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O75460 (ERN1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 139. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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:

  1. Serine/threonine-protein kinase
    EC=2.7.11.1
  2. Endoribonuclease
    EC=3.1.26.-
Gene names
Name:ERN1
Synonyms:IRE1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length977 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.1 Ref.8 Ref.9 UniProtKB Q9EQY0

Catalytic activity

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

Cofactor

Magnesium. Ref.1

Enzyme regulation

The kinase domain is activated by trans-autophosphorylation. Kinase activity is required for activation of the endoribonuclease domain. Ref.1 Ref.9

Subunit structure

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. Ref.7 Ref.9

Subcellular location

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

Tissue specificity

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

Post-translational modification

Autophosphorylated. Ref.1

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

Sequence similarities

Belongs to the protein kinase superfamily. Ser/Thr protein kinase family.

Contains 1 KEN domain.

Contains 1 protein kinase domain.

Ontologies

Keywords
   Biological processApoptosis
Transcription
Transcription regulation
Unfolded protein response
   Cellular componentEndoplasmic reticulum
Membrane
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainSignal
Transmembrane
Transmembrane helix
   LigandATP-binding
Magnesium
Metal-binding
Nucleotide-binding
   Molecular functionHydrolase
Kinase
Serine/threonine-protein kinase
Transferase
   PTMADP-ribosylation
Disulfide bond
Glycoprotein
Phosphoprotein
   Technical term3D-structure
Complete proteome
Multifunctional enzyme
Reference proteome
Gene Ontology (GO)
   Biological_processHAC1-type intron splice site recognition and cleavage

Inferred from direct assay PubMed 11779465. Source: WormBase

RNA phosphodiester bond hydrolysis, endonucleolytic

Inferred from direct assay PubMed 11779465Ref.1. Source: GOC

activation of signaling protein activity involved in unfolded protein response

Inferred from direct assay Ref.1. Source: UniProtKB

cell cycle arrest

Inferred from sequence or structural similarity. Source: UniProtKB

cellular protein metabolic process

Traceable author statement. Source: Reactome

endoplasmic reticulum unfolded protein response

Traceable author statement. Source: Reactome

intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress

Inferred from electronic annotation. Source: Ensembl

positive regulation of endoplasmic reticulum unfolded protein response

Inferred from mutant phenotype PubMed 16645094. Source: UniProtKB

protein autophosphorylation

Inferred from electronic annotation. Source: Ensembl

protein phosphorylation

Inferred from direct assay Ref.1. Source: UniProtKB

regulation of transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentendoplasmic reticulum membrane

Traceable author statement. Source: Reactome

integral component of endoplasmic reticulum membrane

Inferred from direct assay Ref.1. Source: UniProtKB

mitochondrion

Inferred from electronic annotation. Source: Ensembl

nuclear inner membrane

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionATP binding

Inferred from direct assay Ref.1. Source: UniProtKB

endoribonuclease activity

Inferred from direct assay Ref.1. Source: UniProtKB

enzyme binding

Inferred from physical interaction Ref.12. Source: UniProt

identical protein binding

Inferred from physical interaction Ref.9PubMed 21317875. Source: IntAct

magnesium ion binding

Inferred from direct assay Ref.1. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.7PubMed 16645094PubMed 18369366. Source: IntAct

protein serine/threonine kinase activity

Inferred from direct assay Ref.1. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

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

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O75460-1)

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.
Isoform 2 (identifier: O75460-2)

The sequence of this isoform differs from the canonical sequence as follows:
     19-70: IFGSTSTVTL...VLQVPTHVEE → VSDRGAWGGG...SPAVGGSGRA
     71-977: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818 Potential
Chain19 – 977959Serine/threonine-protein kinase/endoribonuclease IRE1
PRO_0000024327

Regions

Topological domain19 – 443425Lumenal Potential
Transmembrane444 – 46421Helical; Potential
Topological domain465 – 977513Cytoplasmic Potential
Domain571 – 832262Protein kinase
Domain835 – 963129KEN
Nucleotide binding577 – 5859ATP By similarity UniProtKB P32361

Sites

Active site6881Proton acceptor By similarity UniProtKB P32361
Binding site5991ATP Ref.1

