beta strandi243 – 246Combined sources4
Helixi247 – 264Combined sources18
Helixi273 – 279Combined sources7
Beta strandi280 – 284Combined sources5
Beta strandi286 – 288Combined sources3
Beta strandi297 – 300Combined sources4
Turni359 – 361Combined sources3
Beta strandi564 – 566Combined sources3
Beta strandi567 – 580Combined sources14
Turni581 – 583Combined sources3
Beta strandi584 – 591Combined sources8
Beta strandi594 – 601Combined sources8
Helixi603 – 605Combined sources3
Helixi606 – 617Combined sources12
Beta strandi628 – 633Combined sources6
Beta strandi638 – 642Combined sources5
Beta strandi645 – 648Combined sources4
Helixi649 – 655Combined sources7
Helixi657 – 661Combined sources5
Helixi665 – 681Combined sources17
Turni691 – 693Combined sources3
Beta strandi694 – 697Combined sources4
Turni701 – 703Combined sources3
Beta strandi707 – 709Combined sources3
Helixi712 – 714Combined sources3
Helixi740 – 743Combined sources4
Helixi754 – 768Combined sources15
Helixi778 – 780Combined sources3
Helixi781 – 787Combined sources7
Beta strandi793 – 795Combined sources3
Helixi800 – 812Combined sources13
Helixi817 – 819Combined sources3
Helixi823 – 827Combined sources5
Helixi830 – 832Combined sources3
Helixi835 – 849Combined sources15
Beta strandi854 – 856Combined sources3
Helixi857 – 865Combined sources9
Helixi867 – 870Combined sources4
Beta strandi874 – 878Combined sources5
Helixi880 – 887Combined sources8
Beta strandi888 – 890Combined sources3
Helixi897 – 909Combined sources13
Helixi911 – 913Combined sources3
Helixi916 – 922Combined sources7
Helixi927 – 936Combined sources10
Helixi940 – 947Combined sources8
Helixi948 – 951Combined sources4
Beta strandi952 – 954Combined sources3
Helixi955 – 957Combined sources3
Turni958 – 960Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2HZ6X-ray3.10A24-390[»]
3P23X-ray2.70A/B/C/D547-977[»]
4U6RX-ray2.50A547-977[»]
4YZ9X-ray2.46A/B/C562-966[»]
4YZCX-ray2.49A/B562-966[»]
4YZDX-ray3.10A/B/C562-966[»]
4Z7GX-ray2.60A/B562-977[»]
4Z7HX-ray2.90A/B562-977[»]
5HGIX-ray2.58A547-977[»]
ProteinModelPortaliO75460.
SMRiO75460.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO75460.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini571 – 832Protein kinasePROSITE-ProRule annotationAdd BLAST262
Domaini835 – 963KENPROSITE-ProRule annotationAdd BLAST129

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

eggNOGiKOG1027. Eukaryota.
COG0515. LUCA.
GeneTreeiENSGT00390000015684.
HOGENOMiHOG000012929.
HOVERGENiHBG051506.
InParanoidiO75460.
KOiK08852.
OMAiSEDCKDN.
OrthoDBiEOG091G049V.
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.
IPR018997. PUB_domain.
IPR027295. Quinoprotein_ADH-like_fam.
IPR011047. Quinoprotein_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.
SM00220. S_TKc. 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 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

        10         20         30         40         50
MPARRLLLLL TLLLPGLGIF GSTSTVTLPE TLLFVSTLDG SLHAVSKRTG
60 70 80 90 100
SIKWTLKEDP VLQVPTHVEE PAFLPDPNDG SLYTLGSKNN EGLTKLPFTI
110 120 130 140 150
PELVQASPCR SSDGILYMGK KQDIWYVIDL LTGEKQQTLS SAFADSLCPS
160 170 180 190 200
TSLLYLGRTE YTITMYDTKT RELRWNATYF DYAASLPEDD VDYKMSHFVS
210 220 230 240 250
NGDGLVVTVD SESGDVLWIQ NYASPVVAFY VWQREGLRKV MHINVAVETL
260 270 280 290 300
RYLTFMSGEV GRITKWKYPF PKETEAKSKL TPTLYVGKYS TSLYASPSMV
310 320 330 340 350
HEGVAVVPRG STLPLLEGPQ TDGVTIGDKG ECVITPSTDV KFDPGLKSKN
360 370 380 390 400
KLNYLRNYWL LIGHHETPLS ASTKMLERFP NNLPKHRENV IPADSEKKSF
410 420 430 440 450
EEVINLVDQT SENAPTTVSR DVEEKPAHAP ARPEAPVDSM LKDMATIILS
460 470 480 490 500
TFLLIGWVAF IITYPLSMHQ QQQLQHQQFQ KELEKIQLLQ QQQQQLPFHP
510 520 530 540 550
PGDTAQDGEL LDTSGPYSES SGTSSPSTSP RASNHSLCSG SSASKAGSSP
560 570 580 590 600
SLEQDDGDEE TSVVIVGKIS FCPKDVLGHG AEGTIVYRGM FDNRDVAVKR
610 620 630 640 650
ILPECFSFAD REVQLLRESD EHPNVIRYFC TEKDRQFQYI AIELCAATLQ
660 670 680 690 700
EYVEQKDFAH LGLEPITLLQ QTTSGLAHLH SLNIVHRDLK PHNILISMPN
710 720 730 740 750
AHGKIKAMIS DFGLCKKLAV GRHSFSRRSG VPGTEGWIAP EMLSEDCKEN
760 770 780 790 800
PTYTVDIFSA GCVFYYVISE GSHPFGKSLQ RQANILLGAC SLDCLHPEKH
810 820 830 840 850
EDVIARELIE KMIAMDPQKR PSAKHVLKHP FFWSLEKQLQ FFQDVSDRIE
860 870 880 890 900
KESLDGPIVK QLERGGRAVV KMDWRENITV PLQTDLRKFR TYKGGSVRDL
910 920 930 940 950
LRAMRNKKHH YRELPAEVRE TLGSLPDDFV CYFTSRFPHL LAHTYRAMEL
960 970
CSHERLFQPY YFHEPPEPQP PVTPDAL
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