Amino acid modifications

Modified residue9731Phosphothreonine Ref.10
Glycosylation1761N-linked (GlcNAc...) Potential

Natural variations

Alternative sequence19 – 7052IFGST…THVEE → VSDRGAWGGGQLATAGSGPG QRRGAGAGVRAGSATAAARC PVSPAVGGSGRA in isoform 2.
VSP_034582
Alternative sequence71 – 977907Missing in isoform 2.
VSP_034583
Natural variant2441N → S in a renal clear cell carcinoma sample; somatic mutation. Ref.14
VAR_040488
Natural variant4181V → M. Ref.14
Corresponds to variant rs55869215 [ dbSNP | Ensembl ].
VAR_040489
Natural variant4741L → R in a lung adenocarcinoma sample; somatic mutation. Ref.14
Corresponds to variant rs186305118 [ dbSNP | Ensembl ].
VAR_040490
Natural variant6351R → W in a gastric adenocarcinoma sample; somatic mutation. Ref.14
VAR_040491
Natural variant7001N → S. Ref.14
VAR_040492
Natural variant7691S → F in a glioblastoma multiforme sample; somatic mutation. Ref.14
VAR_040493
Natural variant8301P → L in an ovarian serous carcinoma sample; somatic mutation. Ref.14
VAR_040494

Experimental info

Mutagenesis1091C → S: No effect on dimerization. Ref.9
Mutagenesis1481C → S: No effect on dimerization. Weakens dimer; when associated with S-148. Ref.9
Mutagenesis3321C → S: No effect on dimerization. Weakens dimer; when associated with S-332. Ref.9
Mutagenesis5991K → A: Loss of autophosphorylation and of endoribonuclease activity. Inhibition of growth arrest. Ref.1 Ref.8
Sequence conflict190 – 1912DV → EG in AAC25991. Ref.1
Sequence conflict7681I → V in AAC25991. Ref.1
Sequence conflict8161D → G in BAF85092. Ref.2
Sequence conflict824 – 8252KH → ND in AAC25991. Ref.1
Sequence conflict8801V → D in AAC25991. Ref.1
Sequence conflict9041M → T in BAF85092. Ref.2
Sequence conflict9241S → T in AAC25991. Ref.1

Secondary structure

..................................................................................................................... 977
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified July 1, 2008. Version 2.
Checksum: A2DF808CCE015536

FASTA977109,735
        10         20         30         40         50         60 
MPARRLLLLL TLLLPGLGIF GSTSTVTLPE TLLFVSTLDG SLHAVSKRTG SIKWTLKEDP 

        70         80         90        100        110        120 
VLQVPTHVEE PAFLPDPNDG SLYTLGSKNN EGLTKLPFTI PELVQASPCR SSDGILYMGK 

       130        140        150        160        170        180 
KQDIWYVIDL LTGEKQQTLS SAFADSLCPS TSLLYLGRTE YTITMYDTKT RELRWNATYF 

       190        200        210        220        230        240 
DYAASLPEDD VDYKMSHFVS NGDGLVVTVD SESGDVLWIQ NYASPVVAFY VWQREGLRKV 

       250        260        270        280        290        300 
MHINVAVETL RYLTFMSGEV GRITKWKYPF PKETEAKSKL TPTLYVGKYS TSLYASPSMV 

       310        320        330        340        350        360 
HEGVAVVPRG STLPLLEGPQ TDGVTIGDKG ECVITPSTDV KFDPGLKSKN KLNYLRNYWL 

       370        380        390        400        410        420 
LIGHHETPLS ASTKMLERFP NNLPKHRENV IPADSEKKSF EEVINLVDQT SENAPTTVSR 

       430        440        450        460        470        480 
DVEEKPAHAP ARPEAPVDSM LKDMATIILS TFLLIGWVAF IITYPLSMHQ QQQLQHQQFQ 

       490        500        510        520        530        540 
KELEKIQLLQ QQQQQLPFHP PGDTAQDGEL LDTSGPYSES SGTSSPSTSP RASNHSLCSG 

       550        560        570        580        590        600 
SSASKAGSSP SLEQDDGDEE TSVVIVGKIS FCPKDVLGHG AEGTIVYRGM FDNRDVAVKR 