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti190 – 191DV → EG in AAC25991 (PubMed:9637683).Curated2
Sequence conflicti768I → V in AAC25991 (PubMed:9637683).Curated1
Sequence conflicti816D → G in BAF85092 (PubMed:14702039).Curated1
Sequence conflicti824 – 825KH → ND in AAC25991 (PubMed:9637683).Curated2
Sequence conflicti880V → D in AAC25991 (PubMed:9637683).Curated1
Sequence conflicti904M → T in BAF85092 (PubMed:14702039).Curated1
Sequence conflicti924S → T in AAC25991 (PubMed:9637683).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_040488244N → S in a renal clear cell carcinoma sample; somatic mutation. 1 Publication1
Natural variantiVAR_040489418V → M.1 PublicationCorresponds to variant rs55869215dbSNPEnsembl.1
Natural variantiVAR_040490474L → R in a lung adenocarcinoma sample; somatic mutation. 1 PublicationCorresponds to variant rs186305118dbSNPEnsembl.1
Natural variantiVAR_040491635R → W in a gastric adenocarcinoma sample; somatic mutation. 1 PublicationCorresponds to variant rs146710304dbSNPEnsembl.1
Natural variantiVAR_040492700N → S.1 Publication1
Natural variantiVAR_040493769S → F in a glioblastoma multiforme sample; somatic mutation. 1 Publication1
Natural variantiVAR_040494830P → L in an ovarian serous carcinoma sample; somatic mutation. 1 Publication1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_03458219 – 70IFGST…THVEE → VSDRGAWGGGQLATAGSGPG QRRGAGAGVRAGSATAAARC PVSPAVGGSGRA in isoform 2. 2 PublicationsAdd BLAST52
Alternative sequenceiVSP_03458371 – 977Missing in isoform 2. 2 PublicationsAdd BLAST907

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.3. human. [O75460-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2HZ6X-ray3.10A24-390[»]
3P23X-ray2.70A/B/C/D547-977[»]
4U6RX-ray2.50A547-977[»]
4YZ9X-ray2.46A/B/C562-966[»]
4YZCX-ray2.49A/B562-966[»]
4YZDX-ray3.10A/B/C562-966[»]
4Z7GX-ray2.60A/B562-977[»]
4Z7HX-ray2.90A/B562-977[»]
5HGIX-ray2.58A547-977[»]
ProteinModelPortaliO75460.
SMRiO75460.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108391. 28 interactors.
DIPiDIP-31711N.
IntActiO75460. 17 interactors.
MINTiMINT-3001268.
STRINGi9606.ENSP00000401445.

Chemistry databases

BindingDBiO75460.
ChEMBLiCHEMBL1163101.
GuidetoPHARMACOLOGYi2020.

PTM databases

iPTMnetiO75460.
PhosphoSitePlusiO75460.

Polymorphism and mutation databases

BioMutaiERN1.

Proteomic databases

MaxQBiO75460.
PaxDbiO75460.
PeptideAtlasiO75460.
PRIDEiO75460.

Protocols and materials databases

DNASUi2081.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000433197; ENSP00000401445; ENSG00000178607. [O75460-1]
ENST00000606895; ENSP00000475519; ENSG00000178607. [O75460-2]
GeneIDi2081.
KEGGihsa:2081.
UCSCiuc002jdz.3. human. [O75460-1]

Organism-specific databases

CTDi2081.
DisGeNETi2081.
GeneCardsiERN1.
H-InvDBHIX0014084.
HGNCiHGNC:3449. ERN1.
HPAiCAB009495.
HPA027730.
MIMi604033. gene.
neXtProtiNX_O75460.
OpenTargetsiENSG00000178607.
PharmGKBiPA27861.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1027. Eukaryota.
COG0515. LUCA.
GeneTreeiENSGT00390000015684.
HOGENOMiHOG000012929.
HOVERGENiHBG051506.
InParanoidiO75460.
KOiK08852.
OMAiSEDCKDN.
OrthoDBiEOG091G049V.
PhylomeDBiO75460.
TreeFamiTF313986.

Enzyme and pathway databases

BioCyciZFISH:HS17093-MONOMER.
ReactomeiR-HSA-381070. IRE1alpha activates chaperones.
SignaLinkiO75460.

Miscellaneous databases

ChiTaRSiERN1. human.
EvolutionaryTraceiO75460.
GeneWikiiERN1.
GenomeRNAii2081.
PROiO75460.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000178607.
CleanExiHS_ERN1.
GenevisibleiO75460. HS.

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. 1 hit.
PF06479. Ribonuc_2-5A. 1 hit.
[Graphical view]
SMARTiSM00564. PQQ. 5 hits.
SM00580. PUG. 1 hit.
SM00220. S_TKc. 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...

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: November 30, 2016
This is version 164 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

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.