       610        620        630        640        650        660 
ILPECFSFAD REVQLLRESD EHPNVIRYFC TEKDRQFQYI AIELCAATLQ EYVEQKDFAH 

       670        680        690        700        710        720 
LGLEPITLLQ QTTSGLAHLH SLNIVHRDLK PHNILISMPN AHGKIKAMIS DFGLCKKLAV 

       730        740        750        760        770        780 
GRHSFSRRSG VPGTEGWIAP EMLSEDCKEN PTYTVDIFSA GCVFYYVISE GSHPFGKSLQ 

       790        800        810        820        830        840 
RQANILLGAC SLDCLHPEKH EDVIARELIE KMIAMDPQKR PSAKHVLKHP FFWSLEKQLQ 

       850        860        870        880        890        900 
FFQDVSDRIE KESLDGPIVK QLERGGRAVV KMDWRENITV PLQTDLRKFR TYKGGSVRDL 

       910        920        930        940        950        960 
LRAMRNKKHH YRELPAEVRE TLGSLPDDFV CYFTSRFPHL LAHTYRAMEL CSHERLFQPY 

       970 
YFHEPPEPQP PVTPDAL 

« Hide

Isoform 2 [UniParc].

Checksum: C93BA0CB092E6204
Show »

FASTA706,649

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-973, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS45762.1. [O75460-1]
RefSeqNP_001424.3. NM_001433.3. [O75460-1]
UniGeneHs.133982.
Hs.700027.
Hs.744953.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2HZ6X-ray3.10A24-390[»]
3P23X-ray2.70A/B/C/D547-977[»]
ProteinModelPortalO75460.
SMRO75460. Positions 29-368, 561-964.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108391. 16 interactions.
DIPDIP-31711N.
IntActO75460. 10 interactions.
MINTMINT-3001268.
STRING9606.ENSP00000401445.

Chemistry

BindingDBO75460.
ChEMBLCHEMBL1163101.
GuidetoPHARMACOLOGY2020.

PTM databases

PhosphoSiteO75460.

Proteomic databases

MaxQBO75460.
PaxDbO75460.
PRIDEO75460.

Protocols and materials databases

DNASU2081.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000433197; ENSP00000401445; ENSG00000178607. [O75460-1]
ENST00000606895; ENSP00000475519; ENSG00000178607. [O75460-2]
GeneID2081.
KEGGhsa:2081.
UCSCuc002jdz.2. human. [O75460-1]

Organism-specific databases

CTD2081.
GeneCardsGC17M062120.
H-InvDBHIX0014084.
HGNCHGNC:3449. ERN1.
HPACAB009495.
HPA027730.
MIM604033. gene.
neXtProtNX_O75460.
PharmGKBPA27861.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000012929.
HOVERGENHBG051506.
InParanoidO75460.
KOK08852.
OMAGLRKVMH.
OrthoDBEOG7C2R0H.
PhylomeDBO75460.
TreeFamTF313986.

Enzyme and pathway databases

ReactomeREACT_17015. Metabolism of proteins.
SignaLinkO75460.

Gene expression databases

BgeeO75460.
CleanExHS_ERN1.
GenevestigatorO75460.

Family and domain databases

Gene3D2.140.10.10. 1 hit.
InterProIPR010513. 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]
PfamPF00069. Pkinase. 1 hit.
PF06479. Ribonuc_2-5A. 1 hit.
[Graphical view]
SMARTSM00564. PQQ. 5 hits.
SM00580. PUG. 1 hit.
[Graphical view]
SUPFAMSSF50998. SSF50998. 1 hit.
SSF56112. SSF56112. 1 hit.
PROSITEPS51392. KEN. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
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ChiTaRSERN1. human.
EvolutionaryTraceO75460.
GeneWikiERN1.
GenomeRNAi2081.
NextBio8459.
PROO75460.
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Entry information

Entry nameERN1_HUMAN
AccessionPrimary (citable) accession number: O75460
Secondary accession number(s): A1L457 expand/collapse secondary AC list , A8K8N8, A8MXS7, Q59EE2
Entry history
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: July 1, 2008
Last modified: July 9, 2014
This is version 139 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM